Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27641

- XRCC5_MOUSE

UniProt

P27641 - XRCC5_MOUSE

Protein

X-ray repair cross-complementing protein 5

Gene

Xrcc5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 4 (05 Feb 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. expression. The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription By similarity.By similarity

    GO - Molecular functioni

    1. 5'-deoxyribose-5-phosphate lyase activity Source: Ensembl
    2. ATP binding Source: UniProtKB-KW
    3. ATP-dependent DNA helicase activity Source: InterPro
    4. damaged DNA binding Source: InterPro
    5. double-stranded telomeric DNA binding Source: Ensembl
    6. transcription regulatory region DNA binding Source: Ensembl

    GO - Biological processi

    1. brain development Source: Ensembl
    2. cell proliferation Source: MGI
    3. cellular hyperosmotic salinity response Source: Ensembl
    4. cellular response to fatty acid Source: Ensembl
    5. cellular response to X-ray Source: Ensembl
    6. DNA recombination Source: UniProtKB-KW
    7. double-strand break repair Source: MGI
    8. double-strand break repair via nonhomologous end joining Source: UniProtKB
    9. hematopoietic stem cell differentiation Source: MGI
    10. negative regulation of transcription, DNA-templated Source: UniProtKB
    11. positive regulation of neurogenesis Source: MGI
    12. response to drug Source: Ensembl
    13. telomere maintenance Source: InterPro
    14. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196447. IRF3-mediated induction of type I IFN.
    REACT_224809. Processing of DNA ends prior to end rejoining.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    X-ray repair cross-complementing protein 5 (EC:3.6.4.-)
    Alternative name(s):
    ATP-dependent DNA helicase 2 subunit 2
    ATP-dependent DNA helicase II 80 kDa subunit
    CTC box-binding factor 85 kDa subunit
    Short name:
    CTC85
    Short name:
    CTCBF
    DNA repair protein XRCC5
    Ku autoantigen protein p86 homolog
    Ku80
    Nuclear factor IV
    Gene namesi
    Name:Xrcc5
    Synonyms:G22p2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:104517. Xrcc5.

    Subcellular locationi

    Nucleus. Nucleusnucleolus By similarity. Chromosome

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. Ku70:Ku80 complex Source: UniProtKB
    3. nonhomologous end joining complex Source: UniProtKB
    4. nuclear chromosome, telomeric region Source: Ensembl
    5. nucleolus Source: UniProtKB-SubCell
    6. nucleus Source: MGI

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 732731X-ray repair cross-complementing protein 5PRO_0000084341Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei265 – 2651N6-acetyllysineBy similarity
    Modified residuei332 – 3321N6-acetyllysineBy similarity
    Modified residuei578 – 5781Phosphoserine; by PRKDCBy similarity
    Modified residuei580 – 5801Phosphoserine; by PRKDCBy similarity
    Modified residuei581 – 5811Phosphoserine; by PRKDCBy similarity
    Modified residuei666 – 6661N6-acetyllysineBy similarity
    Modified residuei716 – 7161Phosphothreonine; by PRKDCBy similarity

    Post-translational modificationi

    Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity By similarity.By similarity
    Sumoylated.By similarity
    Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA damage, leading to its degradation and removal from DNA damage sites.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP27641.
    PaxDbiP27641.
    PRIDEiP27641.

    PTM databases

    PhosphoSiteiP27641.

    Expressioni

    Developmental stagei

    Expression increases during promyelocyte differentiation.1 Publication

    Inductioni

    Up-regulation during myogenesis is inhibited by cAMP, 3-aminobenzamide and sodium butyrate. Expression in myoblasts is unaffected by X-rays and UV light.1 Publication

    Gene expression databases

    ArrayExpressiP27641.
    BgeeiP27641.
    GenevestigatoriP27641.

    Interactioni

    Subunit structurei

    Heterodimer of a 70 kDa and a 80 kDa subunit. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex. The dimer also associates with NAA15, and this complex displays DNA binding activity towards the osteocalcin FGF response element (OCFRE). In addition, the 80 kDa subunit binds to the osteoblast-specific transcription factors MSX2 and RUNX2. Interacts with ELF3. May interact with APLF. The XRCC5/6 dimer associates in a DNA-dependent manner with APEX1 By similarity. Identified in a complex with DEAF1 and XRCC6 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204608. 6 interactions.
    IntActiP27641. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP27641.
    SMRiP27641. Positions 6-545, 591-710.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini251 – 460210KuAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni138 – 16528Leucine-zipperAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi720 – 7289EEXXXDL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi478 – 52043Pro-richAdd
    BLAST

    Domaini

    The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage.By similarity

    Sequence similaritiesi

    Belongs to the ku80 family.Curated
    Contains 1 Ku domain.Curated

    Phylogenomic databases

    eggNOGiNOG299744.
    GeneTreeiENSGT00390000015674.
    HOVERGENiHBG006237.
    InParanoidiP27641.
    KOiK10885.
    OMAiGYMLGGT.
    OrthoDBiEOG7DVD9X.
    PhylomeDBiP27641.
    TreeFamiTF101205.

    Family and domain databases

    Gene3Di1.10.1600.10. 1 hit.
    1.25.40.240. 1 hit.
    2.40.290.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProiIPR006164. Ku70/Ku80_beta-barrel_dom.
    IPR024193. Ku80.
    IPR005160. Ku_C.
    IPR005161. Ku_N.
    IPR014893. Ku_PK_bind.
    IPR016194. SPOC_like_C_dom.
    IPR002035. VWF_A.
    [Graphical view]
    PANTHERiPTHR12604:SF3. PTHR12604:SF3. 1 hit.
    PfamiPF02735. Ku. 1 hit.
    PF03730. Ku_C. 1 hit.
    PF03731. Ku_N. 1 hit.
    PF08785. Ku_PK_bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016570. Ku80. 1 hit.
    SMARTiSM00559. Ku78. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF100939. SSF100939. 1 hit.
    SSF101420. SSF101420. 1 hit.
    SSF53300. SSF53300. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P27641-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAWSGNKAAV VLCVDVGVAM GNSFPGEESP IEQAKKVMTM FVQRQVFSES    50
    KDEIALVLYG TDGTDNALAG KDQYQNITVC RHLMLPDFDL LEDIGNKIQP 100
    SSQQADFLDA LIVCMDLIQR ETIGKKFGKK HIEVFTDLSS PFSQDQLDVI 150
    ICNLKKSGIS LQFFLPFPID KNGEPGERGD LDSGLDHLKP SFPQKGLTEQ 200
    QKEGIRMVTR VMLSLEGEDG LDEIYSFSES LRQLCVFKKI ERRSMPWPCQ 250
    LTIGPNLSIK IVAYKSIVQE KFKKSWVVVD ARTLKKEDIQ KETVYCLNDD 300
    DETEVSKEDT IQGYRYGSDI IPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ 350
    VHRRFFMGHQ VLKVFAAKDD EAAAVALSSL VHALDELNMV AIVRYAYDKR 400
    SNPQVGVAFP YIKDAYECLV YVQLPFMEDL RQYMFSSLKN NKKCTPTEAQ 450
    LSAIDDLIDS MSLVKKNEEE DIVEDLFPTS KIPNPEFQRL YQCLLHRALH 500
    LQERLPPIQQ HILNMLDPPT EMKAKCESPL SKVKTLFPLT EVIKKKNQVT 550
    AQDVFQDNHE EGPAAKKYKT EKEEDHISIS SLAEGNITKV GSVNPVENFR 600
    FLVRQKIASF EEASLQLISH IEQFLDTNET LYFMKSMDCI KAFREEAIQF 650
    SEEQRFNSFL EALREKVEIK QLNHFWEIVV QDGVTLITKD EGPGSSITAE 700
    EATKFLAPKD KAKEDTTGPE EAGDVDDLLD MI 732
    Length:732
    Mass (Da):83,057
    Last modified:February 5, 2008 - v4
    Checksum:i391F0FAF7EB04288
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51G → V in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti24 – 241F → I in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti57 – 571V → A in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti66 – 694NALA → MPLS in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti120 – 1201R → H in AAD49720. 1 PublicationCurated
    Sequence conflicti139 – 1391S → G in BAE38207. (PubMed:16141072)Curated
    Sequence conflicti139 – 1391S → R in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti144 – 1441Q → K in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti157 – 1571S → C in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti226 – 2261S → F in AAD49720. 1 PublicationCurated
    Sequence conflicti409 – 4102FP → SL in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti414 – 4141D → G in BAC38276. (PubMed:16141072)Curated
    Sequence conflicti415 – 4151A → T in AAD49720. 1 PublicationCurated
    Sequence conflicti418 – 4181C → R in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti442 – 4421K → M in AAD49720. 1 PublicationCurated
    Sequence conflicti479 – 4791T → A in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti515 – 5162ML → IW in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti524 – 5241A → Q in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti530 – 5312LS → PL in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti558 – 5581N → H in AAD49720. 1 PublicationCurated
    Sequence conflicti692 – 6921G → A in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti703 – 7031T → K in CAA46999. (PubMed:1641347)Curated
    Sequence conflicti708 – 7081P → H in BAE39415. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66323 mRNA. Translation: CAA46999.1.
    AF166486 mRNA. Translation: AAD49720.1.
    AK081633 mRNA. Translation: BAC38276.1.
    AK165470 mRNA. Translation: BAE38207.1.
    AK167312 mRNA. Translation: BAE39415.1.
    AK168913 mRNA. Translation: BAE40726.1.
    AK169838 mRNA. Translation: BAE41402.1.
    BC029218 mRNA. Translation: AAH29218.1.
    BC051660 mRNA. Translation: AAH51660.1.
    CCDSiCCDS35608.1.
    PIRiS26303.
    RefSeqiNP_033559.2. NM_009533.2.
    UniGeneiMm.246952.

    Genome annotation databases

    EnsembliENSMUST00000027379; ENSMUSP00000027379; ENSMUSG00000026187.
    GeneIDi22596.
    KEGGimmu:22596.
    UCSCiuc007bkl.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66323 mRNA. Translation: CAA46999.1 .
    AF166486 mRNA. Translation: AAD49720.1 .
    AK081633 mRNA. Translation: BAC38276.1 .
    AK165470 mRNA. Translation: BAE38207.1 .
    AK167312 mRNA. Translation: BAE39415.1 .
    AK168913 mRNA. Translation: BAE40726.1 .
    AK169838 mRNA. Translation: BAE41402.1 .
    BC029218 mRNA. Translation: AAH29218.1 .
    BC051660 mRNA. Translation: AAH51660.1 .
    CCDSi CCDS35608.1.
    PIRi S26303.
    RefSeqi NP_033559.2. NM_009533.2.
    UniGenei Mm.246952.

    3D structure databases

    ProteinModelPortali P27641.
    SMRi P27641. Positions 6-545, 591-710.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204608. 6 interactions.
    IntActi P27641. 4 interactions.

    PTM databases

    PhosphoSitei P27641.

    Proteomic databases

    MaxQBi P27641.
    PaxDbi P27641.
    PRIDEi P27641.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027379 ; ENSMUSP00000027379 ; ENSMUSG00000026187 .
    GeneIDi 22596.
    KEGGi mmu:22596.
    UCSCi uc007bkl.2. mouse.

    Organism-specific databases

    CTDi 7520.
    MGIi MGI:104517. Xrcc5.

    Phylogenomic databases

    eggNOGi NOG299744.
    GeneTreei ENSGT00390000015674.
    HOVERGENi HBG006237.
    InParanoidi P27641.
    KOi K10885.
    OMAi GYMLGGT.
    OrthoDBi EOG7DVD9X.
    PhylomeDBi P27641.
    TreeFami TF101205.

    Enzyme and pathway databases

    Reactomei REACT_196447. IRF3-mediated induction of type I IFN.
    REACT_224809. Processing of DNA ends prior to end rejoining.

    Miscellaneous databases

    NextBioi 302945.
    PROi P27641.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27641.
    Bgeei P27641.
    Genevestigatori P27641.

    Family and domain databases

    Gene3Di 1.10.1600.10. 1 hit.
    1.25.40.240. 1 hit.
    2.40.290.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProi IPR006164. Ku70/Ku80_beta-barrel_dom.
    IPR024193. Ku80.
    IPR005160. Ku_C.
    IPR005161. Ku_N.
    IPR014893. Ku_PK_bind.
    IPR016194. SPOC_like_C_dom.
    IPR002035. VWF_A.
    [Graphical view ]
    PANTHERi PTHR12604:SF3. PTHR12604:SF3. 1 hit.
    Pfami PF02735. Ku. 1 hit.
    PF03730. Ku_C. 1 hit.
    PF03731. Ku_N. 1 hit.
    PF08785. Ku_PK_bind. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016570. Ku80. 1 hit.
    SMARTi SM00559. Ku78. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF100939. SSF100939. 1 hit.
    SSF101420. SSF101420. 1 hit.
    SSF53300. SSF53300. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of a mouse cDNA encoding the 80 kDa subunit of the Ku (p70/p80) autoantigen."
      Falzon M., Kuff E.L.
      Nucleic Acids Res. 20:3784-3784(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. "Ku gene mutation of radiosensitive mouse mammary carcinoma cell line SX-9."
      Jiang G.C., Yuan L.Z., Wei K.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary carcinoma.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Embryonic head, Embryonic heart, Embryonic liver, Kidney and Thymus.
    4. "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].
      Strain: 129/Sv X 129SvCp and FVB/N.
      Tissue: Embryonic stem cell and Mammary tumor.
    5. "Non-histone protein 1 (NHP1) is a member of the Ku protein family which is upregulated in differentiating mouse myoblasts and human promyelocytes."
      Oderwald H., Hughes M.J., Jost J.-P.
      FEBS Lett. 382:313-318(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, INDUCTION.

    Entry informationi

    Entry nameiXRCC5_MOUSE
    AccessioniPrimary (citable) accession number: P27641
    Secondary accession number(s): Q3TE46
    , Q3TJT0, Q3TN82, Q80UT1, Q8C4N6, Q8K1K7, Q9R169
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 132 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3