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Q13426 (XRCC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein XRCC4
Alternative name(s):
X-ray repair cross-complementing protein 4
Gene names
Name:XRCC4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processDNA damage
DNA recombination
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA ligation involved in DNA repair

Inferred from direct assay PubMed 12517771. Source: UniProtKB

DNA repair

Traceable author statement. Source: Reactome

T cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Inferred from electronic annotation. Source: Ensembl

double-strand break repair

Inferred from direct assay Ref.12. Source: UniProtKB

double-strand break repair via nonhomologous end joining

Inferred from direct assay PubMed 12517771. Source: UniProtKB

establishment of integrated proviral latency

Traceable author statement. Source: Reactome

immunoglobulin V(D)J recombination

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

isotype switching

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of ligase activity

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of neurogenesis

Inferred from electronic annotation. Source: Ensembl

pro-B cell differentiation

Inferred from electronic annotation. Source: Ensembl

response to X-ray

Inferred from direct assay Ref.12. Source: UniProtKB

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

viral process

Traceable author statement. Source: Reactome

   Cellular_componentDNA 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

cell junction

Inferred from direct assay. Source: HPA

centrosome

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.9. Source: UniProtKB

nonhomologous end joining complex

Inferred from direct assay PubMed 20383123. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 12589063Ref.9. Source: UniProtKB

   Molecular_functionprotein C-terminus binding

Inferred from physical interaction PubMed 9259651. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 336336DNA repair protein XRCC4
PRO_0000066047

Regions

Region180 – 21334Interacts with LIG4
Coiled coil131 – 16535 Potential
Coiled coil184 – 21229 Potential

Amino acid modifications

Modified residue2561Phosphoserine Ref.26
Modified residue2601Phosphoserine; by PRKDC Ref.11
Modified residue3201Phosphoserine; by PRKDC Ref.11
Modified residue3271Phosphoserine Ref.24 Ref.25
Modified residue3281Phosphoserine Ref.24 Ref.25
Cross-link210Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.20

Natural variations

Alternative sequence298 – 33639NSRPD…LFDEI → KGRKKETSEKEAV in isoform 3.
VSP_009474
Alternative sequence298 – 3003NSR → K in isoform 2.
VSP_009473
Natural variant121S → C. Ref.6
Corresponds to variant rs28383138 [ dbSNP | Ensembl ].
VAR_022310
Natural variant561A → T. Ref.6
Corresponds to variant rs28383151 [ dbSNP | Ensembl ].
VAR_022311
Natural variant1341I → T. Ref.6
Corresponds to variant rs28360135 [ dbSNP | Ensembl ].
VAR_022312
Natural variant1421E → Q. Ref.6
Corresponds to variant rs28360136 [ dbSNP | Ensembl ].
VAR_022313
Natural variant2401Q → P.
Corresponds to variant rs2974446 [ dbSNP | Ensembl ].
VAR_017810
Natural variant2471A → S. Ref.6
Corresponds to variant rs3734091 [ dbSNP | Ensembl ].
VAR_017811

Experimental info

Mutagenesis1401K → R: No change in sumoylation. Ref.20
Mutagenesis2101K → R: Abolishes sumoylation. No nuclear location. 5-fold decrease in recombination efficiency. Ref.20

Secondary structure

......................... 336
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: BE5FB99153479A4E

FASTA33638,287
        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 

« Hide

Isoform 2 [UniParc].

Checksum: E32CC403854DCE9B
Show »

FASTA33438,058
Isoform 3 [UniParc].

Checksum: 30B8DCC13C64A548
Show »

FASTA31035,372

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40622 mRNA. Translation: AAC50339.1.
AF055285 expand/collapse EMBL AC list , AF055279, AF055280, AF055281, AF055282, AF055283, AF055284 Genomic DNA. Translation: AAD47297.1.
AF055285 expand/collapse EMBL AC list , 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.
RefSeqNP_003392.1. NM_003401.3.
NP_071801.1. NM_022406.2.
NP_072044.1. NM_022550.2.
XP_005248652.1. XM_005248595.1.
UniGeneHs.567359.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FU1X-ray2.70A/B1-203[»]
1IK9X-ray2.30A/B1-213[»]
3II6X-ray2.40A/B/C/D1-203[»]
3MUDX-ray2.20A/B2-133[»]
3Q4FX-ray5.50C/D/G/H1-157[»]
3RWRX-ray3.94A/B/F/G/J/K/N/P/R/U/V/Y1-157[»]
3SR2X-ray3.97A/B/E/F1-140[»]
3W03X-ray8.49C/D1-164[»]
DisProtDP00152.
ProteinModelPortalQ13426.
SMRQ13426. Positions 1-201.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113352. 28 interactions.
DIPDIP-37957N.
IntActQ13426. 12 interactions.
MINTMINT-1205583.
STRING9606.ENSP00000342011.

PTM databases

PhosphoSiteQ13426.

Polymorphism databases

DMDM44888352.

Proteomic databases

PaxDbQ13426.
PRIDEQ13426.

Protocols and materials databases

DNASU7518.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282268; ENSP00000282268; ENSG00000152422. [Q13426-2]
ENST00000338635; ENSP00000342011; ENSG00000152422. [Q13426-1]
ENST00000396027; ENSP00000379344; ENSG00000152422. [Q13426-2]
ENST00000511817; ENSP00000421491; ENSG00000152422. [Q13426-1]
GeneID7518.
KEGGhsa:7518.
UCSCuc003kia.1. human. [Q13426-3]
uc003kib.3. human. [Q13426-1]
uc003kic.3. human. [Q13426-2]

Organism-specific databases

CTD7518.
GeneCardsGC05P082409.
HGNCHGNC:12831. XRCC4.
HPAHPA006801.
HPA051538.
MIM194363. gene.
neXtProtNX_Q13426.
PharmGKBPA37423.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69713.
HOGENOMHOG000013067.
HOVERGENHBG059517.
InParanoidQ13426.
KOK10886.
OMANFSKESC.
OrthoDBEOG7288TZ.
PhylomeDBQ13426.
TreeFamTF101204.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_216. DNA Repair.

Gene expression databases

BgeeQ13426.
CleanExHS_XRCC4.
GenevestigatorQ13426.

Family and domain databases

Gene3D1.20.5.370. 1 hit.
2.170.210.10. 1 hit.
InterProIPR010585. DNA_repair_prot_XRCC4.
IPR014751. XRCC4_C.
IPR009089. XRCC4_N.
[Graphical view]
PfamPF06632. XRCC4. 1 hit.
[Graphical view]
SUPFAMSSF50809. SSF50809. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ13426.
GeneWikiXRCC4.
GenomeRNAi7518.
NextBio29423.
PMAP-CutDBQ13426.
PROQ13426.
SOURCESearch...

Entry information

Entry nameXRCC4_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM