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Xrcc3 |
Protein FULL name:
DNA repair protein XRCC3 [Mus musculus].
Xrcc3 (Mus musculus) is product of expression of Xrcc3 gene.
FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions (By similarity).
SUBUNIT: Interacts with RAD51C and RAD51. Part of a complex consisting of RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3 (By similarity).
SUBCELLULAR LOCATION: Nucleus (Probable).
SIMILARITY: Belongs to the recA family. RAD51 subfamily.
| NCBI GenPept GI number(s): |
21312694 |
| Species: | Mus musculus |
Links to other databases:
| Database | ID | Link |
| Uniprot | Q9CXE6 |
Q9CXE6 |
| PFAM: | - |
Q9CXE6 (Link - using uniprot id) |
| InterPro: | - |
Q9CXE6 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MDLDQLDLNPRITAAVKRGRLKSVKEILCYSGPDLQRLTGLPSHDVQCLL RAASLHLRGSRVLSALHLFQQKESFPEQHQRLSLGCPVLDQFLGGGLPLE GITGLAGCSSAGKTQLALQLCLAVQFPRQYGGLEAGAVYICTEDAFPSKR LWQLIAQQRRLRTDAPEELIEKIRFSNHIFIEHAADVDTLLECVSKKVPI LLSRGMARLVVVDSIAAPFRCEFHLQASAIRAKLLLSLGATLRRLSSTFR SPVLCINQVTDMVEDQQSVSRSLGASEERLSPALGITWANQLLMRLMVDR THEDDVTTGLPRSPVRTLRVLFAPHLPLSSCCYTVSGEGIRGMPGTQSY |
Xrcc3 (Mus musculus) belongs to following protein families:
References:
| Title | Authors | Journal |
| The transcriptional landscape of the mammalian genome. | Carninci P, Kasukawa T, Katayama S, Gough J, Frith MC, Maeda N, Oyama R, Ravasi T, Lenhard B, Wells C, Kodzius R, Shimokawa K, Bajic VB, Brenner SE, Batalov S, Forrest AR, Zavolan M, Davis MJ, Wilming LG, Aidinis V, Allen JE, Ambesi-Impiombato A, Apweiler R, Aturaliya RN, Bailey TL, Bansal M, Baxter L, Beisel KW, Bersano T, Bono H, Chalk AM, Chiu KP, Choudhary V, Christoffels A, Clutterbuck DR, Crowe ML, Dalla E, Dalrymple BP, de Bono B, Della Gatta G, di Bernardo D, Down T, Engstrom P, Fagiolini M, Faulkner G, Fletcher CF, Fukushima T, Furuno M, Futaki S, Gariboldi M, Georgii-Hemming P, Gingeras TR, Gojobori T, Green RE, Gustincich S, Harbers M, Hayashi Y, Hensch TK, Hirokawa N, Hill D, Huminiecki L, Iacono M, Ikeo K, Iwama A, Ishikawa T, Jakt M, Kanapin A, Katoh M, Kawasawa Y, Kelso J, Kitamura H, Kitano H, Kollias G, Krishnan SP, Kruger A, Kummerfeld SK, Kurochkin IV, Lareau LF, Lazarevic D, Lipovich L, Liu J, Liuni S, McWilliam S, Madan Babu M, Madera M, Marchionni L, Matsuda H, Matsuzawa S, Miki H, Mignone F, Miyake S, Morris K, Mottagui-Tabar S, Mulder N, Nakano N, Nakauchi H, Ng P, Nilsson R, Nishiguchi S, Nishikawa S, Nori F, Ohara O, Okazaki Y, Orlando V, Pang KC, Pavan WJ, Pavesi G, Pesole G, Petrovsky N, Piazza S, Reed J, Reid JF, Ring BZ, Ringwald M, Rost B, Ruan Y, Salzberg SL, Sandelin A, Schneider C, Schonbach C, Sekiguchi K, Semple CA, Seno S, Sessa L, Sheng Y, Shibata Y, Shimada H, Shimada K, Silva D, Sinclair B, Sperling S, Stupka E, Sugiura K, Sultana R, Takenaka Y, Taki K, Tammoja K, Tan SL, Tang S, Taylor MS, Tegner J, Teichmann SA, Ueda HR, van Nimwegen E, Verardo R, Wei CL, Yagi K, Yamanishi H, Zabarovsky E, Zhu S, Zimmer A, Hide W, Bult C, Grimmond SM, Teasdale RD, Liu ET, Brusic V, Quackenbush J, Wahlestedt C, Mattick JS, Hume DA, Kai C, Sasaki D, Tomaru Y, Fukuda S, Kanamori-Katayama M, Suzuki M, Aoki J, Arakawa T, Iida J, Imamura K, Itoh M, Kato T, Kawaji H, Kawagashira N, Kawashima T, Kojima M, Kondo S, Konno H, Nakano K, Ninomiya N, Nishio T, Okada M, Plessy C, Shibata K, Shiraki T, Suzuki S, Tagami M, Waki K, Watahiki A, Okamura-Oho Y, Suzuki H, Kawai J, Hayashizaki Y | Science Sept. 2, 2005 |
Last modification of this entry: Oct. 6, 2010.
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