NOL3
entrez
8996
canonical
uniprot
O60936
canonical
ensembl
ENSG00000140939
resolver
ensp
ENSP00000454598
resolver
ensp
ENSP00000455808
resolver
ensp
ENSP00000457243
resolver
ensp
ENSP00000457720
resolver
ensp
ENSP00000556653
resolver
ensp
ENSP00000609604
resolver
ensp
ENSP00000609605
resolver
ensp
ENSP00000703809
resolver
ensp
ENSP00000703810
resolver
ensp
ENSP00000773866
resolver
genesymbol
NOL3
resolver
genesymbol_syn
ARC
resolver
genesymbol_syn
NOP
resolver
hgnc
HGNC:7869
resolver
uniprot
B4DFL0
resolver
uniprot
O60937
resolver
uniprot
Q5TZN6
resolver
uniprot_entry
NOL3_HUMAN
resolver
uniprot_entry
Q5TZN6_HUMAN
resolver
uniprot_sec
B4DFL0
resolver
uniprot_sec
O60937
resolver
amino_acid_sequence
MGNAQERPSETIDRERKRLVETLQADSGLLLDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRTAGAPDPAWDWQHVGPGYRDRSYDPPCPGHWTPEAPGSGTTCPGLPRASDPDEAGGPEGSEAVQSGTPEEPEPELEAEASKEAEPEPEPEPELEPEAEAEPEPELEPEPDPEPEPDFEERDESEDS
uniprot
proteins
disease_involvement
DISEASE: Myoclonus, familial, 1 (MYOCL1) [MIM:614937]: An autosomal dominant neurologic condition characterized by adult onset of cortical myoclonus manifest as involuntary jerks or movements affecting the face and limbs. Affected individuals can also experience falls without seizure activity or loss of consciousness. {ECO:0000269|PubMed:22926851, ECO:0000269|PubMed:25138476}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: [Isoform 1]: May be involved in RNA splicing. {ECO:0000269|PubMed:10196175}.; FUNCTION: [Isoform 2]: Functions as an apoptosis repressor that blocks multiple modes of cell death. Inhibits extrinsic apoptotic pathways through two different ways. Firstly by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly (By similarity). Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation (By similarity). Inhibits intrinsic apoptotic pathway in response to a wide range of stresses, through its interaction with BAX resulting in BAX inactivation, preventing mitochondrial dysfunction and release of pro-apoptotic factors (PubMed:15004034). Inhibits calcium-mediated cell death by functioning as a cytosolic calcium buffer, dissociating its interaction with CASP8 and maintaining calcium homeostasis (PubMed:15509781). Negatively regulates oxidative stress-induced apoptosis by phosphorylation-dependent suppression of the mitochondria-mediated intrinsic pathway, by blocking CASP2 activation and BAX translocation (By similarity). Negatively regulates hypoxia-induced apoptosis in part by inhibiting the release of cytochrome c from mitochondria in a caspase-independent manner (By similarity). Also inhibits TNF-induced necrosis by preventing TNF-signaling pathway through TNFRSF1A interaction abrogating the recruitment of RIPK1 to complex I (By similarity). Finally through its role as apoptosis repressor, promotes vascular remodeling through inhibition of apoptosis and stimulation of proliferation, in response to hypoxia (By similarity). Inhibits too myoblast differentiation through caspase inhibition (By similarity). {ECO:0000250|UniProtKB:Q62881, ECO:0000250|UniProtKB:Q9D1X0, ECO:0000269|PubMed:15004034, ECO:0000269|PubMed:15509781}.
uniprot
proteins
mass_dalton
22629
uniprot
proteins
mutagenesis
MUTAGEN 17; /note="K->R: Abolished ubiquitination in response to an apoptotic stimulus; when associated with R-68 and R-163."; /evidence="ECO:0000269|PubMed:17142452"; MUTAGEN 31; /note="L->F: Did not reduce creatine kinase release or infarct size after myocardial ischemia/reperfusion. Causes loss of mitochondrial membrane potential and nuclear condensation. Fails to prevent the increase in Bax. Interacts with BAX."; /evidence="ECO:0000269|PubMed:15004034"; MUTAGEN 68; /note="K->R: Abolished ubiquitination in response to an apoptotic stimulus; when associated with R-17 and R-163."; /evidence="ECO:0000269|PubMed:17142452"; MUTAGEN 163; /note="K->R: Abolished ubiquitination in response to an apoptotic stimulus; when associated with R-17 and R-68."; /evidence="ECO:0000269|PubMed:17142452
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-149 is required for its antiapoptotic effect by blocking death-inducing signaling complex death-inducing signaling complex (DISC) activity through the control of interaction with CASP8. Phosphorylation at Thr-149 results in translocation to mitochondria and this translocation enables the binding to CASP8. Dephosphorylated at Thr-149 by calcineurin; doesn't inhibit the association between FADD and CASP8 and the consequent apoptosis. {ECO:0000250|UniProtKB:Q62881}.; PTM: Polyubiquitinated by MDM2; promoting proteasomal-dependent degradation in response to apoptotic stimuli. {ECO:0000250|UniProtKB:Q62881, ECO:0000269|PubMed:17142452}.
uniprot
proteins
pubmed
10196175
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15004034
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15509781
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
16505176
uniprot
proteins
pubmed
17142452
uniprot
proteins
pubmed
22926851
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25138476
uniprot
proteins
pubmed
25255805
uniprot
proteins
pubmed
9560245
uniprot
proteins
sequence_length
208
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus {ECO:0000269|PubMed:10196175}. Note=The SR-rich C-terminus mediates nuclear localization. {ECO:0000269|PubMed:10196175}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:10196175}. Mitochondrion {ECO:0000250|UniProtKB:Q62881}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q62881}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Phosphorylation at Thr-149 results in translocation to mitochondria. Colocalized with mitochondria in response to oxidative stress. {ECO:0000250|UniProtKB:Q62881}.
uniprot
proteins