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 27-MAR-2024, entry version 231. 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="https://atlasgeneticsoncology.org/gene/104/XPA"; 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8EBT; EM; 3.90 A; K=102-273. DR PDB; 8EBU; EM; 3.30 A; K=1-273. DR PDB; 8EBX; EM; 3.60 A; K=1-273. DR PDB; 8EBY; EM; 3.60 A; K=1-273. DR PDBsum; 1D4U; -. DR PDBsum; 1XPA; -. DR PDBsum; 2JNW; -. DR PDBsum; 6J44; -. DR PDBsum; 6LAE; -. DR PDBsum; 6RO4; -. DR PDBsum; 7AD8; -. DR PDBsum; 8EBT; -. DR PDBsum; 8EBU; -. DR PDBsum; 8EBX; -. DR PDBsum; 8EBY; -. DR AlphaFoldDB; P23025; -. DR BMRB; P23025; -. DR EMDB; EMD-27997; -. DR EMDB; EMD-27998; -. DR EMDB; EMD-28001; -. DR EMDB; EMD-28002; -. DR EMDB; EMD-29673; -. DR EMDB; EMD-4970; -. DR SASBDB; P23025; -. DR SMR; P23025; -. DR BioGRID; 113344; 86. 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 GlyGen; P23025; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000364270; -. DR PeptideAtlas; P23025; -. DR ProteomicsDB; 54051; -. DR Pumba; P23025; -. DR Antibodypedia; 3603; 525 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 AGR; HGNC:12814; -. 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; DEYTHTC; -. DR OrthoDB; 5489071at2759; -. 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 1158 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 198 other cell types or tissues. DR ExpressionAtlas; P23025; baseline and differential. 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:0006289; P:nucleotide-excision repair; IMP:CACAO. 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:0034504; P:protein localization to nucleus; IMP:CAFA. DR GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl. DR GO; GO:0009650; P:UV protection; IDA:CAFA. DR GO; GO:0070914; P:UV-damage excision repair; IBA:GO_Central. DR CDD; cd21076; DBD_XPA; 1. DR DisProt; DP00243; -. DR Gene3D; 3.90.530.10; XPA C-terminal domain; 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 NCBIfam; TIGR00598; rad14; 1. DR PANTHER; PTHR10142; DNA REPAIR PROTEIN COMPLEMENTING XP-A CELLS; 1. DR PANTHER; PTHR10142:SF0; DNA REPAIR PROTEIN COMPLEMENTING XP-A CELLS; 1. DR Pfam; PF05181; XPA_C; 1. DR Pfam; PF01286; XPA_N; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF46955; Putative DNA-binding domain; 1. DR PROSITE; PS00752; XPA_1; 1. DR PROSITE; PS00753; XPA_2; 1. DR Genevisible; P23025; HS. 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:8EBU" 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" FT TURN 232..234 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 256..261 FT /evidence="ECO:0007829|PDB:8EBU" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 267..271 FT /evidence="ECO:0007829|PDB:8EBU" 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 //