RFWD2

COP1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	5IGQ, 5HQG
Identifiers
Aliases	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 HomoloGene: 115565 GeneCards: COP1
Gene location (Human)
Chr.	Chromosome 1 (human)[1]
End	176,207,286 bp[1]
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)[2]
End	159,347,640 bp[2]
Gene ontology
Molecular function	• GO:0001948 protein binding; • metal ion binding; • ubiquitin-protein transferase activity; • transferase activity; • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity; • zinc ion binding;
Cellular component	• nuclear speck; • cytosol; • Golgi membrane; • cell 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 modification; • proteasome-mediated ubiquitin-dependent protein catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	64326
	26374
	ENSG00000143207
	ENSMUSG00000040782
	Q8NHY2
	Q9R1A8
	NM_001001740; NM_001286644; NM_022457
	NM_011931; NM_001360878
	NP_001001740; NP_001273573; NP_071902
	NP_036061; NP_001347807
	Wikidata
View/Edit Human	View/Edit Mouse

E3 ubiquitin-protein ligase RFWD2 is an enzyme that in humans is encoded by the RFWD2 gene.[5][6]

Interactions

RFWD2 has been shown to interact with C-jun.[7][8]

References

GRCh38: Ensembl release 89: ENSG00000143207 - Ensembl, May 2017
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. doi:10.1016/S0960-9822(99)80314-5. PMID 10395541.
"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. doi:10.1126/science.1093549. PMID 14739464.
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. PMID 12615916.

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. 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. doi:10.1126/science.1093549. PMID 14739464.
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. doi:10.1038/nature02514. PMID 15103385.
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.
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. doi:10.1126/science.1127335. PMID 16931761.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000143207 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000040782 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10395541-5] 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. doi:10.1016/S0960-9822(99)80314-5. PMID 10395541.

[entrez-6] "Entrez Gene: RFWD2 ring finger and WD repeat domain 2".

[pmid14739464-7] 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. doi:10.1126/science.1093549. PMID 14739464.

[pmid12615916-8] 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. PMID 12615916.

RFWD2

Interactions

References

Further reading