All terms in GO

Label Id Description
activin complex GO_0048180 [A nonsteroidal regulator, composed of two covalently linked inhibin beta subunits, inhibin beta-A and inhibin beta-B (sometimes known as activin beta or activin/inhibin beta). There are three forms of activin complex, activin A, which is composed of 2 inhibin beta-A subunits, activin B, which is composed of 2 inhibin beta-B subunits, and activin AB, which is composed of an inhibin beta-A and an inhibin beta-B subunit.]
Set1C/COMPASS complex GO_0048188 [A conserved protein complex that catalyzes methylation of histone H3. In Saccharomyces the complex contains Shg1p, Sdc1p, Swd1p, Swd2p, Swd3p, Spp1p, Bre2p, and the trithorax-related Set1p; in mammals it contains the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30.]
Lid2 complex GO_0048189 [A protein complex involved in regulation of chromatin remodeling. In Schizosaccharomyces the complex contains Lid2, Ash2, Jmj3, Snt2, and Sdc1.]
GO_0048186 GO_0048186
GO_0048187 GO_0048187
neuronal stem cell population maintenance GO_0097150 [Any process in by an organism or tissue maintains a population of neuronal stem cells.]
positive regulation of inhibitory postsynaptic potential GO_0097151 [Any process that activates or increases the frequency, rate or extent of inhibitory postsynaptic potential (IPSP). IPSP is a temporary decrease in postsynaptic membrane potential due to the flow of negatively charged ions into the postsynaptic cell. The flow of ions that causes an IPSP is an inhibitory postsynaptic current (IPSC) and makes it more difficult for the neuron to fire an action potential.]
modulation of inhibitory postsynaptic potential GO_0098828 [Any process that modulates the frequency, rate or extent of inhibitory postsynaptic potential (IPSP). IPSP is a temporary decrease in postsynaptic membrane potential due to the flow of negatively charged ions into the postsynaptic cell. The flow of ions that causes an IPSP is an inhibitory postsynaptic current (IPSC) and makes it more difficult for the neuron to fire an action potential.]
positive regulation of nervous system process GO_0031646 [Any process that activates or increases the frequency, rate or extent of a neurophysiological process.]
obsolete cysteine-type endopeptidase activity involved in apoptotic process GO_0097153 [OBSOLETE. Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile, and contributing to the apoptotic process.]
GABAergic neuron differentiation GO_0097154 [The process in which a neuroblast acquires the specialized structural and functional features of a GABAergic neuron.]
fasciculation of sensory neuron axon GO_0097155 [The collection of sensory neuron axons into a bundle of rods, known as a fascicle.]
axonal fasciculation GO_0007413 [The collection of axons into a bundle of rods, known as a fascicle.]
fasciculation of motor neuron axon GO_0097156 [The collection of motor neuron axons into a bundle of rods, known as a fascicle.]
pre-mRNA intronic binding GO_0097157 [Binding to an intronic sequence of a pre-messenger RNA (pre-mRNA).]
pre-mRNA binding GO_0036002 [Binding to a pre-messenger RNA (pre-mRNA), an intermediate molecule between DNA and protein that may contain introns and, at least in part, encodes one or more proteins. Introns are removed from pre-mRNA to form a mRNA molecule.]
pre-mRNA intronic pyrimidine-rich binding GO_0097158 [Binding to a pyrimidine-rich (CU-rich) intronic sequence of a pre-messenger RNA (pre-mRNA).]
polychlorinated biphenyl binding GO_0097160 [Binding to a polychlorinated biphenyl (PCB), a biphenyl compound containing between 2 and 10 chlorine atoms attached to the two benzene rings.]
DH domain binding GO_0097161 [Binding to a DH (Dbl homology) domain of a protein. The DH domain contains three structurally conserved regions separated by more variable regions. It is composed of 11 alpha helices that are folded into a flattened, elongated alpha-helix bundle in which two of the three conserved regions, conserved region 1 (CR1) and conserved region 3 (CR3), are exposed near the centre of one surface. CR1 and CR3, together with a part of alpha-6 and the DH/PH (pleckstrin homology) junction site, constitute the Rho GTPase interacting pocket.]
MADS box domain binding GO_0097162 [Binding to a MADS box domain, a protein domain that encodes the DNA-binding MADS domain. The MADS domain binds to DNA sequences of high similarity to the motif CC[A/T]6GG termed the CArG-box. MADS-domain proteins are generally transcription factors. The length of the MADS-box is in the range of 168 to 180 base pairs.]