XPA_HUMAN
ID XPA_HUMAN Reviewed; 273 AA.
AC P23025; Q5T1U9; Q6LCW7; Q6LD02;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=DNA repair protein complementing XP-A cells;
DE AltName: Full=Xeroderma pigmentosum group A-complementing protein;
GN Name=XPA; Synonyms=XPAC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=2234061; DOI=10.1038/348073a0;
RA Tanaka K., Miura N., Satokata I., Miyamoto I., Yoshida M.C., Satoh Y.,
RA Kondo S., Yasui A., Okayama H., Okada Y.;
RT "Analysis of a human DNA excision repair gene involved in group A Xeroderma
RT pigmentosum and containing a zinc-finger domain.";
RL Nature 348:73-76(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-78 DEL.
RG NIEHS SNPs program;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-57.
RC TISSUE=Spermatocyte;
RX PubMed=8294029; DOI=10.1016/0378-1119(93)90493-m;
RA Satokata I., Iwai K., Matsuda T., Okada Y., Tanaka K.;
RT "Genomic characterization of the human DNA excision repair-controlling gene
RT XPAC.";
RL Gene 136:345-348(1993).
RN [8]
RP INTERACTION WITH RPA1 AND RPA2.
RX PubMed=7700386; DOI=10.1038/374566a0;
RA He Z., Henricksen L.A., Wold M.S., Ingles C.J.;
RT "RPA involvement in the damage-recognition and incision steps of nucleotide
RT excision repair.";
RL Nature 374:566-569(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-273, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=8543191; DOI=10.1016/0378-1119(95)00649-4;
RA Topping R.S., Myrand S.P., Williams B.L., Albert J.C., States J.C.;
RT "Characterization of the human XPA promoter.";
RL Gene 166:341-342(1995).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1918083; DOI=10.1016/s0021-9258(18)55060-2;
RA Miura N., Miyamoto I., Asahina H., Satokata I., Tanaka K., Okada Y.;
RT "Identification and characterization of xpac protein, the gene product of
RT the human XPAC (Xeroderma pigmentosum group A complementing) gene.";
RL J. Biol. Chem. 266:19786-19789(1991).
RN [11]
RP MUTAGENESIS.
RX PubMed=1601884; DOI=10.1016/s0021-9258(19)49821-9;
RA Miyamoto I., Miura N., Niwa H., Miyazaki J., Tanaka K.;
RT "Mutational analysis of the structure and function of the Xeroderma
RT pigmentosum group A complementing protein. Identification of essential
RT domains for nuclear localization and DNA excision repair.";
RL J. Biol. Chem. 267:12182-12187(1992).
RN [12]
RP REVIEW ON VARIANTS XP-A.
RX PubMed=8504220; DOI=10.1007/bf01891230;
RA Tanaka K.;
RT "Molecular analysis of Xeroderma pigmentosum group A gene.";
RL Jpn. J. Hum. Genet. 38:1-14(1993).
RN [13]
RP REVIEW ON VARIANTS XP-A.
RX PubMed=10447254;
RX DOI=10.1002/(sici)1098-1004(1999)14:1<9::aid-humu2>3.0.co;2-6;
RA Cleaver J.E., Thompson L.H., Richardson A.S., States J.C.;
RT "A summary of mutations in the UV-sensitive disorders: xeroderma
RT pigmentosum, Cockayne syndrome, and trichothiodystrophy.";
RL Hum. Mutat. 14:9-22(1999).
RN [14]
RP PHOSPHORYLATION AT SER-196.
RX PubMed=16540648; DOI=10.1158/0008-5472.can-05-3403;
RA Wu X., Shell S.M., Yang Z., Zou Y.;
RT "Phosphorylation of nucleotide excision repair factor xeroderma pigmentosum
RT group A by ataxia telangiectasia mutated and Rad3-related-dependent
RT checkpoint pathway promotes cell survival in response to UV irradiation.";
RL Cancer Res. 66:2997-3005(2006).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP FUNCTION, INTERACTION WITH CEP164, AND SUBCELLULAR LOCATION.
RX PubMed=19197159; DOI=10.4161/cc.8.4.7844;
RA Pan Y.R., Lee E.Y.;
RT "UV-dependent interaction between Cep164 and XPA mediates localization of
RT Cep164 at sites of DNA damage and UV sensitivity.";
RL Cell Cycle 8:655-664(2009).
RN [17]
RP UBIQUITINATION, SUBCELLULAR LOCATION, AND INTERACTION WITH HERC2.
RC TISSUE=Embryonic kidney, and Lung adenocarcinoma;
RX PubMed=20304803; DOI=10.1073/pnas.0915085107;
RA Kang T.H., Lindsey-Boltz L.A., Reardon J.T., Sancar A.;
RT "Circadian control of XPA and excision repair of cisplatin-DNA damage by
RT cryptochrome and HERC2 ubiquitin ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4890-4895(2010).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-145, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63 AND LYS-86, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [22]
RP STRUCTURE BY NMR OF 98-219, DNA-BINDING, AND INTERACTION WITH RPA1.
RX PubMed=9699634; DOI=10.1038/1400;
RA Ikegami T., Kuraoka I., Saijo M., Kodo N., Kyogoku Y., Morikawa K.,
RA Tanaka K., Shirakawa M.;
RT "Solution structure of the DNA- and RPA-binding domain of the human repair
RT factor XPA.";
RL Nat. Struct. Biol. 5:701-706(1998).
RN [23]
RP STRUCTURE BY NMR OF 98-208, DNA-BINDING, AND INTERACTION WITH RPA1.
RX PubMed=10563794; DOI=10.1021/bi991755p;
RA Buchko G.W., Daughdrill G.W., de Lorimier R., Sudha Rao B.K., Isern N.G.,
RA Lingbeck J.M., Taylor J.-S., Wold M.S., Gochin M., Spicer L.D., Lowry D.F.,
RA Kennedy M.A.;
RT "Interactions of human nucleotide excision repair protein XPA with DNA and
RT RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies.";
RL Biochemistry 38:15116-15128(1999).
RN [24]
RP VARIANT XP-A PHE-108.
RX PubMed=1339397; DOI=10.1007/bf02265282;
RA Satokata I., Tanaka K., Okada Y.;
RT "Molecular basis of group A Xeroderma pigmentosum: a missense mutation and
RT two deletions located in a zinc finger consensus sequence of the XPAC
RT gene.";
RL Hum. Genet. 88:603-607(1992).
RN [25]
RP VARIANT XP-A ARG-244.
RX PubMed=1372103; DOI=10.1016/0921-8777(92)90081-d;
RA Satokata I., Tanaka K., Yuba S., Okada Y.;
RT "Identification of splicing mutations of the last nucleotides of exons, a
RT nonsense mutation, and a missense mutation of the XPAC gene as causes of
RT group A Xeroderma pigmentosum.";
RL Mutat. Res. 273:203-212(1992).
RN [26]
RP VARIANT XP-A PHE-108.
RX PubMed=9671271;
RX DOI=10.1002/(sici)1098-1004(1998)12:2<103::aid-humu5>3.0.co;2-6;
RA States J.C., McDuffie E.R., Myrand S.P., McDowell M., Cleaver J.E.;
RT "Distribution of mutations in the human Xeroderma pigmentosum group A gene
RT and their relationships to the functional regions of the DNA damage
RT recognition protein.";
RL Hum. Mutat. 12:103-113(1998).
CC -!- FUNCTION: Involved in DNA excision repair. Initiates repair by binding
CC to damaged sites with various affinities, depending on the photoproduct
CC and the transcriptional state of the region. Required for UV-induced
CC CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane
CC pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation.
CC {ECO:0000269|PubMed:19197159}.
CC -!- SUBUNIT: Interacts with GPN1. Interacts with RPA1 and RPA2; the
CC interaction is direct and associates XPA with the RPA complex.
CC Interacts (via N-terminus) with CEP164 upon UV irradiation. Interacts
CC with HERC2. {ECO:0000269|PubMed:10563794, ECO:0000269|PubMed:19197159,
CC ECO:0000269|PubMed:20304803, ECO:0000269|PubMed:7700386,
CC ECO:0000269|PubMed:9699634}.
CC -!- INTERACTION:
CC P23025; Q99856: ARID3A; NbExp=3; IntAct=EBI-295222, EBI-5458244;
CC P23025; Q92997: DVL3; NbExp=3; IntAct=EBI-295222, EBI-739789;
CC P23025; P07992: ERCC1; NbExp=7; IntAct=EBI-295222, EBI-750962;
CC P23025; P07992-3: ERCC1; NbExp=3; IntAct=EBI-295222, EBI-12699417;
CC P23025; O95714: HERC2; NbExp=4; IntAct=EBI-295222, EBI-1058922;
CC P23025; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-295222, EBI-16439278;
CC P23025; Q9GZM8: NDEL1; NbExp=6; IntAct=EBI-295222, EBI-928842;
CC P23025; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-295222, EBI-79165;
CC P23025; O15160: POLR1C; NbExp=3; IntAct=EBI-295222, EBI-1055079;
CC P23025; P20618: PSMB1; NbExp=3; IntAct=EBI-295222, EBI-372273;
CC P23025; P15927: RPA2; NbExp=8; IntAct=EBI-295222, EBI-621404;
CC P23025; Q96EB6: SIRT1; NbExp=8; IntAct=EBI-295222, EBI-1802965;
CC P23025; P12757: SKIL; NbExp=3; IntAct=EBI-295222, EBI-2902468;
CC P23025; O15079: SNPH; NbExp=3; IntAct=EBI-295222, EBI-4401902;
CC P23025; Q9P0N9: TBC1D7; NbExp=3; IntAct=EBI-295222, EBI-3258000;
CC P23025; P14373: TRIM27; NbExp=6; IntAct=EBI-295222, EBI-719493;
CC P23025; O14972: VPS26C; NbExp=3; IntAct=EBI-295222, EBI-7207091;
CC P23025; Q9HCS7: XAB2; NbExp=2; IntAct=EBI-295222, EBI-295232;
CC P23025; Q8N720: ZNF655; NbExp=3; IntAct=EBI-295222, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1918083,
CC ECO:0000269|PubMed:19197159, ECO:0000269|PubMed:20304803}.
CC -!- TISSUE SPECIFICITY: Expressed in various cell lines and in skin
CC fibroblasts. {ECO:0000269|PubMed:1918083, ECO:0000269|PubMed:8543191}.
CC -!- PTM: ATR-dependent phosphorylation of XPA at Ser-196 is important for
CC cell survival in response to UV damage. {ECO:0000269|PubMed:16540648}.
CC -!- PTM: Ubiquitinated by HERC2 leading to degradation by the proteasome.
CC {ECO:0000269|PubMed:20304803}.
CC -!- DISEASE: Xeroderma pigmentosum complementation group A (XP-A)
CC [MIM:278700]: An autosomal recessive pigmentary skin disorder
CC characterized by solar hypersensitivity of the skin, high
CC predisposition for developing cancers on areas exposed to sunlight and,
CC in some cases, neurological abnormalities. The skin develops marked
CC freckling and other pigmentation abnormalities. XP-A patients show the
CC most severe skin symptoms and progressive neurological disorders.
CC {ECO:0000269|PubMed:10447254, ECO:0000269|PubMed:1339397,
CC ECO:0000269|PubMed:1372103, ECO:0000269|PubMed:8504220,
CC ECO:0000269|PubMed:9671271}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the XPA family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/XPAID104.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/xpa/";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Nature's flaws - Issue 142
CC of September 2012;
CC URL="https://web.expasy.org/spotlight/back_issues/142";
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DR EMBL; D14533; BAA03403.1; -; mRNA.
DR EMBL; BT019518; AAV38325.1; -; mRNA.
DR EMBL; AF503166; AAM18969.1; -; Genomic_DNA.
DR EMBL; AL445531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW58855.1; -; Genomic_DNA.
DR EMBL; BC014965; AAH14965.1; -; mRNA.
DR EMBL; U16815; AAB60404.1; -; Genomic_DNA.
DR EMBL; U10347; AAA92883.1; -; Genomic_DNA.
DR EMBL; U10343; AAA92883.1; JOINED; Genomic_DNA.
DR EMBL; U10344; AAA92883.1; JOINED; Genomic_DNA.
DR EMBL; U10345; AAA92883.1; JOINED; Genomic_DNA.
DR EMBL; U10346; AAA92883.1; JOINED; Genomic_DNA.
DR CCDS; CCDS6729.1; -.
DR PIR; I38886; I38886.
DR PIR; JG0190; JG0190.
DR RefSeq; NP_000371.1; NM_000380.3.
DR PDB; 1D4U; NMR; -; A=98-208.
DR PDB; 1XPA; NMR; -; A=98-219.
DR PDB; 2JNW; NMR; -; B=67-80.
DR PDB; 6J44; X-ray; 2.06 A; A=98-239.
DR PDB; 6LAE; X-ray; 2.81 A; A/B=98-239.
DR PDB; 6RO4; EM; 3.50 A; G=1-273.
DR PDB; 7AD8; EM; 3.50 A; G=1-273.
DR PDBsum; 1D4U; -.
DR PDBsum; 1XPA; -.
DR PDBsum; 2JNW; -.
DR PDBsum; 6J44; -.
DR PDBsum; 6LAE; -.
DR PDBsum; 6RO4; -.
DR PDBsum; 7AD8; -.
DR AlphaFoldDB; P23025; -.
DR BMRB; P23025; -.
DR SASBDB; P23025; -.
DR SMR; P23025; -.
DR BioGRID; 113344; 77.
DR CORUM; P23025; -.
DR DIP; DIP-24191N; -.
DR ELM; P23025; -.
DR IntAct; P23025; 46.
DR MINT; P23025; -.
DR STRING; 9606.ENSP00000364270; -.
DR BindingDB; P23025; -.
DR ChEMBL; CHEMBL4105801; -.
DR iPTMnet; P23025; -.
DR PhosphoSitePlus; P23025; -.
DR BioMuta; XPA; -.
DR DMDM; 139816; -.
DR EPD; P23025; -.
DR jPOST; P23025; -.
DR MassIVE; P23025; -.
DR MaxQB; P23025; -.
DR PaxDb; P23025; -.
DR PeptideAtlas; P23025; -.
DR PRIDE; P23025; -.
DR ProteomicsDB; 54051; -.
DR Antibodypedia; 3603; 494 antibodies from 36 providers.
DR DNASU; 7507; -.
DR Ensembl; ENST00000375128.5; ENSP00000364270.5; ENSG00000136936.11.
DR GeneID; 7507; -.
DR KEGG; hsa:7507; -.
DR MANE-Select; ENST00000375128.5; ENSP00000364270.5; NM_000380.4; NP_000371.1.
DR UCSC; uc004axr.5; human.
DR CTD; 7507; -.
DR DisGeNET; 7507; -.
DR GeneCards; XPA; -.
DR GeneReviews; XPA; -.
DR HGNC; HGNC:12814; XPA.
DR HPA; ENSG00000136936; Low tissue specificity.
DR MalaCards; XPA; -.
DR MIM; 278700; phenotype.
DR MIM; 611153; gene.
DR neXtProt; NX_P23025; -.
DR OpenTargets; ENSG00000136936; -.
DR Orphanet; 910; Xeroderma pigmentosum.
DR PharmGKB; PA368; -.
DR VEuPathDB; HostDB:ENSG00000136936; -.
DR eggNOG; KOG4017; Eukaryota.
DR GeneTree; ENSGT00390000002721; -.
DR HOGENOM; CLU_053731_1_0_1; -.
DR InParanoid; P23025; -.
DR OMA; VWKRETV; -.
DR OrthoDB; 1542306at2759; -.
DR PhylomeDB; P23025; -.
DR TreeFam; TF101241; -.
DR PathwayCommons; P23025; -.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR SignaLink; P23025; -.
DR SIGNOR; P23025; -.
DR BioGRID-ORCS; 7507; 24 hits in 1080 CRISPR screens.
DR ChiTaRS; XPA; human.
DR EvolutionaryTrace; P23025; -.
DR GeneWiki; XPA; -.
DR GenomeRNAi; 7507; -.
DR Pharos; P23025; Tchem.
DR PRO; PR:P23025; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P23025; protein.
DR Bgee; ENSG00000136936; Expressed in calcaneal tendon and 196 other tissues.
DR ExpressionAtlas; P23025; baseline and differential.
DR Genevisible; P23025; HS.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:CAFA.
DR GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IBA:GO_Central.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IMP:CACAO.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:CAFA.
DR GO; GO:0009650; P:UV protection; IDA:CAFA.
DR GO; GO:0070914; P:UV-damage excision repair; IBA:GO_Central.
DR DisProt; DP00243; -.
DR Gene3D; 3.90.530.10; -; 1.
DR IDEAL; IID00196; -.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000465; XPA.
DR InterPro; IPR022656; XPA_C.
DR InterPro; IPR022658; XPA_CS.
DR InterPro; IPR037129; XPA_sf.
DR InterPro; IPR022652; Znf_XPA_CS.
DR PANTHER; PTHR10142; PTHR10142; 1.
DR Pfam; PF05181; XPA_C; 1.
DR Pfam; PF01286; XPA_N; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR TIGRFAMs; TIGR00598; rad14; 1.
DR PROSITE; PS00752; XPA_1; 1.
DR PROSITE; PS00753; XPA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; DNA damage; DNA repair;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Xeroderma pigmentosum; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..273
FT /note="DNA repair protein complementing XP-A cells"
FT /id="PRO_0000208648"
FT ZN_FING 105..129
FT REGION 4..97
FT /note="Interaction with CEP164 and required for UV
FT resistance"
FT /evidence="ECO:0000269|PubMed:19197159"
FT MOTIF 26..47
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16540648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VARIANT 78
FT /note="Missing"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_014203"
FT VARIANT 94
FT /note="P -> L (in XP-A)"
FT /id="VAR_007727"
FT VARIANT 97
FT /note="V -> I (in dbSNP:rs10983315)"
FT /id="VAR_037907"
FT VARIANT 108
FT /note="C -> F (in XP-A; severe form; dbSNP:rs104894131)"
FT /evidence="ECO:0000269|PubMed:1339397,
FT ECO:0000269|PubMed:9671271"
FT /id="VAR_007728"
FT VARIANT 130
FT /note="R -> K (in XP-A; dbSNP:rs1324310300)"
FT /id="VAR_007729"
FT VARIANT 185
FT /note="Q -> H (in XP-A; dbSNP:rs746617574)"
FT /id="VAR_007730"
FT VARIANT 228
FT /note="R -> Q (in dbSNP:rs1805160)"
FT /id="VAR_014799"
FT VARIANT 234
FT /note="V -> L (in dbSNP:rs3176749)"
FT /id="VAR_029325"
FT VARIANT 244
FT /note="H -> R (in XP-A; mild form; dbSNP:rs144725456)"
FT /evidence="ECO:0000269|PubMed:1372103"
FT /id="VAR_007731"
FT VARIANT 252
FT /note="L -> V (in dbSNP:rs3176750)"
FT /id="VAR_020324"
FT VARIANT 256
FT /note="M -> V (in dbSNP:rs57519506)"
FT /id="VAR_061987"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2JNW"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6J44"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6J44"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6J44"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:6J44"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6J44"
FT TURN 132..136
FT /evidence="ECO:0007829|PDB:6J44"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6J44"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:6J44"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:6J44"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6J44"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6J44"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6J44"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:6J44"
FT HELIX 197..230
FT /evidence="ECO:0007829|PDB:6J44"
SQ SEQUENCE 273 AA; 31368 MW; F89F735219A8494B CRC64;
MAAADGALPE AAALEQPAEL PASVRASIER KRQRALMLRQ ARLAARPYSA TAAAATGGMA
NVKAAPKIID TGGGFILEEE EEEEQKIGKV VHQPGPVMEF DYVICEECGK EFMDSYLMNH
FDLPTCDNCR DADDKHKLIT KTEAKQEYLL KDCDLEKREP PLKFIVKKNP HHSQWGDMKL
YLKLQIVKRS LEVWGSQEAL EEAKEVRQEN REKMKQKKFD KKVKELRRAV RSSVWKRETI
VHQHEYGPEE NLEDDMYRKT CTMCGHELTY EKM
