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P23025

- XPA_HUMAN

UniProt

P23025 - XPA_HUMAN

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Protein

DNA repair protein complementing XP-A cells

Gene
XPA, XPAC
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
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 – 11Removed1 Publication
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.
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.

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 signal Reviewed predictionAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the XPA family.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 159 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

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