UIMC1

{{Short description|Protein-coding gene in the species Homo sapiens}} {{Infobox_gene}} '''BRCA1-A complex subunit RAP80''' is a protein that in humans is encoded by the ''UIMC1'' gene.<ref name="pmid12080054">{{cite journal | vauthors = Yan Z, Kim YS, Jetten AM | title = RAP80, a novel nuclear protein that interacts with the retinoid-related testis-associated receptor | journal = J Biol Chem | volume = 277 | issue = 35 | pages = 32379–88 |date=Aug 2002 | pmid = 12080054 | doi = 10.1074/jbc.M203475200 | doi-access = free }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UIMC1 ubiquitin interaction motif containing 1| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=51720}}</ref>

==Repair of DNA damage==

RAP80, the protein product of the UIMC1 gene, is a core component of the deubiquitin complex BRCA1-A.<ref name = Rabl2020>{{cite journal |vauthors=Rabl J |title=BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling |journal=Biomolecules |volume=10 |issue=11 |pages= |date=October 2020 |pmid=33142801 |pmc=7692841 |doi=10.3390/biom10111503 |doi-access=free}}</ref> Other core components of the BRCA1-A complex are the BRCC36 protein (BRCC3 gene), BRE protein (BRE (gene)), and MERIT40 protein (BABAM1 gene).<ref name = Rabl2020/>

BRCA1, as distinct from BRCA1-A, is employed in the repair of chromosomal damage with an important role in the error-free homologous recombinational (HR) repair of DNA double-strand breaks. Sequestration of BRCA1 away from the DNA damage site suppresses homologous recombination and redirects the cell in the direction of repair by the process of non-homologous end joining (NHEJ).<ref name = Rabl2020/> The role of BRCA1-A complex appears to be to bind BRCA1 with high affinity and withdraw it away from the site of DNA damage to the periphery where it remains sequestered, thus promoting NHEJ in preference to HR.

==References== {{reflist}}

==Further reading== {{refbegin | 2}} * {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }} * {{cite journal |vauthors=Kim YS, Nakanishi G, Oudes AJ, etal |title=Tsp57: a novel gene induced during a specific stage of spermatogenesis. |journal=Biol. Reprod. |volume=70 |issue= 1 |pages= 106–13 |year= 2004 |pmid= 12954732 |doi= 10.1095/biolreprod.103.018465 |doi-access= free }} * {{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |doi-access= free }} * {{cite journal |vauthors=Colland F, Jacq X, Trouplin V, etal |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 | pmc=442148 }} * {{cite journal |vauthors=Beausoleil SA, Jedrychowski M, Schwartz D, etal |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 | pmc=514446 |bibcode=2004PNAS..10112130B |doi-access=free }} * {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }} * {{cite journal |vauthors=Olsen JV, Blagoev B, Gnad F, etal |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |s2cid=7827573 |doi-access=free }} * {{cite journal |vauthors=Wang B, Matsuoka S, Ballif BA, etal |title=Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response. |journal=Science |volume=316 |issue= 5828 |pages= 1194–8 |year= 2007 |pmid= 17525340 |doi= 10.1126/science.1139476 |pmc=3573690|bibcode=2007Sci...316.1194W }} * {{cite journal |vauthors=Sobhian B, Shao G, Lilli DR, etal |title=RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites. |journal=Science |volume=316 |issue= 5828 |pages= 1198–202 |year= 2007 |pmid= 17525341 |doi= 10.1126/science.1139516 | pmc=2706583 |bibcode=2007Sci...316.1198S }} * {{cite journal | vauthors=Kim H, Chen J, Yu X |title=Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response. |journal=Science |volume=316 |issue= 5828 |pages= 1202–5 |year= 2007 |pmid= 17525342 |doi= 10.1126/science.1139621 |bibcode=2007Sci...316.1202K |s2cid=31636419 }} * {{cite journal |vauthors=Shebzukhov YV, Koroleva EP, Khlgatian SV, etal |title=RAP80/UIMC1 as cancer-associated antigen: alternative splice variants and their immunogenicity. |journal=Cancer Lett. |volume=255 |issue= 2 |pages= 255–62 |year= 2007 |pmid= 17562356 |doi= 10.1016/j.canlet.2007.04.013 }} * {{cite journal |vauthors=Yan J, Kim YS, Yang XP, etal |title=The ubiquitin-interacting motif containing protein RAP80 interacts with BRCA1 and functions in DNA damage repair response. |journal=Cancer Res. |volume=67 |issue= 14 |pages= 6647–56 |year= 2007 |pmid= 17621610 |doi= 10.1158/0008-5472.CAN-07-0924 | pmc=2391092 }} * {{cite journal |vauthors=Yan J, Yang XP, Kim YS, etal |title=RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation. |journal=Biochem. Biophys. Res. Commun. |volume=362 |issue= 1 |pages= 132–8 |year= 2007 |pmid= 17698038 |doi= 10.1016/j.bbrc.2007.07.158 | pmc=2049087 }} {{refend}}