RAD51

RAD51 homolog (S. cerevisiae)

Rad51 filament baziran na 1SZP.^[1]

Dostupne strukture

1B22, 1N0W

Identifikatori

Simboli

RAD51; BRCC5; HRAD51; HsRad51; HsT16930; RAD51A; RECA

Vanjski ID

OMIM: 179617 MGI: 97890 HomoloGene: 2155 GeneCards: RAD51 Gene

Ontologija gena
Molekularna funkcija	• vezivanje nukleotida • vezivanje za oštećenu DNK • vezivanje za dvolančanu DNK • vezivanje za jednolančanu DNK • proteinsko vezivanje • ATP vezivanje • vezivanje za proteinski C-terminus • aktivnost DNK-zavisne ATPaze • aktivnost nukleozidne trifosfataze • vezivanje identičnih proteina • aktivnost jednolančane DNK zavisne ATPaze
Celularna komponenta	• kondenzovani hromozom • lateralni element • nukleus • nukleoplazma • citoplazma • mitohondrija • mitohondrijski matriks • PML telo • perinuklearni region citoplazme
Biološki proces	• popravka dvolančanog prekida putem homologne rekombinacije • formiranje DNK rekombinaze • DNA odmotavanje tokom replikacije • popravka DNK

Pregled RNK izražavanja

podaci

Ortolozi

Vrsta

Čovek

Miš

Entrez

5888

19361

Ensembl

ENSG00000051180

ENSMUSG00000027323

UniProt

Q06609

Q08297

RefSeq (mRNA)

NM_001164269.1

NM_011234.4

RefSeq (protein)

NP_001157741.1

NP_035364.1

Lokacija (UCSC)

Chr 15:
40.99 - 41.02 Mb

Chr 2:
118.94 - 118.97 Mb

PubMed pretraga

[1]

[2]

RAD51 je eukariotski gen. Protein kodiran ovim genom je član RAD51 proteinske familije koja pomaže u popravci dvolančanih prekida DNK. Članovi RAD51 familije su homologni sa bakterijkim RecA i kvaščanim Rad51. Ovaj protein je visoko konzerviran kod većine eukariota, od kvasca do ljudi.

Varijante

Dve alternativno splajsovane transkriptne varijante ovog gena, koje kodiraju zasebne proteina, su poznate. Transkriptne varijante koje koriste alternativne polyA signale postoje.

Interakcije

RAD51 možed da formira interakcije sa BRE,^[2] RAD54B,^[3] Serinska proteinska kinaza ATM,^[4] BRCC3,^[2] BARD1,^[2] BRCA2,^[2]^[5]^[6]^[7]^[8]^[9]^[10]^[11]^[12]^[13]^[14]^[15]^[16] UBE2I,^[17]^[18] Abl gen,^[4] BRCA1,^[2]^[15]^[19]^[20] ATRX,^[3]^[21] RAD52,^[4] DMC1,^[22] P53^[2]^[23]^[24] i Protein Blumovog sindroma.^[25]

Reference

^ Conway AB, Lynch TW, Zhang Y, Fortin GS, Fung CW, Symington LS, Rice PA (2004). „Crystal structure of a Rad51 filament”. Nat Struct Mol Biol. 11 (8): 791—6. PMID 15235592.
^ ^а ^б ^в ^г ^д ^ђ Dong, Yuanshu; Hakimi Mohamed-Ali; et al. (2003). „Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair”. Mol. Cell. United States. 12 (5): 1087—99. ISSN 1097-2765. PMID 14636569. doi:10.1016/S1097-2765(03)00424-6.
^ ^а ^б Tanaka, K; Hiramoto T; et al. (2000). „A novel human rad54 homologue, Rad54B, associates with Rad51”. J. Biol. Chem. UNITED STATES. 275 (34): 26316—21. ISSN 0021-9258. PMID 10851248. doi:10.1074/jbc.M910306199.
^ ^а ^б ^в Chen, G; Yuan S S; et al. (1999). „Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl”. J. Biol. Chem. UNITED STATES. 274 (18): 12748—52. ISSN 0021-9258. PMID 10212258. doi:10.1074/jbc.274.18.12748.
^ Sharan, S K; Morimatsu M; et al. (1997). „Embryonic lethality and radiation hypersensitivity mediated by Rad51 in mice lacking Brca2”. Nature. ENGLAND. 386 (6627): 804—10. ISSN 0028-0836. PMID 9126738. doi:10.1038/386804a0.
^ Lin, Horng-Ru; Ting Nicholas S Y; et al. (2003). „M phase-specific phosphorylation of BRCA2 by Polo-like kinase 1 correlates with the dissociation of the BRCA2-P/CAF complex”. J. Biol. Chem. United States. 278 (38): 35979—87. ISSN 0021-9258. PMID 12815053. doi:10.1074/jbc.M210659200.
^ Yu, David S; Sonoda Eiichiro; et al. (2003). „Dynamic control of Rad51 recombinase by self-association and interaction with BRCA2”. Mol. Cell. United States. 12 (4): 1029—41. ISSN 1097-2765. PMID 14580352. doi:10.1016/S1097-2765(03)00394-0.
^ Chen, P L; Chen C F; et al. (1998). „The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment”. Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 95 (9): 5287—92. ISSN 0027-8424. PMC 20253 . PMID 9560268. doi:10.1073/pnas.95.9.5287.
^ Sarkisian, C J; Master S R; et al. (2001). „Analysis of murine Brca2 reveals conservation of protein-protein interactions but differences in nuclear localization signals”. J. Biol. Chem. United States. 276 (40): 37640—8. ISSN 0021-9258. PMID 11477095. doi:10.1074/jbc.M106281200.
^ Wong, A K; Pero R; et al. (1997). „RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2”. J. Biol. Chem. UNITED STATES. 272 (51): 31941—4. ISSN 0021-9258. PMID 9405383. doi:10.1074/jbc.272.51.31941.
^ Katagiri, T; Saito H; et al. (1998). „Multiple possible sites of BRCA2 interacting with DNA repair protein RAD51”. Genes Chromosomes Cancer. UNITED STATES. 21 (3): 217—22. ISSN 1045-2257. PMID 9523196. doi:10.1002/(SICI)1098-2264(199803)21:3<217::AID-GCC5>3.0.CO;2-2.
^ Pellegrini, Luca; Yu David S; et al. (2002). „Insights into DNA recombination from the structure of a RAD51-BRCA2 complex”. Nature. England. 420 (6913): 287—93. ISSN 0028-0836. PMID 12442171. doi:10.1038/nature01230.
^ Tarsounas, Madalena; Davies Adelina A; et al. (2004). „RAD51 localization and activation following DNA damage”. Philos. Trans. R. Soc. Lond., B, Biol. Sci. England. 359 (1441): 87—93. ISSN 0962-8436. PMC 1693300 . PMID 15065660. doi:10.1098/rstb.2003.1368.
^ Liu, J; Yuan Y; et al. (2001). „Inhibition of breast and brain cancer cell growth by BCCIPalpha, an evolutionarily conserved nuclear protein that interacts with BRCA2”. Oncogene. England. 20 (3): 336—45. ISSN 0950-9232. PMID 11313963. doi:10.1038/sj.onc.1204098.
^ ^а ^б Chen, J; Silver D P; et al. (1998). „Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells”. Mol. Cell. UNITED STATES. 2 (3): 317—28. ISSN 1097-2765. PMID 9774970. doi:10.1016/S1097-2765(00)80276-2.
^ Marmorstein, L Y; Ouchi T; Aaronson S A (1998). „The BRCA2 gene product functionally interacts with p53 and RAD51”. Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 95 (23): 13869—74. ISSN 0027-8424. PMC 24938 . PMID 9811893. doi:10.1073/pnas.95.23.13869.
^ Kovalenko, O V; Plug A W; et al. (1996). „Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes”. Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 93 (7): 2958—63. ISSN 0027-8424. PMC 39742 . PMID 8610150. doi:10.1073/pnas.93.7.2958.
^ Shen, Z; Pardington-Purtymun P E; et al. (1996). „Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system”. Genomics. UNITED STATES. 37 (2): 183—6. ISSN 0888-7543. PMID 8921390. doi:10.1006/geno.1996.0540.
^ Scully, R; Chen J; et al. (1997). „Association of BRCA1 with Rad51 in mitotic and meiotic cells”. Cell. UNITED STATES. 88 (2): 265—75. ISSN 0092-8674. PMID 9008167. doi:10.1016/S0092-8674(00)81847-4.
^ Wang, Q; Zhang H; et al. (2001). „Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1”. Oncogene. England. 20 (34): 4640—9. ISSN 0950-9232. PMID 11498787. doi:10.1038/sj.onc.1204625.
^ Sigurdsson, Stefan; Van Komen Stephen; et al. (2002). „Homologous DNA pairing by human recombination factors Rad51 and Rad54”. J. Biol. Chem. United States. 277 (45): 42790—4. ISSN 0021-9258. PMID 12205100. doi:10.1074/jbc.M208004200.
^ Masson, J Y; Davies A A; et al. (1999). „The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51”. EMBO J. ENGLAND. 18 (22): 6552—60. ISSN 0261-4189. PMC 1171718 . PMID 10562567. doi:10.1093/emboj/18.22.6552.
^ Stürzbecher, H W; Donzelmann B; et al. (1996). „p53 is linked directly to homologous recombination processes via RAD51/RecA protein interaction”. EMBO J. ENGLAND. 15 (8): 1992—2002. ISSN 0261-4189. PMC 450118 . PMID 8617246.
^ Buchhop, S; Gibson M K; et al. (1997). „Interaction of p53 with the human Rad51 protein”. Nucleic Acids Res. ENGLAND. 25 (19): 3868—74. ISSN 0305-1048. PMC 146972 . PMID 9380510. doi:10.1093/nar/25.19.3868.
^ Wu, L; Davies S L; et al. (2001). „Potential role for the BLM helicase in recombinational repair via a conserved interaction with RAD51”. J. Biol. Chem. United States. 276 (22): 19375—81. ISSN 0021-9258. PMID 11278509. doi:10.1074/jbc.M009471200.