Rhea list of ChEBI terms representing the major species at pH 7.3.
Term not to be used for direct annotation
Term not to be used for direct manual annotation
The production of new individuals that contain some portion of genetic material inherited from one or more parent organisms.
Binding to a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein.
Acetylcholine synaptic vesicle docking and priming
Release of noradrenaline at the synapse
Noradrenalin synaptic vesicle docking and priming
Vamp7 associated Lysosome to Plasma membrane transport
Vamp8 associated secretory vesicle to plasma membrane transport
Vamp2 associated secretory vesicle to plasma membrane transport
Dopamine synaptic vesicle docking and priming
Release of docked dopamine loaded synaptic vesicle
Release of docked serotonin loaded synaptic vesicle
Serotonin loaded synaptic vesicle docking and priming
Insulin secretory granule docks at the plasma membrane
GABA loaded synaptic vesicle Docking and Priming
Glutamate synaptic vesicle docking and priming
Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
Catalysis of the reaction: 2'-phospho-[ligated tRNA] + NAD+ = mature tRNA + ADP ribose 1'',2''-phosphate + nicotinamide + H2O. This reaction is the transfer of the splice junction 2-phosphate from ligated tRNA to NAD+ to produce ADP-ribose 1'-2' cyclic phosphate.
2'-phospho-[ligated tRNA]:NAD+ phosphotransferase activity
2'-phospho-tRNA:NAD+ phosphotransferase activity
A chromosome that encodes the nuclear genome and is found in the nucleus of a eukaryotic cell during the cell cycle phases when the nucleus is intact.
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.
Note that this term should not be confused with 'GO:0140014 ; mitotic nuclear division'. 'GO:0000278 ; mitotic cell cycle represents the entire mitotic cell cycle, while 'GO:0140014 ; mitotic nuclear division' specifically represents the actual nuclear division step of the mitotic cell cycle.
The developmental process in which the size or shape of a cell is generated and organized.
Naturally occurring peptide that is an opioid (any non-alkaloid having an opiate-like effect that can be reversed by naloxone or other recognized morphine antagonist). These include Leu- and Met-enkephalin, dynorphin and neoendorphin, alpha, beta, gamma and delta endorphins formed from beta-lipotropin, various pronase-resistant peptides such as beta casamorphin, and other peptides whose opiate-like action seems to be indirect.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + N-acetyl-D-glucosamine = adenosine 3',5'-bisphosphate + N-acetyl-D-glucosamine 6-sulfate.
N-acetylglucosamine 6-O-sulphotransferase activity
N-acetylglucosamine 6-O-sulfotransferase activity
CHST2,5,6 transfer SO4(2-) to GlcNAc residues on keratan-PG to form KSPG
Defective CHST6 does not transfer SO4(2-) to GlcNAc residues on keratan-PG
CHST4 transfers SO4(2-) from PAPS to Core 2 mucins
Binding to an amyloid-beta peptide/protein.
Combining with a virus component and mediating entry of the virus into the cell.
Binding to a fibronectin, a group of related adhesive glycoproteins of high molecular weight found on the surface of animal cells, connective tissue matrices, and in extracellular fluids.
Any process involved in the development or functioning of the immune system, an organismal system for calibrated responses to potential internal or invasive threats.
Note that this term is a direct child of 'biological_process ; GO:0008150' because some immune system processes are types of cellular process (GO:0009987), whereas others are types of multicellular organism process (GO:0032501).
A organ system process carried out by any of the organs or tissues of the circulatory system. The circulatory system is an organ system that moves extracellular fluids to and from tissue within a multicellular organism.
A molecular process that can be carried out by the action of a single macromolecular machine, usually via direct physical interactions with other molecular entities. Function in this sense denotes an action, or activity, that a gene product (or a complex) performs.
Note that, in addition to forming the root of the molecular function ontology, this term is recommended for the annotation of gene products whose molecular function is unknown. 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 'no data' (ND), is used to indicate this. Despite its name, this is not a type of 'function' in the sense typically defined by upper ontologies such as Basic Formal Ontology (BFO). It is instead a BFO:process carried out by a single gene product or complex.
Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
Binding to 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
A transcription regulator activity that modulates transcription of gene sets via selective and non-covalent binding to a specific double-stranded genomic DNA sequence (sometimes referred to as a motif) within a cis-regulatory region. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units, and include bacterial operons.
nucleic acid binding transcription factor activity
DNA binding transcription factor activity
gene-specific transcription factor activity
sequence-specific DNA binding transcription factor activity
bacterial-type DNA binding transcription factor activity
bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding transcription factor activity
bacterial-type RNA polymerase transcription enhancer sequence-specific DNA binding transcription factor activity
bacterial-type RNA polymerase transcription factor activity, metal ion regulated sequence-specific DNA binding
bacterial-type RNA polymerase transcription factor activity, sequence-specific DNA binding
metal ion regulated sequence-specific DNA binding bacterial-type RNA polymerase transcription factor activity
metal ion regulated sequence-specific DNA binding transcription factor activity
sequence-specific DNA binding bacterial-type RNA polymerase transcription factor activity
transcription factor activity, bacterial-type RNA polymerase core promoter proximal region sequence-specific binding
transcription factor activity, bacterial-type RNA polymerase proximal promoter sequence-specific DNA binding
transcription factor activity, bacterial-type RNA polymerase transcription enhancer sequence-specific binding
transcription factor activity, metal ion regulated sequence-specific DNA binding
Usage guidance: Most DNA-binding transcription factors do not have enzymatic activity. The presence of specific DNA-binding domains known to be present in DNA-binding transcription factors (HOX, GATA etc) should be used to help decide whether a protein is a DNA binding transcription factor or a coregulator. If a protein has an enzymatic activity (for example, ubiquitin ligase, histone acetyl transferase) and no known DNA binding domain, consider annotating to GO:0003712 transcription coregulator activity. Special care should be taken with proteins containing zinc fingers, Myb/SANT and ARID domains, since only a subset of proteins containing these domains directly and selectively bind to regulatory DNA motifs in cis-regulatory regions.
DNA-binding transcription factor activity
Binding to an RNA molecule or a portion thereof.
Exportin-5 recognizes 3' overhang of pre-miRNA
Binding to 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.
Binding to an antigen, any substance which is capable of inducing a specific immune response and of reacting with the products of that response, the specific antibody or specifically sensitized T-lymphocytes, or both. Binding may counteract the biological activity of the antigen. Antigen binding by an MHC protein complex allows the antigen to be displayed to a T cell or NK cell.
major histocompatibility complex activity
major histocompatibility complex antigen display activity
Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
Catalysis of the reaction: 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.
2-acetyl-1-alkylglycerophosphocholine esterase activity
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetohydrolase activity
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetylhydrolase activity
LDL-associated phospholipase A(2) activity
alkylacetyl-GPC:acetylhydrolase activity
platelet-activating factor acetylhydrolase activity
1-alkyl-2-acetylglycerophosphocholine esterase activity
PAFAH2 hydrolyses PAF to lyso-PAF and acetate
Catalysis of the reaction: 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + ATP = (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + AMP + 2 H+.
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase activity
6-hydroxymethyl-7,8-dihydropterin diphosphokinase activity
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase activity
7,8-dihydro-6-hydroxymethylpterin diphosphokinase activity
7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase activity
7,8-dihydroxymethylpterin-pyrophosphokinase activity
ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-diphosphotransferase activity
H2-pteridine-CH2OH pyrophosphokinase activity
hydroxymethyldihydropteridine pyrophosphokinase activity
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
Catalysis of the reaction: GTP + H2O = GDP + H+ + 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
G alpha (s) auto-inactivates by hydrolysing GTP to GDP
Adenylate cyclase increases the GTPase activity of G alpha-olf
Adenylaye cyclase increases the GTPase activity of G alpha-olf
Adenylate cyclase increases the GTPase activity of Gi alpha
Endocytosis (internalization) of clathrin-coated vesicle
Translocation of TGN-lysosome vesicle to lysosome
Internalization of MHC II:Ii clathrin coated vesicle
GNAT1-GTP hydrolyses its bound GTP to GDP
G alpha (z) auto-inactivates by hydrolysing GTP to GDP
G alpha (i) auto-inactivates by hydrolysing GTP to GDP
G alpha (12/13) auto-inactivates by hydrolysing GTP to GDP
G alpha (q) auto-inactivates by hydrolysing GTP to GDP
P2Y purinoceptor 1 activates MAP kinase p38 alpha
trans-Golgi Network Lysosomal Vesicle Scission
80S:Met-tRNAi:mRNA:SECISBP2:Sec-tRNA(Sec):EEFSEC:GTP is hydrolysed to 80S:Met-tRNAi:mRNA:SECISBP2:Sec and EEFSEC:GDP by EEFSEC
39S subunit binds 28S subunit:mRNA:fMet-tRNA
TUFM hydrolyzes GTP and TUFM:GDP dissociates from 55S ribosome
Hydrolysis of GTP and dissociation of 28S and 39S subunits
Translocation of peptidyl-tRNA from A-site to P-site (and translocation of 55S ribosome by 3 bases along mRNA)
ASAP1 stimulates GTPase activity of ARF4
SRGAP2 stimulates RAC1 GTP-ase activity and ends FMNL1-mediated elongation of actin filaments
Rheb in the MTORC1 complex hydrolyses GTP
TBC1D20 stimulates GTPase activity of RAB1, resulting in hydrolysis of GTP
CYTH proteins stimulate ARF1 GTPase activity
ARHGAP35 stimulates RHOA GTPase activity
TBC RabGAPs accelerate GTP hydrolysis by RAB35
TBC1D2A accelerates GTP hydrolysis by RAB7
TBC1D15 accelerates GTP hydrolysis by RAB7
TBC1D16 accelerates GTP hydrolysis by RAB4A
TBC1D25 accelerates GTP hydrolysis by RAB33B
Dynamin-mediated GTP hydrolysis promotes vesicle scission
G alpha (i)i1/i2/i3 in G (i):RGS complex is inactivated
G alpha (z) in G alpha (z):RGS complex is inactivated
G alpha (q) in G (q):RGS complex is inactivated
RAS intrinsic GTPase activity hydrolyzes GTP to GDP
Catalysis of the reaction: acetylcholine + H2O = choline + acetate.
acetyl.beta-methylcholinesterase activity
AcCho is hydrolyzed to Cho and acetate by ACHE
Catalysis of the reaction: S-adenosyl-L-homocysteine + H2O = adenosine + L-homocysteine.
S-adenosylhomocysteine hydrolase activity
S-adenosyl-L-homocysteine hydrolase activity
S-adenosylhomocysteine synthase activity
Defective AHCY does not hydrolyse AdoHcy
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate.
3'-phosphoadenylyl-sulfate:alcohol sulfotransferase activity
3-hydroxysteroid sulfotransferase activity
3beta-hydroxy steroid sulfotransferase activity
3beta-hydroxysteroid sulfotransferase activity
5alpha-androstenol sulfotransferase activity
alcohol/hydroxysteroid sulfotransferase activity
dehydroepiandrosterone sulfotransferase activity
delta5-3beta-hydroxysteroid sulfokinase activity
hydroxysteroid sulfotransferase activity
cholesterol + PAPS => cholesterol sulfate + PAP
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate.
1-naphthol phenol sulfotransferase activity
3'-phosphoadenylyl-sulfate:phenol sulfotransferase activity
SULT1A1 dimer sulfonates PARA to PARA-SO4
3,3'-diiodothyronine + PAPS => 3,3'-diiodothyronine 4-sulfate + PAP
3,5,3'-triiodothyronine + PAPS => 3,5,3'-triiodothyronine 4-sulfate + PAP
p-nitrophenol + PAPS => p-nitrophenol sulfate + PAP
Catalysis of the reaction: an acylcholine + H2O = choline + a carboxylic acid anion.
choline esterase II (unspecific) activity
Catalysis of the reaction: dUTP + H2O = dUMP + H+ + diphosphate.
desoxyuridine 5'-triphosphatase activity
desoxyuridine 5'-triphosphate nucleotidohydrolase activity
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
Activated thrombin (factor IIa) cleaves PAR3,4, activating them
factor XIII -> factor XIII cleaved tetramer + 2 factor XIII A activation peptides
prothrombin -> activated thrombin (factor IIa) + thrombin activation peptide (prothrombinase catalyst)
factor V -> factor Va + factor V activation peptide
prothrombin -> activated thrombin (factor IIa) + thrombin activation peptide (Xa catalyst)
factor X -> factor Xa + factor X activation peptide (TF:F7a catalyst)
factor X -> factor Xa + factor X activation peptide (TF:F7 catalyst)
factor IX -> factor IXa + factor IX activation peptide (TF:F7a catalyst)
fibrinogen -> fibrin monomer + 2 fibrinopeptide A + 2 fibrinopeptide B
thrombin:antithrombin III:heparin -> thrombin:cleaved antithrombin III:heparin
Activated protein C cleaves factor Va to factor Vi intermediate form
Activated thrombin:thrombomodulin cleaves PROCR:Protein C to PROCR:Activated protein C
E-cadherin degradation by MMP3, MMP7 and plasmin.
Collagen type II degradation by MMP1,3,8,13,PRSS2
Elastin degradation by elastin-degrading extracellular proteinases
Laminin-332 degradation by laminin-322 degrading extracellular proteinases
Fibronectin degradation by MMP1, 3, 7, 12, 13, 19, CTSS
factor VIII:von Willibrand factor multimer -> factor VIIIa + factor VIIIa B A3 acidic polypeptide + von Willibrand factor multimer
factor X -> factor Xa + factor X activation peptide (VIIIa:IXa catalyst)
factor XI:platelet glycoprotein (GP) Ib:IX:V complex -> factor XIa:platelet glycoprotein (GP) Ib:IX:V complex (XIIa catalyst)
kallikrein:kininogen:C1q binding protein tetramer -> kallikrein + activated kininogen:C1q binding protein tetramer + bradykinin
factor IX -> factor IXa + factor IX activation peptide (factor XIa catalyst)
factor XI:platelet glycoprotein (GP) Ib:IX:V complex -> factor XIa:platelet glycoprotein (GP) Ib:IX:V complex (thrombin catalyst)
crosslinked fibrin multimer:tissue plasminogen activator (two-chain):plasminogen -> crosslinked fibrin multimer:tissue plasminogen activator (two-chain) + plasmin
crosslinked fibrin multimer:tissue plasminogen activator (one-chain) -> crosslinked fibrin multimer:tissue plasminogen activator (two-chain)
crosslinked fibrin multimer:tissue plasminogen activator (one-chain):plasminogen -> crosslinked fibrin multimer:tissue plasminogen activator (one-chain) + plasmin
fibrin multimer, crosslinked -> fibrin digestion products (plasmin)
plasminogen:histidine-rich glycoprotein -> plasmin + histidine-rich glycoprotein (uPA [two-chain] catalyst)
urokinase plasminogen activator (one-chain):uPAR -> urokinase plasminogen activator (two-chain):uPAR
plasminogen:histidine-rich glycoprotein -> plasmin + histidine-rich glycoprotein (uPA [one-chain] catalyst)
HSPG2 (perlecan) degradation by MMP3, plasmin, (MMP12)
Furin cleaves pro-prothrombin to prothrombin
Furin cleaves pro-protein C to protein C
Furin cleaves pro-protein S to protein S
Furin cleaves pro-factor IX to factor IX
Furin cleaves pro-factor VII to factor VII
Initial activation of proMMP13 by plasmin and trypsin
Initial activation of proMMP2 by MMP1, 7
Autocatalytic activation of bound proMMP2
Activation of MMP9 intermediate form by MMPs
Initial activation of proMMP7 by trypsin
Initial activation of proMMP13 by MMP14 (MT1-MMP)
Furin cleaves pro-protein Z to protein Z
Cleavage of the viral Env gp160 precursor polyprotein
Formation of alternative pathway C5 convertase
Signal peptidase hydrolyzes signal peptide from ribosome-associated nascent protein
C3(H2O):Factor Bb cleaves C3 to C3b and C3a
Part of pro-beta-NGF is processed to mature beta-NGF
NOTCH precursor cleaved to form mature NOTCH
Fringe-modified Pre-NOTCH is cleaved by FURIN
Cathepsin G hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-8)
Cleavage of collagen VII NC2 region by BMP1
Fibrillin-1 degradation by MMP3, CTSK, CTSL2
HSPG2 (perlecan) degradation by MMP13, CTSS
E-cadherin degradation by PS1:NCSTN (Gamma-secretase)
E-cadherin degradation by caspase-3 and calpain-1
Prostate-specific Antigen proteolyzes IGF:IGFBP3:ALS
HSPG2 (perlecan) is cleaved by BMP1, TLL1, TLL2, Cathepsin L1
PCSK1 hydrolyzes Proglucagon to Glucagon-like Peptide-1
Signal peptidase hydrolyzes preproGLP-1 to proGLP-1
Signal peptidase hydrolyzes preproGIP to proGIP
PCSK1 hydrolyzes acyl Proghrelin to acyl Ghrelin
Cleavage of the signal peptide of Preproghrelin
Furin cleaves ANTXR2-bound pagA to yield pagA(197-794)
Furin cleaves ANTXR1-bound pagA to yield pagA(197-794)
CORIN(802-1042) hydrolyses NPPA to form NPPA(124-151)
Activated protein C cleaves Factor Va intermediate form for Factor Va
Activated protein C cleaves factor VIIIa
HPN heterodimer cleaves pro-MST1 to form MST1 dimer
HPN heterodimer cleaves pro-HGF to form HGF dimer
PRTN3 cleaves CAMP(31-170) to generate CAMP(134-170)
PCSK2 cleaves Insulin(57-110) to yield Insulin(90-110) and C-peptide (Insulin(57-89))
PCSK1 cleaves proinsulin to yield Insulin(25-56) and Insulin(57-110)
DPP4(39-766) hydrolyzes Glucose-dependent Insulinotropic Polypeptide (GIP)
DPP4(1-766) hydrolyzes Glucose-dependent Insulinotropic Polypeptide (GIP)
DPP4(39-766) hydrolyzes Glucagon-like Peptide-1 (GLP-1)
DPP4(1-766) hydrolyzes Glucagon-like Peptide-1 (GLP-1)
Cleavage of factor XII variant by activated thrombin
Hyperactivation of factor X by FVIIIa:FIXa R384L
FVIIIa variant:FIXa does not convert FX to the active FXa
FIXa variant:FVIIIa does not convert FX to the active FXa
FIX(29-461) variant is not activated (factor XIa catalyst)
TMPRSS2 Mediated SARS-CoV-1 Spike Protein Cleavage and Endocytosis
TMPRSS2 Mediated SARS-CoV-2 Spike Protein Cleavage and Endocytosis
Direct Host Cell Membrane Membrane Fusion and Release of SARS-CoV-2 Nucleocapsid
FURIN Mediated SARS-CoV-2 Spike Protein Cleavage and Endocytosis
Activated thrombin (factor IIa) cleaves F2R (PAR1), activating it
Factor I inactivates plasma Factor H-bound C3b
FURIN Mediated SARS-CoV-2 Spike Protein Cleavage
S2 Cleavage by TMPRSS2 Exposes S2' Initiating Cell-Cell Fusion
Factor I inactivates MCP/CR1-bound C4b/C3b
Nascent F signal peptide is cleaved at ER membrane
F0 is cleaved, releasing F1, F2, F(110-136)
Nascent sG localizes to ER lumen, gets glycosylated
Nascent G signal peptide is cleaved at ER membrane
Catalysis of the reaction: an epoxide + H2O = an ethanediol.
EET(1) is hydrolysed to DHET(1) by EPHX2
LTA4H:Zn2+ hydrolyses 5S,6S-epoxy-18(S)-HEPE to 18(S)-RvE1
LTA4H:Zn2+ hydrolyses 5S,6S-epoxy-18(R)-HEPE to 18(R)-RvE1
LTA4H:Zn2+ hydrolyses 7S(8)-epoxy-17(R)-HDHA to AT-RvD1 or AT-RvD2
LTA4H:Zn2+ hydrolyses 4S(5)-epoxy-17(S)-HDHA to RvD3 or RvD4
LTA4H:Zn2+ hydrolyses 17R(16)-epoxy-DHA to AT-(N)PD1
LTA4H:Zn2+ hydrolyses 7S(8)-epoxy-17(S)-HDHA to RvD1 or RvD2
LTA4H:Zn2+ hydrolyses 4S(5)-epoxy-17(R)-HDHA to AT-RvD3 or AT-RvD4
LTA4H:Zn2+ hydrolyses 16S,17S-epoxy-DHA to (N)PD1
Epoxide hydrolase hydrolyses 13(S),14(S)-epoxy-DHA to MaR1
EPHX2 dimer hydrolyses 13(S),14(S)-epoxy-DHA to MaR2
Epoxide hydrolase hydrolyses 13,14-epoxy-DPAn-3 to MaR1n-3 DPA or MaR2n-3 DPA
Epoxide hydrolase hydrolyses 16(S),17(S)-epoxy-DPAn-3 to PD1n-3DPA or PD2n-3DPA
Epoxide hydrolase hydrolyses 7,8-epoxy-HDPAn-3 to RvD1n-3DPA or RvD2n-3DPA
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
Note that most helicases catalyze processive duplex unwinding.
BLM mediates dissolution of double Holliday junction
ERCC2 and ERCC3 DNA helicases form an open bubble structure in damaged DNA
Catalysis of the reaction: methyl (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate + H2O = (2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate + methanol. A carboxylesterase that hydrolyzes the ester linkage of juvenile hormone.
juvenile hormone analog esterase activity
juvenile hormone carboxyesterase activity
methyl-(2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate acylhydrolase activity
Catalysis of the hydrolysis of ester linkages within nucleic acids.
Note that 'tRNA nucleotidyltransferase activity ; GO:0009022', also known as 'ribonuclease PH', and 'DNA-(apurinic or apyrimidinic site) lyase activity ; GO:0003906' do 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.
Catalysis of the hydrolysis of a glycerophospholipid.
Catalysis of the reaction: 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.
2-lysophosphatidylcholine acylhydrolase activity
lysophosphatidylcholine hydrolase activity
2-acyl LPE is hydrolyzed to GPETA by PLA2G4C
1-acyl LPE is hydrolyzed to GPETA by PLA2G4C
2-acyl LPC is hydrolyzed to GPCho by PLA2[8]
2-acyl LPC is hydrolyzed to GPCho by PLA2G4C
1-acyl LPC is hydrolyzed to GPCho by PLA2[8]
1-acyl LPC is hydrolyzed to GPCho by PLA2G4C
Catalysis of the reaction: a 1,2-diacyl-sn-glycero-3-phospholipid + H2O = 1-acyl-sn-glycero-3-phospholipid + a fatty acid. This reaction removes the fatty acid attached to the sn2-position. Substrates include phosphatidylcholine, phosphatidylethanolamine, choline plasmalogen and phosphatides.
phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine)
phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine)
phosphatidylcholine 2-acylhydrolase activity
PA is hydrolyzed to 1-acyl LPA by PLA2[1] (OM)
PA is hydrolysed to 1-acyl LPA by PLA2[1]
PA is hydrolysed to 1-acyl LPA by PLA2G2A
PG is hydrolyzed to 1-acyl LPG by PLA2G4B (IM)
MLCL is hydrolyzed to DLCL by PLA2G4A (IM)
PS is hydrolyzed to 1-acyl LPS by PLA2[9]
PS is hydrolyzed to 1-acyl LPS by PLA2G2A
PC is hydrolyzed to 1-acyl LPC by PLA2[6]
PI is hydrolyzed to 1-acyl LPI by PLA2[11]
PC is hydrolyzed to 1-acyl LPC by PLA2[5]
PI is hydrolyzed to 1-acyl LPI by PLA2[12]
PE is hydrolyzed to 1-acyl LPE by PLA2[2]
PE is hydrolyzed to 1-acyl LPE by PLA2[3]
PS is hydrolyzed to 2-acyl LPS by PLA2[10]
PG is hydrolyzed to 1-acyl LPG by PLA2[1]
PG is hydrolyzed to 1-acyl LPG by PLA2G2A
PG is hydrolyzed to 1-acyl LPG by PLA2[16]
PS is hydrolyzed to 1-acyl LPS by PLA2[15]
PI is hydrolyzed to 1-acyl LPI by PLA2[15]
PE is hydrolyzed to 1-acyl LPE by PLA2[16]
PC is hydrolyzed to 1-acyl LPC by PLA2[16]
PA is hydrolyzed to 1-acyl LPA by PLA2[15]
PLA2s hydrolyze phospholipids at the Golgi membrane
Catalysis of the reaction: a phosphatidylcholine + H2O = choline + a phosphatidate.
phosphatidylcholine phosphatidohydrolase activity
PC is transphosphatidylated to PG by PLD1-4/6
PC is hydrolyzed to PA and choline by PLD1/2
Catalysis of the reaction: H2O + sphingomyelin = ceramide + choline phosphate + H+.
sphingomyelin cholinephosphohydrolase activity
sphingomyelin phosphodiesterase activity
SMPD2 and 3 hydrolyze sphingomyelin (plasma membrane)
SMPD4 hydrolyzes sphingomyelin (ER membrane)
Production of ceramide which can activate JNK and other targets
Catalysis of the reaction: a steryl ester + H2O = a sterol + a fatty acid.
Digestion of cholesterol esters by extracellular CEL (bile salt-dependent lipase)
LIPA hydrolyses sterol esters to sterols and fatty acids
Catalysis of the reaction: triacylglycerol + H2O = diacylglycerol + a carboxylate.
hepatic monoacylglycerol acyltransferase
post-heparin plasma protamine-resistant lipase
triacylglycerol ester hydrolase activity
triacylglycerol + H2O -> diacylglycerol + fatty acid
Receiving an asialoglycoprotein, and delivering the asialoglycoprotein into the cell via endocytosis. An asialoglycoprotein is a plasma glycoproteins from which the terminal sialic acid residue on their complex carbohydrate groups has been removed. The asialoglycoprotein receptor recognizes the terminal galactose and N-acetylgalactosamine units of the asialoglycoprotein, the receptor-ligand complex is internalized and transported to a sorting organelle where disassociation occurs before the receptor is recycled to the cell membrane.
Combining with an extracellular signal and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Epstein-Barr Virus-induced receptor activity
G-protein coupled receptor activity, unknown ligand
orphan G protein coupled receptor activity
orphan G-protein coupled receptor activity
super conserved receptor expressed in brain receptor activity
The high affinity receptor complex binds to G-protein
Combining with any modified low-density lipoprotein (LDL) or other polyanionic ligand and delivering the ligand into the cell via endocytosis. Ligands include acetylated and oxidized LDL, Gram-positive and Gram-negative bacteria, apoptotic cells, amyloid-beta fibrils, and advanced glycation end products (AGEs).
Note that many gene products that are called scavenger receptors have a broad range of potential ligands and also can be annotated to 'pattern recognition receptor activity ; GO:0038187' or its child terms, or to 'lipoprotein receptor activity ; GO:0030228' or its child terms. For receptors that transduce a signal rather than endocytose their ligand, consider instead the terms 'signaling receptor activity ; GO:0038023' and its children.
Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.
guanyl-nucleotide release factor activity
ARF guanyl-nucleotide exchange factor activity
Rab guanyl-nucleotide exchange factor activity
Rac guanyl-nucleotide exchange factor activity
Ral guanyl-nucleotide exchange factor activity
Ran guanyl-nucleotide exchange factor activity
Rap guanyl-nucleotide exchange factor activity
Ras guanyl-nucleotide exchange factor activity
Rho guanyl-nucleotide exchange factor activity
Sar guanyl-nucleotide exchange factor activity
cAMP-dependent guanyl-nucleotide exchange factor activity
guanyl-nucleotide exchange factor activity
GRB2:SOS:p-Y427-SHC1 mediated nucleotide exchange of RAS
GRB2:SOS1:p-Y-IRS1,p-Y-IRS2 mediated nucleotide exchange of RAS
p-RasGRP1,3:DAG cause RAS to exchange GDP for GTP
SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with ligand-responsive p-6Y-EGFR mutants)
SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with phosphorylated SHC1 and ligand-responsive p-6Y-EGFR mutants)
RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and p-Y349,350-SHC1:p-ERBB4
RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and p-SHC1:Phosphorylated ERBB2 heterodimers
RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and phosphorylated EGFR:ERBB2 heterodimers.
RAS guanyl nucleotide exchange mediated by SOS1 bound to GRB2 in complex with phosphorylated ERBB4:ERBB2 heterodimers
Regeneration of eEF1A:GTP by eEF1B activity
C3G stimulates nucleotide exchange on Rap1
(Frs2)C3G stimulates nucleotide exchange on Rap1
SOS1-mediated nucleotide exchange of RAS (EGF:EGFR:GRB2:SOS1)
SOS1-mediated nucleotide exchange of RAS (EGF:EGFR:SHC1:GRB2:SOS1)
SOS-mediated nucleotide exchange on RAS (PDGF receptor:GRB2:SOS)
RhoA is activated by nucleotide exchange and inhibits axonal growth
An unknown GEF exchanges GTP for GDP on CDC42:GDP
Activation of RAC1 by CRKII:DOCK180:ELMO
p75NTR indirectly activates RAC and Cdc42 via a guanyl-nucleotide exchange factor
Sos-mediated nucleotide exchange of Ras (Tie2 receptor:Grb2:Sos)
SOS1-mediated nucleotide exchange of RAS (HB-EFG-initiated)
SOS mediated nucleotide exchange of RAS (SHC)
Liganded Gs-activating GPCR acts as a GEF for Gs
Liganded Gq/11-activating GPCRs act as GEFs for Gq/11
Liganded Gi-activating GPCR acts as a GEF for Gi
NCAM1:pFAK:Grb2:Sos-mediated nucleotide exchange of Ras
p190RhoGEF exchanges GTP for GDP on RHOA, activating it
KALRN exchanges GTP for GDP on RAC1, activating it
VAV exchanges GTP for GDP on RAC1, activating it
ITSN1 exchanges GTP for GDP on CDC42, activating it
bPIX exchanges GTP for GDP on RAC, activating it
TIAM1 exchanges GTP for GDP on RAC1, activating it
WNT:FZD complex promotes G-protein nucleotide exchange
Muscarinic Acetylcholine Receptor M3 activates Gq
p-TIAM1 exchanges GTP for GDP on RAC1, activating it
Activation of Rho by LARG and PDZ-RhoGEF
VAV1 is a GEF for Rho/Rac family GTPases
VAV2 is a GEF for Rho/Rac family kinases
VAV3 is a GEF for Rho/Rac family kinases
VEGF induces CDC42 activation by unknown mechanism
DOCK180:ELMO exchanges GTP for GDP, activating RAC1
RAB3IP stimulates nucleotide exchange on RAB8A
GBF1 stimulates nucleotide exchange on ARF4
SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with p-EGFRvIII)
SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with phosphorylated SHC1 and p-EGFRvIII)
Activated FGFR1:p-FRS:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR2:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR3:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR4:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR1:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR2:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR3:p-SHC1:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR4:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR2 mutants:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR3 point, translocation and fusion mutants:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR1 mutants:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange
Activated FGFR4 mutants:p-FRS2:GRB2:SOS1 activates RAS nucleotide exchange
RAS GEFs promote RAS nucleotide exchange
GRB2-1:SOS1:p-Y-SHC mediated nucleotide exchange of RAS
GRB2-1:SOS1:p-3Y-SHC1 mediated nucleotide exchange of RAS
GBF1 stimulates nucleotide exchange on ARF
ARFGAPs stimulate ARF GTPase activity at the Golgi membrane
RIC1:RGP1 stimulates nucleotide RAB6 nucleotide exchange
Liganded Gz-activating GPCR acts as a GEF for Gz
Liganded G12/13-activating GPCR acts as a GEF for G12/13
Activation of RAC1 by the PXN:CRK complex
RAB3GAP1:RAB3GAP2 promotes nucleotide exchange on RAB18
RAS guanyl nucleotide exchange by MET-bound GRB2:SOS1
RAS guanyl nucleotide exchange by SOS1 associated with RANBP9 and MET
RAS guanyl nucleotide exchange by SOS1 bound to GRB2, SCH1-2 and MET
RAB13 GEFs exchange GTP for GDP on RAB13
RAB21 GEFs exchange GTP for GDP on RAB21
RAB31 GEFs exchange GTP for GDP on RAB31
TRAPPC complexes exchange GTP for GDP on RAB1
HPS1:HPS4 exchange GTP for GDP on RAB32 and RAB38
RAB3GAP1:RAB3GAP2 exchanges GTP for GDP on RAB18
CDC42 in GNB/GNG:PAK1:ARHGEF6:CDC42 is activated
G-alpha(t):G-beta-gamma:Opsins complex dissociates to active G-alpha(t)
NTRK2 activates RAS signaling through SHC1
EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-CRKL:RAPGEF1:GRB2-1:SOS1,phospho-VAV1 mediates exchange of GTP for GDP bound to RAS
NTRK2 activates RAS signaling through FRS2
NTRK2 and CDK5 promote activation of RAC1 by TIAM1
ESTG stimulates GTP exchange on GPER:heterotrimeric G-protein s
Activation of Rap1 by membrane-associated GEFs
SOS1-mediated nucleotide exchange of RAS downstream of FLT3
RCC1 stimulates GDP to GTP exchange on RAN
RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and ERBB2 homodimer:p-SHC1
ADORA2B (in Ade-Rib:ADORA2B:Heterotrimeric G-protein Gs) exchanges GDP for GTP on Gs
RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants
RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR
RAS guanyl nucleotide exchange mediated by the p-6Y- ERBB2 ECD mutants:EGF:p-6Y-EGFR:p-SHC1:GRB2:SOS1
RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR through GRB2
RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants
RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR
DOCK180 exchanges GTP for GDP on RAC1:GDP
p-VAV1,2,3 exchanges GTP for GDP on RAC1:GDP
p-KIT mutants:GRB2:SOS catalyzes nucleotide exchange on RAS
SOS-mediated nucleotide exchange on RAS downstream of PDGFRA extracellular domain dimers
SOS-mediated nucleotide exchange of RAS downstream of mutant PDGFR receptors
CSF1R-associated SOS1 mediates exchange of GTP for GDP bound to RAS
FLT3 mutants:GRB2:SOS1-mediated nucleotide exchange on RAS
SOS1-mediated nucleotide exchange of RAS downstream of FLT3 fusion mutants
p-VAV1,2,3 exchange 6TGTP for GDP on RAC1
Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
Where appropriate, also consider annotating to 'receptor agonist activity ; GO:0048018'.
Binding to a member of the death receptor (DR) family. The DR family falls within the tumor necrosis factor receptor superfamily and is characterized by a cytoplasmic region of ~80 residues termed the death domain (DD).
death receptor interacting protein activity
death receptor-associated factor activity
The activity of a soluble extracellular gene product that interacts with a receptor to effect a change in the activity of the receptor to control the survival, growth, differentiation and effector function of tissues and cells.
Binding to an epidermal growth factor receptor.
transforming growth factor alpha receptor binding
transforming growth factor alpha receptor ligand
epidermal growth factor receptor binding
Binding to a tumor necrosis factor receptor.
The action characteristic of a hormone, any substance formed in very small amounts in one specialized organ or group of cells and carried (sometimes in the bloodstream) to another organ or group of cells in the same organism, upon which it has a specific regulatory action. The term was originally applied to agents with a stimulatory physiological action in vertebrate animals (as opposed to a chalone, which has a depressant action). Usage is now extended to regulatory compounds in lower animals and plants, and to synthetic substances having comparable effects; all bind receptors and trigger some biological process.
Also consider annotating to 'receptor agonist activity ; GO:0048018'.
The action characteristic of a neuropeptide hormone, any peptide hormone that acts in the central nervous system. A neuropeptide is any of several types of molecules found in brain tissue, composed of short chains of amino acids; they include endorphins, enkephalins, vasopressin, and others. They are often localized in axon terminals at synapses and are classified as putative neurotransmitters, although some are also hormones.
The action of a molecule that contributes to the structural integrity of a complex.
Enables the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, or between cells.
Some transporters, such as certain members of the SLC family, are referred to as 'carriers'; however GO uses carrier with a different meaning: a carrier binds to and transports the substance (see GO:0140104 molecular carrier activity), whereas a transporter forms some pore that allows the passing of molecules.
Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion.
Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
Binding to an insulin-like growth factor, any member of a group of polypeptides that are structurally homologous to insulin and share many of its biological activities, but are immunologically distinct from it.
Binding to mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans.
Transport of glycoproteins with Man8 (or Man9) N-glycans to the Golgi
Binding to a glycan (polysaccharide) containing a substantial proportion of aminomonosaccharide residues.
A location, relative to cellular compartments and structures, occupied by a macromolecular machine. There are three types of cellular components described in the gene ontology: (1) the cellular anatomical entity where a gene product carries out a molecular function (e.g., plasma membrane, cytoskeleton) or membrane-enclosed compartments (e.g., mitochondrion); (2) virion components, where viral proteins act, and (3) the stable macromolecular complexes of which gene product are parts (e.g., the clathrin complex).
Note that, in addition to forming the root of the cellular component ontology, this term is recommended for the annotation of gene products whose cellular component is unknown. 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 'no data' (ND), 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'.
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
Note that for multicellular organisms, the extracellular space refers to everything outside a cell, but still within the organism (excluding the extracellular matrix). Gene products from a multi-cellular organism that are secreted from a cell into the interstitial fluid or blood can therefore be annotated to this term.
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.
Not to be used for manual annotation. Please choose a more specific term: for bacteria, annotate to GO:0009274; peptidoglycan-based cell wall, for plants: annotate to GO:0009505 ; plant-type cell wall, for fungi: GO:0009277 ; fungal-type cell wall, and for archae, use GO:0030115 S-layer (see PMID:31214995).
A component of a cell contained within (but not including) the plasma membrane. In eukaryotes it includes the nucleus and cytoplasm.
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.
The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
That part of the nuclear content other than the chromosomes or the nucleolus.
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.
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.)
A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions.
A vacuole to which materials ingested by endocytosis are delivered.
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 membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
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 non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.
Note that this term does not refer to vesicles, but instead to structures in which lipids do not necessarily form bilayers.
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.
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.
A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes 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 specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
Note that we deem cilium and microtubule-based flagellum to be equivalent. In most eukaryotic species, intracellular sub-components of the cilium, such as the ciliary base and rootlet, are located near the plasma membrane. In Diplomonads such as Giardia, instead, the same ciliary parts are located further intracellularly. Also, 'cilium' may be used when axonemal structure and/or motility are unknown, or when axonemal structure is unusual. For all other cases, please refer to children of 'cilium'. Finally, note that any role of ciliary proteins in sensory events should be captured by annotating to relevant biological process terms.
The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
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
Any cellular metabolic process involving deoxyribonucleic acid. This is one of the two main types of nucleic acid, consisting of a long, unbranched macromolecule formed from one, or more commonly, two, strands of linked deoxyribonucleotides.
Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
The chemical reactions and pathways involving tRNA, transfer RNA, a class of relatively small RNA molecules responsible for mediating the insertion of amino acids into the sequence of nascent polypeptide chains during protein synthesis. Transfer RNA is characterized by the presence of many unusual minor bases, the function of which has not been completely established.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
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
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
This term was intentionally placed under 'protein metabolic process ; GO:0019538' rather than 'protein catabolic process ; GO:0030163' to cover all processes centered on breaking peptide bonds, including those involved in protein processing.
The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
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.
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.
The chemical reactions and pathways involving the nonmetallic element sulfur or compounds that contain sulfur, such as the amino acids methionine and cysteine or the tripeptide glutathione.
The chemical reactions and pathways involving a xenobiotic compound, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
The directed movement of substances (such as macromolecules, small molecules, ions) or cellular components (such as complexes and organelles) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter or a transporter complex, a pore or a motor protein.
Note that this term should not be used for direct annotation. It should be possible to make a more specific annotation to one of the children of this term, for e.g. to transmembrane transport, to microtubule-based transport or to vesicle-mediated transport.
The directed movement of molecules between the nucleus and the cytoplasm.
Note that transport through the nuclear pore complex is not transmembrane because the nuclear membrane is a double membrane, and is not traversed.
The cellular catabolic process in which cells digest cellular materials, such as organelles and other macromolecular constituents, or non-self materials such as intracellular pathogens. Autophagy serves to provide essential nutrients under conditions of cellular stress; or can remodel intracellular structures during cell differentiation.
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 disturbance in organismal or cellular homeostasis, usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).
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.
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 the plasma membrane.
plasma membrane 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
Any cellular process that depends upon or alters the microtubule cytoskeleton, that part of the cytoskeleton comprising microtubules and their associated proteins.
The directed movement of substances into, out of or within a vacuole.
The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
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.
The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules.
The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
signal transduction by cis-phosphorylation
signal transduction by conformational transition
signal transduction by protein phosphorylation
signal transduction by trans-phosphorylation
Note that signal transduction is defined broadly to include a ligand interacting with a receptor, downstream signaling steps and a response being triggered. A change in form of the signal in every step is not necessary. Note that in many cases the end of this process is regulation of the initiation of transcription. Note that specific transcription factors may be annotated to this term, but core/general transcription machinery such as RNA polymerase should not.
Any process that mediates the transfer of information from one cell to another. This process includes signal transduction in the receiving cell and, where applicable, release of a ligand and any processes that actively facilitate its transport and presentation to the receiving cell. Examples include signaling via soluble ligands, via cell adhesion molecules and via gap junctions.
The biological process whose specific outcome is the progression of a multicellular organism over time from an initial condition (e.g. a zygote or a young adult) to a later condition (e.g. a multicellular animal or an aged adult).
Note that this term was 'developmental process'.
The set of physiological processes that allow an embryo or foetus to develop within the body of a female animal. It covers the time from fertilization of a female ovum by a male spermatozoon until birth.
The process of gaseous exchange between an organism and its environment. In plants, microorganisms, and many small animals, air or water makes direct contact with the organism's cells or tissue fluids, and the processes of diffusion supply the organism with dioxygen (O2) and remove carbon dioxide (CO2). In larger animals the efficiency of gaseous exchange is improved by specialized respiratory organs, such as lungs and gills, which are ventilated by breathing mechanisms.
respiratory gaseous exchange by respiratory system
The whole of the physical, chemical, and biochemical processes carried out by multicellular organisms to break down ingested nutrients into components that may be easily absorbed and directed into metabolism.
The function of a family of small chemotactic cytokines; their name is derived from their ability to induce directed chemotaxis in nearby responsive cells. All chemokines possess a number of conserved cysteine residues involved in intramolecular disulfide bond formation. Some chemokines are considered pro-inflammatory and can be induced during an immune response to recruit cells of the immune system to a site of infection, while others are considered homeostatic and are involved in controlling the migration of cells during normal processes of tissue maintenance or development. Chemokines are found in all vertebrates, some viruses and some bacteria.
Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.
TDP1 and TDP2 process unligatable DSB ends
The function that stimulates a cell to grow or proliferate. Most growth factors have other actions besides the induction of cell growth or proliferation.
Binding to a protein component of a cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
Binding to a transcription factor, a protein required to initiate or regulate transcription.
Note that this term should not be used for direct annotation. Please consier one of the more specific descendants, GO:0140297 ; DNA-binding transcription factor binding, GO:0140296 ; general transcription initiation factor binding or GO:0001221 ; transcription coregulator binding.
Functions during translation by binding to RNA during polypeptide synthesis at the ribosome.
translation factor activity, nucleic acid binding
translation factor activity, RNA binding
Catalysis of the transfer of a sulfate group from 3'-phosphoadenosine 5'-phosphosulfate to the hydroxyl group of an acceptor, producing the sulfated derivative and 3'-phosphoadenosine 5'-phosphate.
lithocholate + PAPS => lithocholate sulfate + PAP
taurolithocholate + PAPS => taurolithocholate sulfate + PAP
N-hydroxy-2-acetylaminofluorene + PAPS => 2-acetylaminofluorene-N-sulfate + PAP
Dermatan sulfate can be further sulfated on position 2 of iduronate
A biological process is the execution of a genetically-encoded biological module or program. It consists of all the steps required to achieve the specific biological objective of the module. A biological process is accomplished by a particular set of molecular functions carried out by specific gene products (or macromolecular complexes), often in a highly regulated manner and in a particular temporal sequence.
Note that, in addition to forming the root of the biological process ontology, this term is recommended for the annotation of gene products whose biological process is unknown. 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 'no data' (ND), is used to indicate this.
The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation.
metabolic process resulting in cell growth
multicellular organism metabolic process
Note that metabolic processes do not include single functions or processes such as protein-protein interactions, protein-nucleic acids, nor receptor-ligand interactions.
Catalysis of the transfer of a methyl group to an acceptor molecule.
DNMT1,3A,3B:PRC2 methylates cytosine and histone H3
N6AMT1:TRMT112 transfers CH3 group from AdoMet to MMAIII
guanidinoacetate + S-adenosylmethionine => creatine + S-adenosylhomocysteine
The GSDME gene promoter is hypermethylated
The production of light by certain enzyme-catalyzed reactions in cells.
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.
peptidase activity, acting on D-amino acid peptides
peptidase activity, acting on L-amino acid peptides
gamma-secretase cleaves p75NTR, releasing NRIF and TRAF6
Unknown lysosomal protease degrades CBLIF:RCbl to release Cbl
The multiplication or reproduction of cells, resulting in the expansion of a cell population.
This term was moved out from being a child of 'cellular process' because it is a cell population-level process, and cellular processes are restricted to those processes that involve individual cells. Also note that this term is intended to be used for the proliferation of cells within a multicellular organism, not for the expansion of a population of single-celled organisms.
Catalysis of the reaction: palmitoyl-protein + H2O = palmitate + protein.
palmitoyl-protein thiolesterase activity
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate.
protein-tyrosine sulphotransferase activity
3'-phosphoadenylyl-sulfate:protein-tyrosine O-sulfotransferase activity
tyrosylprotein sulfotransferase activity
protein-tyrosine sulfotransferase activity
TPST1,2 transfer SO4(2-) from PAPS to PODXL2
TPST1,2 transfer SO4(2-) from PAPS to FVIII
Catalysis of the reaction: UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine + undecaprenyl phosphate = UMP + N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenol.
UDP-MurAc(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala):undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide-transferase activity
UDP-MurNAc-Ala-gamma-DGlu-Lys-DAla-DAla:undecaprenylphosphate transferase activity
UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla:undecaprenylphosphate transferase activity
UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C(55)-isoprenoid alcohol transferase activity
UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C55-isoprenoid alcohol transferase activity
UDP-MurNAc-pentapeptide phosphotransferase activity
phospho-MurNAc-pentapeptide transferase activity
phospho-N-acetylmuramoyl pentapeptide translocase activity
phospho-NAc-muramoyl-pentapeptide translocase (UMP) activity
phosphoacetylmuramoylpentapeptide translocase activity
phosphoacetylmuramoylpentapeptidetransferase activity
Note that EC classifies all three 'UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity ; GO:0051992' and 'phospho-N-acetylmuramoyl-pentapeptide-transferase activity ; GO:0008963' under EC:2.7.8.13.
phospho-N-acetylmuramoyl-pentapeptide-transferase activity
Catalysis of the reaction: phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate.
phosphatidylcholine 1-acylhydrolase activity
PC is hydrolyzed to 2-acyl LPC by PLA2G4C
PE is hydrolyzed to 2-acyl LPE by PLA2[4]
PG is hydrolysed to 2-acyl LPG by PLA2G4B (IM)
PC is hydrolysed to 2-acyl LPC by PLA2[7]
PE is hydrolyzed to 2-acyl LPE by PLA2G4C
PG is hydrolyzed to 2-acyl LPG by PLA2[14]
PI is hydrolyzed to 2-acyl LPI by PLA2[13]
The chemical reactions and pathways resulting in the breakdown of substances, including the breakdown of carbon compounds with the liberation of energy for use by the cell or organism.
multicellular organismal catabolic process
The chemical reactions and pathways resulting in the formation of substances; typically the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
multicellular organismal biosynthetic process
The chemical reactions and pathways involving any organic compound that is weakly basic in character and contains an amino or a substituted amino group. Amines are called primary, secondary, or tertiary according to whether one, two, or three carbon atoms are attached to the nitrogen atom.
Any member of a family of organelles found in the cytoplasm of plants and some protists, which are membrane-bounded and contain DNA. Plant plastids develop from a common type, the proplastid.
A membranous cellular structure that bears the photosynthetic pigments in plants, algae, and cyanobacteria. In cyanobacteria thylakoids are of various shapes and are attached to, or continuous with, the plasma membrane. In eukaryotes they are flattened, membrane-bounded disk-like structures located in the chloroplasts; in the chloroplasts of higher plants the thylakoids form dense stacks called grana. Isolated thylakoid preparations can carry out photosynthetic electron transport and the associated phosphorylation.
A thylakoid is not considered an organelle, but some thylakoids are part of organelles.
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 toxic stimulus.
The chemical reactions and pathways involving cytokinins, a class of adenine-derived compounds that can function in plants as growth regulators.
The process whose specific outcome is the progression of an embryo from its formation until the end of its embryonic life stage. The end of the embryonic stage is organism-specific. For example, for mammals, the process would begin with zygote formation and end with birth. For insects, the process would begin at zygote formation and end with larval hatching. For plant zygotic embryos, this would be from zygote formation to the end of seed dormancy. For plant vegetative embryos, this would be from the initial determination of the cell or group of cells to form an embryo until the point when the embryo becomes independent of the parent plant.
The chemical reactions and pathways involving alkaloids, nitrogen containing natural products which are not otherwise classified as peptides, nonprotein amino acids, amines, cyanogenic glycosides, glucosinolates, cofactors, phytohormones or primary metabolites (such as purine or pyrimidine bases).
Any process that decreases the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins.
negative regulation of endopeptidase activity
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
Note that this term should be used to annotate gene products in the organism undergoing the programmed cell death. To annotate genes in another organism whose products modulate programmed cell death in a host organism, consider the term 'modulation by symbiont of host programmed cell death ; GO:0052040'. Also, note that 'programmed cell death ; GO:0012501' should be used to refer to instances of caspase-independent cell death mechanisms, in the absence of further indications on the process taking place. At present, caspase-independent cell death is not yet represented in GO due to the lack of consensus and in-depth research on the topic. 'programmed cell death ; GO:0012501' may also be used to annotate gene products in taxa where apoptosis as defined in GO:0006915 does not occur, such as plants. You may also consider these specific children: GO:0097468 'programmed cell death in response to reactive oxygen species' (with descendants GO:0010421 'hydrogen peroxide-mediated programmed cell death' and GO:0010343 'singlet oxygen-mediated programmed cell death'), and GO:0009626 'plant-type hypersensitive response' and its children.
The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
A series of processes that forms an integrated mechanism by which a cell or an organism detects the depletion of primary carbon sources and then activates genes to scavenge the last traces of the primary carbon source and to transport and metabolize alternative carbon sources such as carbon dioxide or carbonic acid. The utilization process begins when the cell or organism detects carbon levels, includes the activation of genes whose products detect, transport or metabolize carbon-containing substances, and ends when carbon is incorporated into the cell or organism's metabolism.
carbon utilization by utilization of organic compounds
The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide (CO2) using energy obtained from light rather than from the oxidation of chemical compounds.
A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane.
Catalysis of the hydrolysis of a lipid or phospholipid.
diacylglycerol + H2O -> 2-acylglycerol + fatty acid
cholesterol ester + H2O -> cholesterol + fatty acid
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.
The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
protein maturation by peptide bond cleavage
protein maturation by peptide bond hydrolysis
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
SUMF1 mediates the oxidation of cysteine to formylglycine, producing active arylsulfatases
Monoiodinated tyrosine can be deiodinated
Dopachrome is transformed to DHICA by DCT
MARC1,MARC2 reduce N-hydroxylated compounds
Hydroperoxy reductase reduces 4(S)-Hp-17(S)-HDHA to RvD6
Hydroperoxy reducatse reduces 7(S)-Hp-17(S)-HDHA to RvD5
Hydroperoxy reductase reduces 4(S)-Hp-17(R)-HDHA to AT-RvD6
Hydroperoxy reductase reduces 7(S)-Hp-17(R)-HDHA to AT-RvD5
Hydroperoxy reductase reduces 7(S),14(S)-diHp-DHA to 7-epi-MaR1
Hydroperoxy reductase reduces 7,17-diHp-DPAn-3 to RvD5n-3DPA
Lipoxygenase dehydrogenates 7(S),17(S)-diHp-DHA to 7S(8)-epoxy-17(S)-HDHA
Hydroperoxy reducatase reduces 14(S)-Hp-DHA to 14(S)-HDHA
Unknown sepiapterin synthase transforms PTHP to sepiapterin
Processing which a protein carries out itself. This involves actions such as the autolytic removal of residues to generate the mature form of the 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.
TRAF2 ubiquitinates cIAP1,2 in cIAP1,2:TRAF1:TRAF2:TRAF3:NIK
TSR3 transfers aminocarboxypropyl group from S-adenosylmethionine to N(1)-methylpseudouridine-1248 of 18SE rRNA yielding N(1)-methyl-N(3)-aminocarboxypropylpseudouridine-1248
Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
transferase activity, transferring acyl groups
Cytosolic chenodeoxycholoyl-CoA or choloyl-CoA are conjugated with glycine or taurine
Choloyl CoA reacts with glycine or taurine to form glycocholate or taurocholate
Chenodeoxycholoyl CoA reacts with glycine or taurine to form glycochenodeoxycholate or taurochenodeoxycholate
LIPT1 transfers lipoyl group from lipoyl-GCSH to DHs
HRASLS transfer acyl group from PC to PE to form NAPE
Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
transferase activity, transferring glycosyl groups
transferase activity, transferring other glycosyl groups
B3GALTL transfers glucose to O-fucosyl-proteins
Defective B3GALTL does not transfer glucose to O-fucosyl-proteins
Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor).
transferase activity, transferring alkyl or aryl groups, other than methyl groups
transferase activity, transferring alkyl or aryl (other than methyl) groups
DHDDS:NUS1 elongates E,E-FPP with (n)IPPP to form pPPP
Defective DHDDS does not elongate E,E-FPP
TRMT12 transforms yW-187 yielding yW-86 at nucleotide 37 of tRNA(Phe)
Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
Note that this term encompasses all kinase activities, as well as activities that transfer other phosphorus-containing groups such as diphosphate or nucleotides.
transferase activity, transferring phosphorus-containing groups
Catalysis of the transfer of a nucleotidyl group to a reactant.
THG1L transfers GMP to 5' end of tRNA(His)
Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
Partial proteolysis of antigen in phagolysosomes
Production of AA by iPLA2 upon FCGR activation
Phospholipid phosphatase 6 hydrolyses Presqualene diphosphate to presqualene monophosphate
Catalysis of the hydrolysis of any ester bond.
hydrolase activity, acting on ester bonds
uPAR-acyl-GPI + H2O -> uPAR + long-chain fatty acid
Butyrylcholinesterase hydrolyzes acyl Ghrelin
Platelet-activating factor acetylhydrolase (PLA2G7) hydrolyzes acyl Ghrelin
Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
Unknown pPPP phosphatase dephosphorylates pPPP to pPNOL
Catalysis of the hydrolysis of any glycosyl bond.
hydrolase activity, acting on glycosyl bonds
Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in other compounds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
NAAA hydrolyses NAEs to FAs and ethanolamine
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.
PXLP-K278-PHYKPL tetramer hydrolyses 5PHL
TYW1:FMN:4Fe-4S transforms 1-methylguanosine yielding yW-187 (4-demethylwyosine) at nucleotide 37 of tRNA(Phe)
Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
TSTA3 dimer epimerises GDP-DHDMan to GDP-KDGal
Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.
Binding to a glycoside in which the sugar group is galactose.
Catalysis of the reaction: a ribonucleoside triphosphate + H2O = a ribonucleoside diphosphate + H+ + phosphate.
nucleoside triphosphate hydrolase activity
nucleoside triphosphate phosphatase activity
nucleoside triphosphate phosphohydrolase activity
nucleoside-5-triphosphate phosphohydrolase activity
ribonucleoside triphosphate phosphatase activity
NTPDase1 hydrolyzes nucleoside triphosphates
NTPDase2 hydrolyzes nucleoside triphosphates
NTPDase3 hydrolyzes nucleoside triphosphates
NTPDase4 hydrolyzes nucleoside triphosphates
NTPDase7 hydrolyzes nucleoside triphosphates
NTPDase8 hydrolyzes nucleoside triphosphates
Binding to a Wnt-protein, a secreted growth factor involved in signaling.
Catalysis of the reaction: S-formylglutathione + H2O = formate + glutathione + H+.
The complete protein-nucleic acid complex that is the packaged form of the genome in a virus particle.
The protein coat that surrounds the infective nucleic acid in some virus particles. It comprises numerous regularly arranged subunits, or capsomeres.
The lipid bilayer of a virion that surrounds the protein capsid. May also contain glycoproteins.
The chemical reactions and pathways resulting in many of the chemical changes of compounds that are not necessarily required for growth and maintenance of cells, and are often unique to a taxon. In multicellular organisms secondary metabolism is generally carried out in specific cell types, and may be useful for the organism as a whole. In unicellular organisms, secondary metabolism is often used for the production of antibiotics or for the utilization and acquisition of unusual nutrients.
The rupture of cell membranes and the loss of cytoplasm.
Binding to a growth factor, proteins or polypeptides that stimulate a cell or organism to grow or proliferate.
Binding to an immunoglobulin of an IgG isotype.
Binding to an enzyme, a protein with catalytic activity.
Binding to a specific domain of a protein.
A developmental process, independent of morphogenetic (shape) change, that is required for an anatomical structure, cell or cellular component to attain its fully functional state.
The aggregation, arrangement and bonding together of a cellular component.
cellular component assembly at cellular level
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a ribonucleoprotein complex.
Enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other.
substrate-specific transmembrane transporter activity
uptake transmembrane transporter activity
Egress of internalized antigen to the cytosol via sec61
Defective SLC2A9 does not transport Fru, Glc, urate
Fe3+ dissociates from SLC22A17:LCN2:2,5DHBA
An unknown carrier transports cytosolic glyoxylate to the peroxisome
An unknown carrier transports mitochondrial glyoxylate to the cytosol
The cellular developmental process in which a relatively unspecialized cell, e.g. embryonic or regenerative cell, acquires specialized structural and/or functional features that characterize a specific cell. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state.
Binding to a low-density lipoprotein particle, a lipoprotein particle that is rich in cholesterol esters and low in triglycerides, is typically composed of APOB100 and APOE, and has a density of 1.02-1.06 g/ml and a diameter of between 20-25 nm.
low-density lipoprotein particle binding
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix.
extracellular matrix organization and biogenesis
Binds to and modulates the activity of an enzyme.
This term should only be used in cases when the regulator directly interacts with the enzyme.
Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
A structure that lies outside the plasma membrane and surrounds the entire cell or cells. This does not include the periplasmic space.
The outer membrane (of gram negative bacteria) or cell wall (of yeast or Gram positive bacteria) are defined as parts of this structure, see 'external encapsulating structure part'.
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
Binding to an adenyl nucleotide, an adenosine esterified with (ortho)phosphate.
The binding activity of a protein that brings together two or more macromolecules in contact, permitting those molecules to function in a coordinated way. The adaptor can bring together two proteins, or a protein and another macromolecule such as a lipid or a nucleic acid.
The directed movement of substances along cytoskeletal fibers such as microfilaments or microtubules within a cell.
cytoskeleton-dependent intracellular transport
A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
A vesicle found in the cytoplasm of a cell.
The proteolytic processing of an inactive enzyme to an active form.
zymogen activation by proteolytic cleavage
The process in which inactive plasminogen is processed to active plasmin. This process includes cleavage at an internal Arg-Val site to form an N-terminal A-chain and C-terminal B-chain held together by a disulfide bond, and can include further proteolytic cleavage events to remove the preactivation peptide.
Binding to insulin-like growth factor I.
Binding to insulin-like growth factor II.
Binding to 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. For elements that are transcribed as the first step of transposition, the process starts with the transcription of the transposable element, its translation and maturation, and ending with integration into DNA. For elements that are cut out, the process starts with the excision of the donor DNA and integrated into another site.
The process in which a methyl group is covalently attached to a molecule.
Any process that modulates the frequency, rate or extent of any process in which a protein is transported to, or maintained in, a specific location.
regulation of cellular protein localisation
regulation of cellular protein localization
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
A protein complex in this context is meant as a stable set of interacting proteins which can be co-purified by an acceptable method, and where the complex has been shown to exist as an isolated, functional unit in vivo. Acceptable experimental methods include stringent protein purification followed by detection of protein interaction. The following methods should be considered non-acceptable: simple immunoprecipitation, pull-down experiments from cell extracts without further purification, colocalization and 2-hybrid screening. Interactions that should not be captured as protein complexes include: 1) enzyme/substrate, receptor/ligand or any similar transient interactions, unless these are a critical part of the complex assembly or are required e.g. for the receptor to be functional; 2) proteins associated in a pull-down/co-immunoprecipitation assay with no functional link or any evidence that this is a defined biological entity rather than a loose-affinity complex; 3) any complex where the only evidence is based on genetic interaction data; 4) partial complexes, where some subunits (e.g. transmembrane ones) cannot be expressed as recombinant proteins and are excluded from experiments (in this case, independent evidence is necessary to find out the composition of the full complex, if known). Interactions that may be captured as protein complexes include: 1) enzyme/substrate or receptor/ligand if the complex can only assemble and become functional in the presence of both classes of subunits; 2) complexes where one of the members has not been shown to be physically linked to the other(s), but is a homologue of, and has the same functionality as, a protein that has been experimentally demonstrated to form a complex with the other member(s); 3) complexes whose existence is accepted based on localization and pharmacological studies, but for which experimental evidence is not yet available for the complex as a whole.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
benzo(a)pyrene-4,5-epoxide hydratase activity
benzo[a]pyrene-4,5-oxide hydratase activity
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a cell junction. A cell junction is a specialized region of connection between two cells or between a cell and the extracellular matrix.
The chemical reactions and pathways involving various organic and inorganic nitrogenous compounds, as carried out by individual cells.
cellular nitrogen compound metabolic process
The chemical reactions and pathways resulting in the breakdown of nucleobases, nucleosides, nucleotides and nucleic acids.
nucleobase, nucleoside, nucleotide and nucleic acid breakdown
nucleobase, nucleoside, nucleotide and nucleic acid catabolism
nucleobase, nucleoside, nucleotide and nucleic acid degradation
nucleobase, nucleoside, nucleotide and nucleic acid catabolic process
nucleobase-containing compound catabolic process
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 exposure to a stilbenoid. Stilbenoids are secondary products of heartwood formation in trees that can act as phytoalexins. Stilbenoids are hydroxylated derivatives of stilbene. They belong to the family of phenylpropanoids and share most of their biosynthesis pathway with chalcones.
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
process resulting in protein modification
Receiving a signal and transmitting it in the cell to initiate a change in cell activity. A signal is a physical entity or change in state that is used to transfer information in order to trigger a response.
receptor activity involved in signal transduction
The increase in size or mass of an entire organism, a part of an organism or a cell.
See also the biological process term 'cell growth ; GO:0016049'.
Self-propelled movement of a cell or organism from one location to another.
Providing the environmental signal that initiates the directed movement of a motile cell or organism towards a higher concentration of that signal.
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of ribosome subunits; includes transport to the sites of protein synthesis.
Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds.
Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription.
Binding to an hormone, a naturally occurring substance secreted by specialized cells that affect the metabolism or behavior of cells possessing functional receptors for the hormone. Hormones may be produced by the same, or different, cell as express the receptor.
Any biological process involved in the maintenance of an internal steady state.
negative regulation of homeostatic process
positive regulation of homeostatic process
Note that this term can be used to describe the binding of a peptide to an MHC molecule.
Binding to an identical protein or proteins.
Binding to an identical protein to form a homodimer.
Combining with a Wnt protein and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Binding to a protein or protein complex using energy from ATP hydrolysis.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
This term should only be used when it is not possible to determine which phase or subtype of the apoptotic process is positively regulated by a gene product. Whenever detailed information is available, the more granular children terms should be used.
positive regulation of apoptotic process
Any process that activates or increases the activity of an enzyme.
positive regulation of metalloenzyme activity
positive regulation of catalytic activity
Binding to an ion, a charged atoms or groups of atoms.
Organized structure of distinctive morphology and function. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton, and prokaryotic structures such as anammoxosomes and pirellulosomes. Excludes the plasma membrane.
The accumulation of pigment in an organism, tissue or cell, either by increased deposition or by increased number of cells.
Binding to a domain within the same polypeptide.
The cytolytic destruction of red blood cells, with the release of intracellular hemoglobin, in one organism by another.
hemolysis of erythrocytes in other organism
hemolysis of red blood cells in other organism
envenomation resulting in hemolysis in another organism
envenomation resulting in hemolysis in other organism
Binding to a protein or a protein-containing complex to assist the protein folding process.
protein binding involved in protein folding
The chemical reactions and pathways involving small molecules, any low molecular weight, monomeric, non-encoded molecule.
Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.
Binding to a transmembrane transporter, a protein or protein complex that enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other.
A process carried out by gene products in an organism that enable the organism to engage in a symbiotic relationship, a more or less intimate association, with another organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
symbiosis, encompassing mutualism through parasitism
symbiotic interaction between host and organism
biological process involved in symbiotic interaction
Any constituent part of a virion, a complete fully infectious extracellular virus particle.
Binding to TRAIL (TNF-related apoptosis inducing ligand), a member of the tumor necrosis factor ligand family that rapidly induces apoptosis in a variety of transformed cell lines.
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 an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
Binding to a receptor on the host cell surface.
cell surface antigen activity, host-interacting
Binding to a nonidentical protein to form a heterodimer.
Catalysis of the reaction: H2O + acylglycerol = a fatty acid + glycerol.
2-MAG is hydrolyzed to fatty acid and glycerol by MGLL
2-acylglycerol + H2O -> glycerol + fatty acid
Digestion of triacylglycerols by extracellular PTL:colipase
Digestion of monoacylglycerols by extracellular CEL (bile salt-dependent lipase)
Digestion of triacylglycerols by extracellular CEL (bile salt-dependent lipase)
Digestion of diacylglycerols by extracellular PTL:colipase
Digestion of triacylglycerols by extracellular pancreatic lipase-related protein 2
Catalysis of the reaction: phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. This reaction does not require Ca2+.
calcium-independent cytosolic phospholipase A2 activity
calcium-independent phospholipase A2 activity
PLA2G15 hydrolyses LPC to GPCho and LCFA(-)
Catalysis of the reaction: a fatty acyl-CoA + H2O = a fatty acid + CoA + H+.
Peroxisomal ACOT4,6,8 hydrolyse MCFA-CoA, LCFA-CoA
Cytosolic ACOTs hydrolyse MCFA-CoA, LCFA-CoA
ACOT2,9,THEM4,5 hydrolyse MCFA-CoA, LCFA-CoA
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + taurolithocholate = adenosine 3',5'-bisphosphate + taurolithocholate sulfate.
glycolithocholate sulfotransferase activity
3'-phosphoadenylyl-sulfate:glycolithocholate sulfotransferase activity
bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase activity
bile salt:3'phosphoadenosine-5'-phosphosulfate:sulfotransferase activity
Catalysis of the reaction: 3'-phospho-5'-adenylyl sulfate + quercetin = adenosine 3',5'-diphosphate + H+ + quercetin 3-sulfate.
3'-phosphoadenylyl-sulfate:quercetin 3-sulfotransferase activity
The activity of a gene product that interacts with a receptor to effect a change in the activity of the receptor. Ligands may be produced by the same, or different, cell that expresses the receptor. Ligands may diffuse extracellularly from their point of origin to the receiving cell, or remain attached to an adjacent cell surface (e.g. Notch ligands).
The developmental process pertaining to the initial formation of an anatomical structure from unspecified parts. This process begins with the specific processes that contribute to the appearance of the discrete structure and ends when the structural rudiment is recognizable. An anatomical structure is any biological entity that occupies space and is distinguished from its surroundings. Anatomical structures can be macroscopic such as a carpel, or microscopic such as an acrosome.
formation of an anatomical structure involved in morphogenesis
Note that, for example, the formation of a pseudopod in an amoeba would not be considered formation involved in morphogenesis because it would not be thought of as the formation of an anatomical structure that was part of the shaping of the amoeba during its development. The formation of an axon from a neuron would be considered the formation of an anatomical structure involved in morphogenesis because it contributes to the creation of the form of the neuron in a developmental sense.
anatomical structure formation involved in morphogenesis
The biological process whose specific outcome is the progression of an anatomical structure from an initial condition to its mature state. This process begins with the formation of the structure and ends with the mature structure, whatever form that may be including its natural destruction. An anatomical structure is any biological entity that occupies space and is distinguished from its surroundings. Anatomical structures can be macroscopic such as a carpel, or microscopic such as an acrosome.
Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + a phenolic steroid = adenosine 3',5'-bisphosphate + steroid O-sulfate.
3'-phosphoadenylyl-sulfate:phenolic-steroid sulfotransferase activity
beta-estradiol + PAPS => beta-estradiol 3-sulfate + PAP
dehydroepiandrosterone (DHEA) + PAPS => DHEA sulfate + PAP
Any process that modulates the activity of an enzyme.
Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
positive regulation of protein stability
Binding to a component of the extracellular matrix.
extracellular matrix constituent binding
adhesive extracellular matrix constituent
A organ system process carried out by any of the organs or tissues of neurological system.
A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of chromosomes, structures composed of a very long molecule of DNA and associated proteins that carries hereditary information. This term covers covalent modifications at the molecular level as well as spatial relationships among the major components of a chromosome.
Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
nicotinamide adenine dinucleotide binding
The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
Note that this term differs from 'cytokinesis ; GO:0000910' in that cytokinesis does not include nuclear division.
Binding to a Bcl-2 homology (BH) protein domain. Bcl-2-related proteins share homology in one to four conserved regions designated the Bcl-2 homology (BH) domains BH1, BH2, BH3 and BH4. These domains contribute at multiple levels to the function of these proteins in cell death and survival. Anti-apoptotic members of the Bcl-2 family have four BH domains (BH1-BH4). Pro-apoptotic members have fewer BH domains.
Binding to a receptor for a peptide hormone.
Binding to a BH3 protein domain, present in Bcl-2 family members. The BH3 domain is a potent death domain and has an important role in protein-protein interactions and in cell death.
Any process leading to the attainment of the full functional capacity of a protein.
Catalysis of the reaction: UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine + di-trans,poly-cis-undecaprenyl phosphate = UMP + N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol.
Note that EC classifies 'UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity ; GO:0051992' and 'phospho-N-acetylmuramoyl-pentapeptide-transferase activity ; GO:0008963' under the same EC number, EC:2.7.8.13.
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
Catalysis of the reaction: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamatic acid.
Catalysis of the reaction: 2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoic acid + L-glutamatic acid.
Catalysis of the reaction: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoic acid + L-glutamic acid.
The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
ATP hydrolysis coupled transmembrane transport
Transmembrane transport is the 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.
A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins.
The aggregation, arrangement and bonding together of a set of macromolecules to form a protein-containing complex.
cellular protein-containing complex assembly
Catalysis of the release of N-acylethanolamine from N-acyl-phosphatidylethanolamine (NAPE) to generate N-acylethanolamine (NAE).
N-acyl-phosphatidylethanolamine-specific phospholipase D activity
N-acylphosphatidylethanolamine-specific phospholipase D activity
Binding to thyroxine (T4) or triiodothyronine (T3), tyrosine-based hormones produced by the thyroid gland.
Binding to a proteasome, a large multisubunit protein complex that catalyzes protein degradation.
Binding to a Toll-Interleukin receptor (TIR) domain of a protein. The TIR domain is an intracellular 200 residue domain that is found in the Toll protein, the interleukin-1 receptor (IL-1R), and MyD88; it contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components.
Toll-Interleukin receptor domain binding
The process of removing one or more methyl groups from a molecule, involving the oxidation (i.e. electron loss) of one or more atoms in the substrate.
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 from a xenobiotic, a compound foreign to the organism exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
cellular response to xenobiotic stimulus
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
A nitrogen compound metabolic process that contributes to the nitrogen cycle. The nitrogen cycle is a series of metabolic pathways by which nitrogen is converted between various forms and redox states; it encompasses pathways in which nitrogen is acted upon directly, such as nitrification, denitrification, nitrogen fixation, and mineralization.
A mitotic cell cycle process comprising the steps by which the nucleus of a eukaryotic cell divides; the process involves condensation of chromosomal DNA into a highly compacted form. Canonically, mitosis produces two daughter nuclei whose chromosome complement is identical to that of the mother cell.
A molecular function characterized by the coupling of ATP hydrolysis to other steps of a reaction mechanism to make the reaction energetically favorable, for example to catalyze a reaction or drive transport against a concentration gradient.
Note that this term represents a grouping class that includes all proteins that use ATP hydrolysis to drive a reaction; it is not meant to capture the ATP hydrolysis reaction itself. To annotate ATP hydrolysis, please use 'ATP hydrolysis activity ; GO:0016887'.
This relation is currently used to connect two regulation processes p1 and p2, such that if r1 regulates p1 and r2 regulates p2, and r1 results_in r2 then the regulation of p1 is required for the regulation of p2. For an example of use, see GO:0035958 'regulation of glyoxylate cycle by regulation of transcription from RNA polymerase II promoter'. Note that a precise definition of this relation is under discussion. After it has been formalized it will be added to RO, where it will have a RO ID. Note that the existing identifier and label are subject to change.
has negative regulatory component activity
results in changes to anatomical or cellular structure