RFWD2

Ring finger and WD repeat domain 2, E3 ubiquitin protein ligase
Identifiers
Symbols	RFWD2 ; COP1; RNF200
External IDs	OMIM: 608067 HomoloGene: 115565 GeneCards: RFWD2 Gene
Gene ontology Molecular function • protein binding • zinc ion binding • ligase activity • ubiquitin protein ligase activity Cellular component • Golgi membrane • nucleoplasm • cytoplasm • centrosome • cytosol • focal adhesion • nuclear speck Biological process • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest • response to ionizing radiation • protein ubiquitination • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	64326	26374
Ensembl	ENSG00000143207	ENSMUSG00000040782
UniProt	Q8NHY2	Q9R1A8
RefSeq (mRNA)	NM_001001740	NM_011931
RefSeq (protein)	NP_001001740	NP_036061
Location (UCSC)	Chr 1: 175.94 – 176.21 Mb	Chr 1: 159.23 – 159.35 Mb
PubMed search

E3 ubiquitin-protein ligase RFWD2 is an enzyme that in humans is encoded by the RFWD2 gene.^[1][2]

Interactions

RFWD2 has been shown to interact with C-jun.^[3][4]

References

1. 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.
2. "Entrez Gene: RFWD2 ring finger and WD repeat domain 2".
3. 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". Science 303 (5662): 1371–4. doi:10.1126/science.1093549. PMID 14739464.
4. 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.

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. 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". 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.