Cop1
entrez
26374
canonical
uniprot
Q9R1A8
canonical
ensembl
ENSMUSG00000040782
resolver
ensp
ENSMUSP00000076160
resolver
ensp
ENSMUSP00000220479
resolver
enst
ENSMUST00000076894
resolver
genesymbol
Cop1
resolver
genesymbol_syn
RNF200
resolver
genesymbol_syn
Rfwd2
resolver
uniprot_entry
COP1_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: TRIB1 competes with substrates for RFWD2 binding. {ECO:0000250|UniProtKB:Q8NHY2}.
uniprot
proteins
amino_acid_sequence
MSGSRQAGSGSAGTSPGSSAASSVTSASSSLSSSPSPPSVAASAATLVSGGVAPAAGSGGLGGPGRPVLVAAAVSGSASAGGAVSAGQSRLSCAARPSAGVGGSSSSLGSSSRKRPLLVPLCNGLLNSYEDKSNDFVCPICFDMIEEAYMTKCGHSFCYKCIHQSLEDNNRCPKCNYVVDNIDHLYPNFLVNELILKQKQRFEEKRFKLDHSVSSTNGHRWQIFQDLLGTDQDNLDLANVNLMLELLVQKKKQLEAESHAAQLQILMEFLKVARRNKREQLEQIQKELSVLEEDIKRVEEMSGLYSPVSEDSTVPQFEAPSPSHSSIIDSTEYSQPPGFSGTSQTKKQPWYNSTLASRRKRLTAHFEDLEQCYFSTRMSRISDDSRTASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNGSSIVSSIEFDRDCDYFAIAGVTKKIKVYEYGTVIQDAVDIHYPENEMTCNSKISCISWSSYHKNLLASSDYEGTVILWDGFTGQRSKVYQEHEKRCWSVDFNLMDPKLLASGSDDAKVKLWSTNLDNSVASIEAKANVCCVKFSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVFKGHRKAVSYAKFVSGEEIVSASTDSQLKLWNVGKPYCLRSFKGHINEKNFVGLASNGDYIACGSENNSLYLYYKGLSKTLLTFKFDTVKSVLDKDRKEDDTNEFVSAVCWRALSDGESNVLIAANSQGTIKVLELV
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. {ECO:0000250|UniProtKB:Q8NHY2}.
uniprot
proteins
mass_dalton
80441
uniprot
proteins
mutagenesis
MUTAGEN 113..114; /note="RK->SN: Abolishes nuclear localization."; /evidence="ECO:0000269|PubMed:10395541"; MUTAGEN 197..201; /note="KQKQR->NQNQS: Does not affect the subcellular localization."; /evidence="ECO:0000269|PubMed:10395541"; MUTAGEN 205..208; /note="KRFK->TSFT: Abolishes nuclear localization."; /evidence="ECO:0000269|PubMed:10395541"; MUTAGEN 244..246; /note="LEL->AEA: Abolishes nuclear export."; /evidence="ECO:0000269|PubMed:10395541"; MUTAGEN 358..360; /note="RRK->SRT: Abolishes the nuclear speckle localization but not the nuclear localization."; /evidence="ECO:0000269|PubMed:10395541
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
protein_family
COP1 family
uniprot
proteins
pubmed
10395541
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
733
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:10395541}. Cytoplasm {ECO:0000269|PubMed:10395541}. Note=In the nucleus, it forms nuclear speckles.
uniprot
proteins