Q13426 (XRCC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA repair protein XRCC4

Alternative name(s):
X-ray repair cross-complementing protein 4

Gene names

Name:

XRCC4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.13 Ref.14 Ref.18
Subunit structure	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 (XRCC6/XRCC5) 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. Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.23
Subcellular location	Nucleus Ref.9 Ref.20.
Tissue specificity	Widely expressed. Ref.1
Post-translational modification	Phosphorylated by PRKDC. The phosphorylation seems not to be necessary for binding to DNA. Phosphorylation by CK2 promotes interaction with APTX. Ref.9 Ref.10 Ref.11 Ref.16 Ref.17 Ref.18 Monoubiquitinated. Sumoylation at Lys-210 is required for nuclear localization and recombination efficiency. Has no effect on ubiquitination. Ref.20
Sequence similarities	Belongs to the XRCC4 family.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA ligation involved in DNA repair Inferred from direct assay PubMed 12517771. Source: UniProtKB T cell differentiation in thymus Inferred from electronic annotation. Source: Compara cellular response to lithium ion Inferred from electronic annotation. Source: Compara central nervous system development Inferred from electronic annotation. Source: Compara double-strand break repair via nonhomologous end joining Inferred from direct assay PubMed 12517771. Source: UniProtKB immunoglobulin V(D)J recombination Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara isotype switching Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of fibroblast proliferation Inferred from electronic annotation. Source: Compara positive regulation of ligase activity Inferred from direct assay Ref.12. Source: UniProtKB positive regulation of neurogenesis Inferred from electronic annotation. Source: Compara pro-B cell differentiation Inferred from electronic annotation. Source: Compara response to X-ray Inferred from direct assay Ref.12. Source: UniProtKB response to gamma radiation Inferred from electronic annotation. Source: Compara viral reproduction Traceable author statement. Source: Reactome
Cellular_component	DNA ligase IV complex Inferred from direct assay Ref.12. Source: UniProtKB DNA-dependent protein kinase-DNA ligase 4 complex Inferred from direct assay PubMed 15194694. Source: MGI cytosol Inferred from direct assay Ref.9. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BIN1	O00499	4	EBI-717592,EBI-719094
NHEJ1	Q9H9Q4	5	EBI-717592,EBI-847807

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13426-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13426-2)

The sequence of this isoform differs from the canonical sequence as follows:
     298-300: NSR → K

Isoform 3 (identifier: Q13426-3)

The sequence of this isoform differs from the canonical sequence as follows:
     298-336: NSRPDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI → KGRKKETSEKEAV

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 336

336

DNA repair protein XRCC4

PRO_0000066047

Regions

Region

180 – 213

34

Interacts with LIG4

Coiled coil

131 – 165

35

Potential

Coiled coil

184 – 212

29

Potential

Amino acid modifications

Modified residue

232

1

Phosphoserine By similarity

Modified residue

233

1

Phosphothreonine By similarity

Modified residue

256

1

Phosphoserine Ref.26

Modified residue

260

1

Phosphoserine; by PRKDC Ref.11

Modified residue

320

1

Phosphoserine; by PRKDC Ref.11

Modified residue

327

1

Phosphoserine Ref.24 Ref.25

Modified residue

328

1

Phosphoserine Ref.24 Ref.25

Cross-link

210

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.20

Natural variations

Alternative sequence

298 – 336

39

NSRPD…LFDEI → KGRKKETSEKEAV in isoform 3.

VSP_009474

Alternative sequence

298 – 300

3

NSR → K in isoform 2.

VSP_009473

Natural variant

12

1

S → C. Ref.6
Corresponds to variant rs28383138 [ dbSNP | Ensembl ].

VAR_022310

Natural variant

56

1

A → T. Ref.6
Corresponds to variant rs28383151 [ dbSNP | Ensembl ].

VAR_022311

Natural variant

134

1

I → T. Ref.6
Corresponds to variant rs28360135 [ dbSNP | Ensembl ].

VAR_022312

Natural variant

142

1

E → Q. Ref.6
Corresponds to variant rs28360136 [ dbSNP | Ensembl ].

VAR_022313

Natural variant

240

1

Q → P.
Corresponds to variant rs2974446 [ dbSNP | Ensembl ].

VAR_017810

Natural variant

247

1

A → S. Ref.6
Corresponds to variant rs3734091 [ dbSNP | Ensembl ].

VAR_017811

Experimental info

Mutagenesis

140

1

K → R: No change in sumoylation. Ref.20

Mutagenesis

210

1

K → R: Abolishes sumoylation. No nuclear location. 5-fold decrease in recombination efficiency. Ref.20

Secondary structure

1

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336

Helix Strand Turn

Details...

Beta strand

2 – 10

9

Beta strand

13 – 26

14

Helix

28 – 30

3

Beta strand

31 – 37

7

Beta strand

42 – 48

7

Helix

49 – 58

10

Helix

63 – 74

12

Beta strand

84 – 88

5

Turn

90 – 92

3

Beta strand

94 – 100

7

Beta strand

105 – 112

8

Helix

119 – 133

15

Turn

173 – 176

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: BE5FB99153479A4E	FASTA	336	38,287
	10 20 30 40 50 60 MERKISRIHL VSEPSITHFL QVSWEKTLES GFVITLTDGH SAWTGTVSES EISQEADDMA 70 80 90 100 110 120 MEKGKYVGEL RKALLSGAGP ADVYTFNFSK ESCYFFFEKN LKDVSFRLGS FNLEKVENPA 130 140 150 160 170 180 EVIRELICYC LDTIAENQAK NEHLQKENER LLRDWNDVQG RFEKCVSAKE ALETDLYKRF 190 200 210 220 230 240 ILVLNEKKTK IRSLHNKLLN AAQEREKDIK QEGETAICSE MTADRDPVYD ESTDEESENQ 250 260 270 280 290 300 TDLSGLASAA VSKDDSIISS LDVTDIAPSR KRRQRMQRNL GTEPKMAPQE NQLQEKENSR 310 320 330 PDSSLPETSK KEHISAENMS LETLRNSSPE DLFDEI
	Isoform 2 [UniParc]. Checksum: E32CC403854DCE9B	FASTA	334	38,058
	10 20 30 40 50 60 MERKISRIHL VSEPSITHFL QVSWEKTLES GFVITLTDGH SAWTGTVSES EISQEADDMA 70 80 90 100 110 120 MEKGKYVGEL RKALLSGAGP ADVYTFNFSK ESCYFFFEKN LKDVSFRLGS FNLEKVENPA 130 140 150 160 170 180 EVIRELICYC LDTIAENQAK NEHLQKENER LLRDWNDVQG RFEKCVSAKE ALETDLYKRF 190 200 210 220 230 240 ILVLNEKKTK IRSLHNKLLN AAQEREKDIK QEGETAICSE MTADRDPVYD ESTDEESENQ 250 260 270 280 290 300 TDLSGLASAA VSKDDSIISS LDVTDIAPSR KRRQRMQRNL GTEPKMAPQE NQLQEKEKPD 310 320 330 SSLPETSKKE HISAENMSLE TLRNSSPEDL FDEI
	Isoform 3 [UniParc]. Checksum: 30B8DCC13C64A548	FASTA	310	35,372
	10 20 30 40 50 60 MERKISRIHL VSEPSITHFL QVSWEKTLES GFVITLTDGH SAWTGTVSES EISQEADDMA 70 80 90 100 110 120 MEKGKYVGEL RKALLSGAGP ADVYTFNFSK ESCYFFFEKN LKDVSFRLGS FNLEKVENPA 130 140 150 160 170 180 EVIRELICYC LDTIAENQAK NEHLQKENER LLRDWNDVQG RFEKCVSAKE ALETDLYKRF 190 200 210 220 230 240 ILVLNEKKTK IRSLHNKLLN AAQEREKDIK QEGETAICSE MTADRDPVYD ESTDEESENQ 250 260 270 280 290 300 TDLSGLASAA VSKDDSIISS LDVTDIAPSR KRRQRMQRNL GTEPKMAPQE NQLQEKEKGR 310 KKETSEKEAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 H.L., Seed B., Stamato T.D., Taccioli G.E., Alt F.W. Cell 83:1079-1089(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
[2]	"The genomic structure of the human XRCC4 gene." Fugmann S.D., Schwarz K. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Human lymphoblastoid cell line TK-6 lacking in a novel component involved in V(D)J recombination." Tatsumi K. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]	"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 T.-O., 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. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	NIEHS SNPs program Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-12; THR-56; THR-134; GLN-142 AND SER-247.
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Bone marrow.
[9]	"Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV." Critchlow S.E., Bowater R.P., Jackson S.P. Curr. Biol. 7:588-598(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LIG4, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[10]	"The XRCC4 gene product is a target for and interacts with the DNA-dependent protein kinase." Leber R., Wise T.W., Mizuta R., Meek K. J. Biol. Chem. 273:1794-1801(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY PRKDC.
[11]	"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 K.J., Jovanovic M., Udayakumar D., Bladen C.L., Dynan W.S. DNA Repair 3:267-276(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-260 AND SER-320.
[12]	"Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells." Grawunder U., Wilm M., Wu X., Kulesza P., Wilson T.E., Mann M., Lieber M.R. Nature 388:492-495(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LIG4.
[13]	"Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase." Chen L., Trujillo K., Sung P., Tomkinson A.E. J. Biol. Chem. 275:26196-26205(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH LIG4; XRCC6; XRCC5 AND PRKDC.
[14]	"Ku recruits the XRCC4-ligase IV complex to DNA ends." Nick McElhinny S.A., Snowden C.M., McCarville J., Ramsden D.A. Mol. Cell. Biol. 20:2996-3003(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH XRCC6 AND XRCC5.
[15]	"Defining interactions between DNA-PK and ligase IV/XRCC4." Hsu H.-L., Yannone S.M., Chen D.J. DNA Repair 1:225-235(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRKDC.
[16]	"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. 326:93-103(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH G22P1; G22P2 AND PRKDC, PHOSPHORYLATION.
[17]	"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 P.M., Breslin C., Deeks E.D., Byrd P.J., Ju L., Bieganowski P., Brenner C., Moreira M.-C., Taylor A.M.R., Caldecott K.W. DNA Repair 3:1493-1502(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APTX, PHOSPHORYLATION.
[18]	"Monoubiquitination of the nonhomologous end joining protein XRCC4." Foster R.E., Nnakwe C., Woo L., Frank K.M. Biochem. Biophys. Res. Commun. 341:175-183(2006) [PubMed] [Europe PMC] [Abstract] Cited for: MONOUBIQUITINATION, PHOSPHORYLATION, FUNCTION.
[19]	"XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining." Ahnesorg P., Smith P., Jackson S.P. Cell 124:301-313(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH XLF.
[20]	"SUMO modification of human XRCC4 regulates its localization and function in DNA double-strand break repair." Yurchenko V., Xue Z., Sadofsky M.J. Mol. Cell. Biol. 26:1786-1794(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-210, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-140 AND LYS-210.
[21]	"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. 26:2094-2103(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APLF.
[22]	"APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks." Iles N., Rulten S., El-Khamisy S.F., Caldecott K.W. Mol. Cell. Biol. 27:3793-3803(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APLF.
[23]	"APLF (C2orf13) facilitates nonhomologous end-joining and undergoes ATM-dependent hyperphosphorylation following ionizing radiation." Macrae C.J., McCulloch R.D., Ylanko J., Durocher D., Koch C.A. DNA Repair 7:292-302(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APLF.
[24]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-328, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-328, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]	"Crystal structure of an Xrcc4-DNA ligase IV complex." Sibanda B.L., Critchlow S.E., Begun J., Pei X.Y., Jackson S.P., Blundell T.L., Pellegrini L. Nat. Struct. Biol. 8:1015-1019(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-113 IN COMPLEX WITH LIG4.
[30]	"Tetramerization and DNA ligase IV interaction of the DNA double-strand break repair protein XRCC4 are mutually exclusive." Modesti M., Junop M.S., Ghirlando R., van de Rakt M., Gellert M., Yang W., Kanaar R. J. Mol. Biol. 334:215-228(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-203.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U40622 mRNA. Translation: AAC50339.1.
AF055285 , AF055279, AF055280, AF055281, AF055282, AF055283, AF055284 Genomic DNA. Translation: AAD47297.1.
AF055285 , AF055279, AF055280, AF055281, AF055282, AF055283, AF055284 Genomic DNA. Translation: AAD47298.1.
AB017445 mRNA. Translation: BAB20668.1.
BT007216 mRNA. Translation: AAP35880.1.
AK290739 mRNA. Translation: BAF83428.1.
AY940097 Genomic DNA. Translation: AAX14046.1.
CH471084 Genomic DNA. Translation: EAW95898.1.
BC005259 mRNA. Translation: AAH05259.1.
BC016314 mRNA. Translation: AAH16314.1.

IPI

IPI00007672.
IPI00019678.
IPI00401064.

RefSeq

NP_003392.1. NM_003401.3.
NP_071801.1. NM_022406.2.
NP_072044.1. NM_022550.2.

UniGene

Hs.567359.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FU1	X-ray	2.70	A/B	1-203	[»]
1IK9	X-ray	2.30	A/B	1-213	[»]
3II6	X-ray	2.40	A/B/C/D	1-203	[»]
3MUD	X-ray	2.20	A/B	2-133	[»]
3Q4F	X-ray	5.50	C/D/G/H	1-157	[»]
3RWR	X-ray	3.94	A/B/F/G/J/K/N/P/R/U/V/Y	1-157	[»]
3SR2	X-ray	3.97	A/B/E/F	1-140	[»]
3W03	X-ray	8.49	C/D	1-164	[»]

DisProt

DP00152.

ProteinModelPortal

Q13426.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37957N.

IntAct

Q13426. 10 interactions.

MINT

MINT-1205583.

STRING

9606.ENSP00000342011.

PTM databases

PhosphoSite

Q13426.

Polymorphism databases

DMDM

44888352.

Proteomic databases

PaxDb

Q13426.

PRIDE

Q13426.

Protocols and materials databases

DNASU

7518.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000282268; ENSP00000282268; ENSG00000152422.
ENST00000338635; ENSP00000342011; ENSG00000152422.
ENST00000396027; ENSP00000379344; ENSG00000152422.
ENST00000511817; ENSP00000421491; ENSG00000152422.

GeneID

7518.

KEGG

hsa:7518.

UCSC

uc003kia.1. human.
uc003kib.3. human.
uc003kic.3. human.

Organism-specific databases

CTD

7518.

GeneCards

GC05P082409.

HGNC

HGNC:12831. XRCC4.

HPA

HPA006801.

MIM

194363. gene.

neXtProt

NX_Q13426.

PharmGKB

PA37423.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG69713.

HOGENOM

HOG000013067.

HOVERGEN

HBG059517.

InParanoid

Q13426.

KO

K10886.

OMA

LETDLYK.

OrthoDB

EOG48WC3N.

PhylomeDB

Q13426.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_216. DNA Repair.

Gene expression databases

Bgee

Q13426.

CleanEx

HS_XRCC4.

Genevestigator

Q13426.

GermOnline

ENSG00000152422. Homo sapiens.

Family and domain databases

Gene3D

1.20.5.370. 1 hit.
2.170.210.10. 1 hit.

InterPro

IPR010585. DNA_repair_prot_XRCC4.
IPR014751. XRCC4_C.
IPR009089. XRCC4_N.
[Graphical view]

Pfam

PF06632. XRCC4. 1 hit.
[Graphical view]

SUPFAM

SSF50809. XRCC4_N. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q13426.

GenomeRNAi

7518.

NextBio

29423.

PMAP-CutDB

Q13426.

SOURCE

Search...

Entry information

Entry name

XRCC4_HUMAN

Accession

Primary (citable) accession number: Q13426
Secondary accession number(s): A8K3X4, Q9BS72, Q9UP94

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	March 1, 2004
Last modified:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.