E3 ubiquitin-protein ligase COP1

COP1

Identifiers

COP1, RNF200, ring finger and WD repeat domain 2, E3 ubiquitin ligase, RFWD2, COP1 E3 ubiquitin ligase, FAP78, CFAP78

External IDs

OMIM: 608067; MGI: 1347046; GeneCards: COP1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
5IGQ, 5HQG

Enzyme activity
EC #	BRENDA	ExPASy	KEGG	MetaCyc
2.3.2.27	↗	↗	↗	↗

Gene location (Human)

Chr.	Chromosome 1 (human)

Band	1q25.1-q25.2	Start	175,944,831 bp
Band	1q25.1-q25.2	End	176,207,286 bp

Gene location (Mouse)

Chr.	Chromosome 1 (mouse)

Band	1\|1 H1	Start	159,059,890 bp
Band	1\|1 H1	End	159,175,210 bp

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

mucosa of ileum

mucosa of transverse colon

ganglionic eminence

blood

ventricular zone

gonad

white blood cell

monocyte

bone marrow cell

skin of arm

Top expressed in

zygote

tail of embryo

genital tubercle

granulocyte

ventricular zone

muscle of thigh

spermatocyte

esophagus

dentate gyrus of hippocampal formation granule cell

spermatid

More reference expression data

n/a

Gene ontology
Molecular function	protein binding metal ion binding ubiquitin-protein transferase activity transferase activity ubiquitin protein ligase activity zinc ion binding
Cellular component	nuclear speck cytosol Golgi membrane nucleus cytoplasm nucleoplasm Cul4A-RING E3 ubiquitin ligase complex centrosome focal adhesion
Biological process	protein ubiquitination response to ionizing radiation positive regulation of proteasomal ubiquitin-dependent protein catabolic process post-translational protein modification proteasome-mediated ubiquitin-dependent protein catabolic process
Sources:Amigo / QuickGO

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


64326


26374


ENSG00000143207


ENSMUSG00000040782


Q8NHY2


Q9R1A8

RefSeq (mRNA)


NM_001001740 NM_001286644 NM_022457


NM_011931 NM_001360878

RefSeq (protein)


NP_001001740 NP_001273573 NP_071902


NP_036061 NP_001347807

Location (UCSC)

Chr 1: 175.94 – 176.21 Mb

Chr 1: 159.06 – 159.18 Mb

PubMed search

View/Edit Human

View/Edit Mouse

E3 ubiquitin-protein ligase COP1 is an enzyme that in humans is encoded by the COP1 gene (previously RFWD2).

Interactions

COP1 has been shown to interact with C-jun.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000143207 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000040782 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Wang H, Kang D, Deng XW, Wei N (Sep 1999). "Evidence for functional conservation of a mammalian homologue of the light-responsive plant protein COP1". Curr Biol. 9 (13): 711–4. Bibcode:1999CBio....9..711W. doi:10.1016/S0960-9822(99)80314-5. PMID 10395541. S2CID 2822539.
↑ "Entrez Gene: RFWD2 ring finger and WD repeat domain 2".
↑ Wertz IE, O'Rourke KM, Zhang Z, Dornan D, Arnott D, Deshaies RJ, Dixit VM (Feb 2004). "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase" (PDF). Science. 303 (5662): 1371–4. Bibcode:2004Sci...303.1371W. doi:10.1126/science.1093549. PMID 14739464. S2CID 40501515.
↑ Bianchi E, Denti S, Catena R, Rossetti G, Polo S, Gasparian S, Putignano S, Rogge L, Pardi R (May 2003). "Characterization of human constitutive photomorphogenesis protein 1, a RING finger ubiquitin ligase that interacts with Jun transcription factors and modulates their transcriptional activity". J. Biol. Chem. 278 (22): 19682–90. doi:10.1074/jbc.M212681200. hdl:2434/518351. PMID 12615916.

Further reading

Hoecker U, Quail PH (2001). "The phytochrome A-specific signaling intermediate SPA1 interacts directly with COP1, a constitutive repressor of light signaling in Arabidopsis". J. Biol. Chem. 276 (41): 38173–8. doi:10.1074/jbc.M103140200. PMID 11461903.
Yi C, Wang H, Wei N, Deng XW (2003). "An initial biochemical and cell biological characterization of the mammalian homologue of a central plant developmental switch, COP1". BMC Cell Biol. 3: 30. doi:10.1186/1471-2121-3-30. PMC 138799. PMID 12466024.
Bianchi E, Denti S, Catena R, Rossetti G, Polo S, Gasparian S, Putignano S, Rogge L, Pardi R (2003). "Characterization of human constitutive photomorphogenesis protein 1, a RING finger ubiquitin ligase that interacts with Jun transcription factors and modulates their transcriptional activity". J. Biol. Chem. 278 (22): 19682–90. doi:10.1074/jbc.M212681200. hdl:2434/518351. PMID 12615916.
Wertz IE, O'Rourke KM, Zhang Z, Dornan D, Arnott D, Deshaies RJ, Dixit VM (2004). "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase" (PDF). Science. 303 (5662): 1371–4. Bibcode:2004Sci...303.1371W. doi:10.1126/science.1093549. PMID 14739464. S2CID 40501515.
Dornan D, Wertz I, Shimizu H, Arnott D, Frantz GD, Dowd P, O'Rourke K, Koeppen H, Dixit VM (2004). "The ubiquitin ligase COP1 is a critical negative regulator of p53". Nature. 429 (6987): 86–92. Bibcode:2004Natur.429...86D. doi:10.1038/nature02514. PMID 15103385. S2CID 4319187.
Dornan D, Bheddah S, Newton K, Ince W, Frantz GD, Dowd P, Koeppen H, Dixit VM, French DM (2004). "COP1, the negative regulator of p53, is overexpressed in breast and ovarian adenocarcinomas". Cancer Res. 64 (20): 7226–30. doi:10.1158/0008-5472.CAN-04-2601. PMID 15492238. S2CID 21636114.
Dornan D, Shimizu H, Mah A, Dudhela T, Eby M, O'rourke K, Seshagiri S, Dixit VM (2006). "ATM engages autodegradation of the E3 ubiquitin ligase COP1 after DNA damage". Science. 313 (5790): 1122–6. Bibcode:2006Sci...313.1122D. doi:10.1126/science.1127335. PMID 16931761. S2CID 34368821.

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