Class: ?X DisjointWith: RO_0002162 some ?Y

Term not to be used for direct annotation

Term not to be used for direct manual annotation

Catalytic activity terms in need of attention

Terms created by TermGenie that do not follow a template and require additional vetting by editors

The directed movement of a ribosomal subunit from the nucleus into the cytoplasm.
ribosomal subunit export from cell nucleus
ribosomal subunit transport from nucleus to cytoplasm

Progression through the phases of the mitotic cell cycle, the most common eukaryotic cell cycle, which canonically comprises four successive phases called G1, S, G2, and M and includes replication of the genome and the subsequent segregation of chromosomes into daughter cells. In some variant cell cycles nuclear replication or nuclear division may not be followed by cell division, or G1 and G2 phases may be absent.

Cell Cycle, Mitotic, Taeniopygia guttata

Cell Cycle, Mitotic, Saccharomyces cerevisiae

Cell Cycle, Mitotic, Plasmodium falciparum

Cell Cycle, Mitotic, Schizosaccharomyces pombe

Cell Cycle, Mitotic, Caenorhabditis elegans

Cell Cycle, Mitotic, Arabidopsis thaliana

Cell Cycle, Mitotic, Drosophila melanogaster

Cell Cycle, Mitotic, Dictyostelium discoideum

Cell Cycle, Mitotic, Mycobacterium tuberculosis

The union or introduction of genetic information from compatible mating types that results in a genetically different individual. Conjugation requires direct cellular contact between the organisms.

The developmental process in which the size or shape of a cell is generated and organized.

The division of the cytoplasm and the plasma membrane of a cell and its partitioning into two daughter cells.
Note that when annotating eukaryotic species, mitotic or meiotic cytokinesis should always be specified for manual annotation and for prokaryotic species use 'FtsZ-dependent cytokinesis ; GO:0043093' or Cdv-dependent cytokinesis ; GO:0061639. Also, note that cytokinesis does not necessarily result in physical separation and detachment of the two daughter cells from each other.

Mitotic Telophase /Cytokinesis, Mus musculus

Mitotic Telophase /Cytokinesis, Dictyostelium discoideum

Mitotic Telophase /Cytokinesis, Homo sapiens

Mitotic Telophase /Cytokinesis, Schizosaccharomyces pombe

Mitotic Telophase /Cytokinesis, Bos taurus

Mitotic Telophase /Cytokinesis, Danio rerio

Mitotic Telophase /Cytokinesis, Gallus gallus

Mitotic Telophase /Cytokinesis, Xenopus tropicalis

Mitotic Telophase /Cytokinesis, Taeniopygia guttata

Mitotic Telophase /Cytokinesis, Canis familiaris

Mitotic Telophase /Cytokinesis, Drosophila melanogaster

Mitotic Telophase /Cytokinesis, Rattus norvegicus

Mitotic Telophase /Cytokinesis, Caenorhabditis elegans

Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules), in order to modulate transcription. A protein binding transcription factor may or may not also interact with the template nucleic acid (either DNA or RNA) as well.
protein binding transcription factor activity
Note that this term is in the subset of terms that should not be used for direct gene product annotation. This term does not provide specificity with respect to the type of protein binding, e.g. transcription factor binding or RNA polymerase binding. Please use a child term that provides that specificity or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC.
transcription factor activity, protein binding

Interacting selectively and non-covalently with a DNA or RNA sequence in order to modulate transcription. The transcription factor may or may not also interact selectively with a protein or macromolecular complex.
Note that this term is in the subset of terms that should not be used for direct gene product annotation. This term does not provide specificity with respect to the type of nucleic acid binding, e.g. RNA or DNA. Please use a child term that provides that specificity or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC.
nucleic acid binding transcription factor activity

A growth pattern exhibited by budding haploid cells under certain growth conditions, in which cells retain the typical axial budding pattern of haploids, but become elongated and fail to separate after division; during growth on a solid substrate, this results in penetration of cells into the agar medium. An example of this process is found in Saccharomyces cerevisiae.
Note that this term should not be used to describe the invasion of host tissues by pathogenic organisms, which is described by the biological process term 'entry into host ; GO:0044409', nor should it be used to describe growth of diseased cells of an organism into the surrounding normal tissue, which is outside of the scope of GO.
invasive growth in response to glucose limitation

The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein.
Note that this term applies to translation performed by cytoplasmic ribosomes, which is distinct from translation performed by organellar ribosomes. For mitochondrial translation, consider GO:0032543 'mitochondrial translation' or its child terms.

Elemental activities, such as catalysis or binding, describing the actions of a gene product at the molecular level. A given gene product may exhibit one or more molecular functions.
Note that, in addition to forming the root of the molecular function ontology, this term is recommended for use for the annotation of gene products whose molecular function is unknown. Note that when this term is used for annotation, it indicates that no information was available about the molecular function of the gene product annotated as of the date the annotation was made; the evidence code ND, no data, is used to indicate this.

Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).

Interacting selectively and non-covalently with chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
nuclear membrane vesicle binding to chromatin

Interacting selectively and non-covalently with an RNA molecule or a portion thereof.

Exportin-5 recognizes 3' overhang of pre-miRNA, Xenopus tropicalis

Exportin-5 recognizes 3' overhang of pre-miRNA, Dictyostelium discoideum

Exportin-5 recognizes 3' overhang of pre-miRNA, Mus musculus

Exportin-5 recognizes 3' overhang of pre-miRNA, Drosophila melanogaster

Exportin-5 recognizes 3' overhang of pre-miRNA, Oryza sativa

Exportin-5 recognizes 3' overhang of pre-miRNA, Saccharomyces cerevisiae

Exportin-5 recognizes 3' overhang of pre-miRNA, Arabidopsis thaliana

Exportin-5 recognizes 3' overhang of pre-miRNA, Homo sapiens

Exportin-5 recognizes 3' overhang of pre-miRNA, Canis familiaris

Exportin-5 recognizes 3' overhang of pre-miRNA, Gallus gallus

Exportin-5 recognizes 3' overhang of pre-miRNA, Sus scrofa

Exportin-5 recognizes 3' overhang of pre-miRNA, Schizosaccharomyces pombe

Exportin-5 recognizes 3' overhang of pre-miRNA, Rattus norvegicus

Exportin-5 recognizes 3' overhang of pre-miRNA, Danio rerio

Exportin-5 recognizes 3' overhang of pre-miRNA, Taeniopygia guttata

Interacting selectively and non-covalently with messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.

The action of a molecule that contributes to the structural integrity of the ribosome.
Note that this term may be used to annotate ribosomal RNAs as well as ribosomal proteins.

Catalysis of the reaction: GTP + H2O = GDP + phosphate.
hydrolase activity, acting on acid anhydrides, acting on GTP, involved in cellular and subcellular movement
heterotrimeric G-protein GTPase activity
protein-synthesizing GTPase activity, elongation
protein-synthesizing GTPase activity, initiation
protein-synthesizing GTPase activity, termination
signal-recognition-particle GTPase activity
heterotrimeric G-protein GTPase, alpha-subunit
heterotrimeric G-protein GTPase, beta-subunit
heterotrimeric G-protein GTPase, gamma-subunit

Adenylate cyclase increases the GTPase activity of G alpha-olf, Danio rerio

Adenylate cyclase increases the GTPase activity of Gi alpha, Gallus gallus

trans-Golgi Network Vesicle Scission, Bos taurus

trans-Golgi Network Lysosomal Vesicle Scission, Sus scrofa

G alpha (i) auto-inactivates by hydrolysing GTP to GDP, Mus musculus

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Canis familiaris

Loss of Sar1b GTPase, Dictyostelium discoideum

trans-Golgi Network Vesicle Scission, Canis familiaris

G-protein alpha subunit is inactivated, Saccharomyces cerevisiae

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Xenopus tropicalis

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Taeniopygia guttata

Vesicle Uncoating, Saccharomyces cerevisiae

Hydrolysis of eEF1A:GTP, Dictyostelium discoideum

Adenylate cyclase increases the GTPase activity of G alpha-olf, Mus musculus

trans-Golgi Network Lysosomal Vesicle Scission, Canis familiaris

G alpha (z) auto-inactivates by hydrolysing GTP to GDP, Taeniopygia guttata

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Rattus norvegicus

G alpha (z) auto-inactivates by hydrolysing GTP to GDP, Saccharomyces cerevisiae

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Canis familiaris

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Drosophila melanogaster

G-protein alpha subunit is inactivated, Bos taurus

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Drosophila melanogaster

trans-Golgi Network Vesicle Scission, Xenopus tropicalis

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Sus scrofa

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Danio rerio

G alpha (i) auto-inactivates by hydrolysing GTP to GDP, Gallus gallus

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Xenopus tropicalis

trans-Golgi Network Vesicle Scission, Danio rerio

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Caenorhabditis elegans

G-protein alpha subunit is inactivated, Canis familiaris

G-protein alpha subunit is inactivated, Sus scrofa

G alpha (z) auto-inactivates by hydrolysing GTP to GDP, Xenopus tropicalis

Endocytosis (internalization) of clathrin-coated vesicle, Sus scrofa

Endocytosis (internalization) of clathrin-coated vesicle, Xenopus tropicalis

Disassembly of COPII coated vesicle, Gallus gallus

trans-Golgi Network Vesicle Scission, Schizosaccharomyces pombe

Vesicle Uncoating, Plasmodium falciparum

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Saccharomyces cerevisiae

G alpha (z) auto-inactivates by hydrolysing GTP to GDP, Schizosaccharomyces pombe

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Saccharomyces cerevisiae

Formation of clathrin coated vesicle, Bos taurus

Formation of clathrin coated vesicle, Schizosaccharomyces pombe

Endocytosis (internalization) of clathrin-coated vesicle, Schizosaccharomyces pombe

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Schizosaccharomyces pombe

Loss of Sar1b GTPase, Xenopus tropicalis

Formation of clathrin coated vesicle, Sus scrofa

G-protein alpha subunit is inactivated, Schizosaccharomyces pombe

trans-Golgi Network Vesicle Scission, Taeniopygia guttata

Formation of clathrin coated vesicle, Taeniopygia guttata

Formation of clathrin coated vesicle, Xenopus tropicalis

Endocytosis (internalization) of clathrin-coated vesicle, Taeniopygia guttata

trans-Golgi Network Lysosomal Vesicle Scission, Taeniopygia guttata

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Schizosaccharomyces pombe

Endocytosis (internalization) of clathrin-coated vesicle, Bos taurus

Endocytosis (internalization) of clathrin-coated vesicle, Homo sapiens

Endocytosis of clathrin-coated vesicle, Rattus norvegicus

G-protein alpha subunit is inactivated, Homo sapiens

Adenylate cyclase increases the GTPase activity of G alpha-olf, Homo sapiens

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Homo sapiens

Adenylate cyclase increases the GTPase activity of Gi alpha, Homo sapiens

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Homo sapiens

G alpha (z) auto-inactivates by hydrolysing GTP to GDP, Homo sapiens

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Homo sapiens

trans-Golgi Network Lysosomal Vesicle Scission, Homo sapiens

G alpha (i) auto-inactivates by hydrolysing GTP to GDP, Homo sapiens

trans-Golgi Network Vesicle Scission, Homo sapiens

G alpha (i)1 auto-inactivates by hydrolysing GTP to GDP, Rattus norvegicus

Formation of clathrin coated vesicle, Homo sapiens

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Gallus gallus

trans-Golgi Network Lysosomal Vesicle Scission, Mus musculus

Hydrolysis of eEF1A:GTP, Plasmodium falciparum

Adenylate cyclase increases the GTPase activity of G alpha-olf, Bos taurus

Endocytosis (internalization) of clathrin-coated vesicle, Caenorhabditis elegans

G-protein alpha subunit is inactivated, Xenopus tropicalis

trans-Golgi Network Vesicle Scission, Caenorhabditis elegans

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Mus musculus

Formation of clathrin coated vesicle, Danio rerio

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Caenorhabditis elegans

trans-Golgi Network Lysosomal Vesicle Scission, Danio rerio

Hydrolysis of eEF1A:GTP, Drosophila melanogaster

Adenylate cyclase increases the GTPase activity of G alpha-olf, Taeniopygia guttata

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Gallus gallus

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Danio rerio

Vesicle Uncoating, Dictyostelium discoideum

trans-Golgi Network Lysosomal Vesicle Scission, Rattus norvegicus

Vesicle Uncoating, Schizosaccharomyces pombe

G-protein alpha subunit is inactivated, Caenorhabditis elegans

G alpha (i) auto-inactivates by hydrolysing GTP to GDP, Xenopus tropicalis

Adenylate cyclase increases the GTPase activity of Gi alpha, Taeniopygia guttata

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Homo sapiens

trans-Golgi Network Lysosomal Vesicle Scission, Bos taurus

G alpha (i) auto-inactivates by hydrolysing GTP to GDP, Sus scrofa

Hydrolysis of Ran:GTP to Ran:GDP, Homo sapiens

Hydrolysis of reEF1A:GTP, Oryctolagus cuniculus

Disassembly of COPII coated vesicle, Homo sapiens

Hydrolysis of eEF1A:GTP, Canis familiaris

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Danio rerio

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Caenorhabditis elegans

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Taeniopygia guttata

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Bos taurus

G-protein alpha subunit is inactivated, Rattus norvegicus

G alpha (i) auto-inactivates by hydrolysing GTP to GDP, Taeniopygia guttata

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Mus musculus

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Bos taurus

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Canis familiaris

Loss of Sar1b GTPase, Taeniopygia guttata

Endocytosis (internalization) of clathrin-coated vesicle, Canis familiaris

Disassembly of COPII coated vesicle, Mus musculus

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Caenorhabditis elegans

Vesicle Uncoating, Drosophila melanogaster

Formation of clathrin coated vesicle, Canis familiaris

G-protein alpha subunit is inactivated, Taeniopygia guttata

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Taeniopygia guttata

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Canis familiaris

Adenylate cyclase increases the GTPase activity of G alpha-olf, Rattus norvegicus

G-protein alpha subunit is inactivated, Drosophila melanogaster

Hydrolysis of eEF1A:GTP, Schizosaccharomyces pombe

Loss of Sar1b GTPase, Plasmodium falciparum

Endocytosis (internalization) of clathrin-coated vesicle, Danio rerio

G-protein alpha subunit is inactivated, Danio rerio

Hydrolysis of eEF1A:GTP, Saccharomyces cerevisiae

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Rattus norvegicus

Disassembly of COPII coated vesicle, Danio rerio

Adenylate cyclase increases the GTPase activity of G alpha-olf, Canis familiaris

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Dictyostelium discoideum

trans-Golgi Network Lysosomal Vesicle Scission, Caenorhabditis elegans

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Dictyostelium discoideum

Adenylate cyclase increases the GTPase activity of G alpha-olf, Gallus gallus

G alpha (z) auto-inactivates by hydrolysing GTP to GDP, Dictyostelium discoideum

Formation of clathrin coated vesicle, Rattus norvegicus

G alpha (z) auto-inactivates by hydrolysing GTP to GDP, Mus musculus

Endocytosis (internalization) of clathrin-coated vesicle, Mus musculus

Formation of clathrin coated vesicle, Drosophila melanogaster

G alpha (z) auto-inactivates by hydrolysing GTP to GDP, Canis familiaris

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Gallus gallus

G alpha (i) auto-inactivates by hydrolysing GTP to GDP, Bos taurus

trans-Golgi Network Lysosomal Vesicle Scission, Xenopus tropicalis

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Mus musculus

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Xenopus tropicalis

G-protein alpha subunit is inactivated, Dictyostelium discoideum

Adenylate cyclase increases the GTPase activity of Gi alpha, Bos taurus

trans-Golgi Network Vesicle Scission, Drosophila melanogaster

Endocytosis (internalization) of clathrin-coated vesicle, Drosophila melanogaster

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Bos taurus

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Danio rerio

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Dictyostelium discoideum

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Gallus gallus

G-protein alpha subunit is inactivated, Mus musculus

G alpha (z) auto-inactivates by hydrolysing GTP to GDP, Gallus gallus

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Sus scrofa

trans-Golgi Network Vesicle Scission, Sus scrofa

Adenylate cyclase increases the GTPase activity of Gi alpha, Xenopus tropicalis

Adenylate cyclase increases the GTPase activity of Gi alpha, Danio rerio

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Rattus norvegicus

Adenylate cyclase increases the GTPase activity of Gi alpha, Canis familiaris

Loss of Sar1b GTPase, Drosophila melanogaster

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Drosophila melanogaster

G alpha (z) auto-inactivates by hydrolysing GTP to GDP, Sus scrofa

Adenylate cyclase increases the GTPase activity of Gi alpha, Rattus norvegicus

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Xenopus tropicalis

Loss of Sar1b GTPase, Saccharomyces cerevisiae

Adenylaye cyclase increases the GTPase activity of G alpha-olf, Taeniopygia guttata

G alpha (i) auto-inactivates by hydrolysing GTP to GDP, Danio rerio

Loss of Sar1b GTPase, Schizosaccharomyces pombe

Formation of clathrin coated vesicle, Caenorhabditis elegans

G alpha (i) auto-inactivates by hydrolysing GTP to GDP, Canis familiaris

Adenylate cyclase increases the GTPase activity of Gi alpha, Mus musculus

G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP, Mus musculus

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Sus scrofa

Formation of clathrin coated vesicle, Mus musculus

trans-Golgi Network Vesicle Scission, Mus musculus

G alpha (q) auto-inactivates by hydrolysing GTP to GDP, Bos taurus

trans-Golgi Network Vesicle Scission, Rattus norvegicus

G alpha (s) auto-inactivates by hydrolysing GTP to GDP, Drosophila melanogaster

Loss of Sar1b GTPase, Arabidopsis thaliana

G-protein alpha subunit is inactivated, Gallus gallus

Adenylate cyclase increases the GTPase activity of G alpha-olf, Xenopus tropicalis

Catalysis of the reaction: NTP + H2O = NDP + phosphate, to drive the unwinding of a DNA or RNA helix.
Note that most helicases catalyze processive duplex unwinding.

Addition of the third nucleotide on the nascent transcript, Saccharomyces cerevisiae

Formation of open bubble structure in DNA by helicases, Bos taurus

MCM8 mediated fork unwinding, Danio rerio

Formation of open bubble structure in DNA by helicases, Oryza sativa

MCM2-7 mediated fork unwinding, Plasmodium falciparum

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Xenopus tropicalis

Addition of the third nucleotide on the nascent transcript, Rattus norvegicus

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Gallus gallus

MCM2-7 mediated fork unwinding, Oryza sativa

Formation of open bubble structure in DNA by helicases, Homo sapiens

MCM8 mediated fork unwinding, Bos taurus

RNA Polymerase II Promoter Opening: First Transition, Dictyostelium discoideum

MCM8 mediated fork unwinding, Mus musculus

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Rattus norvegicus

MCM2-7 mediated fork unwinding, Rattus norvegicus

MCM2-7 mediated fork unwinding, Xenopus tropicalis

Formation of open bubble structure in DNA by helicases, Taeniopygia guttata

Formation of open bubble structure in DNA by helicases, Mus musculus

RNA Polymerase II Promoter Opening: First Transition, Taeniopygia guttata

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Dictyostelium discoideum

Addition of the third nucleotide on the nascent transcript, Arabidopsis thaliana

MCM2-7 mediated fork unwinding, Schizosaccharomyces pombe

RNA Polymerase II Promoter Opening: First Transition, Schizosaccharomyces pombe

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Arabidopsis thaliana

MCM8 mediated fork unwinding, Xenopus tropicalis

Formation of open bubble structure in DNA by helicases, Danio rerio

Cap-bound mRNA is activated by helicases, Mus musculus

MCM8 mediated fork unwinding, Drosophila melanogaster

Cap-bound mRNA is activated by helicases, Schizosaccharomyces pombe

Formation of open bubble structure in DNA by helicases, Caenorhabditis elegans

Cap-bound mRNA is activated by helicases, Homo sapiens

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Homo sapiens

RNA Polymerase II Promoter Opening: First Transition, Homo sapiens

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Drosophila melanogaster

MCM2-7 mediated fork unwinding, Danio rerio

Addition of the third nucleotide on the nascent transcript, Oryza sativa

MCM2-7 mediated fork unwinding, Drosophila melanogaster

Addition of the third nucleotide on the nascent transcript, Drosophila melanogaster

Formation of open bubble structure in DNA by helicases, Xenopus tropicalis

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Oryza sativa

RNA Polymerase II Promoter Opening: First Transition, Saccharomyces cerevisiae

MCM8 mediated fork unwinding, Rattus norvegicus

MCM8 mediated fork unwinding, Arabidopsis thaliana

Cap-bound mRNA is activated by helicases, Danio rerio

MCM2-7 mediated fork unwinding, Gallus gallus

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Schizosaccharomyces pombe

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Caenorhabditis elegans

MCM8 mediated fork unwinding, Canis familiaris

Formation of open bubble structure in DNA by helicases, Rattus norvegicus

MCM2-7 mediated fork unwinding, Dictyostelium discoideum

MCM8 mediated fork unwinding, Sus scrofa

Addition of the third nucleotide on the nascent transcript, Homo sapiens

HIV-1 Promoter Opening: First Transition, Homo sapiens

Addition of the fourth nucleotide on the nascent HIV-1 transcript: Second Transition, Homo sapiens

Addition of the third nucleotide on the nascent HIV-1 transcript, Homo sapiens

Xenopus Mcm8 mediated fork unwinding, Xenopus laevis

MCM8 mediated fork unwinding, Homo sapiens

Yeast Mcm2-7 mediated fork unwinding, Saccharomyces cerevisiae

MCM2-7 mediated fork unwinding, Homo sapiens

RNA Polymerase II Promoter Opening: First Transition, Rattus norvegicus

Formation of open bubble structure in DNA by helicases, Drosophila melanogaster

MCM2-7 mediated fork unwinding, Canis familiaris

MCM8 mediated fork unwinding, Dictyostelium discoideum

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Mus musculus

RNA Polymerase II Promoter Opening: First Transition, Arabidopsis thaliana

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Danio rerio

MCM8 mediated fork unwinding, Gallus gallus

Addition of the third nucleotide on the nascent transcript, Gallus gallus

Addition of the third nucleotide on the nascent transcript, Mus musculus

Addition of the third nucleotide on the nascent transcript, Schizosaccharomyces pombe

RNA Polymerase II Promoter Opening: First Transition, Gallus gallus

MCM8 mediated fork unwinding, Taeniopygia guttata

MCM8 mediated fork unwinding, Oryza sativa

Formation of open bubble structure in DNA by helicases, Canis familiaris

RNA Polymerase II Promoter Opening: First Transition, Danio rerio

Formation of open bubble structure in DNA by helicases, Gallus gallus

Formation of open bubble structure in DNA by helicases, Schizosaccharomyces pombe

Cap-bound mRNA is activated by helicases, Canis familiaris

MCM2-7 mediated fork unwinding, Mus musculus

MCM2-7 mediated fork unwinding, Taeniopygia guttata

Cap-bound mRNA is activated by helicases, Drosophila melanogaster

MCM2-7 mediated fork unwinding, Arabidopsis thaliana

MCM2-7 mediated fork unwinding, Caenorhabditis elegans

Addition of the third nucleotide on the nascent transcript, Caenorhabditis elegans

MCM2-7 mediated fork unwinding, Bos taurus

Formation of open bubble structure in DNA by helicases, Saccharomyces cerevisiae

Addition of the third nucleotide on the nascent transcript, Xenopus tropicalis

RNA Polymerase II Promoter Opening: First Transition, Drosophila melanogaster

MCM8 mediated fork unwinding, Plasmodium falciparum

RNA Polymerase II Promoter Opening: First Transition, Oryza sativa

RNA Polymerase II Promoter Opening: First Transition, Mus musculus

RNA Polymerase II Promoter Opening: First Transition, Xenopus tropicalis

RNA Polymerase II Promoter Opening: First Transition, Caenorhabditis elegans

Addition of the fourth nucleotide on the Nascent Transcript: Second Transition, Saccharomyces cerevisiae

Formation of open bubble structure in DNA by helicases, Arabidopsis thaliana

Addition of the third nucleotide on the nascent transcript, Dictyostelium discoideum

Formation of open bubble structure in DNA by helicases, Sus scrofa

Cap-bound mRNA is activated by helicases, Xenopus tropicalis

Addition of the third nucleotide on the nascent transcript, Danio rerio

Catalysis of the hydrolysis of ester linkages within nucleic acids.
Note that 'tRNA nucleotidyltransferase activity ; GO:0009022', also known as 'ribonuclease PH', does not have parentage in the 'nuclease activity' branch of the ontology because both GO and the Enzyme Commission define nuclease activity as a type of hydrolysis.

Conveys a signal across a cell to trigger a change in cell function or state. A signal is a physical entity or change in state that is used to transfer information in order to trigger a response.
hematopoietin/interferon-class (D200-domain) cytokine receptor signal transducer activity
quorum sensing response regulator activity
quorum sensing signal generator activity
Ligands do NOT have the molecular function 'signal transducer activity'.

Stimulates the exchange of guanyl nucleotides associated with a GTPase. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase.
guanyl-nucleotide release factor activity
Note that guanyl-nucleotide exchange factor (GEF) activity alters binding affinity, but not GTPase catalytic activity directly. Therefore GO:0005085 is under 'regulation of GTPase activity' but is not a 'GTPase regulator', which is reserved for cases where the action of one gene product directly alters the rate of catalysis by another gene product.
guanyl-nucleotide exchange factor activity

Liganded Gs-activating GPCR acts as a GEF for Gs, Gallus gallus

(Frs2)C3G stimulates nucleotide exchange on Rap1, Bos taurus

Liganded Gi-activating GPCR acts as a GEF for Gi, Dictyostelium discoideum

Liganded Gs-activating GPCR acts as a GEF for Gs, Sus scrofa

C3G stimulates nucleotide exchange on Rap1, Bos taurus

Activation of Cdc42 by pVav1, Rattus norvegicus

Gi activation by P2Y purinoceptor 12, Gallus gallus

Gq activation by P2Y purinoceptor 1, Rattus norvegicus

Activation of Rap1 by membrane-associated GEFs, Sus scrofa

Liganded Gi-activating GPCR acts as a GEF for Gi, Bos taurus

Opsins that act as GEFs for G alpha-t, Mus musculus

Activation of Rap1 by membrane-associated GEFs, Rattus norvegicus

(Frs2)C3G stimulates nucleotide exchange on Rap1, Xenopus tropicalis

Liganded Gz-activating GPCR acts as a GEF for Gz, Mus musculus

Gs activation by prostacyclin receptor, Danio rerio

Activation of Rap1 by membrane-associated GEFs, Caenorhabditis elegans

Activation of Rac1 by pVav1, Rattus norvegicus

Liganded Gq/11-activating GPCRs act as GEFs for Gq/11, Sus scrofa

Activation of Rac1 by pVav1, Gallus gallus

Sar1p Activation And Membrane Binding, Danio rerio

Liganded Gi-activating GPCR acts as a GEF for Gi, Taeniopygia guttata

Activation of Cdc42 by pVav1, Xenopus tropicalis

C3G stimulates nucleotide exchange on Rap1, Rattus norvegicus

Liganded G12/13-activating GPCR acts as a GEF for G12/13, Taeniopygia guttata

Liganded Gz-activating GPCR acts as a GEF for Gz, Bos taurus

p115-RhoGEF activation of Rac1, Canis familiaris

G13 activation by TP receptor, Rattus norvegicus

G13 activation by TP receptor, Danio rerio

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Gallus gallus

VAV2 is a GEF for Rho/Rac family kinases, Caenorhabditis elegans

Gq activation by P2Y purinoceptor 1, Xenopus tropicalis

Gq activation by P2Y purinoceptor 1, Danio rerio

Opsins that act as GEFs for G alpha-t, Danio rerio

Liganded Gi-activating GPCR acts as a GEF for Gi, Sus scrofa

Activation of Rap1 by cytosolic GEFs, Bos taurus

Liganded Gi-activating GPCR acts as a GEF for Gi, Gallus gallus

Liganded Gq/11-activating GPCRs act as GEFs for Gq/11, Rattus norvegicus

Activation of Rac1 by pVav1, Taeniopygia guttata

Gq activation by TP receptor, Mus musculus

Activation of Rac1 by pVav1, Canis familiaris

Liganded G12/13-activating GPCR acts as a GEF for G12/13, Xenopus tropicalis

Opsins that act as GEFs for G alpha-t, Bos taurus

VAV2 is a GEF for Rho/Rac family kinases, Taeniopygia guttata

Activation of Gq by Fatty Acid Receptor 1: Fatty Acid Complex, Canis familiaris

Liganded Gz-activating GPCR acts as a GEF for Gz, Gallus gallus

Gi activation by P2Y purinoceptor 12, Bos taurus

Liganded Gs-activating GPCR acts as a GEF for Gs, Mus musculus

Gs activation by prostacyclin receptor, Taeniopygia guttata

Sar1p Activation And Membrane Binding, Oryza sativa

(Frs2)C3G stimulates nucleotide exchange on Rap1, Mus musculus

C3G stimulates nucleotide exchange on Rap1, Gallus gallus

VAV3 is a GEF for Rho/Rac family kinases, Rattus norvegicus

Activation of Gq by Muscarinic Acetylcholine Receptor M3, Danio rerio

VAV2 is a GEF for Rho/Rac family kinases, Schizosaccharomyces pombe

p115-RhoGEF activation of Rac1, Caenorhabditis elegans

VAV2 is a GEF for Rho/Rac family kinases, Saccharomyces cerevisiae

Activation of Rap1 by membrane-associated GEFs, Drosophila melanogaster

p115-RhoGEF activation of Rac1, Xenopus tropicalis

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Dictyostelium discoideum

Activation of Gq by Fatty Acid Receptor 1: Fatty Acid Complex, Danio rerio

VAV3 is a GEF for Rho/Rac family kinases, Saccharomyces cerevisiae

VAV1 is a GEF for Rho/Rac family kinases, Caenorhabditis elegans

VAV3 is a GEF for Rho/Rac family kinases, Schizosaccharomyces pombe

Activation of RAC1, Drosophila melanogaster

C3G stimulates nucleotide exchange on Rap1, Homo sapiens

(Frs2)C3G stimulates nucleotide exchange on Rap1, Homo sapiens

p115-RhoGEF activation of Rac1, Homo sapiens

Sar1p Activation And Membrane Binding, Homo sapiens

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Homo sapiens

Liganded Gq/11-activating GPCRs act as GEFs for Gq/11, Homo sapiens

Activation of Rap1 by cytosolic GEFs, Homo sapiens

Liganded Gi-activating GPCR acts as a GEF for Gi, Homo sapiens

Liganded Gs-activating GPCR acts as a GEF for Gs, Homo sapiens

Activation of Gq by Muscarinic Acetylcholine Receptor M3, Homo sapiens

Opsins that act as GEFs for G alpha-t, Homo sapiens

Activation of Rac1 by pVav1, Homo sapiens

Activation of Cdc42 by pVav1, Homo sapiens

Activation of Gq by Fatty Acid Receptor 1: Fatty Acid Complex, Homo sapiens

Gi activation by P2Y purinoceptor 12, Homo sapiens

Gq activation by TP receptor, Homo sapiens

G13 activation by TP receptor, Homo sapiens

Gq activation by P2Y purinoceptor 1, Homo sapiens

Glucagon:GCGR mediates GTP-GDP exchange, Homo sapiens

Activation of Gq by Muscarinic Acetylcholine Receptor M3 (mouse), Mus musculus

Activation of Rac1 by VAV2, Homo sapiens

Liganded G12/13-activating GPCR acts as a GEF for G12/13, Homo sapiens

Liganded Gz-activating GPCR acts as a GEF for Gz, Homo sapiens

VAV2 is a GEF for Rho/Rac family kinases, Homo sapiens

Gs activation by prostacyclin receptor, Homo sapiens

Activation of Rap1 by membrane-associated GEFs, Homo sapiens

VAV3 is a GEF for Rho/Rac family kinases, Homo sapiens

VAV1 is a GEF for Rho/Rac family kinases, Homo sapiens

Liganded G12/13-activating GPCR acts as a GEF for G12/13, Bos taurus

VAV2 is a GEF for Rho/Rac family kinases, Bos taurus

Liganded G12/13-activating GPCR acts as a GEF for G12/13, Sus scrofa

Regeneration of eEF1A:GTP by eEF1B activity, Mus musculus

Liganded Gs-activating GPCR acts as a GEF for Gs, Xenopus tropicalis

Liganded Gi-activating GPCR acts as a GEF for Gi, Mus musculus

Gq activation by TP receptor, Gallus gallus

VAV1 is a GEF for Rho/Rac family kinases, Xenopus tropicalis

Liganded Gs-activating GPCR acts as a GEF for Gs, Taeniopygia guttata

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Drosophila melanogaster

Liganded G12/13-activating GPCR acts as a GEF for G12/13, Canis familiaris

Opsins that act as GEFs for G alpha-t, Canis familiaris

Sar1p Activation And Membrane Binding, Sus scrofa

Liganded Gq/11-activating GPCRs act as GEFs for Gq/11, Gallus gallus

Liganded Gq/11-activating GPCRs act as GEFs for Gq/11, Mus musculus

VAV3 is a GEF for Rho/Rac family kinases, Drosophila melanogaster

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Bos taurus

Liganded Gz-activating GPCR acts as a GEF for Gz, Rattus norvegicus

VAV2 is a GEF for Rho/Rac family kinases, Gallus gallus

Gi activation by P2Y purinoceptor 12, Canis familiaris

Activation of Gq by Muscarinic Acetylcholine Receptor M3, Xenopus tropicalis

(Frs2)C3G stimulates nucleotide exchange on Rap1, Danio rerio

p115-RhoGEF activation of Rac1, Drosophila melanogaster

G13 activation by TP receptor, Taeniopygia guttata

Activation of Rap1 by cytosolic GEFs, Xenopus tropicalis

Activation of Gq by Muscarinic Acetylcholine Receptor M3, Gallus gallus

Sar1p Activation And Membrane Binding, Bos taurus

Gi activation by P2Y purinoceptor 12, Rattus norvegicus

GDP is exchanged for GTP on DRheb, Drosophila melanogaster

Regeneration of eEF1A:GTP by eEF1B activity, Homo sapiens

Sar1p Activation And Membrane Binding, Canis familiaris

Liganded Gz-activating GPCR acts as a GEF for Gz, Taeniopygia guttata

G13 activation by TP receptor, Sus scrofa

Liganded Gs-activating GPCR acts as a GEF for Gs, Danio rerio

Liganded Gi-activating GPCR acts as a GEF for Gi, Danio rerio

Gq activation by TP receptor, Xenopus tropicalis

Liganded Gi-activating GPCR acts as a GEF for Gi, Rattus norvegicus

Activation of Rap1 by cytosolic GEFs, Mus musculus

Sar1p Activation And Membrane Binding, Rattus norvegicus

Activation of Cdc42 by pVav1, Bos taurus

Gq activation by TP receptor, Canis familiaris

Activation of Rap1 by membrane-associated GEFs, Bos taurus

Liganded Gz-activating GPCR acts as a GEF for Gz, Canis familiaris

Liganded Gz-activating GPCR acts as a GEF for Gz, Xenopus tropicalis

VAV2 is a GEF for Rho/Rac family kinases, Canis familiaris

Gq activation by P2Y purinoceptor 1, Taeniopygia guttata

VAV1 is a GEF for Rho/Rac family kinases, Mus musculus

Gs activation by prostacyclin receptor, Bos taurus

Activation of Rap1 by membrane-associated GEFs, Canis familiaris

Liganded G12/13-activating GPCR acts as a GEF for G12/13, Mus musculus

VAV3 is a GEF for Rho/Rac family kinases, Canis familiaris

Liganded Gs-activating GPCR acts as a GEF for Gs, Canis familiaris

Gi activation by P2Y purinoceptor 12, Mus musculus

Liganded Gi-activating GPCR acts as a GEF for Gi, Xenopus tropicalis

Regeneration of eEF1A:GTP by eEF1B activity, Plasmodium falciparum

(Frs2)C3G stimulates nucleotide exchange on Rap1, Canis familiaris

p115-RhoGEF activation of Rac1, Sus scrofa

Gs activation by prostacyclin receptor, Mus musculus

VAV2 is a GEF for Rho/Rac family kinases, Sus scrofa

Opsins that act as GEFs for G alpha-t, Xenopus tropicalis

Activation of Rap1 by membrane-associated GEFs, Gallus gallus

Activation of Gq by Muscarinic Acetylcholine Receptor M3, Rattus norvegicus

Sar1p Activation And Membrane Binding, Arabidopsis thaliana

VAV3 is a GEF for Rho/Rac family kinases, Bos taurus

Activation of Cdc42 by pVav1, Sus scrofa

Gq activation by TP receptor, Danio rerio

VAV1 is a GEF for Rho/Rac family kinases, Drosophila melanogaster

Activation of Rap1 by membrane-associated GEFs, Mus musculus

p115-RhoGEF activation of Rac1, Rattus norvegicus

p115-RhoGEF activation of Rac1, Mus musculus

VAV3 is a GEF for Rho/Rac family kinases, Sus scrofa

Liganded Gq/11-activating GPCRs act as GEFs for Gq/11, Xenopus tropicalis

G13 activation by TP receptor, Mus musculus

G13 activation by TP receptor, Xenopus tropicalis

VAV2 is a GEF for Rho/Rac family kinases, Xenopus tropicalis

Activation of Rap1 by cytosolic GEFs, Danio rerio

Activation of Rap1 by cytosolic GEFs, Canis familiaris

C3G stimulates nucleotide exchange on Rap1, Danio rerio

Gq activation by TP receptor, Taeniopygia guttata

Activation of Gq by Fatty Acid Receptor 1: Fatty Acid Complex, Rattus norvegicus

Liganded Gz-activating GPCR acts as a GEF for Gz, Danio rerio

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Mus musculus

VAV3 is a GEF for Rho/Rac family kinases, Danio rerio

Gi activation by P2Y purinoceptor 12, Taeniopygia guttata

Gi activation by P2Y purinoceptor 12, Sus scrofa

Gi activation by P2Y purinoceptor 12, Danio rerio

Opsins that act as GEFs for G alpha-t, Taeniopygia guttata

Gs activation by prostacyclin receptor, Gallus gallus

Liganded Gq/11-activating GPCRs act as GEFs for Gq/11, Canis familiaris

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Canis familiaris

(Frs2)C3G stimulates nucleotide exchange on Rap1, Gallus gallus

G13 activation by TP receptor, Bos taurus

Activation of Rap1 by cytosolic GEFs, Taeniopygia guttata

C3G stimulates nucleotide exchange on Rap1, Canis familiaris

Activation of Rap1 by cytosolic GEFs, Sus scrofa

Gs activation by prostacyclin receptor, Canis familiaris

VAV1 is a GEF for Rho/Rac family kinases, Canis familiaris

Activation of Gq by Fatty Acid Receptor 1: Fatty Acid Complex, Mus musculus

Activation of Gq by Muscarinic Acetylcholine Receptor M3, Bos taurus

Gq activation by TP receptor, Bos taurus

G13 activation by TP receptor, Gallus gallus

Liganded Gz-activating GPCR acts as a GEF for Gz, Sus scrofa

VAV3 is a GEF for Rho/Rac family kinases, Gallus gallus

VAV3 is a GEF for Rho/Rac family kinases, Caenorhabditis elegans

Gq activation by P2Y purinoceptor 1, Bos taurus

VAV2 is a GEF for Rho/Rac family kinases, Danio rerio

Activation of Cdc42 by pVav1, Mus musculus

Activation of Rap1 by cytosolic GEFs, Caenorhabditis elegans

Activation of Cdc42 by pVav1, Taeniopygia guttata

Activation of Gq by Muscarinic Acetylcholine Receptor M3, Canis familiaris

Gq activation by TP receptor, Sus scrofa

Activation of Rac1 by pVav1, Xenopus tropicalis

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Taeniopygia guttata

Activation of Gq by Fatty Acid Receptor 1: Fatty Acid Complex, Xenopus tropicalis

Liganded Gq/11-activating GPCRs act as GEFs for Gq/11, Bos taurus

Liganded Gi-activating GPCR acts as a GEF for Gi, Canis familiaris

Gq activation by P2Y purinoceptor 1, Mus musculus

Sar1p Activation And Membrane Binding, Mus musculus

Activation of Rac1 by pVav1, Mus musculus

G13 activation by TP receptor, Canis familiaris

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Xenopus tropicalis

C3G stimulates nucleotide exchange on Rap1, Mus musculus

Gq activation by TP receptor, Rattus norvegicus

(Frs2)C3G stimulates nucleotide exchange on Rap1, Sus scrofa

C3G stimulates nucleotide exchange on Rap1, Taeniopygia guttata

p115-RhoGEF activation of Rac1, Danio rerio

Liganded G12/13-activating GPCR acts as a GEF for G12/13, Gallus gallus

Activation of Rap1 by cytosolic GEFs, Rattus norvegicus

Liganded Gq/11-activating GPCRs act as GEFs for Gq/11, Taeniopygia guttata

VAV3 is a GEF for Rho/Rac family kinases, Mus musculus

Gi activation by P2Y purinoceptor 12, Xenopus tropicalis

(Frs2)C3G stimulates nucleotide exchange on Rap1, Taeniopygia guttata

VAV2 is a GEF for Rho/Rac family kinases, Drosophila melanogaster

Activation of Rap1 by membrane-associated GEFs, Danio rerio

Gq activation by P2Y purinoceptor 1, Canis familiaris

VAV1 is a GEF for Rho/Rac family kinases, Sus scrofa

Liganded G12/13-activating GPCR acts as a GEF for G12/13, Danio rerio

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Rattus norvegicus

Activation of Gq by Muscarinic Acetylcholine Receptor M3, Taeniopygia guttata

Activation of Cdc42 by pVav1, Gallus gallus

p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor, Danio rerio

Liganded G12/13-activating GPCR acts as a GEF for G12/13, Rattus norvegicus

Activation of Rap1 by membrane-associated GEFs, Taeniopygia guttata

Activation of Rap1 by cytosolic GEFs, Gallus gallus

Regeneration of eEF1A:GTP by eEF1B activity, Danio rerio

Liganded Gs-activating GPCR acts as a GEF for Gs, Bos taurus

C3G stimulates nucleotide exchange on Rap1, Xenopus tropicalis

Activation of Rap1 by membrane-associated GEFs, Xenopus tropicalis

Gq activation by P2Y purinoceptor 1, Sus scrofa

VAV2 is a GEF for Rho/Rac family kinases, Mus musculus

Gs activation by prostacyclin receptor, Xenopus tropicalis

Gq activation by P2Y purinoceptor 1, Gallus gallus

VAV2 is a GEF for Rho/Rac family kinases, Rattus norvegicus

Sar1p Activation And Membrane Binding, Drosophila melanogaster

Liganded Gq/11-activating GPCRs act as GEFs for Gq/11, Danio rerio

The action of a molecule that contributes to the structural integrity of a complex or assembly within or outside a cell.

The part of a cell or its extracellular environment in which a gene product is located. A gene product may be located in one or more parts of a cell and its location may be as specific as a particular macromolecular complex, that is, a stable, persistent association of macromolecules that function together.
Note that, in addition to forming the root of the cellular component ontology, this term is recommended for use for the annotation of gene products whose cellular component is unknown. Note that when this term is used for annotation, it indicates that no information was available about the cellular component of the gene product annotated as of the date the annotation was made; the evidence code ND, no data, is used to indicate this.

The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
Note that this term is intended to annotate gene products that are not attached to the cell surface. For gene products from multicellular organisms which are secreted from a cell but retained within the organism (i.e. released into the interstitial fluid or blood), consider the cellular component term 'extracellular space ; GO:0005615'.

The rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal, most prokaryotic cells and some protozoan parasites, maintaining their shape and protecting them from osmotic lysis. In plants it is made of cellulose and, often, lignin; in fungi it is composed largely of polysaccharides; in bacteria it is composed of peptidoglycan; in protozoan parasites such as Giardia species, it's made of carbohydrates and proteins.

OBSOLETE: That fraction of cells, prepared by disruptive biochemical methods, that includes the plasma and other membranes.
This term was made obsolete because it refers to a cell fractionation experimental result and not a bona fide cellular component.

A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
Chromosomes include parts that are not part of the chromatin. Examples include the kinetochore.

A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.

All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
Some anaerobic or microaerophilic organisms (e.g. Entamoeba histolytica, Giardia intestinalis and several Microsporidia species) do not have mitochondria, and contain mitochondrion-related organelles (MROs) instead, called mitosomes or hydrogenosomes, very likely derived from mitochondria. To annotate gene products located in these mitochondrial relics in species such as Entamoeba histolytica, Giardia intestinalis or others, please use GO:0032047 'mitosome' or GO:0042566 'hydrogenosome'. (See PMID:24316280 for a list of species currently known to contain mitochondrion-related organelles.)

The double lipid bilayer enclosing the mitochondrion and separating its contents from the cell cytoplasm; includes the intermembrane space.

A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol.

A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).

A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
Note that the Golgi apparatus can be located in various places in the cytoplasm. In plants and lower animal cells, the Golgi apparatus exists as many copies of discrete stacks dispersed throughout the cytoplasm, while the Golgi apparatus of interphase mammalian cells is a juxtanuclear, often pericentriolar reticulum, where the discrete Golgi stacks are stitched together to form a compact and interconnected ribbon, sometimes called the Golgi ribbon.

An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides.

An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.

Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.

The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

A protuberance from a cell of an organism that reproduces by budding, which will grow larger and become a separate daughter cell after nuclear division, cytokinesis, and cell wall formation (when appropriate). The daughter cell may completely separate from the mother cell, or the mother and daughter cells may remain associated.

The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.

The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.

Metabolism of carbohydrates, Mus musculus

Metabolism of carbohydrates, Mycobacterium tuberculosis

Metabolism of carbohydrates, Gallus gallus

Metabolism of carbohydrates, Escherichia coli

Metabolism of carbohydrates, Drosophila melanogaster

Metabolism of carbohydrates, Caenorhabditis elegans

Metabolism of carbohydrates, Xenopus tropicalis

Metabolism of carbohydrates, Staphylococcus aureus N315

Metabolism of carbohydrates, Taeniopygia guttata

Metabolism of carbohydrates, Rattus norvegicus

Metabolism of carbohydrates, Danio rerio

Metabolism of carbohydrates, Homo sapiens

Metabolism of carbohydrates, Plasmodium falciparum

Metabolism of carbohydrates, Schizosaccharomyces pombe

Metabolism of carbohydrates, Arabidopsis thaliana

Metabolism of carbohydrates, Saccharomyces cerevisiae

Metabolism of carbohydrates, Canis familiaris

Metabolism of carbohydrates, Dictyostelium discoideum

Metabolism of carbohydrates, Oryza sativa

The chemical reactions and pathways resulting in the formation of precursor metabolites, substances from which energy is derived, and any process involved in the liberation of energy from these substances.
generation of precursor metabolites and energy

The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
DNA biosynthesis is only part of this process. See also the biological process terms 'DNA-dependent DNA replication ; GO:0006261' and 'RNA-dependent DNA replication ; GO:0006278'.

Activation of ATR in response to replication stress, Mus musculus

Activation of claspin, Xenopus tropicalis

Activation of ATR in response to replication stress, Gallus gallus

Stalling of DNA replication fork and RPA binding, Taeniopygia guttata

Recruitment and activation of Chk1, Gallus gallus

Activation of ATR in response to replication stress, Xenopus tropicalis

Loading of claspin onto DNA during replication origin firing, Danio rerio

Stalling of DNA replication fork and RPA binding, Gallus gallus

Recruitment of Rad17-RFC complex to DNA, Gallus gallus

Binding of ATR-ATRIP to the RPA-ssDNA complex, Bos taurus

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Drosophila melanogaster

Recruitment and activation of Chk1, Canis familiaris

Activation of ATR in response to replication stress, Danio rerio

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Caenorhabditis elegans

Recruitment and activation of Chk1, Bos taurus

Loading of claspin onto DNA during replication origin firing, Mus musculus

Binding of ATR-ATRIP to the RPA-ssDNA complex, Xenopus tropicalis

Activation of ATR in response to replication stress, Bos taurus

Activation of ATR in response to replication stress, Drosophila melanogaster

Stalling of DNA replication fork and RPA binding, Rattus norvegicus

Activation of ATR in response to replication stress, Saccharomyces cerevisiae

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Gallus gallus

Activation of ATR in response to replication stress, Schizosaccharomyces pombe

Binding of ATR-ATRIP to the RPA-ssDNA complex, Taeniopygia guttata

Activation of ATR in response to replication stress, Rattus norvegicus

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Taeniopygia guttata

Activation of claspin, Rattus norvegicus

Recruitment of Rad17-RFC complex to DNA, Xenopus tropicalis

Loading of claspin onto DNA during replication origin firing, Rattus norvegicus

Recruitment of Rad17-RFC complex to DNA, Mus musculus

Recruitment and activation of Chk1, Taeniopygia guttata

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Dictyostelium discoideum

Recruitment and activation of Chk1, Xenopus tropicalis

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Rattus norvegicus

Loading of claspin onto DNA during replication origin firing, Canis familiaris

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Homo sapiens

Loading of claspin onto DNA during replication origin firing, Homo sapiens

Activation of ATR in response to replication stress, Homo sapiens

Recruitment of Rad17-RFC complex to DNA, Homo sapiens

Recruitment and activation of Chk1, Homo sapiens

Stalling of DNA replication fork and RPA binding, Homo sapiens

Binding of ATR-ATRIP to the RPA-ssDNA complex, Homo sapiens

Stalling of DNA replication fork and RPA binding, Canis familiaris

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Canis familiaris

Activation of ATR in response to replication stress, Dictyostelium discoideum

Loading of claspin onto DNA during replication origin firing, Taeniopygia guttata

Recruitment and activation of Chk1, Sus scrofa

Loading of claspin onto DNA during replication origin firing, Bos taurus

Recruitment of Rad17-RFC complex to DNA, Canis familiaris

Recruitment of Rad17-RFC complex to DNA, Danio rerio

Binding of ATR-ATRIP to the RPA-ssDNA complex, Danio rerio

Binding of ATR-ATRIP to the RPA-ssDNA complex, Rattus norvegicus

Stalling of DNA replication fork and RPA binding, Mus musculus

Recruitment and activation of Chk1, Rattus norvegicus

Binding of ATR-ATRIP to the RPA-ssDNA complex, Canis familiaris

Recruitment of Rad17-RFC complex to DNA, Rattus norvegicus

Recruitment of Rad17-RFC complex to DNA, Bos taurus

Binding of ATR-ATRIP to the RPA-ssDNA complex, Gallus gallus

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Schizosaccharomyces pombe

Activation of ATR in response to replication stress, Sus scrofa

Loading of claspin onto DNA during replication origin firing, Drosophila melanogaster

Stalling of DNA replication fork and RPA binding, Bos taurus

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Danio rerio

Recruitment of Rad17-RFC complex to DNA, Taeniopygia guttata

Recruitment and activation of Chk1, Danio rerio

Activation of ATR in response to replication stress, Canis familiaris

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Mus musculus

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Xenopus tropicalis

Stalling of DNA replication fork and RPA binding, Danio rerio

Stalling of DNA replication fork and RPA binding, Xenopus tropicalis

Activation of ATR in response to replication stress, Taeniopygia guttata

Activation of claspin, Taeniopygia guttata

Binding of ATR-ATRIP to the RPA-ssDNA complex, Mus musculus

Recruitment and activation of Chk1, Mus musculus

Recruitment of the Rad9-Hus1-Rad1 complex to DNA, Bos taurus

Loading of claspin onto DNA during replication origin firing, Gallus gallus

Activation of ATR in response to replication stress, Caenorhabditis elegans

Loading of claspin onto DNA during replication origin firing, Xenopus tropicalis

The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.

DNA Damage Reversal, Taeniopygia guttata

Fanconi Anemia Pathway in DNA repair, Gallus gallus

DNA Damage Reversal, Saccharomyces cerevisiae

DNA Damage Reversal, Staphylococcus aureus N315

DNA Damage Reversal, Caenorhabditis elegans

DNA Damage Reversal, Dictyostelium discoideum

DNA Damage Reversal, Mycobacterium tuberculosis

DNA Damage Reversal, Drosophila melanogaster

DNA Damage Reversal, Arabidopsis thaliana

Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Intrachromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.

Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic chromatin.
establishment or maintenance of chromatin architecture

Any process involved in the assembly of the RNA polymerase preinitiation complex (PIC) at the core promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. The initiation phase ends just before and does not include promoter clearance, or release, which is the transition between the initiation and elongation phases of transcription.
DNA-dependent RNA polymerase complex assembly at promoter
initiation of DNA-dependent transcription
initiation of transcription, DNA-dependent
transcription initiation factor activity
Note that promoter clearance is represented as a separate step, not part_of either initiation or elongation.

The cellular process that completes DNA-templated transcription; the formation of phosphodiester bonds ceases, the RNA-DNA hybrid dissociates, and RNA polymerase releases the DNA.
DNA-dependent transcription, termination
termination of DNA-dependent transcription
termination of transcription, DNA-dependent
transcription termination factor activity
transcription termination, DNA-dependent
DNA-templated transcription, termination

The extension of an RNA molecule after transcription initiation and promoter clearance at a DNA-dependent RNA polymerase promoter by the addition of ribonucleotides catalyzed by an RNA polymerase.
transcriptional elongation, DNA-dependent

The synthesis of RNA from a DNA template by RNA polymerase I (RNAP I), originating at an RNAP I promoter.
RNA polymerase I transcription factor activity
transcription from RNA polymerase I promoter

RNA Polymerase I Transcription, Mus musculus

RNA Polymerase I Transcription, Xenopus tropicalis

RNA Polymerase I Transcription, Saccharomyces cerevisiae

RNA Polymerase I Transcription, Drosophila melanogaster

RNA Polymerase I Transcription, Homo sapiens

RNA Polymerase I Transcription, Taeniopygia guttata

RNA Polymerase I Transcription, Canis familiaris

RNA Polymerase I Transcription, Caenorhabditis elegans

RNA Polymerase I Transcription, Gallus gallus

RNA Polymerase I Transcription, Bos taurus

RNA Polymerase I Transcription, Rattus norvegicus

RNA Polymerase I Transcription, Sus scrofa

RNA Polymerase I Transcription, Danio rerio

RNA Polymerase I Transcription, Oryza sativa

RNA Polymerase I Transcription, Dictyostelium discoideum

RNA Polymerase I Transcription, Schizosaccharomyces pombe

RNA Polymerase I Transcription, Arabidopsis thaliana

Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules.

The synthesis of RNA from a DNA template by RNA polymerase II, originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs).
RNA polymerase II transcription factor activity
gene-specific transcription from RNA polymerase II promoter
general transcription from RNA polymerase II promoter
specific transcription from RNA polymerase II promoter
transcription from RNA polymerase II promoter

RNA Polymerase II Transcription, Bos taurus

RNA Polymerase II Transcription, Caenorhabditis elegans

RNA Polymerase II Transcription, Canis familiaris

RNA Polymerase II Transcription, Xenopus tropicalis

RNA Polymerase II Transcription, Homo sapiens

RNA Polymerase II Transcription, Taeniopygia guttata

RNA Polymerase II Transcription, Danio rerio

RNA Polymerase II Transcription, Rattus norvegicus

RNA Polymerase II Transcription, Sus scrofa

RNA Polymerase II Transcription, Schizosaccharomyces pombe

RNA Polymerase II Transcription, Plasmodium falciparum

RNA Polymerase II Transcription, Oryza sativa

RNA Polymerase II Transcription, Mus musculus

RNA Polymerase II Transcription, Arabidopsis thaliana

RNA Polymerase II Transcription, Gallus gallus

RNA Polymerase II Transcription, Drosophila melanogaster

RNA Polymerase II Transcription, Dictyostelium discoideum

RNA Polymerase II Transcription, Saccharomyces cerevisiae

The synthesis of RNA from a DNA template by RNA polymerase III, originating at an RNAP III promoter.
RNA polymerase III transcription factor activity
transcription from RNA polymerase III promoter

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Bos taurus

RNA Polymerase III Promoter Opening at Type 1 Promoters, Bos taurus

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Rattus norvegicus

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Gallus gallus

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Rattus norvegicus

RNA Polymerase III Productive Transcription, Rattus norvegicus

Initiation of RNA Polymerase III Productive Transcription, Mus musculus

Resumption of RNA Polymerase III Productive Transcription, Taeniopygia guttata

Resumption of RNA Polymerase III Productive Transcription, Danio rerio

RNA Polymerase III Promoter Opening at Type 1 Promoters, Xenopus tropicalis

RNA Polymerase III Productive Transcription, Taeniopygia guttata

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Rattus norvegicus

Resumption of RNA Polymerase III Productive Transcription, Rattus norvegicus

RNA Polymerase III Transcription, Caenorhabditis elegans

RNA Polymerase III Promoter Opening at Type 1 Promoters, Homo sapiens

RNA Polymerase III Transcription, Xenopus tropicalis

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Canis familiaris

RNA Polymerase III Productive Transcription, Gallus gallus

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Danio rerio

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Arabidopsis thaliana

RNA Polymerase III Productive Transcription, Schizosaccharomyces pombe

Resumption of RNA Polymerase III Productive Transcription, Canis familiaris

RNA Polymerase III Productive Transcription, Sus scrofa

RNA Polymerase III Transcription, Bos taurus

RNA Polymerase III Transcription, Rattus norvegicus

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Gallus gallus

Resumption of RNA Polymerase III Productive Transcription, Gallus gallus

RNA Polymerase III Transcription, Danio rerio

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Danio rerio

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Mus musculus

RNA Polymerase III Promoter Opening at Type 1 Promoters, Taeniopygia guttata

RNA Polymerase III Transcription, Sus scrofa

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Xenopus tropicalis

RNA Polymerase III Transcription, Canis familiaris

RNA Polymerase III Transcription, Arabidopsis thaliana

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Gallus gallus

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Danio rerio

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Sus scrofa

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Gallus gallus

Initiation of RNA Polymerase III Productive Transcription, Dictyostelium discoideum

RNA Polymerase III Productive Transcription, Danio rerio

Resumption of RNA Polymerase III Productive Transcription, Sus scrofa

RNA Polymerase III Productive Transcription, Bos taurus

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Danio rerio

RNA Polymerase III Promoter Opening at Type 1 Promoters, Canis familiaris

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Taeniopygia guttata

Initiation of RNA Polymerase III Productive Transcription, Bos taurus

RNA Polymerase III Productive Transcription, Drosophila melanogaster

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Mus musculus

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Mus musculus

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Sus scrofa

Initiation of RNA Polymerase III Productive Transcription, Taeniopygia guttata

Initiation of RNA Polymerase III Productive Transcription, Arabidopsis thaliana

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Danio rerio

RNA Polymerase III Transcription, Drosophila melanogaster

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Taeniopygia guttata

Initiation of RNA Polymerase III Productive Transcription, Rattus norvegicus

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Bos taurus

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Gallus gallus

RNA Polymerase III Promoter Opening at Type 1 Promoters, Sus scrofa

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Xenopus tropicalis

RNA Polymerase III Transcription, Oryza sativa

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Xenopus tropicalis

RNA Polymerase III Productive Transcription, Oryza sativa

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Oryza sativa

Resumption of RNA Polymerase III Productive Transcription, Arabidopsis thaliana

RNA Polymerase III Transcription, Dictyostelium discoideum

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Dictyostelium discoideum

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Gallus gallus

RNA Polymerase III Productive Transcription, Arabidopsis thaliana

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Xenopus tropicalis

RNA Polymerase III Transcription, Mus musculus

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Xenopus tropicalis

Resumption of RNA Polymerase III Productive Transcription, Oryza sativa

Resumption of RNA Polymerase III Productive Transcription, Caenorhabditis elegans

Initiation of RNA Polymerase III Productive Transcription, Xenopus tropicalis

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Sus scrofa

RNA Polymerase III Productive Transcription, Dictyostelium discoideum

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Bos taurus

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Danio rerio

Resumption of RNA Polymerase III Productive Transcription, Bos taurus

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Mus musculus

RNA Polymerase III Productive Transcription, Caenorhabditis elegans

RNA Polymerase III Promoter Opening at Type 1 Promoters, Danio rerio

Initiation of RNA Polymerase III Productive Transcription, Caenorhabditis elegans

Initiation of RNA Polymerase III Productive Transcription, Schizosaccharomyces pombe

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Rattus norvegicus

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Canis familiaris

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Rattus norvegicus

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Mus musculus

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Sus scrofa

RNA Polymerase III Promoter Opening at Type 1 Promoters, Gallus gallus

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Danio rerio

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Bos taurus

RNA Polymerase III Transcription, Gallus gallus

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Rattus norvegicus

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Caenorhabditis elegans

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Taeniopygia guttata

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Drosophila melanogaster

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Mus musculus

RNA Polymerase III Transcription, Taeniopygia guttata

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Sus scrofa

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Schizosaccharomyces pombe

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Sus scrofa

Resumption of RNA Polymerase III Productive Transcription, Dictyostelium discoideum

RNA Polymerase III Transcription, Schizosaccharomyces pombe

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Caenorhabditis elegans

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Homo sapiens

Initiation of RNA Polymerase III Productive Transcription, Gallus gallus

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Caenorhabditis elegans

Initiation of RNA Polymerase III Productive Transcription, Sus scrofa

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Bos taurus

Resumption of RNA Polymerase III Productive Transcription, Mus musculus

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Taeniopygia guttata

RNA Polymerase III Transcription, Saccharomyces cerevisiae

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Gallus gallus

RNA Polymerase III Promoter Opening at Type 1 Promoters, Mus musculus

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Sus scrofa

Initiation of RNA Polymerase III Productive Transcription, Canis familiaris

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Xenopus tropicalis

Resumption of RNA Polymerase III Productive Transcription, Schizosaccharomyces pombe

Initiation of RNA Polymerase III Productive Transcription, Drosophila melanogaster

RNA Polymerase III Productive Transcription, Mus musculus

Resumption of RNA Polymerase III Productive Transcription, Drosophila melanogaster

RNA Polymerase III Productive Transcription, Xenopus tropicalis

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Drosophila melanogaster

RNA Polymerase III Promoter Opening at Type 1 Promoters, Drosophila melanogaster

Initiation of RNA Polymerase III Productive Transcription, Oryza sativa

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Taeniopygia guttata

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Drosophila melanogaster

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Rattus norvegicus

Initiation of RNA Polymerase III Productive Transcription, Danio rerio

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Drosophila melanogaster

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Dictyostelium discoideum

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Dictyostelium discoideum

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Drosophila melanogaster

Initiation of RNA Polymerase III Productive Transcription, Homo sapiens

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Caenorhabditis elegans

RNA Polymerase III Promoter Opening at Type 1 Promoters, Caenorhabditis elegans

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Caenorhabditis elegans

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Homo sapiens

RNA Polymerase III Transcription, Homo sapiens

Resumption of RNA Polymerase III Productive Transcription, Homo sapiens

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Homo sapiens

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Homo sapiens

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Homo sapiens

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Homo sapiens

RNA Polymerase III Productive Transcription, Homo sapiens

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Homo sapiens

RNA Polymerase III Productive Transcription, Canis familiaris

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Xenopus tropicalis

RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites, Bos taurus

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Canis familiaris

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Canis familiaris

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Taeniopygia guttata

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Canis familiaris

RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters, Taeniopygia guttata

RNA Polymerase III Promoter Opening at Type 1 Promoters, Rattus norvegicus

RNA Polymerase III Abortive Initiation At Type 2 Open Promoters, Drosophila melanogaster

RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters, Canis familiaris

Resumption of RNA Polymerase III Productive Transcription, Xenopus tropicalis

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Drosophila melanogaster

RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters, Mus musculus

RNA Polymerase III Abortive Initiation At Type 3 Open Promoters, Canis familiaris

RNA Polymerase III Abortive Initiation At Type 1 Open Promoters, Bos taurus

Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.

Processing of Capped Intronless Pre-mRNA, Dictyostelium discoideum

Processing of Capped Intronless Pre-mRNA, Xenopus tropicalis

Processing of Capped Intronless Pre-mRNA, Canis familiaris

Processing of Capped Intronless Pre-mRNA, Saccharomyces cerevisiae

Processing of Capped Intronless Pre-mRNA, Schizosaccharomyces pombe

Processing of Capped Intronless Pre-mRNA, Arabidopsis thaliana

Processing of Capped Intronless Pre-mRNA, Homo sapiens

Processing of Capped Intronless Pre-mRNA, Bos taurus

Processing of Capped Intronless Pre-mRNA, Caenorhabditis elegans

Processing of Capped Intronless Pre-mRNA, Gallus gallus

Processing of Capped Intronless Pre-mRNA, Drosophila melanogaster

Processing of Capped Intronless Pre-mRNA, Danio rerio

Processing of Capped Intronless Pre-mRNA, Sus scrofa

Processing of Capped Intronless Pre-mRNA, Taeniopygia guttata

Processing of Capped Intronless Pre-mRNA, Oryza sativa

Processing of Capped Intronless Pre-mRNA, Rattus norvegicus

Processing of Capped Intronless Pre-mRNA, Mus musculus

The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage.

The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA, and an initiation complex that contains the first aminoacyl-tRNA.

Eukaryotic Translation Initiation, Gallus gallus

Eukaryotic Translation Initiation, Xenopus tropicalis

Eukaryotic Translation Initiation, Homo sapiens

Eukaryotic Translation Initiation, Dictyostelium discoideum

Eukaryotic Translation Initiation, Oryza sativa

Eukaryotic Translation Initiation, Caenorhabditis elegans

Eukaryotic Translation Initiation, Taeniopygia guttata

Eukaryotic Translation Initiation, Drosophila melanogaster

Eukaryotic Translation Initiation, Rattus norvegicus

Eukaryotic Translation Initiation, Bos taurus

Eukaryotic Translation Initiation, Schizosaccharomyces pombe

Eukaryotic Translation Initiation, Arabidopsis thaliana

Eukaryotic Translation Initiation, Plasmodium falciparum

Eukaryotic Translation Initiation, Mus musculus

Eukaryotic Translation Initiation, Canis familiaris

Eukaryotic Translation Initiation, Sus scrofa

Eukaryotic Translation Initiation, Saccharomyces cerevisiae

Eukaryotic Translation Initiation, Danio rerio

The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.

Eukaryotic Translation Elongation, Dictyostelium discoideum

Eukaryotic Translation Elongation, Canis familiaris

Eukaryotic Translation Elongation, Gallus gallus

Eukaryotic Translation Elongation, Escherichia coli

Eukaryotic Translation Elongation, Mus musculus

Eukaryotic Translation Elongation, Danio rerio

Eukaryotic Translation Elongation, Xenopus tropicalis

Eukaryotic Translation Elongation, Taeniopygia guttata

Eukaryotic Translation Elongation, Caenorhabditis elegans

Eukaryotic Translation Elongation, Homo sapiens

Eukaryotic Translation Elongation, Arabidopsis thaliana

Eukaryotic Translation Elongation, Sus scrofa

Eukaryotic Translation Elongation, Bos taurus

Eukaryotic Translation Elongation, Rattus norvegicus

Eukaryotic Translation Elongation, Drosophila melanogaster

Eukaryotic Translation Elongation, Saccharomyces cerevisiae

Eukaryotic Translation Elongation, Schizosaccharomyces pombe

Eukaryotic Translation Elongation, Oryza sativa

Eukaryotic Translation Elongation, Plasmodium falciparum

Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA.

The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA, to be used in ribosome-mediated polypeptide synthesis.
tRNA aminoacylation for protein translation

Mitochondrial tRNA aminoacylation, Escherichia coli

Cytosolic tRNA aminoacylation, Sus scrofa

Mitochondrial tRNA aminoacylation, Drosophila melanogaster

tRNA Aminoacylation, Plasmodium falciparum

Mitochondrial tRNA aminoacylation, Taeniopygia guttata

tRNA Aminoacylation, Arabidopsis thaliana

Mitochondrial tRNA aminoacylation, Oryza sativa

Cytosolic tRNA aminoacylation, Staphylococcus aureus N315

Cytosolic tRNA aminoacylation, Schizosaccharomyces pombe

Cytosolic tRNA aminoacylation, Plasmodium falciparum

Mitochondrial tRNA aminoacylation, Rattus norvegicus

tRNA Aminoacylation, Schizosaccharomyces pombe

Cytosolic tRNA aminoacylation, Caenorhabditis elegans

Mitochondrial tRNA aminoacylation, Homo sapiens

Cytosolic tRNA aminoacylation, Homo sapiens

tRNA Aminoacylation, Staphylococcus aureus N315

tRNA Aminoacylation, Mycobacterium tuberculosis

Cytosolic tRNA aminoacylation, Dictyostelium discoideum

Cytosolic tRNA aminoacylation, Oryza sativa

Cytosolic tRNA aminoacylation, Bos taurus

tRNA Aminoacylation, Caenorhabditis elegans

Mitochondrial tRNA aminoacylation, Caenorhabditis elegans

Cytosolic tRNA aminoacylation, Mus musculus

Mitochondrial tRNA aminoacylation, Dictyostelium discoideum

tRNA Aminoacylation, Drosophila melanogaster

Mitochondrial tRNA aminoacylation, Saccharomyces cerevisiae

Cytosolic tRNA aminoacylation, Escherichia coli

Cytosolic tRNA aminoacylation, Danio rerio

Mitochondrial tRNA aminoacylation, Bos taurus

Cytosolic tRNA aminoacylation, Xenopus tropicalis

tRNA Aminoacylation, Taeniopygia guttata

Cytosolic tRNA aminoacylation, Taeniopygia guttata

Mitochondrial tRNA aminoacylation, Mycobacterium tuberculosis

Cytosolic tRNA aminoacylation, Drosophila melanogaster

Cytosolic tRNA aminoacylation, Rattus norvegicus

Mitochondrial tRNA aminoacylation, Arabidopsis thaliana

Cytosolic tRNA aminoacylation, Gallus gallus

Cytosolic tRNA aminoacylation, Canis familiaris

Mitochondrial tRNA aminoacylation, Xenopus tropicalis

Mitochondrial tRNA aminoacylation, Staphylococcus aureus N315

Mitochondrial tRNA aminoacylation, Mus musculus

Mitochondrial tRNA aminoacylation, Danio rerio

Cytosolic tRNA aminoacylation, Saccharomyces cerevisiae

Cytosolic tRNA aminoacylation, Mycobacterium tuberculosis

Mitochondrial tRNA aminoacylation, Plasmodium falciparum

Mitochondrial tRNA aminoacylation, Gallus gallus

tRNA Aminoacylation, Dictyostelium discoideum

Mitochondrial tRNA aminoacylation, Sus scrofa

Mitochondrial tRNA aminoacylation, Schizosaccharomyces pombe

Cytosolic tRNA aminoacylation, Arabidopsis thaliana

tRNA Aminoacylation, Saccharomyces cerevisiae

Mitochondrial tRNA aminoacylation, Canis familiaris

The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
glycoprotein-specific chaperone activity
non-chaperonin molecular chaperone ATPase activity
protein complex assembly, multichaperone pathway

Chaperonin-mediated protein folding, Arabidopsis thaliana

Chaperonin-mediated protein folding, Caenorhabditis elegans

Chaperonin-mediated protein folding, Rattus norvegicus

Chaperonin-mediated protein folding, Canis familiaris

Chaperonin-mediated protein folding, Mus musculus

Formation of tubulin folding intermediates by CCT/TriC, Canis familiaris

Chaperonin-mediated protein folding, Drosophila melanogaster

Formation of tubulin folding intermediates by CCT/TriC, Drosophila melanogaster

Chaperonin-mediated protein folding, Gallus gallus

Formation of tubulin folding intermediates by CCT/TriC, Bos taurus

Formation of tubulin folding intermediates by CCT/TriC, Rattus norvegicus

Formation of tubulin folding intermediates by CCT/TriC, Homo sapiens

Formation of tubulin folding intermediates by CCT/TriC, Mus musculus

Chaperonin-mediated protein folding, Homo sapiens

Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, Bos taurus

N-glycan trimming in the ER and Calnexin/Calreticulin cycle, Homo sapiens

Chaperonin-mediated protein folding, Oryza sativa

Chaperonin-mediated protein folding, Saccharomyces cerevisiae

Chaperonin-mediated protein folding, Schizosaccharomyces pombe

Chaperonin-mediated protein folding, Plasmodium falciparum

Formation of tubulin folding intermediates by CCT/TriC, Saccharomyces cerevisiae

Formation of tubulin folding intermediates by CCT/TriC, Gallus gallus

Formation of tubulin folding intermediates by CCT/TriC, Caenorhabditis elegans

Chaperonin-mediated protein folding, Dictyostelium discoideum

Formation of tubulin folding intermediates by CCT/TriC, Sus scrofa

Formation of tubulin folding intermediates by CCT/TriC, Plasmodium falciparum

Formation of tubulin folding intermediates by CCT/TriC, Arabidopsis thaliana

Formation of tubulin folding intermediates by CCT/TriC, Schizosaccharomyces pombe

Formation of tubulin folding intermediates by CCT/TriC, Dictyostelium discoideum

Chaperonin-mediated protein folding, Xenopus tropicalis

Chaperonin-mediated protein folding, Taeniopygia guttata

Formation of tubulin folding intermediates by CCT/TriC, Taeniopygia guttata

Formation of tubulin folding intermediates by CCT/TriC, Danio rerio

Chaperonin-mediated protein folding, Sus scrofa

Chaperonin-mediated protein folding, Danio rerio

Chaperonin-mediated protein folding, Bos taurus

Formation of tubulin folding intermediates by CCT/TriC, Xenopus tropicalis

Formation of tubulin folding intermediates by CCT/TriC, Oryza sativa

The process of introducing a phosphate group on to a protein.

The process of removing one or more phosphoric residues from a protein.

A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.

The covalent attachment of lipid groups to an amino acid in a protein.
For non-covalent interactions with a lipid, consider instead the term 'lipid binding ; GO:0008289' and its children.

The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells.
cellular amino acid and derivative metabolic process

The process of targeting specific proteins to particular regions of the cell, typically membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif.
Note that protein targeting encompasses the transport of the protein to the specified location, and may also include additional steps such as protein processing.

The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.

Lipid digestion, mobilization, and transport, Drosophila melanogaster

Lipid digestion, mobilization, and transport, Xenopus tropicalis

Lipid digestion, mobilization, and transport, Canis familiaris

Lipid digestion, mobilization, and transport, Staphylococcus aureus N315

Lipid digestion, mobilization, and transport, Saccharomyces cerevisiae

Lipid digestion, mobilization, and transport, Sus scrofa

Lipid digestion, mobilization, and transport, Bos taurus

Lipid digestion, mobilization, and transport, Rattus norvegicus

Lipid digestion, mobilization, and transport, Homo sapiens

Lipid digestion, mobilization, and transport, Danio rerio

Lipid digestion, mobilization, and transport, Arabidopsis thaliana

Lipid digestion, mobilization, and transport, Plasmodium falciparum

Lipid digestion, mobilization, and transport, Oryza sativa

Lipid digestion, mobilization, and transport, Taeniopygia guttata

Lipid digestion, mobilization, and transport, Escherichia coli

Lipid digestion, mobilization, and transport, Caenorhabditis elegans

Lipid digestion, mobilization, and transport, Mus musculus

Lipid digestion, mobilization, and transport, Mycobacterium tuberculosis

Lipid digestion, mobilization, and transport, Gallus gallus

Lipid digestion, mobilization, and transport, Schizosaccharomyces pombe

Lipid digestion, mobilization, and transport, Dictyostelium discoideum

The chemical reactions and pathways involving vitamins. Vitamin is a general term for a number of unrelated organic substances that occur in many foods in small amounts and that are necessary in trace amounts for the normal metabolic functioning of the body. Vitamins may be water-soluble or fat-soluble and usually serve as components of coenzyme systems.

Metabolism of vitamins and cofactors, Bos taurus

Metabolism of vitamins and cofactors, Saccharomyces cerevisiae

Metabolism of vitamins and cofactors, Staphylococcus aureus N315

Metabolism of vitamins and cofactors, Danio rerio

Metabolism of vitamins and cofactors, Xenopus tropicalis

Metabolism of vitamins and cofactors, Rattus norvegicus

Metabolism of vitamins and cofactors, Sus scrofa

Metabolism of vitamins and cofactors, Homo sapiens

Metabolism of vitamins and cofactors, Oryza sativa

Metabolism of vitamins and cofactors, Mycobacterium tuberculosis

Metabolism of vitamins and cofactors, Mus musculus

Metabolism of vitamins and cofactors, Caenorhabditis elegans

Metabolism of vitamins and cofactors, Gallus gallus

Metabolism of vitamins and cofactors, Taeniopygia guttata

Metabolism of vitamins and cofactors, Arabidopsis thaliana

Metabolism of vitamins and cofactors, Schizosaccharomyces pombe

Metabolism of vitamins and cofactors, Dictyostelium discoideum

Metabolism of vitamins and cofactors, Plasmodium falciparum

Metabolism of vitamins and cofactors, Drosophila melanogaster

Metabolism of vitamins and cofactors, Escherichia coli

Metabolism of vitamins and cofactors, Canis familiaris

The directed movement of charged atoms or small charged molecules into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

Transport of inorganic cations/anions and amino acids/oligopeptides, Xenopus tropicalis

Transport of inorganic cations/anions and amino acids/oligopeptides, Staphylococcus aureus N315

Transport of inorganic cations/anions and amino acids/oligopeptides, Sus scrofa

Transport of inorganic cations/anions and amino acids/oligopeptides, Saccharomyces cerevisiae

Transport of inorganic cations/anions and amino acids/oligopeptides, Arabidopsis thaliana

Transport of inorganic cations/anions and amino acids/oligopeptides, Homo sapiens

Transport of inorganic cations/anions and amino acids/oligopeptides, Oryza sativa

Transport of inorganic cations/anions and amino acids/oligopeptides, Mus musculus

Transport of inorganic cations/anions and amino acids/oligopeptides, Danio rerio

Transport of inorganic cations/anions and amino acids/oligopeptides, Gallus gallus

Transport of inorganic cations/anions and amino acids/oligopeptides, Caenorhabditis elegans

Transport of inorganic cations/anions and amino acids/oligopeptides, Escherichia coli

Transport of inorganic cations/anions and amino acids/oligopeptides, Bos taurus

Transport of inorganic cations/anions and amino acids/oligopeptides, Dictyostelium discoideum

Transport of inorganic cations/anions and amino acids/oligopeptides, Drosophila melanogaster

Transport of inorganic cations/anions and amino acids/oligopeptides, Mycobacterium tuberculosis

Transport of inorganic cations/anions and amino acids/oligopeptides, Canis familiaris

Transport of inorganic cations/anions and amino acids/oligopeptides, Rattus norvegicus

Transport of inorganic cations/anions and amino acids/oligopeptides, Plasmodium falciparum

Transport of inorganic cations/anions and amino acids/oligopeptides, Taeniopygia guttata

Transport of inorganic cations/anions and amino acids/oligopeptides, Schizosaccharomyces pombe

The directed movement of amino acids, organic acids containing one or more amino substituents, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

Amino acid transport across the plasma membrane, Rattus norvegicus

Amino acid transport across the plasma membrane, Mus musculus

Amino acid transport across the plasma membrane, Caenorhabditis elegans

Amino acid transport across the plasma membrane, Dictyostelium discoideum

Amino acid transport across the plasma membrane, Arabidopsis thaliana

Amino acid transport across the plasma membrane, Gallus gallus

Amino acid transport across the plasma membrane, Escherichia coli

Amino acid transport across the plasma membrane, Mycobacterium tuberculosis

Amino acid transport across the plasma membrane, Saccharomyces cerevisiae

Amino acid transport across the plasma membrane, Homo sapiens

Amino acid transport across the plasma membrane, Staphylococcus aureus N315

Amino acid transport across the plasma membrane, Oryza sativa

Amino acid transport across the plasma membrane, Danio rerio

Amino acid transport across the plasma membrane, Bos taurus

Amino acid transport across the plasma membrane, Drosophila melanogaster

Amino acid transport across the plasma membrane, Taeniopygia guttata

Amino acid transport across the plasma membrane, Sus scrofa

Amino acid transport across the plasma membrane, Xenopus tropicalis

Amino acid transport across the plasma membrane, Canis familiaris

The directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Lipids are compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.

Any process involved in the maintenance of an internal steady state of ions at the level of a cell.

A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle by fusion of the vesicle with the plasma membrane of a cell. Steps that prepare vesicles for fusion with the membrane (e.g. docking and priming) are included in this process. This is the process in which most molecules are secreted from eukaryotic cells.

A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.

Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
cellular response to DNA damage stimulus

Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleus.

A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
mitochondrion organization and biogenesis

A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures.
cytoskeletal organization and biogenesis
cytoskeleton organization and biogenesis

A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a peroxisome. A peroxisome is a small, membrane-bounded organelle that uses dioxygen (O2) to oxidize organic molecules.

A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a vacuole.

The process in which genetic material, in the form of chromosomes, is organized into specific structures and then physically separated and apportioned to two or more sets. In eukaryotes, chromosome segregation begins with the condensation of chromosomes, includes chromosome separation, and ends when chromosomes have completed movement to the spindle poles.

A form of asexual reproduction, occurring in certain bacteria and fungi (e.g. yeasts) and some primitive animals in which an individual arises from a daughter cell formed by pinching off a part of the parent cell. The budlike outgrowths so formed may sometimes remain attached to the parent cell.

A pattern of cell growth that occurs in conditions of nitrogen limitation and abundant fermentable carbon source. Cells become elongated, switch to a unipolar budding pattern, remain physically attached to each other, and invade the growth substrate.

The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.

Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).

Interacting selectively and non-covalently with a transcription factor, any protein required to initiate or regulate transcription.

Functions during translation by interacting selectively and non-covalently with RNA during polypeptide synthesis at the ribosome.
translation factor activity, nucleic acid binding
translation factor activity, RNA binding

Any process specifically pertinent to the functioning of integrated living units: cells, tissues, organs, and organisms. A process is a collection of molecular events with a defined beginning and end.
Note that, in addition to forming the root of the biological process ontology, this term is recommended for use for the annotation of gene products whose biological process is unknown. Note that when this term is used for annotation, it indicates that no information was available about the biological process of the gene product annotated as of the date the annotation was made; the evidence code ND, no data, is used to indicate this.

Catalysis of the transfer of a methyl group to an acceptor molecule.

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Bos taurus

methylation of Dopamine to form 3-Methoxytyramine, Taeniopygia guttata

methylation of Dopamine to form 3-Methoxytyramine, Xenopus tropicalis

methylation of Dopamine to form 3-Methoxytyramine, Rattus norvegicus

guanidinoacetate + S-adenosylmethionine => creatine + S-adenosylhomocysteine, Danio rerio

guanidinoacetate + S-adenosylmethionine => creatine + S-adenosylhomocysteine, Bos taurus

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Xenopus tropicalis

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Sus scrofa

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Schizosaccharomyces pombe

methylation of Dopamine to form 3-Methoxytyramine, Homo sapiens

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Homo sapiens

guanidinoacetate + S-adenosylmethionine => creatine + S-adenosylhomocysteine, Homo sapiens

methylation of Dopamine to form 3-Methoxytyramine, Bos taurus

guanidinoacetate + S-adenosylmethionine => creatine + S-adenosylhomocysteine, Canis familiaris

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Mycobacterium tuberculosis

methylation of Dopamine to form 3-Methoxytyramine, Mycobacterium tuberculosis

guanidinoacetate + S-adenosylmethionine => creatine + S-adenosylhomocysteine, Rattus norvegicus

methylation of Dopamine to form 3-Methoxytyramine, Canis familiaris

guanidinoacetate + S-adenosylmethionine => creatine + S-adenosylhomocysteine, Mus musculus

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Mus musculus

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Gallus gallus

guanidinoacetate + S-adenosylmethionine => creatine + S-adenosylhomocysteine, Taeniopygia guttata

methylation of Dopamine to form 3-Methoxytyramine, Sus scrofa

methylation of Dopamine to form 3-Methoxytyramine, Schizosaccharomyces pombe

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Rattus norvegicus

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Taeniopygia guttata

methylation of Dopamine to form 3-Methoxytyramine, Gallus gallus

guanidinoacetate + S-adenosylmethionine => creatine + S-adenosylhomocysteine, Xenopus tropicalis

Methylation of 3,4-dihydroxypheylacetic acid to homovanillic acid, Canis familiaris

methylation of Dopamine to form 3-Methoxytyramine, Mus musculus

guanidinoacetate + S-adenosylmethionine => creatine + S-adenosylhomocysteine, Gallus gallus

The addition of an alkyl group to a protein amino acid. An alkyl group is any group derived from an alkane by removal of one hydrogen atom.

Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.

gamma-secretase cleaves p75NTR, releasing NRIF and TRAF6, Rattus norvegicus

gamma-secretase cleaves p75NTR, releasing NRIF and TRAF6, Mus musculus

gamma-secretase cleaves p75NTR, releasing NRIF and TRAF6, Homo sapiens

Proteolytic processing of Slit, Homo sapiens

gamma-secretase cleaves p75NTR, releasing NRIF and TRAF6, Bos taurus

gamma-secretase cleaves p75NTR, releasing NRIF and TRAF6, Gallus gallus

Interacting selectively and non-covalently with a lipid.

The process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA.

mRNA Splicing, Schizosaccharomyces pombe

Enables the directed movement of proteins into, out of or within a cell, or between cells.

The directed movement of carbohydrate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Carbohydrates are any of a group of organic compounds based of the general formula Cx(H2O)y.

The chemical reactions and pathways involving oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.

Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.

The covalent alteration of one or more nucleotides within an RNA molecule to produce an RNA molecule with a sequence that differs from that coded genetically.
The term 'RNA editing' (GO:0016547) was merged into 'RNA modification' (GO:0009451) on the basis of statements in the preface of Modification and Editing of RNA (ISBN:1555811337) that there is no clear distinction between modification and editing.

The infolding of a membrane, resulting in formation of a vesicle.

A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.

The directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
nucleobase, nucleoside, nucleotide and nucleic acid transport
nucleobase-containing compound transport

A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

A membrane-bounded vesicle found in the cytoplasm of the cell.

A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a vesicle.

The directed movement of substances into, out of, or mediated by an endosome, a membrane-bounded organelle that carries materials newly ingested by endocytosis. It passes many of the materials to lysosomes for degradation.

Endosomal Sorting Complex Required For Transport (ESCRT), Homo sapiens

Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
Note that this term encompasses all activities that transfer a single phosphate group; although ATP is by far the most common phosphate donor, reactions using other phosphate donors are included in this term.

Activation of S6K1, Schizosaccharomyces pombe

Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes, Canis familiaris

Inactivation of Myt1 kinase, Mus musculus

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Taeniopygia guttata

Phosphorylation of L1 by CK-II, Rattus norvegicus

Regulation of NUDC by phosphorylation, Caenorhabditis elegans

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Canis familiaris

Phosphorylation of phospho-(Ser45,Thr41,Ser37) at Ser33 by GSK-3, Canis familiaris

Phosphorylation and inactivation of eEF2K by activated S6K1, Dictyostelium discoideum

Cdc6 protein is phosphorylated by CDK, Xenopus tropicalis

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Bos taurus

Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2, Canis familiaris

Phosphorylation of the Scc1:Cohesion Complex, Mus musculus

Phosphorylation and inactivation of eEF2K by activated S6K1, Bos taurus

Phosphorylation of APC component of the destruction complex, Drosophila melanogaster

Activation of the Anaphase Promoting Complex (APC) by PLK1, Mus musculus

Mcm2-7 is phosphorylated by DDK, Danio rerio

CAK-mediated phosphorylation of Cyclin E:Cdk2, Canis familiaris

Phosphorylation of Cyclin D:Cdk4/6 complexes, Canis familiaris

Phosphorylation and activation of CHK2 by ATM, Bos taurus

Down Regulation of Emi1 through Phosphorylation of Emi1, Bos taurus

Phosphorylation of Cdc25C at Ser216, Rattus norvegicus

Myt-1 mediated phosphorylation of Cyclin A:Cdc2, Xenopus tropicalis

Wee1- mediated phosphorylation of Cyclin B1:phospho-Cdc2 complexes, Xenopus tropicalis

Phosphoryation of phospho- (Ser45, Thr41) beta-catenin at Ser37 by GSK-3, Taeniopygia guttata

Phosphorylation and activation of eIF4G by activated S6K1, Danio rerio

Autophosphorylation of PAK-2p34 in the activation loop, Schizosaccharomyces pombe

Phosphorylation of MDM2 at serine-395 by ATM kinase, Xenopus tropicalis

Regulation of KIF23 (MKLP1) by phosphorylation, Xenopus tropicalis

Inactivation of Myt1 kinase, Rattus norvegicus

CAK-mediated phosphorylation of Cyclin A:Cdc2 complexes, Canis familiaris

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Canis familiaris

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Drosophila melanogaster

Phosphorylation of L1 by CK-II, Caenorhabditis elegans

RAF1 phosphorylates MEK1, Xenopus tropicalis

Phosphorylation of L1 by ERK, Mus musculus

Mcm2-7 is phosphorylated by DDK, Rattus norvegicus

Phosphorylation of the Scc1:Cohesion Complex, Rattus norvegicus

Activation of S6K1, Arabidopsis thaliana

Phosphorylation of MDC1/NFBD1 by ATM (within 2 c-term BRCT domains), Arabidopsis thaliana

Phosphorylation of complexed TSC2 by PKB, Drosophila melanogaster

Phosphorylation of Cyclin E2:Cdk2 complexes by Myt1, Rattus norvegicus

Wee1- mediated phosphorylation of Cyclin B1:phospho-Cdc2 complexes, Danio rerio

Activation of Cdc25C, Drosophila melanogaster

Phosphorylation of COP1 at Ser-387 by ATM, Xenopus tropicalis

Phosphorylation of NBS1 by ATM, Drosophila melanogaster

Phosphorylation of AKT2 by PDK1, Canis familiaris

Phosphorylation of NBS1 by ATM, Danio rerio

Phosphorylation of p53 at ser-15 by ATM kinase, Xenopus tropicalis

Phosphorylation and activation of Chk1 by ATM, Sus scrofa

Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2, Danio rerio

Activation of S6K1, Caenorhabditis elegans

Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes, Rattus norvegicus

Phosphorylation and activation of eIF4B by activated S6K1, Bos taurus

Regulation of KIF20A (MKL2) by phosphorylation, Bos taurus

Phosphorylation of L1 by CK-II, Canis familiaris

Activation of the Anaphase Promoting Complex (APC) by PLK1, Schizosaccharomyces pombe

Phosphorylation of COP1 at Ser-387 by ATM, Rattus norvegicus

SOS phosphorylation and dissociation (SHC), Mus musculus

Phosphorylation of Cyclin E:Cdk2 complexes by Wee-1, Xenopus tropicalis

Phosphorylation of Cyclin E:Cdk2 complexes by Wee-1, Danio rerio

Regulation of KIF20A (MKL2) by phosphorylation, Danio rerio

Phosphoryation of phospho- (Ser45, Thr41) beta-catenin at Ser37 by GSK-3, Drosophila melanogaster

Phosphorylation of phospho-(Ser45 ) at Thr 41 by GSK-3, Gallus gallus

Phosphorylation of L1 by ERK, Bos taurus

Phosphorylation of complexed TSC2 by PKB, Xenopus tropicalis

CAK-mediated phosphorylation of Cyclin A:Cdc2 complexes, Xenopus tropicalis

Phosphorylation of p53 at ser-15 by ATM kinase, Canis familiaris

Akt1 phosphorylates BAD protein, Rattus norvegicus

Phosphorylation of PDE3B, Rattus norvegicus

Phosphorylation of Cyclin A:Cdk2 at Tyr 15, Xenopus tropicalis

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Xenopus tropicalis

Akt1 phosphorylates BAD protein, Canis familiaris

Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1, Xenopus tropicalis

Wee1- mediated phosphorylation of Cyclin B1:phospho-Cdc2 complexes, Canis familiaris

Phosphorylation of TSC2 by PKB, Drosophila melanogaster

Activation of the Anaphase Promoting Complex (APC) by PLK1, Canis familiaris

Phosphorylation of Wee1 kinase by Chk1, Schizosaccharomyces pombe

Phosphorylation of L1 by ERK, Xenopus tropicalis

Phosphorylation and inactivation of eEF2K by activated S6K1, Gallus gallus

Regulation of KIF23 (MKLP1) by phosphorylation, Taeniopygia guttata

Phosphorylation of Cdc25A at Ser-123 by Chk2, Drosophila melanogaster

Phosphorylation of histone H2AX at Serine-139 by ATM at the site of DSB, Rattus norvegicus

Phosphorylation of NBS1 by ATM, Mus musculus

CAK-mediated phosphorylation of Cyclin E:Cdk2, Mus musculus

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Xenopus tropicalis

Phosphorylation of Cyclin A:Cdk2 at Tyr 15, Rattus norvegicus

CAK-mediated phosphorylation of Cyclin E:Cdk2, Xenopus tropicalis

SOS phosphorylation and dissociation (IRS, Crk), Canis familiaris

CAK-mediated phosphorylation of Cyclin E:Cdk2, Danio rerio

Phosphorylation of Ribosomal protein S6 by activated S6K1, Arabidopsis thaliana

Phosphorylation of Cdc25C at Ser216, Bos taurus

SOS phosphorylation and dissociation (IRS, Crk), Danio rerio

Phosphorylation of APC component of the destruction complex, Mus musculus

Phosphorylation of TSC2 by PKB, Mus musculus

CAK-mediated phosphorylation of Cyclin A:Cdc2 complexes, Danio rerio

Inactivation of Myt1 kinase, Canis familiaris

Phosphorylation of histone H2AX at Serine-139 by ATM at the site of DSB, Mus musculus

Phosphorylation of Cyclin E:Cdk2 complexes by Wee-1, Sus scrofa

Phosphorylation of the Emi1 DSGxxS degron by Plk1, Danio rerio

Phosphorylation of Cdc25C at Ser216, Sus scrofa

Phosphorylation and activation of CHK2 by ATM, Drosophila melanogaster

Phosphorylation of DLC2 by MAPK-8, Bos taurus

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Canis familiaris

Plk1-mediated phosphorylation of Nlp, Bos taurus

Phosphorylation of beta-catenin at Ser45 by CK1 alpha, Rattus norvegicus

Phosphorylation of Ribosomal protein S6 by activated S6K1, Gallus gallus

Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2, Mus musculus

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Danio rerio

Phosphorylation and activation of Chk1 by ATM, Danio rerio

Inactivation of Myt1 kinase, Xenopus tropicalis

Free APC/C phosphorylated by Plk1, Taeniopygia guttata

Phosphorylation of beta-catenin at Ser45 by CK1 alpha, Canis familiaris

Free APC/C phosphorylated by Plk1, Mus musculus

Phosphorylation of Cyclin B1 in the CRS domain, Xenopus tropicalis

Phosphorylation of cPLA2 by ERK-2, Gallus gallus

Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1, Danio rerio

Phosphorylation of Cdc25A at Ser-123 by Chk2, Taeniopygia guttata

Phosphorylation of 4E-BP1 by activated mTORC1, Dictyostelium discoideum

SOS phosphorylation and dissociation (IRS), Mus musculus

Inactivation of Myt1 kinase, Schizosaccharomyces pombe

Free APC/C phosphorylated by Plk1, Xenopus tropicalis

SOS phosphorylation and dissociation (IRS), Canis familiaris

Activation of the Anaphase Promoting Complex (APC) by PLK1, Drosophila melanogaster

Phosphorylation of APC component of the destruction complex, Gallus gallus

Regulation of KIF20A (MKL2) by phosphorylation, Xenopus tropicalis

CAK-mediated phosphorylation of Cyclin A:Cdk2, Sus scrofa

Free APC/C phosphorylated by Plk1, Gallus gallus

Phosphorylation of Cyclin E:Cdk2 complexes by Wee-1, Mus musculus

Phosphorylation of MDC1/NFBD1 by ATM (within 2 c-term BRCT domains), Mus musculus

Phosphorylation of APC component of the destruction complex, Rattus norvegicus

Phosphorylation and activation of Chk1 by ATM, Schizosaccharomyces pombe

Phosphorylation and inactivation of eEF2K by activated S6K1, Canis familiaris

Phosphorylation of MDC1/NFBD1 by ATM (within 2 c-term BRCT domains), Oryza sativa

Down Regulation of Emi1 through Phosphorylation of Emi1, Mus musculus

Phosphorylation of DLC2 by MAPK-8, Mus musculus

Mcm2-7 is phosphorylated by DDK, Xenopus tropicalis

Phosphorylation of histone H2AX at Serine-139 by ATM at the site of DSB, Danio rerio

Inactivation of Myt1 kinase, Drosophila melanogaster

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Rattus norvegicus

Regulation of KIF23 (MKLP1) by phosphorylation, Drosophila melanogaster

Phosphorylation and activation of eIF4G by activated S6K1, Xenopus tropicalis

FGFR associated PI3K phosphorylates PIP2 to PIP3, Homo sapiens

FGFR-associated PI3K phosphorylates PIP2 to PIP3, Homo sapiens

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Homo sapiens

Phosphorylation of Cdc25A at Ser-123 by Chk2, Caenorhabditis elegans

Regulation of KIF20A (MKL2) by phosphorylation, Homo sapiens

Mcm2-7 is phosphorylated by DDK, Drosophila melanogaster

Phosphorylation of L1 by CK-II, Xenopus tropicalis

Phosphorylation of AKT2 by PDK1, Saccharomyces cerevisiae

Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex, Schizosaccharomyces pombe

Akt1 phosphorylates BAD protein, Xenopus tropicalis

Autophosphorylation of DNA-PKcs, Dictyostelium discoideum

Phosphorylation and activation of eIF4G by activated S6K1, Oryza sativa

Regulation of KIF23 (MKLP1) by phosphorylation, Dictyostelium discoideum

Phosphorylation of Cdc25A at Ser-123 by Chk2, Saccharomyces cerevisiae

Inactivation of Wee1 kinase, Dictyostelium discoideum

Phosphorylation and activation of eIF4G by activated S6K1, Drosophila melanogaster

CAK-mediated phosphorylation of Cyclin E:Cdk2, Saccharomyces cerevisiae

Phosphorylation of L1 by ERK, Saccharomyces cerevisiae

Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex, Drosophila melanogaster

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Caenorhabditis elegans

Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1, Saccharomyces cerevisiae

Phosphorylation of BRCA1 at multiple sites by ATM, Oryza sativa

Autophosphorylation of DNA-PKcs, Rattus norvegicus

Phosphorylation of Cyclin B1 in the CRS domain, Schizosaccharomyces pombe

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Arabidopsis thaliana

Phosphorylation and activation of eIF4B by activated S6K1, Schizosaccharomyces pombe

Phosphorylation of Ribosomal protein S6 by activated S6K1, Saccharomyces cerevisiae

CAK-mediated phosphorylation of Cyclin E:Cdk2, Drosophila melanogaster

Activation of S6K1, Saccharomyces cerevisiae

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Oryza sativa

Autophosphorylation of DNA-PKcs, Bos taurus

Activation of Cdc25C, Saccharomyces cerevisiae

Phosphorylation of Ribosomal protein S6 by activated S6K1, Bos taurus

Phosphorylation of Cyclin B1 in the CRS domain, Saccharomyces cerevisiae

PIP2 conversion to PIP3, Caenorhabditis elegans

Phosphorylation of Cdc25A at Ser-123 by Chk1, Caenorhabditis elegans

Activation of Cdc25C, Schizosaccharomyces pombe

CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes, Saccharomyces cerevisiae

Phosphorylation of the Scc1:Cohesion Complex, Schizosaccharomyces pombe

Phosphorylation of Cdc25A at Ser-123 by Chk1, Schizosaccharomyces pombe

Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1, Schizosaccharomyces pombe

Autophosphorylation of DNA-PKcs, Sus scrofa

Autophosphorylation of DNA-PKcs, Mus musculus

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Schizosaccharomyces pombe

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Saccharomyces cerevisiae

Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex, Caenorhabditis elegans

Activation of Cdc25C, Caenorhabditis elegans

Phosphorylation of DLC1 by MAPK 8, Xenopus tropicalis

Autophosphorylation of DNA-PKcs, Taeniopygia guttata

Phosphorylation of AKT2 by PDK1, Schizosaccharomyces pombe

Phosphorylation of BRCA1 at multiple sites by ATM, Arabidopsis thaliana

Phosphorylation of Cdc25A at Ser-123 by Chk1, Saccharomyces cerevisiae

Phosphorylation of TSC2 by PKB, Schizosaccharomyces pombe

Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1, Drosophila melanogaster

Phosphorylation of Ribosomal protein S6 by activated S6K1, Canis familiaris

Phosphorylation and activation of eIF4G by activated S6K1, Arabidopsis thaliana

Autophosphorylation of DNA-PKcs, Xenopus tropicalis

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Caenorhabditis elegans

Phosphorylation and activation of eIF4G by activated S6K1, Dictyostelium discoideum

Autophosphorylation of DNA-PKcs, Gallus gallus

Autophosphorylation of DNA-PKcs, Canis familiaris

Phosphorylation of Cyclin E:Cdk2 complexes by Wee-1, Drosophila melanogaster

CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes, Schizosaccharomyces pombe

Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex, Danio rerio

Phosphorylation of the SA2 Cohesin Complex, Schizosaccharomyces pombe

CAK-mediated phosphorylation of Cyclin E:Cdk2, Schizosaccharomyces pombe

Autophosphorylation of DNA-PKcs, Danio rerio

Phosphorylation of Cdc25A at Ser-123 by Chk2, Schizosaccharomyces pombe

Phosphorylation of H2AX at S139 by ATM at the site of DSB, Gallus gallus

Phosphorylation of RAD51 by tyrosine kinase Abelson family protein members, Gallus gallus

Phosphorylation of the Scc1:Cohesion Complex, Taeniopygia guttata

Phosphorylation of the SA2 Cohesin Complex, Taeniopygia guttata

Phosphorylation of the Scc1:Cohesion Complex, Saccharomyces cerevisiae

Phosphorylation of the SA2 Cohesin Complex, Gallus gallus

Phosphorylation of the Scc1:Cohesion Complex, Gallus gallus

Phosphorylation of the SA2 Cohesin Complex, Saccharomyces cerevisiae

Phosphorylation (Ser5) of RNA pol II CTD, Homo sapiens

Cdc6 protein is phosphorylated by CDK, Homo sapiens

Phosphorylation of Cdc25C at Ser216, Homo sapiens

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Homo sapiens

Regulation of NUDC by phosphorylation, Homo sapiens

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Homo sapiens

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Oryctolagus cuniculus

Phosphorylation of the Scc1:Cohesion Complex, Homo sapiens

Autophosphorylation of PAK-2p34, Oryctolagus cuniculus

Phosphorylation of PDE3B by AKT-1, Mus musculus

Autophosphorylation of PAK-2p34 in the activation loop, Homo sapiens

SOS phosphorylation and dissociation (SHC), Homo sapiens

Phosphorylation of the SA2 Cohesin Complex, Homo sapiens

Phosphorylation of histone H2AX at Serine-139 by ATM at the site of DSB, Homo sapiens

Plk1-mediated phosphorylation of Nlp, Homo sapiens

Phosphorylation and activation of CHK2 by ATM, Homo sapiens

Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1, Homo sapiens

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Homo sapiens

SOS phosphorylation and dissociation (IRS), Homo sapiens

Phosphorylation of p53 at ser-15 by ATM kinase, Homo sapiens

Phosphorylation of MDC1/NFBD1 by ATM (within 2 c-term BRCT domains), Homo sapiens

Activation of the Anaphase Promoting Complex (APC) by PLK1, Homo sapiens

Akt1 phosphorylates BAD protein, Homo sapiens

Phosphorylation of DLC1 by MAPK 8, Homo sapiens

Regulation of KIF23 (MKLP1) by phosphorylation, Homo sapiens

Inactivation of Wee1 kinase, Homo sapiens

Phosphorylation of DLC2 by MAPK-8, Homo sapiens

Phosphorylation of NBS1 by ATM, Homo sapiens

Raf1 phosphorylates MEK1, Rattus norvegicus

Phosphorylation of CREB by ribosomal protein S6 kinase, Homo sapiens

Phosphorylation of COP1 at Ser-387 by ATM, Homo sapiens

Phosphorylation by MAPK/ERK, Homo sapiens

Phosphorylation of CREB by PKA, Homo sapiens

Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex, Homo sapiens

Orc1 is phosphorylated by cyclin A/CDK2, Homo sapiens

Autophosphorylation of DNA-PKcs, Homo sapiens

Phosphorylation of L1 by ERK, Homo sapiens

Phosphorylation of L1 by CK-II, Homo sapiens

Raf1 phosphorylates MEK2, Rattus norvegicus

Phosphorylation of cPLA2 by ERK-2, Homo sapiens

SOS phosphorylation and dissociation (IRS, Crk), Homo sapiens

Phosphorylation of Wee1 kinase by Chk1, Homo sapiens

Phosphorylation of BRCA1 at multiple sites by ATM, Mus musculus

Inactivation of Wee1 kinase, Canis familiaris

RAF1 phosphorylates MEK1, Taeniopygia guttata

Phosphorylation of MDC1/NFBD1 by ATM (within 2 c-term BRCT domains), Canis familiaris

Phosphorylation of Wee1 kinase by Chk1, Arabidopsis thaliana

Phosphorylation of Ribosomal protein S6 by activated S6K1, Danio rerio

Activation of the Anaphase Promoting Complex (APC) by PLK1, Xenopus tropicalis

Phosphorylation of Cyclin E:Cdk2 complexes by Wee-1, Rattus norvegicus

Phosphorylation and activation of eIF4B by activated S6K1, Xenopus tropicalis

Phosphorylation of MDM2 at serine-395 by ATM kinase, Danio rerio

Down Regulation of Emi1 through Phosphorylation of Emi1, Danio rerio

Phosphorylation of L1 by ERK, Caenorhabditis elegans

Phosphorylation of Cyclin A:Cdk2 at Tyr 15, Canis familiaris

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Saccharomyces cerevisiae

CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes, Drosophila melanogaster

Phosphorylation of beta-catenin at Ser45 by CK1 alpha, Xenopus tropicalis

Phosphorylation of L1 by ERK, Drosophila melanogaster

Phosphorylation of Ribosomal protein S6 by activated S6K1, Rattus norvegicus

Phosphorylation of AKT2 by PDK1, Xenopus tropicalis

Orc1 is phosphorylated by cyclin A/CDK2, Canis familiaris

Regulation of KIF20A (MKL2) by phosphorylation, Rattus norvegicus

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Bos taurus

Phosphorylation of 4E-BP1 by activated mTORC1, Taeniopygia guttata

Regulation of NUDC by phosphorylation, Rattus norvegicus

Cdc6 protein is phosphorylated by CDK, Bos taurus

Phosphorylation of PDE3B, Canis familiaris

Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex, Bos taurus

Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes, Xenopus tropicalis

Phosphorylation of APC component of the destruction complex, Taeniopygia guttata

Down Regulation of Emi1 through Phosphorylation of Emi1, Canis familiaris

Phosphorylation (Ser5) of RNA pol II CTD, Rattus norvegicus

Phosphorylation (Ser5) of RNA pol II CTD, Xenopus tropicalis

Phosphorylation of BRCA1 at multiple sites by ATM, Bos taurus

Phosphorylation of L1 by CK-II, Mus musculus

PIP2 conversion to PIP3, Canis familiaris

SOS phosphorylation and dissociation (IRS, Crk), Drosophila melanogaster

Phosphorylation and activation of eIF4B by activated S6K1, Canis familiaris

Phosphorylation of the Emi1 DSGxxS degron by Plk1, Gallus gallus

Phosphorylation and activation of Chk1 by ATM, Homo sapiens

Phosphorylation of the SA2 Cohesin Complex, Caenorhabditis elegans

Inactivation of Myt1 kinase, Danio rerio

Phosphorylation of the Scc1:Cohesion Complex, Xenopus tropicalis

Phosphorylation and inactivation of eEF2K by activated S6K1, Mus musculus

Phosphorylation of BRCA1 at multiple sites by ATM, Gallus gallus

Phosphorylation and activation of Chk1 by ATM, Xenopus tropicalis

Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex, Canis familiaris

Plk1-mediated phosphorylation of Nlp, Canis familiaris

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Rattus norvegicus

Phosphorylation of TSC2 by PKB, Canis familiaris

Phosphorylation of the Scc1:Cohesion Complex, Danio rerio

Phosphorylation of histone H2AX at Serine-139 by ATM at the site of DSB, Canis familiaris

Regulation of KIF20A (MKL2) by phosphorylation, Gallus gallus

Phosphorylation of the Scc1:Cohesion Complex, Canis familiaris

Orc1 is phosphorylated by cyclin A/CDK2, Rattus norvegicus

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Danio rerio

Phosphorylation and activation of CHK2 by ATM, Danio rerio

Phosphorylation of the SA2 Cohesin Complex, Danio rerio

Phosphorylation of NBS1 by ATM, Taeniopygia guttata

Autophosphorylation of PAK-2p34 in the activation loop, Gallus gallus

Phosphorylation of L1 by ERK, Taeniopygia guttata

SOS phosphorylation and dissociation (SHC), Rattus norvegicus

Phosphorylation and activation of CHK2 by ATM, Canis familiaris

Phosphorylation of L1 by CK-II, Drosophila melanogaster

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Sus scrofa

Phosphorylation (Ser5) of RNA pol II CTD, Arabidopsis thaliana

Wee1- mediated phosphorylation of Cyclin B1:phospho-Cdc2 complexes, Mus musculus

Inactivation of Myt1 kinase, Dictyostelium discoideum

Phosphorylation of MDC1/NFBD1 by ATM (within 2 c-term BRCT domains), Danio rerio

Phosphorylation of COP1 at Ser-387 by ATM, Canis familiaris

Phosphorylation of NBS1 by ATM, Arabidopsis thaliana

Phosphorylation of cPLA2 by ERK-2, Taeniopygia guttata

Phosphorylation of MDM2 at serine-395 by ATM kinase, Canis familiaris

Mcm2-7 is phosphorylated by DDK, Canis familiaris

Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2, Sus scrofa

Phosphorylation of BRCA1 at multiple sites by ATM, Rattus norvegicus

Phosphorylation of NBS1 by ATM, Gallus gallus

Phosphorylation and activation of eIF4B by activated S6K1, Taeniopygia guttata

Phosphorylation of the Emi1 DSGxxS degron by Plk1, Bos taurus

Phosphorylation of Cyclin D:Cdk4/6 complexes, Rattus norvegicus

Phosphorylation and inactivation of eEF2K by activated S6K1, Sus scrofa

Phosphorylation of phospho-(Ser45 ) at Thr 41 by GSK-3, Mus musculus

Phosphorylation of the SA2 Cohesin Complex, Dictyostelium discoideum

Phosphorylation of L1 by ERK, Danio rerio

Phosphorylation of histone H2AX at Serine-139 by ATM at the site of DSB, Taeniopygia guttata

Phosphorylation of NBS1 by ATM, Rattus norvegicus

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Canis familiaris

Phosphorylation of the Emi1 DSGxxS degron by Plk1, Mus musculus

Phosphorylation of complexed TSC2 by PKB, Bos taurus

Phosphorylation of BRCA1 at multiple sites by ATM, Taeniopygia guttata

Regulation of KIF23 (MKLP1) by phosphorylation, Schizosaccharomyces pombe

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Sus scrofa

Phosphorylation of the Emi1 DSGxxS degron by Plk1, Rattus norvegicus

Phosphorylation of Cdc25A at Ser-123 by Chk1, Canis familiaris

Phosphorylation of cPLA2 by ERK-2, Xenopus tropicalis

Phosphorylation of L1 by ERK, Rattus norvegicus

Phosphorylation and activation of Chk1 by ATM, Bos taurus

Phosphorylation (Ser5) of RNA pol II CTD, Danio rerio

Phosphorylation and inactivation of eEF2K by activated S6K1, Danio rerio

Cdc6 protein is phosphorylated by CDK, Canis familiaris

Phosphorylation of 4E-BP1 by activated mTORC1, Bos taurus

Phosphorylation of MDC1/NFBD1 by ATM (within 2 c-term BRCT domains), Rattus norvegicus

Phosphorylation and inactivation of eEF2K by activated S6K1, Xenopus tropicalis

Phosphoryation of phospho- (Ser45, Thr41) beta-catenin at Ser37 by GSK-3, Gallus gallus

Phosphorylation of Cyclin E2:Cdk2 complexes by Myt1, Homo sapiens

Inactivation of Myt1 kinase, Homo sapiens

Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex, Mus musculus

Phosphorylation of Cdc25A at Ser-123 by Chk2, Homo sapiens

Down Regulation of Emi1 through Phosphorylation of Emi1, Homo sapiens

Phosphorylation and activation of eIF4G by activated S6K1, Mus musculus

Phosphorylation and activation of Chk1 by ATM kinase, Mus musculus

CAK-mediated phosphorylation of Cyclin A:Cdc2 complexes, Homo sapiens

Hyperphosphorylation (Ser2) of RNA Pol II CTD by the P-TEFb(Cyclin T1:Cdk9) complex, Homo sapiens

Wee1- mediated phosphorylation of Cyclin B1:phospho-Cdc2 complexes, Homo sapiens

Phosphorylation of NEFL by the P-TEFb(Cyclin T1:Cdk9) complex, Homo sapiens

CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes, Homo sapiens

Phosphorylation of DSIF by the P-TEFb(Cyclin T1:Cdk9) complex, Human immunodeficiency virus 1

Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes, Homo sapiens

Myt-1 mediated phosphorylation of Cyclin A:Cdc2, Homo sapiens

Phosphorylation of Cyclin B1 in the CRS domain, Homo sapiens

Phosphorylation of TSC2 by PKB, Homo sapiens

Phosphorylation and activation of eIF4B by activated S6K1, Homo sapiens

Free APC/C phosphorylated by Plk1, Homo sapiens

Phosphorylation of the Emi1 DSGxxS degron by Plk1, Homo sapiens

Phosphorylation and activation of eIF4G by activated S6K1, Homo sapiens

Phosphorylation of 4E-BP1 by activated mTORC1, Homo sapiens

Phosphorylation and inactivation of eEF2K by activated S6K1, Homo sapiens

Phosphorylation of Ribosomal protein S6 by activated S6K1, Homo sapiens

Phosphorylation of complexed TSC2 by PKB, Homo sapiens

Phosphorylation of Cyclin D:Cdk4/6 complexes, Danio rerio

Phosphorylation of COP1 at Ser-387 by ATM, Oryza sativa

Phosphorylation of MDM2 at serine-395 by ATM kinase, Mus musculus

Phosphorylation of Cdc25A at Ser-123 by Chk2, Bos taurus

Phosphorylation of DLC2 by MAPK-8, Gallus gallus

Plk1-mediated phosphorylation of Nlp, Gallus gallus

Phosphorylation of Cyclin E:Cdk2 complexes by Wee-1, Homo sapiens

RAF1 phosphorylates MEK2, Taeniopygia guttata

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Rattus norvegicus

Phosphorylation of the Emi1 DSGxxS degron by Plk1, Xenopus tropicalis

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Mus musculus

Regulation of NUDC by phosphorylation, Bos taurus

Activation of the Anaphase Promoting Complex (APC) by PLK1, Danio rerio

Phosphorylation of L1 by CK-II, Sus scrofa

Phosphorylation of Cyclin D:Cdk4/6 complexes, Mus musculus

CAK-mediated phosphorylation of Cyclin A:Cdc2 complexes, Drosophila melanogaster

CAK-mediated phosphorylation of Cyclin A:Cdc2 complexes, Gallus gallus

Phosphoryation of phospho- (Ser45, Thr41) beta-catenin at Ser37 by GSK-3, Canis familiaris

Phosphorylation of phospho-(Ser45,Thr41,Ser37) at Ser33 by GSK-3, Gallus gallus

CAK-mediated phosphorylation of Cyclin A:Cdk2, Drosophila melanogaster

Regulation of KIF23 (MKLP1) by phosphorylation, Caenorhabditis elegans

Activation of the Anaphase Promoting Complex (APC) by PLK1, Rattus norvegicus

Phosphorylation (Ser5) of RNA pol II CTD, Drosophila melanogaster

Phosphorylation of Wee1 kinase by Chk1, Taeniopygia guttata

Mcm2-7 is phosphorylated by DDK, Taeniopygia guttata

Autophosphorylation of PAK-2p34 in the activation loop, Sus scrofa

Phosphorylation of Wee1 kinase by Chk1, Drosophila melanogaster

Phosphorylation of Cyclin B1 in the CRS domain, Bos taurus

Plk1-mediated phosphorylation of Nlp, Taeniopygia guttata

Phosphorylation of phospho-(Ser45 ) at Thr 41 by GSK-3, Taeniopygia guttata

Phosphorylation of TSC2 by PKB, Xenopus tropicalis

Phosphorylation of Cdc25A at Ser-123 by Chk2, Gallus gallus

Regulation of NUDC by phosphorylation, Xenopus tropicalis

Phosphoryation of phospho- (Ser45, Thr41) beta-catenin at Ser37 by GSK-3, Rattus norvegicus

Myt-1 mediated phosphorylation of Cyclin A:Cdc2, Danio rerio

Phosphorylation and activation of eIF4B by activated S6K1, Drosophila melanogaster

CAK-mediated phosphorylation of Cyclin A:Cdc2 complexes, Taeniopygia guttata

Phosphorylation of histone H2AX at Serine-139 by ATM at the site of DSB, Bos taurus

Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes, Danio rerio

Down Regulation of Emi1 through Phosphorylation of Emi1, Xenopus tropicalis

Free APC/C phosphorylated by Plk1, Drosophila melanogaster

Phosphorylation and inactivation of eEF2K by activated S6K1, Caenorhabditis elegans

CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes, Rattus norvegicus

Phosphorylation of phospho-(Ser45 ) at Thr 41 by GSK-3, Xenopus tropicalis

Cdc6 protein is phosphorylated by CDK, Drosophila melanogaster

Phosphorylation (Ser5) of RNA pol II CTD, Mus musculus

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Schizosaccharomyces pombe

Autophosphorylation of PAK-2p34 in the activation loop, Caenorhabditis elegans

Phosphorylation of Wee1 kinase by Chk1, Oryza sativa

SOS phosphorylation and dissociation (IRS), Bos taurus

Phosphorylation of Cyclin B1 in the CRS domain, Canis familiaris

Mcm2-7 is phosphorylated by DDK, Bos taurus

Phosphorylation of 4E-BP1 by activated mTORC1, Canis familiaris

Phosphorylation of p53 at ser-15 by ATM kinase, Danio rerio

Cdc6 protein is phosphorylated by CDK, Danio rerio

Phosphorylation of p53 at ser-15 by ATM kinase, Mus musculus

Phosphorylation of the Scc1:Cohesion Complex, Drosophila melanogaster

Autophosphorylation of PAK-2p34 in the activation loop, Xenopus tropicalis

Orc1 is phosphorylated by cyclin A/CDK2, Mus musculus

Phosphorylation of Cyclin E2:Cdk2 complexes by Myt1, Danio rerio

Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2, Drosophila melanogaster

Phosphorylation of complexed TSC2 by PKB, Sus scrofa

Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1, Mus musculus

Phosphorylation of the Scc1:Cohesion Complex, Dictyostelium discoideum

Regulation of KIF20A (MKL2) by phosphorylation, Dictyostelium discoideum

Mcm2-7 is phosphorylated by DDK, Mus musculus

Regulation of KIF20A (MKL2) by phosphorylation, Drosophila melanogaster

Phosphorylation of NBS1 by ATM, Oryza sativa

Inactivation of Wee1 kinase, Xenopus tropicalis

Phosphorylation of L1 by ERK, Schizosaccharomyces pombe

Down Regulation of Emi1 through Phosphorylation of Emi1, Taeniopygia guttata

Phosphorylation of COP1 at Ser-387 by ATM, Arabidopsis thaliana

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Oryza sativa

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Sus scrofa

CAK-mediated phosphorylation of Cyclin A:Cdc2 complexes, Rattus norvegicus

Phosphorylation (Ser5) of RNA pol II CTD, Dictyostelium discoideum

Phosphorylation of MDM2 at serine-395 by ATM kinase, Rattus norvegicus

Phosphorylation of Cdc25A at Ser-123 by Chk1, Drosophila melanogaster

Phosphorylation and activation of CHK2 by ATM, Taeniopygia guttata

Phosphorylation and activation of CHK2 by ATM, Rattus norvegicus

Phosphorylation of APC component of the destruction complex, Xenopus tropicalis

Phosphorylation of phospho-(Ser45 ) at Thr 41 by GSK-3, Bos taurus

Phosphorylation of phospho-(Ser45,Thr41,Ser37) at Ser33 by GSK-3, Xenopus tropicalis

Wee1- mediated phosphorylation of Cyclin B1:phospho-Cdc2 complexes, Bos taurus

Phosphorylation of Cyclin E2:Cdk2 complexes by Myt1, Canis familiaris

Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1, Rattus norvegicus

Phosphorylation of Cdc25A at Ser-123 by Chk1, Rattus norvegicus

Phosphorylation of beta-catenin at Ser45 by CK1 alpha, Drosophila melanogaster

Orc1 is phosphorylated by cyclin A/CDK2, Drosophila melanogaster

Phosphorylation of Cyclin A:Cdk2 at Tyr 15, Danio rerio

Phosphorylation of Cx43 by c-src, Bos taurus

Phosphorylation of Cdc25A at Ser-123 by Chk1, Bos taurus

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Mus musculus

Phosphorylation and activation of Chk1 by ATM, Saccharomyces cerevisiae

Phosphorylation of complexed TSC2 by PKB, Danio rerio

PIP2 conversion to PIP3, Taeniopygia guttata

Phosphorylation of DLC2 by MAPK-8, Xenopus tropicalis

Autophosphorylation of PAK-2p34 in the activation loop, Rattus norvegicus

Phosphorylation of Cyclin D:Cdk4/6 complexes, Xenopus tropicalis

Phosphorylation and activation of Chk1 by ATM, Gallus gallus

CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes, Canis familiaris

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Bos taurus

Phosphorylation of the SA2 Cohesin Complex, Canis familiaris

Phosphorylation of phospho-(Ser45,Thr41,Ser37) at Ser33 by GSK-3, Mus musculus

Phosphorylation of complexed TSC2 by PKB, Rattus norvegicus

Plk1-mediated phosphorylation of Nlp, Mus musculus

Down Regulation of Emi1 through Phosphorylation of Emi1, Rattus norvegicus

Inactivation of Wee1 kinase, Rattus norvegicus

Phosphorylation of DLC2 by MAPK-8, Canis familiaris

PIP2 conversion to PIP3, Rattus norvegicus

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Caenorhabditis elegans

Inactivation of Myt1 kinase, Saccharomyces cerevisiae

Phosphorylation (Ser5) of RNA pol II CTD, Schizosaccharomyces pombe

Phosphorylation and activation of Chk1 by ATM, Oryza sativa

Phosphorylation of the SA2 Cohesin Complex, Mus musculus

Phosphorylation and activation of eIF4G by activated S6K1, Gallus gallus

Phosphorylation of NBS1 by ATM, Canis familiaris

CAK-mediated phosphorylation of Cyclin A:Cdk2, Danio rerio

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Arabidopsis thaliana

Phosphorylation and activation of CHK2 by ATM, Mus musculus

Wee1- mediated phosphorylation of Cyclin B1:phospho-Cdc2 complexes, Drosophila melanogaster

Phosphorylation and activation of Chk1 by ATM, Rattus norvegicus

Phosphorylation of Wee1 kinase by Chk1, Gallus gallus

Plk1-mediated phosphorylation of Nlp, Danio rerio

Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes, Taeniopygia guttata

Free APC/C phosphorylated by Plk1, Bos taurus

Phosphorylation of Cdc25A at Ser-123 by Chk1, Mus musculus

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Gallus gallus

Phosphorylation of MDC1/NFBD1 by ATM (within 2 c-term BRCT domains), Sus scrofa

Phosphorylation of COP1 at Ser-387 by ATM, Mus musculus

Phosphorylation of the SA2 Cohesin Complex, Xenopus tropicalis

Phosphorylation of Wee1 kinase by Chk1, Rattus norvegicus

CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes, Mus musculus

Phosphorylation of L1 by ERK, Sus scrofa

Phosphorylation of COP1 at Ser-387 by ATM, Taeniopygia guttata

Phosphorylation of p53 at ser-15 by ATM kinase, Rattus norvegicus

Phosphorylation of Cdc25A at Ser-123 by Chk1, Homo sapiens

Cdc6 protein is phosphorylated by CDK, Saccharomyces cerevisiae

Phosphoryation of phospho- (Ser45, Thr41) beta-catenin at Ser37 by GSK-3, Bos taurus

Phosphorylation of Wee1 kinase by Chk1, Sus scrofa

Phosphorylation of beta-catenin at Ser45 by CK1 alpha, Taeniopygia guttata

Activation of S6K1, Dictyostelium discoideum

Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1, Canis familiaris

Activation of the Anaphase Promoting Complex (APC) by PLK1, Taeniopygia guttata

Phosphorylation of Cdc25C at Ser216, Mus musculus

Regulation of KIF20A (MKL2) by phosphorylation, Mus musculus

Phosphorylation of Cx43 by c-src, Sus scrofa

Phosphorylation and activation of eIF4G by activated S6K1, Bos taurus

Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes, Gallus gallus

Phosphorylation of Cyclin B1 in the CRS domain, Rattus norvegicus

Phosphorylation of L1 by ERK, Canis familiaris

CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes, Xenopus tropicalis

Phosphorylation of BRCA1 at multiple sites by ATM, Canis familiaris

Phosphorylation and activation of Chk1 by ATM, Drosophila melanogaster

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Gallus gallus

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Mus musculus

Phosphorylation of the SA2 Cohesin Complex, Bos taurus

Phosphorylation and activation of CHK2 by ATM, Schizosaccharomyces pombe

Phosphorylation of Cyclin E1:Cdk2 complexes by Myt1, Bos taurus

Phosphorylation of COP1 at Ser-387 by ATM, Bos taurus

Activation of the Anaphase Promoting Complex (APC) by PLK1, Saccharomyces cerevisiae

Phosphorylation of Cyclin A:Cdk2 at Tyr 15, Drosophila melanogaster

Regulation of NUDC by phosphorylation, Dictyostelium discoideum

Phosphorylation of TSC2 by PKB, Bos taurus

Phosphorylation and activation of eIF4G by activated S6K1, Rattus norvegicus

Akt1 phosphorylates BAD protein, Mus musculus

Phosphorylation of Cx43 by c-src, Xenopus tropicalis

Phosphorylation of PD-1, Rattus norvegicus

Cdc6 protein is phosphorylated by CDK, Sus scrofa

Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2, Rattus norvegicus

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Danio rerio

Phosphorylation of p53 at ser-15 by ATM kinase, Bos taurus

Phosphorylation of Ribosomal protein S6 by activated S6K1, Sus scrofa

Phosphorylation (Ser5) of RNA pol II CTD, Gallus gallus

Regulation of NUDC by phosphorylation, Danio rerio

Phosphorylation of cPLA2 by ERK-2, Bos taurus

Phosphorylation of L1 by CK-II, Danio rerio

Phosphorylation of Cx43 by c-src, Mus musculus

Cdc6 protein is phosphorylated by CDK, Schizosaccharomyces pombe

Phosphorylation of Cyclin A:Cdk2 at Tyr 15, Sus scrofa

Regulation of KIF23 (MKLP1) by phosphorylation, Mus musculus

Phosphorylation of Cx43 by c-src, Rattus norvegicus

SOS phosphorylation and dissociation (SHC), Danio rerio

Phosphorylation of AKT2 by PDK1, Caenorhabditis elegans

Akt1 phosphorylates BAD protein, Bos taurus

Phosphorylation of Cyclin E2:Cdk2 complexes by Myt1, Xenopus tropicalis

Phosphorylation of Cyclin B1 in the CRS domain, Mus musculus

Phosphorylation of MDM2 at serine-395 by ATM kinase, Gallus gallus

Activation of the Anaphase Promoting Complex (APC) by PLK1, Gallus gallus

Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2, Xenopus tropicalis

Phosphorylation of PDE3B, Xenopus tropicalis

Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes, Bos taurus

CAK-mediated phosphorylation of Cyclin B1:Cdc2 complexes, Danio rerio

Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex, Xenopus tropicalis

Phosphorylation of NBS1 by ATM, Sus scrofa

Phosphorylation of Cdc25A at Ser-123 by Chk1, Xenopus tropicalis

Regulation of KIF23 (MKLP1) by phosphorylation, Rattus norvegicus

Phosphorylation of Cdc25A at Ser-123 by Chk1, Taeniopygia guttata

CAK-mediated phosphorylation of Cyclin A:Cdk2, Canis familiaris

CAK-mediated phosphorylation of Cyclin A:Cdk2, Xenopus tropicalis

Phosphorylation and inactivation of eEF2K by activated S6K1, Rattus norvegicus

Orc1 is phosphorylated by cyclin A/CDK2, Bos taurus

Phosphorylation of Ribosomal protein S6 by activated S6K1, Caenorhabditis elegans

Phosphorylation of cPLA2 by ERK-2, Danio rerio

Inactivation of Wee1 kinase, Taeniopygia guttata

Cdc6 protein is phosphorylated by CDK, Rattus norvegicus

Phosphorylation of the Emi1 DSGxxS degron by Plk1, Taeniopygia guttata

Plk1-mediated phosphorylation of Nlp, Xenopus tropicalis

Phosphorylation of Cdc25A at Ser-123 by Chk2, Rattus norvegicus

Phosphorylation of Cdc25A at Ser-123 by Chk2, Danio rerio

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Drosophila melanogaster

Phosphorylation (Ser5) of RNA pol II CTD, Oryza sativa

Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex, Rattus norvegicus

Autophosphorylation of PAK-2p34 in the activation loop, Drosophila melanogaster

Free APC/C phosphorylated by Plk1, Canis familiaris

Phosphorylation of Cdc25A at Ser-123 by Chk1, Gallus gallus

Phosphorylation of APC component of the destruction complex, Canis familiaris

Phosphorylation of AKT2 by PDK1, Bos taurus

Phosphorylation of phospho-(Ser45,Thr41,Ser37) at Ser33 by GSK-3, Taeniopygia guttata

Phosphorylation of NBS1 by ATM, Xenopus tropicalis

Phosphorylation of Ribosomal protein S6 by activated S6K1, Xenopus tropicalis

Phosphorylation of MDM2 at serine-395 by ATM kinase, Taeniopygia guttata

Phosphorylation of beta-catenin at Ser45 by CK1 alpha, Mus musculus

Phosphoryation of phospho- (Ser45, Thr41) beta-catenin at Ser37 by GSK-3, Mus musculus

Phosphorylation of Ribosomal protein S6 by activated S6K1, Schizosaccharomyces pombe

Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2, Homo sapiens

Phosphorylation of AKT2 by PDK1, Sus scrofa

Phosphorylation of Wee1 kinase by Chk1, Bos taurus

Wee1- mediated phosphorylation of Cyclin B1:phospho-Cdc2 complexes, Rattus norvegicus

Phosphorylation of AKT2 by PDK1, Mus musculus

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Taeniopygia guttata

Regulation of NUDC by phosphorylation, Canis familiaris

Phosphorylation of Wee1 kinase by Chk1, Mus musculus

Phosphorylation of Cyclin E:Cdk2 complexes by Wee-1, Canis familiaris

Regulation of NUDC by phosphorylation, Drosophila melanogaster

Phosphorylation of Cyclin A:Cdk2 at Tyr 15, Homo sapiens

CAK-mediated phosphorylation of Cyclin E:Cdk2, Homo sapiens

Phosphorylation (Ser5) of RNA pol II CTD, Caenorhabditis elegans

Mcm2-7 is phosphorylated by DDK, Homo sapiens

CAK-mediated phosphorylation of Cyclin A:Cdk2, Homo sapiens

Phosphorylation of AKT2 by PDK1, Homo sapiens

Phosphorylation of Wee1 kinase by Chk1, Canis familiaris

SOS phosphorylation and dissociation (IRS, Crk), Mus musculus

Phosphorylation of Cyclin E2:Cdk2 complexes by Myt1, Bos taurus

Inactivation of Wee1 kinase, Danio rerio

Phosphorylation and activation of CHK2 by ATM, Gallus gallus

Phosphorylation (Ser5) of RNA pol II CTD, Saccharomyces cerevisiae

Phosphorylation of 4E-BP1 by activated mTORC1, Mus musculus

Phosphorylation and activation of eIF4B by activated S6K1, Mus musculus

Phosphorylation of Cdc25A at Ser-123 by Chk2, Xenopus tropicalis

Down Regulation of Emi1 through Phosphorylation of Emi1, Gallus gallus

SOS phosphorylation and dissociation (IRS), Danio rerio

Regulation of KIF20A (MKL2) by phosphorylation, Canis familiaris

Phosphorylation of phospho-(Ser45,Thr41,Ser37) at Ser33 by GSK-3, Rattus norvegicus

Phosphorylation of DLC2 by MAPK-8, Rattus norvegicus

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Drosophila melanogaster

Phosphorylation of the SA2 Cohesin Complex, Drosophila melanogaster

Regulation of KIF23 (MKLP1) by phosphorylation, Danio rerio

Phosphorylation of APC component of the destruction complex, Bos taurus

Inactivation of Myt1 kinase, Caenorhabditis elegans

Myt-1 mediated phosphorylation of Cyclin A:Cdc2, Rattus norvegicus

Autophosphorylation of PAK-2p34 in the activation loop, Danio rerio

Phosphorylation of PDE3B, Caenorhabditis elegans

Phosphorylation of the Emi1 DSGxxS degron by Plk1, Canis familiaris

Regulation of KIF23 (MKLP1) by phosphorylation, Canis familiaris

Autophosphorylation of PAK-2p34 in the activation loop, Taeniopygia guttata

Phosphorylation of L1 by ERK, Gallus gallus

Phosphorylation of Wee1 kinase by Chk1, Danio rerio

SOS phosphorylation and dissociation (SHC), Canis familiaris

Phosphorylation of TSC2 by PKB, Sus scrofa

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Danio rerio

Phosphorylation and activation of Chk1 by ATM, Canis familiaris

Phosphorylation of cPLA2 by ERK-2, Rattus norvegicus

CAK-mediated phosphorylation of Cyclin A:Cdc2 complexes, Mus musculus

Phosphorylation of Ribosomal protein S6 by activated S6K1, Dictyostelium discoideum

Phosphorylation and activation of Chk1 by ATM, Taeniopygia guttata

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Xenopus tropicalis

Phosphoryation of phospho- (Ser45, Thr41) beta-catenin at Ser37 by GSK-3, Xenopus tropicalis

Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes, Mus musculus

Phosphorylation of cPLA2 by ERK-2, Canis familiaris

Phosphorylation of Ribosomal protein S6 by activated S6K1, Drosophila melanogaster

Regulation of KIF20A (MKL2) by phosphorylation, Taeniopygia guttata

Regulation of KIF23 (MKLP1) by phosphorylation, Gallus gallus

CAK-mediated phosphorylation of Cyclin A:Cdk2, Rattus norvegicus

Phosphorylation of MDM2 at serine-395 by ATM kinase, Bos taurus

Phosphorylation of BRCA1 at multiple sites by ATM, Homo sapiens

RAF1 phosphorylates MEK1, Canis familiaris

Phosphorylation of Cyclin A:Cdk2 at Tyr 15, Mus musculus

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Gallus gallus

SOS phosphorylation and dissociation (IRS, Crk), Bos taurus

Phosphorylation of Cx43 by c-src, Canis familiaris

Phosphorylation of Wee1 kinase by Chk1, Xenopus tropicalis

SOS phosphorylation and dissociation (SHC), Bos taurus

Phosphorylation of p53 at ser-15 by ATM kinase, Sus scrofa

Phosphorylation of Cyclin B1 in the CRS domain, Danio rerio

Orc1 is phosphorylated by cyclin A/CDK2, Danio rerio

Phosphorylation of MDC1/NFBD1 by ATM (within 2 c-term BRCT domains), Bos taurus

Phosphorylation and activation of eIF4B by activated S6K1, Danio rerio

Phosphorylation of the Scc1:Cohesion Complex, Caenorhabditis elegans

SOS phosphorylation and dissociation (IRS, Crk), Rattus norvegicus

Phosphorylation of Cyclin D1 at T286 by glycogen synthase kinase-3 beta, Rattus norvegicus

Phosphorylation of the SA2 Cohesin Complex, Rattus norvegicus

Autophosphorylation of PAK-2p34 in the activation loop, Canis familiaris

Phosphorylation of Ribosomal protein S6 by activated S6K1, Oryza sativa

Phosphorylation of the Scc1:Cohesion Complex, Bos taurus

Inactivation of Wee1 kinase, Mus musculus

Phosphorylation of Cyclin E:Cdk2 complexes by Wee-1, Bos taurus

Regulation of NUDC by phosphorylation, Taeniopygia guttata

CAK-mediated phosphorylation of Cyclin A:Cdk2, Mus musculus

Phosphorylation of phospho-(Ser45,Thr41,Ser37) at Ser33 by GSK-3, Drosophila melanogaster

Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2, Bos taurus

Phosphorylation of Cdc25C at Ser216, Xenopus tropicalis

PIP2 conversion to PIP3, Xenopus tropicalis

Phosphorylation of Cyclin D:Cdk4/6 complexes, Homo sapiens

Myt-1 mediated phosphorylation of Cyclin A:Cdc2, Canis familiaris

SOS phosphorylation and dissociation (IRS), Rattus norvegicus

Phosphorylation of Cx43 by c-src, Gallus gallus

Phosphorylation and activation of eIF4G by activated S6K1, Taeniopygia guttata

Regulation of NUDC by phosphorylation, Gallus gallus

Phosphorylation of COP1 at Ser-387 by ATM, Sus scrofa

Wee1-mediated phosphorylation of Cyclin A:phospho-Cdc2 complexes, Drosophila melanogaster

Free APC/C phosphorylated by Plk1, Rattus norvegicus

Phosphorylation of L1 by CK-II, Bos taurus

Autophosphorylation of PAK-2p34 in the activation loop, Mus musculus

Phosphorylation of COP1 at Ser-387 by ATM, Gallus gallus

Activation of Cdc25C, Xenopus tropicalis

Plk1-mediated phosphorylation of Nlp, Rattus norvegicus

Phosphorylation and activation of CHK2 by ATM, Saccharomyces cerevisiae

Phosphorylation of Cdc25A at Ser-123 by Chk2, Canis familiaris

CAK-mediated phosphorylation of Cyclin E:Cdk2, Rattus norvegicus

Phosphorylation of MDM2 at serine-395 by ATM kinase, Sus scrofa

Phosphorylation of TSC2 by PKB, Rattus norvegicus

Cdc6 protein is phosphorylated by CDK, Mus musculus

Phosphorylation and activation of eIF4G by activated S6K1, Canis familiaris

Orc1 is phosphorylated by cyclin A/CDK2, Xenopus tropicalis

Phosphorylation of Cyclin E2:Cdk2 complexes by Myt1, Mus musculus

Activation of the Anaphase Promoting Complex (APC) by PLK1, Dictyostelium discoideum

Myt-1 mediated phosphorylation of Cyclin A:Cdc2, Bos taurus

Mcm2-7 is phosphorylated by DDK, Gallus gallus

Phosphorylation of complexed TSC2 by PKB, Canis familiaris

Phosphorylation of cPLA2 by ERK-2, Mus musculus

Phosphorylation of Cx43 by c-src, Danio rerio

Phosphorylation of Cdc25A at Ser-123 by Chk2, Mus musculus

Phosphorylation of BRCA1 at multiple sites by ATM, Xenopus tropicalis

Myt-1 mediated phosphorylation of Cyclin A:Cdc2, Mus musculus

Phosphorylation of Cdc25C at Ser216, Canis familiaris

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Saccharomyces cerevisiae

Regulation of NUDC by phosphorylation, Mus musculus

Phosphorylation of phospho-(Ser45,Thr41,Ser37) at Ser33 by GSK-3, Bos taurus

Phosphorylation of Cdc25A at Ser-123 in response to DNA damage, Xenopus tropicalis

Phosphorylation of Cyclin B1 in the CRS domain, Drosophila melanogaster

Myt-1 mediated phosphorylation of Cyclin A:Cdc2, Drosophila melanogaster

Phosphorylation of COP1 at Ser-387 by ATM, Danio rerio

Phosphorylation and activation of Chk1 by ATM, Arabidopsis thaliana

Phosphorylation and inactivation of eEF2K by activated S6K1, Taeniopygia guttata

Phosphorylation of 4E-BP1 by activated mTORC1, Gallus gallus

Inactivation of Wee1 kinase, Gallus gallus

Partial autophosphorylation of PAK-2 at Ser-19, Ser-20, Ser-55, Ser-192, and Ser-197, Drosophila melanogaster

Autophosphorylation of PAK-2p34 in the activation loop, Saccharomyces cerevisiae

Phosphorylation and activation of CHK2 by ATM, Xenopus tropicalis

Regulation of KIF23 (MKLP1) by phosphorylation, Bos taurus

Phosphorylation of phospho-(Ser45 ) at Thr 41 by GSK-3, Drosophila melanogaster

Phosphorylation of Cdc25A at Ser-123 by Chk1, Danio rerio

Phosphorylation of TSC2 by PKB, Danio rerio

Phosphorylation of beta-catenin at Ser45 by CK1 alpha, Bos taurus

Phosphorylation of Cx43 by c-src, Taeniopygia guttata

Phosphorylation of MDM2 at serine-395 by ATM kinase, Homo sapiens

Phosphorylation of complexed TSC2 by PKB, Mus musculus

Phosphorylation of phospho-(Ser45 ) at Thr 41 by GSK-3, Rattus norvegicus

Phosphorylation of PD-1, Canis familiaris

Phosphorylation of AKT2 by PDK1, Rattus norvegicus

Free APC/C phosphorylated by Plk1, Danio rerio

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Taeniopygia guttata

CAK-mediated phosphorylation of Cyclin E:Cdk2, Sus scrofa

Phosphorylation of NBS1 by ATM, Bos taurus

Inactivation of Wee1 kinase, Drosophila melanogaster

Phosphorylation of Ribosomal protein S6 by activated S6K1, Taeniopygia guttata

Phosphorylation of AKT2 by PDK1, Danio rerio

Activation of the Anaphase Promoting Complex (APC) by PLK1, Caenorhabditis elegans

Phosphorylation of Cyclin D:Cdk4/6 complexes, Sus scrofa

Phosphorylation of phospho-(Ser45 ) at Thr 41 by GSK-3, Homo sapiens

Phosphorylation of Ribosomal protein S6 by activated S6K1, Mus musculus

RAF1 phosphorylates MEK2, Canis familiaris

Phosphoryation of phospho- (Ser45, Thr41) beta-catenin at Ser37 by GSK-3, Homo sapiens

Phosphorylation of Cyclin A:Cdk2 at Tyr 15, Bos taurus

Phosphorylation of DLC2 by MAPK-8, Taeniopygia guttata

Phosphorylation of beta-catenin at Ser45 by CK1 alpha, Homo sapiens

Phosphorylation of phospho-(Ser45 ) at Thr 41 by GSK-3, Canis familiaris

Phosphorylation of APC component of the destruction complex, Homo sapiens

Phosphorylation of phospho-(Ser45,Thr41,Ser37) at Ser33 by GSK-3, Homo sapiens

Phosphorylation of beta-catenin at Ser45 by CK1 alpha, Gallus gallus

Intermolecular autophosphorylation of ATM within dimeric ATM complexes, Schizosaccharomyces pombe

Phosphorylation of Cx43 by c-src, Homo sapiens

Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
oxidoreductase activity, acting on other substrates
Note that enzymes of class EC:1.97.-.- should also be annotated to this term.

Diiodinated tyrosine can be deiodinated, Mus musculus

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Canis familiaris

Monoiodinated tyrosine can be deiodinated, Canis familiaris

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Danio rerio

Monoiodinated tyrosine can be deiodinated, Danio rerio

Monoiodinated tyrosine can be deiodinated, Caenorhabditis elegans

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Rattus norvegicus

Monoiodinated tyrosine can be deiodinated, Rattus norvegicus

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR2], Sus scrofa

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR2], Rattus norvegicus

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Taeniopygia guttata

Monoiodinated tyrosine can be deiodinated, Bos taurus

Diiodinated tyrosine can be deiodinated, Rattus norvegicus

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Drosophila melanogaster

Monoiodinated tyrosine can be deiodinated, Homo sapiens

Diiodinated tyrosine can be deiodinated, Homo sapiens

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Homo sapiens

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR2], Homo sapiens

Diiodinated tyrosine can be deiodinated, Canis familiaris

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR2], Mus musculus

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Gallus gallus

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Bos taurus

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Mus musculus

Monoiodinated tyrosine can be deiodinated, Mus musculus

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR2], Taeniopygia guttata

Diiodinated tyrosine can be deiodinated, Gallus gallus

Monoiodinated tyrosine can be deiodinated, Xenopus tropicalis

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR2], Bos taurus

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR2], Gallus gallus

Diiodinated tyrosine can be deiodinated, Xenopus tropicalis

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Arabidopsis thaliana

Monoiodinated tyrosine can be deiodinated, Gallus gallus

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Xenopus tropicalis

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR2], Canis familiaris

Diiodinated tyrosine can be deiodinated, Drosophila melanogaster

Diiodinated tyrosine can be deiodinated, Taeniopygia guttata

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR2], Danio rerio

Monoiodinated tyrosine can be deiodinated, Sus scrofa

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Caenorhabditis elegans

Diiodinated tyrosine can be deiodinated, Caenorhabditis elegans

Diiodinated tyrosine can be deiodinated, Sus scrofa

Diiodinated tyrosine can be deiodinated, Bos taurus

Monoiodinated tyrosine can be deiodinated, Drosophila melanogaster

palmitoyl-CoA + 2 NADPH + 2 H+ => hexadecanol + 2 NADP+ [FAR1], Oryza sativa

Diiodinated tyrosine can be deiodinated, Danio rerio

Monoiodinated tyrosine can be deiodinated, Taeniopygia guttata

The covalent alteration of one or more amino acid residues within a histone protein.

Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

Molybdenum ion transfer onto molybdopterin, Homo sapiens

Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
transferase activity, transferring other glycosyl groups
Note that enzymes of class EC:2.4.99.- should also be annotated to this term.
transferase activity, transferring glycosyl groups

Catalysis of the transfer of a nucleotidyl group to a reactant.

Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.

Hydrolysis of phosphatidylcholine, Bos taurus

Partial proteolysis of antigen in phagolysosomes, Homo sapiens

Hydrolysis of phosphatidylcholine, Homo sapiens

Hydrolysis of phosphatidylcholine, Danio rerio

Hydrolysis of phosphatidylcholine, Xenopus tropicalis

Hydrolysis of phosphatidylcholine, Gallus gallus

Hydrolysis of phosphatidylcholine, Canis familiaris

Hydrolysis of phosphatidylcholine, Mus musculus

Hydrolysis of phosphatidylcholine, Taeniopygia guttata

Hydrolysis of phosphatidylcholine, Rattus norvegicus

Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
4-nitrophenylphosphate phosphohydrolase activity
p-nitrophenylphosphate phosphohydrolase activity

Catalysis of the hydrolysis of any glycosyl bond.
hydrolase activity, acting on glycosyl bonds

Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
Note that enzymes of class EC:4.99.-.- should also be annotated to this term.

Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
Note that enzymes of class EC:5.99.-.- should also be annotated to this term.

Catalysis of the joining of two substances, or two groups within a single molecule, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.

Ligation of DNA at sites of patch replacement, Gallus gallus

Ligation of newly synthesized repair patch to incised DNA in GG-NER, Gallus gallus

Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
complex V (mitochondrial electron transport)

Trafficking of GluR2-containing AMPA receptors to synapse, Canis familiaris

Trafficking of GluR2-containing AMPA receptors to synapse, Bos taurus

Trafficking of GluR2-containing AMPA receptors to synapse, Danio rerio

Trafficking of GluR2-containing AMPA receptors to synapse, Xenopus tropicalis

Trafficking of GluR2-containing AMPA receptors to synapse, Homo sapiens

Trafficking of GluR2-containing AMPA receptors to synapse, Gallus gallus

Trafficking of GluR2-containing AMPA receptors to synapse, Mus musculus

Trafficking of GluR2-containing AMPA receptors to synapse, Drosophila melanogaster

Trafficking of GluR2-containing AMPA receptors to synapse, Rattus norvegicus

Trafficking of GluR2-containing AMPA receptors to synapse, Taeniopygia guttata

The alteration of an amino acid residue in a peptide.

Interacting selectively and non-covalently with ribosomal RNA.

Interacting selectively and non-covalently with any enzyme.

Enables the transfer of a substance from one side of a membrane to the other.

GLUT9 transports glucose, fructose and urate, Gallus gallus

GLUT9 transports glucose, fructose and urate, Xenopus tropicalis

Egress of internalized antigen to the cytosol via sec61, Homo sapiens

GLUT9 transports glucose, fructose and urate, Plasmodium falciparum

GLUT9 transports glucose, fructose and urate, Dictyostelium discoideum

GLUT9 transports glucose, fructose and urate, Mycobacterium tuberculosis

GLUT9 transports glucose, fructose and urate, Arabidopsis thaliana

GLUT9 transports glucose, fructose and urate, Oryza sativa

GLUT9 transports glucose, fructose and urate, Homo sapiens

GLUT9 transports glucose, fructose and urate, Canis familiaris

GLUT9 transports glucose, fructose and urate, Bos taurus

GLUT9 transports glucose, fructose and urate, Taeniopygia guttata

GLUT9 transports glucose, fructose and urate, Mus musculus

GLUT9 transports glucose, fructose and urate, Rattus norvegicus

The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered.
Note that a signal is any variable property or parameter that serves to convey information, and may be a physical entity such as a gene product or small molecule, a photon, or a change in state such as movement or voltage change.

Binds to and modulates the activity of an enzyme.
GO:0030234 is reserved for cases when the regulator directly interacts with the enzyme. When regulation of enzyme activity is achieved without enzyme binding, or when the mechanism of regulation is unknown, instead annotate to 'regulation of catalytic activity ; GO:0050790'.

Any part of a cell where non-isotropic growth takes place.

The codon binding activity of a tRNA that positions an activated amino acid, mediating its insertion at the correct point in the sequence of a nascent polypeptide chain during protein synthesis.
Note that this term can be used in place of the obsolete term 'transfer RNA ; GO:0005563'.
triplet codon-amino acid adaptor activity

Specifies the site of a posttranscriptional modification in an RNA molecule by base pairing with a short sequence around the target residue.
Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins.

The binding activity of a molecule that brings together two or more protein molecules, or a protein and another macromolecule or complex, through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.

Any process that modulates the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
regulation of protein modification process

Interacting selectively and non-covalently with a small conjugating protein such as ubiquitin or a ubiquitin-like protein.

Any process involved in mediating the movement of discrete segments of DNA between nonhomologous sites.

A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of telomeres, terminal regions of a linear chromosome that include the telomeric DNA repeats and associated proteins.
organization of chromosome, telomeric region

The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.

The chemical reactions and pathways involving monocarboxylic acids, any organic acid containing one carboxyl (COOH) group or anion (COO-).

Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of an organelle.
regulation of organelle organization and biogenesis

Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a chemical stimulus.
Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC.

The aggregation, arrangement and bonding together of the mature ribosome and of its subunits.

A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a large ribosomal subunit; includes transport to the sites of protein synthesis.
ribosomal large subunit biogenesis and assembly

A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a small ribosomal subunit; includes transport to the sites of protein synthesis.
ribosomal small subunit biogenesis and assembly

Interacting selectively and non-covalently with a histone, any of a group of water-soluble proteins found in association with the DNA of plant and animal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity.

Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of nourishment.

Any process involved in the conversion of a primary small nucleolar RNA (snoRNA) transcript into a mature snoRNA.

Interacting selectively and non-covalently with ions, charged atoms or groups of atoms.

The addition of an acyl group, any group or radical of the form RCO- where R is an organic group, to a protein amino acid.

The process whose specific outcome is the progression of a spore over time, from its initiation to the mature structure. A spore is a structure that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction.

The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which either requires oxygen (aerobic respiration) or does not (anaerobic respiration).

The directed movement of substances into, out of or within the Golgi apparatus, mediated by vesicles.

The creation of a single organelle from two or more organelles.

The creation of two or more organelles by division of one organelle.

The partitioning of organelles between daughter cells at cell division.

Any process that modulates the frequency, rate or extent of the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving DNA.

Interacting selectively and non-covalently with an unfolded protein.

The directed movement of substances into, out of, or within the nucleus.

Import of PIC to the Host Nucleus, Homo sapiens

The chemical reactions and pathways involving a cofactor, a substance that is required for the activity of an enzyme or other protein. Cofactors may be inorganic, such as the metal atoms zinc, iron, and copper in certain forms, or organic, in which case they are referred to as coenzymes. Cofactors may either be bound tightly to active sites or bind loosely with the substrate.

Progression through the phases of the meiotic cell cycle, in which canonically a cell replicates to produce four offspring with half the chromosomal content of the progenitor cell via two nuclear divisions.

The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
peptidolysis involved in cellular protein catabolic process
peptidolysis involved in cellular protein catabolism
peptidolysis during cellular protein catabolic process
peptidolysis during cellular protein catabolism
proteolysis during cellular protein catabolic process
proteolysis during cellular protein catabolism
proteolysis involved in cellular protein catabolic process

Any process leading to the attainment of the full functional capacity of a protein.

Any process that modulates the rate or extent of progression through the cell cycle.
regulation of progression through cell cycle

Polo-like kinase mediated events, Homo sapiens

Polo-like kinase mediated events, Schizosaccharomyces pombe

Polo-like kinase mediated events, Dictyostelium discoideum

Polo-like kinase mediated events, Caenorhabditis elegans

Polo-like kinase mediated events, Taeniopygia guttata

Polo-like kinase mediated events, Saccharomyces cerevisiae

Polo-like kinase mediated events, Gallus gallus

Polo-like kinase mediated events, Drosophila melanogaster

Polo-like kinase mediated events, Canis familiaris

Polo-like kinase mediated events, Danio rerio

Polo-like kinase mediated events, Mus musculus

Polo-like kinase mediated events, Rattus norvegicus

Polo-like kinase mediated events, Bos taurus

Polo-like kinase mediated events, Xenopus tropicalis

The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other
Transmembrane transport requires transport of a solute across a lipid bilayer. Note that transport through the nuclear pore complex is not transmembrane because the nuclear membrane is a double membrane and is not traversed. For transport through the nuclear pore, consider instead the term 'nucleocytoplasmic transport ; GO:0006913' and its children. Note also that this term is not intended for use in annotating lateral movement within membranes.

SLC-mediated transmembrane transport, Taeniopygia guttata

SLC-mediated transmembrane transport, Caenorhabditis elegans

SLC-mediated transmembrane transport, Escherichia coli

SLC-mediated transmembrane transport, Sus scrofa

Transmembrane transport of small molecules, Staphylococcus aureus N315

Transmembrane transport of small molecules, Caenorhabditis elegans

SLC-mediated transmembrane transport, Canis familiaris

SLC-mediated transmembrane transport, Xenopus tropicalis

SLC-mediated transmembrane transport, Staphylococcus aureus N315

Transmembrane transport of small molecules, Plasmodium falciparum

ABC-family proteins mediated transport, Mus musculus

ABC-family proteins mediated transport, Staphylococcus aureus N315

ABC-family proteins mediated transport, Escherichia coli

ABC-family proteins mediated transport, Plasmodium falciparum

ABC-family proteins mediated transport, Mycobacterium tuberculosis

ABC-family proteins mediated transport, Homo sapiens

Transmembrane transport of small molecules, Homo sapiens

SLC-mediated transmembrane transport, Homo sapiens

ABC-family proteins mediated transport, Taeniopygia guttata

SLC-mediated transmembrane transport, Gallus gallus

Transmembrane transport of small molecules, Canis familiaris

ABC-family proteins mediated transport, Canis familiaris

Transmembrane transport of small molecules, Saccharomyces cerevisiae

Transmembrane transport of small molecules, Rattus norvegicus

SLC-mediated transmembrane transport, Bos taurus

ABC-family proteins mediated transport, Sus scrofa

SLC-mediated transmembrane transport, Danio rerio

Transmembrane transport of small molecules, Bos taurus

SLC-mediated transmembrane transport, Plasmodium falciparum

SLC-mediated transmembrane transport, Saccharomyces cerevisiae

ABC-family proteins mediated transport, Bos taurus

ABC-family proteins mediated transport, Rattus norvegicus

ABC-family proteins mediated transport, Schizosaccharomyces pombe

ABC-family proteins mediated transport, Caenorhabditis elegans

Transmembrane transport of small molecules, Oryza sativa

SLC-mediated transmembrane transport, Mus musculus

SLC-mediated transmembrane transport, Rattus norvegicus

Transmembrane transport of small molecules, Escherichia coli

ABC-family proteins mediated transport, Oryza sativa

Transmembrane transport of small molecules, Drosophila melanogaster

Transmembrane transport of small molecules, Schizosaccharomyces pombe

SLC-mediated transmembrane transport, Oryza sativa

ABC-family proteins mediated transport, Xenopus tropicalis

Transmembrane transport of small molecules, Taeniopygia guttata

Transmembrane transport of small molecules, Gallus gallus

SLC-mediated transmembrane transport, Schizosaccharomyces pombe

ABC-family proteins mediated transport, Arabidopsis thaliana

SLC-mediated transmembrane transport, Mycobacterium tuberculosis

Transmembrane transport of small molecules, Mycobacterium tuberculosis

ABC-family proteins mediated transport, Gallus gallus

Transmembrane transport of small molecules, Dictyostelium discoideum

Transmembrane transport of small molecules, Mus musculus

ABC-family proteins mediated transport, Drosophila melanogaster

ABC-family proteins mediated transport, Danio rerio

SLC-mediated transmembrane transport, Dictyostelium discoideum

Transmembrane transport of small molecules, Sus scrofa

SLC-mediated transmembrane transport, Arabidopsis thaliana

Transmembrane transport of small molecules, Arabidopsis thaliana

ABC-family proteins mediated transport, Saccharomyces cerevisiae

Transmembrane transport of small molecules, Xenopus tropicalis

SLC-mediated transmembrane transport, Drosophila melanogaster

Transmembrane transport of small molecules, Danio rerio

ABC-family proteins mediated transport, Dictyostelium discoideum

The cellular chemical reactions and pathways involving a nucleobase-containing small molecule: a nucleobase, a nucleoside, or a nucleotide.
nucleobase, nucleoside and nucleotide metabolism
nucleobase, nucleoside and nucleotide metabolic process
nucleobase-containing small molecule metabolic process

Metabolism of nucleotides, Plasmodium falciparum

Metabolism of nucleotides, Schizosaccharomyces pombe

Metabolism of nucleotides, Mycobacterium tuberculosis

Metabolism of nucleotides, Rattus norvegicus

Metabolism of nucleotides, Drosophila melanogaster

Metabolism of nucleotides, Dictyostelium discoideum

Metabolism of nucleotides, Saccharomyces cerevisiae

Metabolism of nucleotides, Taeniopygia guttata

Metabolism of nucleotides, Staphylococcus aureus N315

Metabolism of nucleotides, Caenorhabditis elegans

Metabolism of nucleotides, Canis familiaris

Metabolism of nucleotides, Escherichia coli

Metabolism of nucleotides, Gallus gallus

Metabolism of nucleotides, Arabidopsis thaliana

Metabolism of nucleotides, Xenopus tropicalis

The membrane organization process that joins two lipid bilayers to form a single membrane.

A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a protein complex. Includes the synthesis of non-protein components, and those protein modifications that are involved in synthesis or assembly of the complex.
This classification should should only be used for complexes where synthesis of some non-protein component is necessary for assembly.

A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to or removed from a target protein.
protein modification by small protein conjugation or removal

The aggregation, arrangement and bonding together of a set of components to form an organelle. An organelle is an organized structure of distinctive morphology and function. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane.

A process that results in the biosynthesis of constituent macromolecules, assembly, arrangement of constituent parts, or disassembly of a cell wall.
cell wall organization or biogenesis at cellular level
cellular cell wall organisation or biogenesis
cellular cell wall organization or biogenesis