COP1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0032436Biological processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
GO_0016567Biological processprotein ubiquitination
GO_0010212Biological processresponse to ionizing radiation
GO_0043161Biological processproteasome-mediated ubiquitin-dependent protein catabolic process
GO_0016607Cellular componentnuclear speck
GO_0005654Cellular componentnucleoplasm
GO_0005829Cellular componentcytosol
GO_0031464Cellular componentCul4A-RING E3 ubiquitin ligase complex
GO_0061630Molecular functionubiquitin protein ligase activity
GO_0004842Molecular functionubiquitin-protein transferase activity
GO_0005515Molecular functionprotein binding
GO_0046872Molecular functionmetal ion binding

IV. Literature review

[source]
Gene nameCOP1
Protein nameRing finger and WD repeat domain 2 isoform I
COP1 E3 ubiquitin ligase
Ring finger and WD repeat domain 2 isoform B
Ring finger and WD repeat domain 2 isoform H
Ring finger and WD repeat domain 2 isoform G
Ring finger and WD repeat domain 2 isoform D
Ring finger and WD repeat domain 2 isoform C
Ring finger and WD repeat domain 2 isoform F
RFWD2 protein
E3 ubiquitin-protein ligase COP1 (EC 2.3.2.27) (Constitutive photomorphogenesis protein 1 homolog) (hCOP1) (RING finger and WD repeat domain protein 2) (RING finger protein 200) (RING-type E3 ubiquitin transferase RFWD2)
SynonymsRFWD2
RNF200
DescriptionFUNCTION: 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). .

AccessionsX5D2S9
ENST00000649803.1
X5D7W8
Q05CT6
ENST00000498306.5
ENST00000491600.5
X5DR91
ENST00000367669.8 [Q8NHY2-1]
H0YF49
E9PJB5
ENST00000474194.1 [Q8NHY2-5]
ENST00000308769.12 [Q8NHY2-2]
ENST00000459744.5
X5D7N8
H0Y339
ENST00000367666.5
Q8NHY2
E9PMW8
A0A3B3ISQ9
X5DRD4
H0Y340
ENST00000367667.5
X5D9B8
X5DNY7