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Xrcc5 |
Protein FULL name:
X-ray repair cross-complementing protein 5 [Mus musculus].
Xrcc5 (Mus musculus) is product of expression of Xrcc5 gene.
FUNCTION: Single stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. expression. The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined (By similarity).
SUBUNIT: Heterodimer of a 70 kDa and a 80 kDa subunit. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA- dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex. The dimer also associates with NAA15, and this complex displays DNA binding activity towards the osteocalcin FGF response element (OCFRE). In addition, the 80 kDa subunit binds to the osteoblast-specific transcription factors MSX2 and RUNX2. Interacts with ELF3. May interact with APLF (By similarity).
SUBCELLULAR LOCATION: Nucleus.
DEVELOPMENTAL STAGE: Expression increases during promyelocyte differentiation.
INDUCTION: Up-regulation during myogenesis is inhibited by cAMP, 3-aminobenzamide and sodium butyrate. Expression in myoblasts is unaffected by X-rays and UV light.
DOMAIN: The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage (By similarity).
PTM: Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity (By similarity).
PTM: Sumoylated (By similarity).
SIMILARITY: Belongs to the ku80 family.
SIMILARITY: Contains 1 Ku domain.
| NCBI GenPept GI number(s): |
160333605 |
| Species: | Mus musculus |
Links to other databases:
| Database | ID | Link |
| Uniprot | P27641 |
P27641 |
| PFAM: | - |
P27641 (Link - using uniprot id) |
| InterPro: | - |
P27641 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MAWSGNKAAVVLCVDVGVAMGNSFPGEESPIEQAKKVMTMFVQRQVFSES KDEIALVLYGTDGTDNALAGKDQYQNITVCRHLMLPDFDLLEDIGNKIQP SSQQADFLDALIVCMDLIQRETIGKKFGKKHIEVFTDLSSPFSQDQLDVI ICNLKKSGISLQFFLPFPIDKNGEPGERGDLDSGLDHLKPSFPQKGLTEQ QKEGIRMVTRVMLSLEGEDGLDEIYSFSESLRQLCVFKKIERRSMPWPCQ LTIGPNLSIKIVAYKSIVQEKFKKSWVVVDARTLKKEDIQKETVYCLNDD DETEVSKEDTIQGYRYGSDIIPFSKVDEEQMKYKSEGKCFSVLGFCKSSQ VHRRFFMGHQVLKVFAAKDDEAAAVALSSLVHALDELNMVAIVRYAYDKR SNPQVGVAFPYIKDAYECLVYVQLPFMEDLRQYMFSSLKNNKKCTPTEAQ LSAIDDLIDSMSLVKKNEEEDIVEDLFPTSKIPNPEFQRLYQCLLHRALH LQERLPPIQQHILNMLDPPTEMKAKCESPLSKVKTLFPLTEVIKKKNQVT AQDVFQDNHEEGPAAKKYKTEKEEDHISISSLAEGNITKVGSVNPVENFR FLVRQKIASFEEASLQLISHIEQFLDTNETLYFMKSMDCIKAFREEAIQF SEEQRFNSFLEALREKVEIKQLNHFWEIVVQDGVTLITKDEGPGSSITAE EATKFLAPKDKAKEDTTGPEEAGDVDDLLDMI |
Xrcc5 (Mus musculus) belongs to following protein families:
References:
| Title | Authors | Journal |
| The nucleotide sequence of a mouse cDNA encoding the 80 kDa subunit of the Ku (p70/p80) autoantigen. | Falzon M, Kuff EL | Nucleic Acids Res July 25, 1992 |
| Non-histone protein 1 (NHP1) is a member of the Ku protein family which is upregulated in differentiating mouse myoblasts and human promyelocytes. | Oderwald H, Hughes MJ, Jost JP | FEBS Lett March 18, 1996 |
| 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 |
| 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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