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; OMA:COP1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1q25.1-q25.2 Start 175,944,831 bp [1] End 176,207,286 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1|1 H1 Start 159,059,890 bp [2] End 159,175,210 bp [2]
RNA expression pattern Bgee 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 cells 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 BioGPS 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
Orthologs Species Human Mouse Entrez 64326 26374 Ensembl ENSG00000143207 ENSMUSG00000040782 UniProt 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 [3] [4]
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

1. GRCh38: Ensembl release 89: ENSG00000143207 – Ensembl, May 2017
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.
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. Bibcode:1999CBio....9..711W. doi: 10.1016/S0960-9822(99)80314-5 . PMID   10395541. S2CID   2822539.
6. "Entrez Gene: RFWD2 ring finger and WD repeat domain 2".
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. Bibcode:2004Sci...303.1371W. doi:10.1126/science.1093549. PMID   14739464. S2CID   40501515.
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 . 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.