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Protein

E3 ubiquitin-protein ligase COP1

Gene

Cop1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.By similarity

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.By similarity

Enzyme regulationi

TRIB1 competes with substrates for RFWD2 binding.By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri138 – 176RING-typePROSITE-ProRule annotationAdd BLAST39

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-MMU-8951664 Neddylation
UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase COP1Curated (EC:2.3.2.27By similarity)
Alternative name(s):
Constitutive photomorphogenesis protein 1 homologCurated
Short name:
mCOP1Curated
RING finger and WD repeat domain protein 2Curated
RING-type E3 ubiquitin transferase RFWD2Curated
Gene namesi
Name:Cop1Imported
Synonyms:Rfwd2Imported, RNF200
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1347046 Cop1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi113 – 114RK → SN: Abolishes nuclear localization. 1 Publication2
Mutagenesisi197 – 201KQKQR → NQNQS: Does not affect the subcellular localization. 1 Publication5
Mutagenesisi205 – 208KRFK → TSFT: Abolishes nuclear localization. 1 Publication4
Mutagenesisi244 – 246LEL → AEA: Abolishes nuclear export. 1 Publication3
Mutagenesisi358 – 360RRK → SRT: Abolishes the nuclear speckle localization but not the nuclear localization. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000558801 – 733E3 ubiquitin-protein ligase COP1Add BLAST733

Proteomic databases

MaxQBiQ9R1A8
PaxDbiQ9R1A8
PRIDEiQ9R1A8

PTM databases

iPTMnetiQ9R1A8
PhosphoSitePlusiQ9R1A8

Expressioni

Gene expression databases

BgeeiENSMUSG00000040782
CleanExiMM_RFWD2
ExpressionAtlasiQ9R1A8 baseline and differential
GenevisibleiQ9R1A8 MM

Interactioni

Subunit structurei

Homodimer. Homodimerization is mediated by the coiled coil domain. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Isoform 2 does not interact with CUL4A but still binds to RBX1, suggesting that the interaction may be mediated by another cullin protein. Isoform 1 and isoform 2 interact with CUL5 but not with CUL1, CUL2 not CUL3. Interacts with bZIP transcription factors JUN, JUNB and JUND but not with FOS, ATF2 nor XBP1. Interacts with p53 (TP53). Interacts with COPS6; this interaction stabilizes RFWD2 through reducing its auto-ubiquitination and decelerating its turnover rate. Interacts with SFN; this interaction leads to SFN degradation. Interacts with p53/TP53 and MTA1. Interacts with TRIB1 (via C-terminus) and TRIB2.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei474Interaction with TRIB1By similarity1
Sitei493Interaction with TRIB1By similarity1

Binary interactionsi

WithEntry#Exp.IntActNotes
Crtc2Q3U1823EBI-15656898,EBI-8018890

Protein-protein interaction databases

BioGridi204934, 9 interactors
DIPiDIP-60522N
IntActiQ9R1A8, 1 interactor
STRINGi10090.ENSMUSP00000076160

Structurei

3D structure databases

ProteinModelPortaliQ9R1A8
SMRiQ9R1A8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati421 – 460WD 1Add BLAST40
Repeati470 – 510WD 2Add BLAST41
Repeati513 – 553WD 3Add BLAST41
Repeati555 – 595WD 4Add BLAST41
Repeati599 – 637WD 5Add BLAST39
Repeati640 – 679WD 6Add BLAST40
Repeati695 – 731WD 7Add BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni645 – 647Interaction with TRIB1By similarity3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili231 – 306Sequence analysisAdd BLAST76

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi111 – 115Nuclear localization signal 15
Motifi197 – 208Nuclear localization signal 2Add BLAST12
Motifi237 – 247Nuclear export signalAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 112Ser-richAdd BLAST111

Domaini

The RING finger domain, in addition to its role in ubiquitination, functions as a structural scaffold to bring two clusters of positive-charged residues within spatial proximity to mimic a bipartite nuclear localization signal (NLS).1 Publication
The WD40 domain (386-731) is necessary and sufficient for TRIB1 binding.By similarity

Sequence similaritiesi

Belongs to the COP1 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri138 – 176RING-typePROSITE-ProRule annotationAdd BLAST39

Keywords - Domaini

Coiled coil, Repeat, WD repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IE71 Eukaryota
ENOG410XNTU LUCA
GeneTreeiENSGT00920000149161
HOGENOMiHOG000006123
HOVERGENiHBG054995
InParanoidiQ9R1A8
KOiK10143
OMAiPICFEMI
OrthoDBiEOG091G0ERB
PhylomeDBiQ9R1A8
TreeFamiTF328912

Family and domain databases

Gene3Di2.130.10.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF00400 WD40, 5 hits
SMARTiView protein in SMART
SM00184 RING, 1 hit
SM00320 WD40, 6 hits
SUPFAMiSSF50978 SSF50978, 1 hit
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 1 hit
PS50082 WD_REPEATS_2, 2 hits
PS50294 WD_REPEATS_REGION, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q9R1A8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSRQAGSG SAGTSPGSSA ASSVTSASSS LSSSPSPPSV AASAATLVSG
60 70 80 90 100
GVAPAAGSGG LGGPGRPVLV AAAVSGSASA GGAVSAGQSR LSCAARPSAG
110 120 130 140 150
VGGSSSSLGS SSRKRPLLVP LCNGLLNSYE DKSNDFVCPI CFDMIEEAYM
160 170 180 190 200
TKCGHSFCYK CIHQSLEDNN RCPKCNYVVD NIDHLYPNFL VNELILKQKQ
210 220 230 240 250
RFEEKRFKLD HSVSSTNGHR WQIFQDLLGT DQDNLDLANV NLMLELLVQK
260 270 280 290 300
KKQLEAESHA AQLQILMEFL KVARRNKREQ LEQIQKELSV LEEDIKRVEE
310 320 330 340 350
MSGLYSPVSE DSTVPQFEAP SPSHSSIIDS TEYSQPPGFS GTSQTKKQPW
360 370 380 390 400
YNSTLASRRK RLTAHFEDLE QCYFSTRMSR ISDDSRTASQ LDEFQECLSK
410 420 430 440 450
FTRYNSVRPL ATLSYASDLY NGSSIVSSIE FDRDCDYFAI AGVTKKIKVY
460 470 480 490 500
EYGTVIQDAV DIHYPENEMT CNSKISCISW SSYHKNLLAS SDYEGTVILW
510 520 530 540 550
DGFTGQRSKV YQEHEKRCWS VDFNLMDPKL LASGSDDAKV KLWSTNLDNS
560 570 580 590 600
VASIEAKANV CCVKFSPSSR YHLAFGCADH CVHYYDLRNT KQPIMVFKGH
610 620 630 640 650
RKAVSYAKFV SGEEIVSAST DSQLKLWNVG KPYCLRSFKG HINEKNFVGL
660 670 680 690 700
ASNGDYIACG SENNSLYLYY KGLSKTLLTF KFDTVKSVLD KDRKEDDTNE
710 720 730
FVSAVCWRAL SDGESNVLIA ANSQGTIKVL ELV
Length:733
Mass (Da):80,441
Last modified:October 1, 2002 - v2
Checksum:i894AEA412BACC737
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151110 mRNA Translation: AAD51094.2
BC082804 mRNA Translation: AAH82804.1
CCDSiCCDS35745.1
RefSeqiNP_036061.1, NM_011931.3
UniGeneiMm.328135

Genome annotation databases

EnsembliENSMUST00000076894; ENSMUSP00000076160; ENSMUSG00000040782
GeneIDi26374
KEGGimmu:26374
UCSCiuc007ddz.1 mouse

Similar proteinsi

Entry informationi

Entry nameiCOP1_MOUSE
AccessioniPrimary (citable) accession number: Q9R1A8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: October 1, 2002
Last modified: June 20, 2018
This is version 152 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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