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XRCC2 |
Protein FULL name:
DNA repair protein XRCC2, X-ray repair cross-complementing protein 2
Protein SHORT name:
XRCC-2
XRCC2 (Homo sapiens) is product of expression of XRCC2 gene.
FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. The BCDX2 complex binds single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA.
SUBUNIT: Interacts with RAD51D. Part of a BCDX2 complex consisting of RAD51B, RAD51C, RAD51D and XRCC2. Part of a complex consisting of RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3. In the absence of DNA, XRCC2-RAD51D formed a multimeric ring structure. In the presence of single-stranded DNA, XRCC2-RAD51D formed a filamentous structure.
SUBCELLULAR LOCATION: Nucleus.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
SIMILARITY: Belongs to the recA family. RAD51 subfamily.
WEB RESOURCE: Name=NIEHS-SNPs; [LINK]
| NCBI GenPept GI number(s): |
4885657 |
| Species: | Homo sapiens |
Links to other databases:
| Database | ID | Link |
| Uniprot | O43543 |
O43543 |
| PFAM: | - |
O43543 (Link - using uniprot id) |
| InterPro: | - |
O43543 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MCSAFHRAESGTELLARLEGRSSLKEIEPNLFADEDSPVHGDILEFHGPE GTGKTEMLYHLTARCILPKSEGGLEVEVLFIDTDYHFDMLRLVTILEHRL SQSSEEIIKYCLGRFFLVYCSSSTHLLLTLYSLESMFCSHPSLCLLILDS LSAFYWIDRVNGGESVNLQESTLRKCSQCLEKLVNDYRLVLFATTQTIMQ KASSSSEEPSHASRRLCDVDIDYRPYLCKAWQQLVKHRMFFSKQDDSQSS NQFSLVSRCLKSNSLKKHFFIIGESGVEFC |
XRCC2 (Homo sapiens) is able to recognize following damages:
XRCC2 (Homo sapiens) belongs to following protein families:
References:
| Title | Authors | Journal |
| The XRCC2 DNA repair gene: identification of a positional candidate. | Tambini CE, George AM, Rommens JM, Tsui LC, Scherer SW, Thacker J | Genomics April 1, 1997 |
| XRCC2 and XRCC3, new human Rad51-family members, promote chromosome stability and protect against DNA cross-links and other damages. | Liu N, Lamerdin JE, Tebbs RS, Schild D, Tucker JD, Shen MR, Brookman KW, Siciliano MJ, Walter CA, Fan W, Narayana LS, Zhou ZQ, Adamson AW, Sorensen KJ, Chen DJ, Jones NJ, Thompson LH | Mol Cell May 1, 1998 |
| The XRCC2 DNA repair gene from human and mouse encodes a novel member of the recA/RAD51 family. | Cartwright R, Tambini CE, Simpson PJ, Thacker J | Nucleic Acids Res July 1, 1998 |
| Identification and purification of two distinct complexes containing the five RAD51 paralogs. | Masson JY, Tarsounas MC, Stasiak AZ, Stasiak A, Shah R, McIlwraith MJ, Benson FE, West SC | Genes Dev Dec. 15, 2001 |
| Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells. | Liu N, Schild D, Thelen MP, Thompson LH | Nucleic Acids Res Jan. 15, 2002 |
| Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells. | Wiese C, Collins DW, Albala JS, Thompson LH, Kronenberg A, Schild D | Nucleic Acids Res Jan. 15, 2002 |
| RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51. | Miller KA, Yoshikawa DM, McConnell IR, Clark R, Schild D, Albala JS | J Biol Chem March 8, 2002 |
| Complete sequencing and characterization of 21,243 full-length human cDNAs. | Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S | Nat Genet Feb. 1, 2004 |
| The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). | Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J | Genome Res Oct. 1, 2004 |
| ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. | Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ | Science May 25, 2007 |
Last modification of this entry: Oct. 11, 2010.
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