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XRCC4

Protein FULL name:

DNA repair protein XRCC4, X-ray repair cross-complementing protein 4.,


XRCC4 (Homo sapiens) is product of expression of XRCC4 gene.


XRCC4 is involved in:

NHEJ in Homo sapiens




FUNCTION: Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.

SUBUNIT: Homodimer and homotetramer in solution. The homodimer associates with LIG4, and the LIG4-XRCC4 complex associates in a DNA-dependent manner with the DNA-PK complex formed by the Ku p70/p86 dimer (G22P1/G22P2) and PRKDC. Seems to interact directly with PRKDC but not with the Ku p70/86 dimer. Interacts with XLF/Cernunnos. Interacts with APTX and APLF.

INTERACTION: O00499:BIN1; NbExp=3; IntAct=EBI-717592, EBI-719094; Q9H9Q4:NHEJ1; NbExp=3; IntAct=EBI-717592, EBI-847807; Q96T60:PNKP; NbExp=1; IntAct=EBI-717592, EBI-1045072;

SUBCELLULAR LOCATION: Nucleus.

TISSUE SPECIFICITY: Widely expressed.

PTM: Phosphorylated by PRKDC. The phosphorylation seems not to be necessary for binding to DNA. Phosphorylation by CK2 promotes interaction with APTX.

PTM: Monoubiquitinated.

PTM: Sumoylation at Lys-210 is required for nuclear localization and recombination efficiency. Has no effect on ubiquitination.

SIMILARITY: Belongs to the XRCC4 family.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 44888352
4507945
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q13426 Q13426
PFAM: PF06632
PF06632
InterPro: IPR010585
IPR014751
IPR009089
IPR010585
IPR014751
IPR009089
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MERKISRIHLVSEPSITHFLQVSWEKTLESGFVITLTDGHSAWTGTVSES
EISQEADDMAMEKGKYVGELRKALLSGAGPADVYTFNFSKESCYFFFEKN
LKDVSFRLGSFNLEKVENPAEVIRELICYCLDTIAENQAKNEHLQKENER
LLRDWNDVQGRFEKCVSAKEALETDLYKRFILVLNEKKTKIRSLHNKLLN
AAQEREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAA
VSKDDSIISSLDVTDIAPSRKRRQRMQRNLGTEPKMAPQENQLQEKENSR
PDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI

XRCC4 (Homo sapiens) is able to recognize following damages:
XRCC4 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
The XRCC4 gene encodes a novel protein involved in DNA double-strand break repair and V(D)J recombination. Li Z, Otevrel T, Gao Y, Cheng HL, Seed B, Stamato TD, Taccioli GE, Alt FW Cell Dec. 1, 1995
Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells. Grawunder U, Wilm M, Wu X, Kulesza P, Wilson TE, Mann M, Lieber MR Nature July 31, 1997
Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV. Critchlow SE, Bowater RP, Jackson SP Curr Biol Aug. 1, 1997
The XRCC4 gene product is a target for and interacts with the DNA-dependent protein kinase. Leber R, Wise TW, Mizuta R, Meek K J Biol Chem Feb. 16, 1998
Ku recruits the XRCC4-ligase IV complex to DNA ends. Nick McElhinny SA, Snowden CM, McCarville J, Ramsden DA Mol Cell Biol May 1, 2000
Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase. Chen L, Trujillo K, Sung P, Tomkinson AE J Biol Chem Aug. 25, 2000
Crystal structure of an Xrcc4-DNA ligase IV complex. Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L Nat Struct Biol Dec. 1, 2001
Defining interactions between DNA-PK and ligase IV/XRCC4. Hsu HL, Yannone SM, Chen DJ DNA Repair (Amst) March 28, 2002
Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment. Calsou P, Delteil C, Frit P, Drouet J, Salles B J Mol Biol Jan. 7, 2003
Tetramerization and DNA ligase IV interaction of the DNA double-strand break repair protein XRCC4 are mutually exclusive. Modesti M, Junop MS, Ghirlando R, van de Rakt M, Gellert M, Yang W, Kanaar R J Mol Biol Nov. 21, 2003
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
Identification of DNA-PKcs phosphorylation sites in XRCC4 and effects of mutations at these sites on DNA end joining in a cell-free system. Lee KJ, Jovanovic M, Udayakumar D, Bladen CL, Dynan WS DNA Repair (Amst) March 4, 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
The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4. Clements PM, Breslin C, Deeks ED, Byrd PJ, Ju L, Bieganowski P, Brenner C, Moreira MC, Taylor AM, Caldecott KW DNA Repair (Amst) Nov. 2, 2004
XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining. Ahnesorg P, Smith P, Jackson SP Cell Feb. 27, 2006
SUMO modification of human XRCC4 regulates its localization and function in DNA double-strand break repair. Yurchenko V, Xue Z, Sadofsky MJ Mol Cell Biol March 1, 2006
Monoubiquitination of the nonhomologous end joining protein XRCC4. Foster RE, Nnakwe C, Woo L, Frank KM Biochem Biophys Res Commun March 3, 2006
A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. Kanno S, Kuzuoka H, Sasao S, Hong Z, Lan L, Nakajima S, Yasui A EMBO J April 18, 2007
APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks. Iles N, Rulten S, El-Khamisy SF, Caldecott KW Mol Cell Biol May 1, 2007
APLF (C2orf13) facilitates nonhomologous end-joining and undergoes ATM-dependent hyperphosphorylation following ionizing radiation. Macrae CJ, McCulloch RD, Ylanko J, Durocher D, Koch CA DNA Repair (Amst) Jan. 1, 2008
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A Aug. 5, 2008
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal Jan. 1, 2009


Last modification of this entry: Oct. 6, 2010.

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