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Q13426

- XRCC4_HUMAN

UniProt

Q13426 - XRCC4_HUMAN

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Protein

DNA repair protein XRCC4

Gene

XRCC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. protein C-terminus binding Source: UniProtKB

GO - Biological processi

  1. cellular response to lithium ion Source: Ensembl
  2. central nervous system development Source: Ensembl
  3. DNA ligation involved in DNA repair Source: UniProtKB
  4. DNA repair Source: Reactome
  5. double-strand break repair Source: UniProtKB
  6. double-strand break repair via nonhomologous end joining Source: UniProtKB
  7. establishment of integrated proviral latency Source: Reactome
  8. immunoglobulin V(D)J recombination Source: Ensembl
  9. in utero embryonic development Source: Ensembl
  10. isotype switching Source: Ensembl
  11. negative regulation of neuron apoptotic process Source: Ensembl
  12. positive regulation of fibroblast proliferation Source: Ensembl
  13. positive regulation of ligase activity Source: UniProtKB
  14. positive regulation of neurogenesis Source: Ensembl
  15. pro-B cell differentiation Source: Ensembl
  16. response to gamma radiation Source: Ensembl
  17. response to X-ray Source: UniProtKB
  18. T cell differentiation in thymus Source: Ensembl
  19. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Enzyme and pathway databases

ReactomeiREACT_1022. Nonhomologous End-joining (NHEJ).
REACT_9058. 2-LTR circle formation.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein XRCC4
Alternative name(s):
X-ray repair cross-complementing protein 4
Gene namesi
Name:XRCC4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:12831. XRCC4.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. cell junction Source: HPA
  2. centrosome Source: HPA
  3. cytosol Source: UniProtKB
  4. DNA-dependent protein kinase-DNA ligase 4 complex Source: MGI
  5. DNA ligase IV complex Source: UniProtKB
  6. nonhomologous end joining complex Source: UniProtKB
  7. nucleoplasm Source: Reactome
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi140 – 1401K → R: No change in sumoylation. 1 Publication
Mutagenesisi210 – 2101K → R: Abolishes sumoylation. No nuclear location. 5-fold decrease in recombination efficiency. 1 Publication

Organism-specific databases

PharmGKBiPA37423.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336DNA repair protein XRCC4PRO_0000066047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki210 – 210Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei256 – 2561Phosphoserine1 Publication
Modified residuei260 – 2601Phosphoserine; by PRKDC1 Publication
Modified residuei320 – 3201Phosphoserine; by PRKDC1 Publication
Modified residuei327 – 3271Phosphoserine2 Publications
Modified residuei328 – 3281Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated by PRKDC. The phosphorylation seems not to be necessary for binding to DNA. Phosphorylation by CK2 promotes interaction with APTX.9 Publications
Monoubiquitinated.
Sumoylation at Lys-210 is required for nuclear localization and recombination efficiency. Has no effect on ubiquitination.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13426.
PaxDbiQ13426.
PRIDEiQ13426.

PTM databases

PhosphoSiteiQ13426.

Miscellaneous databases

PMAP-CutDBQ13426.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ13426.
CleanExiHS_XRCC4.
GenevestigatoriQ13426.

Organism-specific databases

HPAiHPA006801.
HPA051538.

Interactioni

Subunit structurei

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.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APLFQ8IW194EBI-717592,EBI-1256044
APTXQ7Z2E33EBI-717592,EBI-847814
BIN1O004994EBI-717592,EBI-719094
NHEJ1Q9H9Q48EBI-717592,EBI-847807
PNKPQ96T603EBI-717592,EBI-1045072

Protein-protein interaction databases

BioGridi113352. 34 interactions.
DIPiDIP-37957N.
IntActiQ13426. 12 interactions.
MINTiMINT-1205583.
STRINGi9606.ENSP00000342011.

Structurei

Secondary structure

1
336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109
Beta strandi13 – 2614
Helixi28 – 303
Beta strandi31 – 377
Beta strandi42 – 487
Helixi49 – 5810
Helixi63 – 7412
Beta strandi84 – 885
Turni90 – 923
Beta strandi94 – 1007
Beta strandi105 – 1128
Helixi119 – 13315
Turni173 – 1764

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00152.
ProteinModelPortaliQ13426.
SMRiQ13426. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13426.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni180 – 21334Interacts with LIG4Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili131 – 16535Sequence AnalysisAdd
BLAST
Coiled coili184 – 21229Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the XRCC4 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG69713.
GeneTreeiENSGT00390000017079.
HOGENOMiHOG000013067.
HOVERGENiHBG059517.
InParanoidiQ13426.
KOiK10886.
OMAiNFSKESC.
OrthoDBiEOG7288TZ.
PhylomeDBiQ13426.
TreeFamiTF101204.

Family and domain databases

Gene3Di1.20.5.370. 1 hit.
2.170.210.10. 1 hit.
InterProiIPR010585. DNA_repair_prot_XRCC4.
IPR014751. XRCC4_C.
IPR009089. XRCC4_N.
[Graphical view]
PfamiPF06632. XRCC4. 1 hit.
[Graphical view]
SUPFAMiSSF50809. SSF50809. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13426-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MERKISRIHL VSEPSITHFL QVSWEKTLES GFVITLTDGH SAWTGTVSES
60 70 80 90 100
EISQEADDMA MEKGKYVGEL RKALLSGAGP ADVYTFNFSK ESCYFFFEKN
110 120 130 140 150
LKDVSFRLGS FNLEKVENPA EVIRELICYC LDTIAENQAK NEHLQKENER
160 170 180 190 200
LLRDWNDVQG RFEKCVSAKE ALETDLYKRF ILVLNEKKTK IRSLHNKLLN
210 220 230 240 250
AAQEREKDIK QEGETAICSE MTADRDPVYD ESTDEESENQ TDLSGLASAA
260 270 280 290 300
VSKDDSIISS LDVTDIAPSR KRRQRMQRNL GTEPKMAPQE NQLQEKENSR
310 320 330
PDSSLPETSK KEHISAENMS LETLRNSSPE DLFDEI
Length:336
Mass (Da):38,287
Last modified:March 1, 2004 - v2
Checksum:iBE5FB99153479A4E
GO
Isoform 2 (identifier: Q13426-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:334
Mass (Da):38,058
Checksum:iE32CC403854DCE9B
GO
Isoform 3 (identifier: Q13426-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:310
Mass (Da):35,372
Checksum:i30B8DCC13C64A548
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121S → C.1 Publication
Corresponds to variant rs28383138 [ dbSNP | Ensembl ].
VAR_022310
Natural varianti56 – 561A → T.1 Publication
Corresponds to variant rs28383151 [ dbSNP | Ensembl ].
VAR_022311
Natural varianti134 – 1341I → T.1 Publication
Corresponds to variant rs28360135 [ dbSNP | Ensembl ].
VAR_022312
Natural varianti142 – 1421E → Q.1 Publication
Corresponds to variant rs28360136 [ dbSNP | Ensembl ].
VAR_022313
Natural varianti240 – 2401Q → P.
Corresponds to variant rs2974446 [ dbSNP | Ensembl ].
VAR_017810
Natural varianti247 – 2471A → S.1 Publication
Corresponds to variant rs3734091 [ dbSNP | Ensembl ].
VAR_017811

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei298 – 33639NSRPD…LFDEI → KGRKKETSEKEAV in isoform 3. 2 PublicationsVSP_009474Add
BLAST
Alternative sequencei298 – 3003NSR → K in isoform 2. 1 PublicationVSP_009473

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4058.1. [Q13426-2]
CCDS4059.1. [Q13426-1]
RefSeqiNP_003392.1. NM_003401.3. [Q13426-2]
NP_071801.1. NM_022406.2. [Q13426-1]
NP_072044.1. NM_022550.2. [Q13426-2]
XP_005248652.1. XM_005248595.1. [Q13426-1]
UniGeneiHs.567359.

Genome annotation databases

EnsembliENST00000282268; ENSP00000282268; ENSG00000152422. [Q13426-2]
ENST00000338635; ENSP00000342011; ENSG00000152422. [Q13426-1]
ENST00000396027; ENSP00000379344; ENSG00000152422. [Q13426-2]
ENST00000511817; ENSP00000421491; ENSG00000152422. [Q13426-1]
GeneIDi7518.
KEGGihsa:7518.
UCSCiuc003kia.1. human. [Q13426-3]
uc003kib.3. human. [Q13426-1]
uc003kic.3. human. [Q13426-2]

Polymorphism databases

DMDMi44888352.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4058.1. [Q13426-2 ]
CCDS4059.1. [Q13426-1 ]
RefSeqi NP_003392.1. NM_003401.3. [Q13426-2 ]
NP_071801.1. NM_022406.2. [Q13426-1 ]
NP_072044.1. NM_022550.2. [Q13426-2 ]
XP_005248652.1. XM_005248595.1. [Q13426-1 ]
UniGenei Hs.567359.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
DisProti DP00152.
ProteinModelPortali Q13426.
SMRi Q13426. Positions 1-201.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113352. 34 interactions.
DIPi DIP-37957N.
IntActi Q13426. 12 interactions.
MINTi MINT-1205583.
STRINGi 9606.ENSP00000342011.

PTM databases

PhosphoSitei Q13426.

Polymorphism databases

DMDMi 44888352.

Proteomic databases

MaxQBi Q13426.
PaxDbi Q13426.
PRIDEi Q13426.

Protocols and materials databases

DNASUi 7518.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282268 ; ENSP00000282268 ; ENSG00000152422 . [Q13426-2 ]
ENST00000338635 ; ENSP00000342011 ; ENSG00000152422 . [Q13426-1 ]
ENST00000396027 ; ENSP00000379344 ; ENSG00000152422 . [Q13426-2 ]
ENST00000511817 ; ENSP00000421491 ; ENSG00000152422 . [Q13426-1 ]
GeneIDi 7518.
KEGGi hsa:7518.
UCSCi uc003kia.1. human. [Q13426-3 ]
uc003kib.3. human. [Q13426-1 ]
uc003kic.3. human. [Q13426-2 ]

Organism-specific databases

CTDi 7518.
GeneCardsi GC05P082409.
HGNCi HGNC:12831. XRCC4.
HPAi HPA006801.
HPA051538.
MIMi 194363. gene.
neXtProti NX_Q13426.
PharmGKBi PA37423.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG69713.
GeneTreei ENSGT00390000017079.
HOGENOMi HOG000013067.
HOVERGENi HBG059517.
InParanoidi Q13426.
KOi K10886.
OMAi NFSKESC.
OrthoDBi EOG7288TZ.
PhylomeDBi Q13426.
TreeFami TF101204.

Enzyme and pathway databases

Reactomei REACT_1022. Nonhomologous End-joining (NHEJ).
REACT_9058. 2-LTR circle formation.

Miscellaneous databases

EvolutionaryTracei Q13426.
GeneWikii XRCC4.
GenomeRNAii 7518.
NextBioi 29423.
PMAP-CutDB Q13426.
PROi Q13426.
SOURCEi Search...

Gene expression databases

Bgeei Q13426.
CleanExi HS_XRCC4.
Genevestigatori Q13426.

Family and domain databases

Gene3Di 1.20.5.370. 1 hit.
2.170.210.10. 1 hit.
InterProi IPR010585. DNA_repair_prot_XRCC4.
IPR014751. XRCC4_C.
IPR009089. XRCC4_N.
[Graphical view ]
Pfami PF06632. XRCC4. 1 hit.
[Graphical view ]
SUPFAMi SSF50809. SSF50809. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiXRCC4_HUMAN
AccessioniPrimary (citable) accession number: Q13426
Secondary accession number(s): A8K3X4, Q9BS72, Q9UP94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: October 29, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3