RFWD2

Protein-coding gene in the species Homo sapiens
COP1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

5IGQ, 5HQG

Identifiers
AliasesCOP1, RNF200, ring finger and WD repeat domain 2, E3 ubiquitin ligase, RFWD2, COP1 E3 ubiquitin ligase, FAP78, CFAP78
External IDsOMIM: 608067; MGI: 1347046; HomoloGene: 115565; GeneCards: COP1; OMA:COP1 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for COP1
Genomic location for COP1
Band1q25.1-q25.2Start175,944,831 bp[1]
End176,207,286 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for COP1
Genomic location for COP1
Band1|1 H1Start159,059,890 bp[2]
End159,175,210 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 1: 159.06 – 159.18 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000143207 – Ensembl, May 2017
  2. ^ a b c 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.


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