COP1
entrez
64326
canonical
uniprot
Q8NHY2
canonical
ensembl
ENSG00000143207
resolver
ensp
ENSP00000310943
resolver
ensp
ENSP00000356638
resolver
ensp
ENSP00000356641
resolver
ensp
ENSP00000566416
resolver
ensp
ENSP00000566417
resolver
ensp
ENSP00000566421
resolver
ensp
ENSP00000566422
resolver
ensp
ENSP00000566430
resolver
ensp
ENSP00000605529
resolver
ensp
ENSP00000612169
resolver
genesymbol
COP1
resolver
genesymbol
RFWD2
resolver
genesymbol_syn
RFWD2
resolver
genesymbol_syn
RNF200
resolver
hgnc
HGNC:17440
resolver
uniprot
E9PKI0
resolver
uniprot
Q504W6
resolver
uniprot
Q6H103
resolver
uniprot
Q9H6L7
resolver
uniprot
X5D7N8
resolver
uniprot
X5D9B4
resolver
uniprot
X5DNY7
resolver
uniprot_entry
COP1_HUMAN
resolver
uniprot_entry
X5D7N8_HUMAN
resolver
uniprot_entry
X5DNY7_HUMAN
resolver
uniprot_sec
E9PKI0
resolver
uniprot_sec
Q504W6
resolver
uniprot_sec
Q6H103
resolver
uniprot_sec
Q9H6L7
resolver
uniprot_sec
X5D9B4
resolver
activity_regulation
ACTIVITY REGULATION: TRIB1 competes with substrates for RFWD2 binding. {ECO:0000269|PubMed:27041596}.
uniprot
proteins
amino_acid_sequence
MSGSRQAGSGSAGTSPGSSAASSVTSASSSLSSSPSPPSVAVSAAALVSGGVAQAAGSGGLGGPVRPVLVAPAVSGSGGGAVSTGLSRHSCAARPSAGVGGSSSSLGSGSRKRPLLAPLCNGLINSYEDKSNDFVCPICFDMIEEAYMTKCGHSFCYKCIHQSLEDNNRCPKCNYVVDNIDHLYPNFLVNELILKQKQRFEEKRFKLDHSVSSTNGHRWQIFQDWLGTDQDNLDLANVNLMLELLVQKKKQLEAESHAAQLQILMEFLKVARRNKREQLEQIQKELSVLEEDIKRVEEMSGLYSPVSEDSTVPQFEAPSPSHSSIIDSTEYSQPPGFSGSSQTKKQPWYNSTLASRRKRLTAHFEDLEQCYFSTRMSRISDDSRTASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNGSSIVSSIEFDRDCDYFAIAGVTKKIKVYEYDTVIQDAVDIHYPENEMTCNSKISCISWSSYHKNLLASSDYEGTVILWDGFTGQRSKVYQEHEKRCWSVDFNLMDPKLLASGSDDAKVKLWSTNLDNSVASIEAKANVCCVKFSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVFKGHRKAVSYAKFVSGEEIVSASTDSQLKLWNVGKPYCLRSFKGHINEKNFVGLASNGDYIACGSENNSLYLYYKGLSKTLLTFKFDTVKSVLDKDRKEDDTNEFVSAVCWRALPDGESNVLIAANSQGTIKVLELV
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif (Probable). {ECO:0000269|PubMed:12466024, ECO:0000269|PubMed:12615916, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15103385, ECO:0000269|PubMed:19805145, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:21625211, ECO:0000303|PubMed:27041596}.
uniprot
proteins
mass_dalton
80474
uniprot
proteins
mutagenesis
MUTAGEN 111..113; /note="RKR->AKA: Abolishes localization to the nucleus."; /evidence="ECO:0000269|PubMed:12615916"; MUTAGEN 136; /note="C->A: Abolishes p53 ubiquitination and degradation but not that of JUN; when associated with A-139."; /evidence="ECO:0000269|PubMed:12615916, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:19805145, ECO:0000269|PubMed:21625211"; MUTAGEN 136; /note="C->S: Loss of SFN and MTA1 ubiquitination and degradation; when associated with S-139. Loss of stabilization by COPS6; when associated with S-139."; /evidence="ECO:0000269|PubMed:12615916, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:19805145, ECO:0000269|PubMed:21625211"; MUTAGEN 139; /note="C->A: Abolishes p53 ubiquitination and degradation but not that of JUN; when associated with A-136."; /evidence="ECO:0000269|PubMed:12615916, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:19805145, ECO:0000269|PubMed:21625211"; MUTAGEN 139; /note="C->S: Loss of SFN and MTA1 ubiquitination and degradation; when associated with S-136. Loss of stabilization by COPS6; when associated with S-136."; /evidence="ECO:0000269|PubMed:12615916, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:19805145, ECO:0000269|PubMed:21625211"; MUTAGEN 156; /note="C->S: Loss of MTA1 ubiquitination and degradation; when associated with S-159."; /evidence="ECO:0000269|PubMed:19805145"; MUTAGEN 159; /note="C->S: Loss of MTA1 ubiquitination and degradation; when associated with S-156."; /evidence="ECO:0000269|PubMed:19805145
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated. MTA1 destabilizes it by promoting its autoubiquitination. {ECO:0000269|PubMed:19805145}.
uniprot
proteins
protein_family
COP1 family
uniprot
proteins
pubmed
12466024
uniprot
proteins
pubmed
12615916
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14739464
uniprot
proteins
pubmed
15103385
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17968316
uniprot
proteins
pubmed
19805145
uniprot
proteins
pubmed
19837670
uniprot
proteins
pubmed
20410507
uniprot
proteins
pubmed
21625211
uniprot
proteins
pubmed
24722188
uniprot
proteins
pubmed
27041596
uniprot
proteins
sequence_length
731
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm. Note=In the nucleus, it forms nuclear speckles.
uniprot
proteins