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P23025

- XPA_HUMAN

UniProt

P23025 - XPA_HUMAN

Protein

DNA repair protein complementing XP-A cells

Gene

XPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Involved in DNA excision repair. Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri105 – 12925Add
    BLAST

    GO - Molecular functioni

    1. damaged DNA binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein domain specific binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: Reactome
    2. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    3. multicellular organism growth Source: Ensembl
    4. nucleotide-excision repair Source: Reactome
    5. nucleotide-excision repair, DNA damage removal Source: Reactome
    6. response to oxidative stress Source: Ensembl
    7. response to toxic substance Source: Ensembl
    8. response to UV Source: Ensembl

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein complementing XP-A cells
    Alternative name(s):
    Xeroderma pigmentosum group A-complementing protein
    Gene namesi
    Name:XPA
    Synonyms:XPAC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12814. XPA.

    Subcellular locationi

    Nucleus 3 Publications

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. Golgi apparatus Source: HPA
    3. intercellular bridge Source: HPA
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Xeroderma pigmentosum complementation group A (XP-A) [MIM:278700]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities. XP-A patients show the most severe skin symptoms and progressive neurological disorders.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941P → L in XP-A.
    VAR_007727
    Natural varianti108 – 1081C → F in XP-A; severe form. 2 Publications
    VAR_007728
    Natural varianti130 – 1301R → K in XP-A.
    VAR_007729
    Natural varianti185 – 1851Q → H in XP-A.
    VAR_007730
    Natural varianti244 – 2441H → R in XP-A; mild form. 1 Publication
    VAR_007731

    Keywords - Diseasei

    Disease mutation, Xeroderma pigmentosum

    Organism-specific databases

    MIMi278700. phenotype.
    Orphaneti276249. Xeroderma pigmentosum complementation group A.
    PharmGKBiPA368.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 273272DNA repair protein complementing XP-A cellsPRO_0000208648Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei196 – 1961Phosphoserine1 Publication

    Post-translational modificationi

    ATR-dependent phosphorylation of XPA at Ser-196 is important for cell survival in response to UV damage.1 Publication
    Ubiquitinated by HERC2 leading to degradation by the proteasome.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP23025.
    PaxDbiP23025.
    PRIDEiP23025.

    PTM databases

    PhosphoSiteiP23025.

    Expressioni

    Tissue specificityi

    Expressed in various cell lines and in skin fibroblasts.2 Publications

    Gene expression databases

    ArrayExpressiP23025.
    BgeeiP23025.
    CleanExiHS_XPA.
    GenevestigatoriP23025.

    Organism-specific databases

    HPAiCAB000155.
    HPA030997.
    HPA056856.

    Interactioni

    Subunit structurei

    Interacts with GPN1. Interacts with RPA1 and RPA2; the interaction is direct and associates XPA with the RPA complex. Interacts (via N-terminus) with CEP164 upon UV irradiation. Interacts with HERC2.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RPA2P159274EBI-295222,EBI-621404
    SIRT1Q96EB68EBI-295222,EBI-1802965
    XAB2Q9HCS72EBI-295222,EBI-295232

    Protein-protein interaction databases

    BioGridi113344. 23 interactions.
    DIPiDIP-24191N.
    IntActiP23025. 8 interactions.
    MINTiMINT-192332.
    STRINGi9606.ENSP00000364270.

    Structurei

    Secondary structure

    1
    273
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi72 – 754
    Turni106 – 1083
    Beta strandi111 – 1133
    Beta strandi115 – 1173
    Turni118 – 1214
    Turni127 – 1293
    Beta strandi131 – 1355
    Helixi141 – 1444
    Turni145 – 1495
    Beta strandi152 – 1543
    Turni155 – 1573
    Beta strandi158 – 1603
    Beta strandi164 – 1685
    Beta strandi170 – 1723
    Beta strandi179 – 1813
    Helixi183 – 19311
    Helixi197 – 20610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D4UNMR-A98-208[»]
    1XPANMR-A98-219[»]
    2JNWNMR-B67-80[»]
    DisProtiDP00243.
    ProteinModelPortaliP23025.
    SMRiP23025. Positions 98-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23025.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4 – 9794Interaction with CEP164 and required for UV resistanceAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi26 – 4722Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi78 – 847Poly-Glu

    Sequence similaritiesi

    Belongs to the XPA family.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri105 – 12925Add
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5145.
    HOGENOMiHOG000045820.
    HOVERGENiHBG009053.
    InParanoidiP23025.
    KOiK10847.
    OMAiVAHQHEY.
    PhylomeDBiP23025.
    TreeFamiTF101241.

    Family and domain databases

    Gene3Di3.90.530.10. 1 hit.
    InterProiIPR009061. DNA-bd_dom_put.
    IPR000465. XPA.
    IPR022656. XPA_C.
    IPR022658. XPA_CS.
    IPR022652. Znf_XPA_CS.
    [Graphical view]
    PANTHERiPTHR10142. PTHR10142. 1 hit.
    PfamiPF05181. XPA_C. 1 hit.
    PF01286. XPA_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF46955. SSF46955. 1 hit.
    TIGRFAMsiTIGR00598. rad14. 1 hit.
    PROSITEiPS00752. XPA_1. 1 hit.
    PS00753. XPA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23025-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAADGALPE AAALEQPAEL PASVRASIER KRQRALMLRQ ARLAARPYSA    50
    TAAAATGGMA NVKAAPKIID TGGGFILEEE EEEEQKIGKV VHQPGPVMEF 100
    DYVICEECGK EFMDSYLMNH FDLPTCDNCR DADDKHKLIT KTEAKQEYLL 150
    KDCDLEKREP PLKFIVKKNP HHSQWGDMKL YLKLQIVKRS LEVWGSQEAL 200
    EEAKEVRQEN REKMKQKKFD KKVKELRRAV RSSVWKRETI VHQHEYGPEE 250
    NLEDDMYRKT CTMCGHELTY EKM 273
    Length:273
    Mass (Da):31,368
    Last modified:November 1, 1991 - v1
    Checksum:iF89F735219A8494B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti78 – 781Missing.1 Publication
    VAR_014203
    Natural varianti94 – 941P → L in XP-A.
    VAR_007727
    Natural varianti97 – 971V → I.
    Corresponds to variant rs10983315 [ dbSNP | Ensembl ].
    VAR_037907
    Natural varianti108 – 1081C → F in XP-A; severe form. 2 Publications
    VAR_007728
    Natural varianti130 – 1301R → K in XP-A.
    VAR_007729
    Natural varianti185 – 1851Q → H in XP-A.
    VAR_007730
    Natural varianti228 – 2281R → Q.
    Corresponds to variant rs1805160 [ dbSNP | Ensembl ].
    VAR_014799
    Natural varianti234 – 2341V → L.
    Corresponds to variant rs3176749 [ dbSNP | Ensembl ].
    VAR_029325
    Natural varianti244 – 2441H → R in XP-A; mild form. 1 Publication
    VAR_007731
    Natural varianti252 – 2521L → V.
    Corresponds to variant rs3176750 [ dbSNP | Ensembl ].
    VAR_020324
    Natural varianti256 – 2561M → V.
    Corresponds to variant rs57519506 [ dbSNP | Ensembl ].
    VAR_061987

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14533 mRNA. Translation: BAA03403.1.
    BT019518 mRNA. Translation: AAV38325.1.
    AF503166 Genomic DNA. Translation: AAM18969.1.
    AL445531 Genomic DNA. Translation: CAI15428.1.
    CH471105 Genomic DNA. Translation: EAW58855.1.
    BC014965 mRNA. Translation: AAH14965.1.
    U16815 Genomic DNA. Translation: AAB60404.1.
    U10347
    , U10343, U10344, U10345, U10346 Genomic DNA. Translation: AAA92883.1.
    CCDSiCCDS6729.1.
    PIRiI38886.
    JG0190.
    RefSeqiNP_000371.1. NM_000380.3.
    UniGeneiHs.654364.

    Genome annotation databases

    EnsembliENST00000375128; ENSP00000364270; ENSG00000136936.
    GeneIDi7507.
    KEGGihsa:7507.
    UCSCiuc004axr.4. human.

    Polymorphism databases

    DMDMi139816.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Allelic variations of the XP genes
    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs
    Protein Spotlight

    Nature's flaws - Issue 142 of September 2012

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14533 mRNA. Translation: BAA03403.1 .
    BT019518 mRNA. Translation: AAV38325.1 .
    AF503166 Genomic DNA. Translation: AAM18969.1 .
    AL445531 Genomic DNA. Translation: CAI15428.1 .
    CH471105 Genomic DNA. Translation: EAW58855.1 .
    BC014965 mRNA. Translation: AAH14965.1 .
    U16815 Genomic DNA. Translation: AAB60404.1 .
    U10347
    , U10343 , U10344 , U10345 , U10346 Genomic DNA. Translation: AAA92883.1 .
    CCDSi CCDS6729.1.
    PIRi I38886.
    JG0190.
    RefSeqi NP_000371.1. NM_000380.3.
    UniGenei Hs.654364.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D4U NMR - A 98-208 [» ]
    1XPA NMR - A 98-219 [» ]
    2JNW NMR - B 67-80 [» ]
    DisProti DP00243.
    ProteinModelPortali P23025.
    SMRi P23025. Positions 98-210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113344. 23 interactions.
    DIPi DIP-24191N.
    IntActi P23025. 8 interactions.
    MINTi MINT-192332.
    STRINGi 9606.ENSP00000364270.

    PTM databases

    PhosphoSitei P23025.

    Polymorphism databases

    DMDMi 139816.

    Proteomic databases

    MaxQBi P23025.
    PaxDbi P23025.
    PRIDEi P23025.

    Protocols and materials databases

    DNASUi 7507.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375128 ; ENSP00000364270 ; ENSG00000136936 .
    GeneIDi 7507.
    KEGGi hsa:7507.
    UCSCi uc004axr.4. human.

    Organism-specific databases

    CTDi 7507.
    GeneCardsi GC09M100437.
    GeneReviewsi XPA.
    HGNCi HGNC:12814. XPA.
    HPAi CAB000155.
    HPA030997.
    HPA056856.
    MIMi 278700. phenotype.
    611153. gene.
    neXtProti NX_P23025.
    Orphaneti 276249. Xeroderma pigmentosum complementation group A.
    PharmGKBi PA368.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5145.
    HOGENOMi HOG000045820.
    HOVERGENi HBG009053.
    InParanoidi P23025.
    KOi K10847.
    OMAi VAHQHEY.
    PhylomeDBi P23025.
    TreeFami TF101241.

    Enzyme and pathway databases

    Reactomei REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.

    Miscellaneous databases

    EvolutionaryTracei P23025.
    GeneWikii XPA.
    GenomeRNAii 7507.
    NextBioi 29387.
    PROi P23025.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23025.
    Bgeei P23025.
    CleanExi HS_XPA.
    Genevestigatori P23025.

    Family and domain databases

    Gene3Di 3.90.530.10. 1 hit.
    InterProi IPR009061. DNA-bd_dom_put.
    IPR000465. XPA.
    IPR022656. XPA_C.
    IPR022658. XPA_CS.
    IPR022652. Znf_XPA_CS.
    [Graphical view ]
    PANTHERi PTHR10142. PTHR10142. 1 hit.
    Pfami PF05181. XPA_C. 1 hit.
    PF01286. XPA_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46955. SSF46955. 1 hit.
    TIGRFAMsi TIGR00598. rad14. 1 hit.
    PROSITEi PS00752. XPA_1. 1 hit.
    PS00753. XPA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of a human DNA excision repair gene involved in group A Xeroderma pigmentosum and containing a zinc-finger domain."
      Tanaka K., Miura N., Satokata I., Miyamoto I., Yoshida M.C., Satoh Y., Kondo S., Yasui A., Okayama H., Okada Y.
      Nature 348:73-76(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fibroblast.
    2. "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].
    3. NIEHS SNPs program
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-78 DEL.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: B-cell.
    7. "Genomic characterization of the human DNA excision repair-controlling gene XPAC."
      Satokata I., Iwai K., Matsuda T., Okada Y., Tanaka K.
      Gene 136:345-348(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-57.
      Tissue: Spermatocyte.
    8. "RPA involvement in the damage-recognition and incision steps of nucleotide excision repair."
      He Z., Henricksen L.A., Wold M.S., Ingles C.J.
      Nature 374:566-569(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPA1 AND RPA2.
    9. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-273, TISSUE SPECIFICITY.
      Tissue: Placenta.
    10. "Identification and characterization of xpac protein, the gene product of the human XPAC (Xeroderma pigmentosum group A complementing) gene."
      Miura N., Miyamoto I., Asahina H., Satokata I., Tanaka K., Okada Y.
      J. Biol. Chem. 266:19786-19789(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "Mutational analysis of the structure and function of the Xeroderma pigmentosum group A complementing protein. Identification of essential domains for nuclear localization and DNA excision repair."
      Miyamoto I., Miura N., Niwa H., Miyazaki J., Tanaka K.
      J. Biol. Chem. 267:12182-12187(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    12. "Molecular analysis of Xeroderma pigmentosum group A gene."
      Tanaka K.
      Jpn. J. Hum. Genet. 38:1-14(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS XP-A.
    13. "A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy."
      Cleaver J.E., Thompson L.H., Richardson A.S., States J.C.
      Hum. Mutat. 14:9-22(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS XP-A.
    14. "Phosphorylation of nucleotide excision repair factor xeroderma pigmentosum group A by ataxia telangiectasia mutated and Rad3-related-dependent checkpoint pathway promotes cell survival in response to UV irradiation."
      Wu X., Shell S.M., Yang Z., Zou Y.
      Cancer Res. 66:2997-3005(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-196.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "UV-dependent interaction between Cep164 and XPA mediates localization of Cep164 at sites of DNA damage and UV sensitivity."
      Pan Y.R., Lee E.Y.
      Cell Cycle 8:655-664(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CEP164, SUBCELLULAR LOCATION.
    17. "Circadian control of XPA and excision repair of cisplatin-DNA damage by cryptochrome and HERC2 ubiquitin ligase."
      Kang T.H., Lindsey-Boltz L.A., Reardon J.T., Sancar A.
      Proc. Natl. Acad. Sci. U.S.A. 107:4890-4895(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH HERC2.
      Tissue: Embryonic kidney and Lung adenocarcinoma.
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA."
      Ikegami T., Kuraoka I., Saijo M., Kodo N., Kyogoku Y., Morikawa K., Tanaka K., Shirakawa M.
      Nat. Struct. Biol. 5:701-706(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 98-219, DNA-BINDING, INTERACTION WITH RPA1.
    20. "Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies."
      Buchko G.W., Daughdrill G.W., de Lorimier R., Sudha Rao B.K., Isern N.G., Lingbeck J.M., Taylor J.-S., Wold M.S., Gochin M., Spicer L.D., Lowry D.F., Kennedy M.A.
      Biochemistry 38:15116-15128(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 98-208, DNA-BINDING, INTERACTION WITH RPA1.
    21. "Molecular basis of group A Xeroderma pigmentosum: a missense mutation and two deletions located in a zinc finger consensus sequence of the XPAC gene."
      Satokata I., Tanaka K., Okada Y.
      Hum. Genet. 88:603-607(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XP-A PHE-108.
    22. "Identification of splicing mutations of the last nucleotides of exons, a nonsense mutation, and a missense mutation of the XPAC gene as causes of group A Xeroderma pigmentosum."
      Satokata I., Tanaka K., Yuba S., Okada Y.
      Mutat. Res. 273:203-212(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XP-A ARG-244.
    23. "Distribution of mutations in the human Xeroderma pigmentosum group A gene and their relationships to the functional regions of the DNA damage recognition protein."
      States J.C., McDuffie E.R., Myrand S.P., McDowell M., Cleaver J.E.
      Hum. Mutat. 12:103-113(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XP-A PHE-108.

    Entry informationi

    Entry nameiXPA_HUMAN
    AccessioniPrimary (citable) accession number: P23025
    Secondary accession number(s): Q5T1U9, Q6LCW7, Q6LD02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 160 of the entry and version 1 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 9
      Human chromosome 9: 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3