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Q13426

- XRCC4_HUMAN

UniProt

Q13426 - XRCC4_HUMAN

Protein

DNA repair protein XRCC4

Gene

XRCC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      Previous versions | rss
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    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 binding Source: UniProtKB
    2. 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

    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

    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. 28 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.
    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

    MERKISRIHL VSEPSITHFL QVSWEKTLES GFVITLTDGH SAWTGTVSES    50
    EISQEADDMA MEKGKYVGEL RKALLSGAGP ADVYTFNFSK ESCYFFFEKN 100
    LKDVSFRLGS FNLEKVENPA EVIRELICYC LDTIAENQAK NEHLQKENER 150
    LLRDWNDVQG RFEKCVSAKE ALETDLYKRF ILVLNEKKTK IRSLHNKLLN 200
    AAQEREKDIK QEGETAICSE MTADRDPVYD ESTDEESENQ TDLSGLASAA 250
    VSKDDSIISS LDVTDIAPSR KRRQRMQRNL GTEPKMAPQE NQLQEKENSR 300
    PDSSLPETSK KEHISAENMS LETLRNSSPE DLFDEI 336
    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. 28 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.
    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

    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 1, 2014
    This is version 136 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