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Protein

DNA repair protein complementing XP-A cells

Gene

XPA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Zinc fingeri105 – 129Add BLAST25

GO - Molecular functioni

  • damaged DNA binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000136936-MONOMER.
ReactomeiR-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6782135. Dual incision in TC-NER.
SIGNORiP23025.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:12814. XPA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Xeroderma pigmentosum complementation group A (XP-A)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:278700
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00772794P → L in XP-A. 1
Natural variantiVAR_007728108C → F in XP-A; severe form. 2 PublicationsCorresponds to variant rs104894131dbSNPEnsembl.1
Natural variantiVAR_007729130R → K in XP-A. 1
Natural variantiVAR_007730185Q → H in XP-A. Corresponds to variant rs746617574dbSNPEnsembl.1
Natural variantiVAR_007731244H → R in XP-A; mild form. 1 PublicationCorresponds to variant rs144725456dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Xeroderma pigmentosum

Organism-specific databases

DisGeNETi7507.
MalaCardsiXPA.
MIMi278700. phenotype.
OpenTargetsiENSG00000136936.
Orphaneti276249. Xeroderma pigmentosum complementation group A.
PharmGKBiPA368.

Polymorphism and mutation databases

BioMutaiXPA.
DMDMi139816.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002086482 – 273DNA repair protein complementing XP-A cellsAdd BLAST272

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Cross-linki145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei196PhosphoserineCombined sources1 Publication1

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, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP23025.
MaxQBiP23025.
PaxDbiP23025.
PeptideAtlasiP23025.
PRIDEiP23025.

PTM databases

iPTMnetiP23025.
PhosphoSitePlusiP23025.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000136936.
CleanExiHS_XPA.
ExpressionAtlasiP23025. baseline and differential.
GenevisibleiP23025. HS.

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
ERCC1P079922EBI-295222,EBI-750962
NDEL1Q9GZM85EBI-295222,EBI-928842
RPA2P159274EBI-295222,EBI-621404
SIRT1Q96EB68EBI-295222,EBI-1802965
TRIM27P143733EBI-295222,EBI-719493
XAB2Q9HCS72EBI-295222,EBI-295232

GO - Molecular functioni

  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi113344. 29 interactors.
DIPiDIP-24191N.
IntActiP23025. 31 interactors.
MINTiMINT-192332.
STRINGi9606.ENSP00000364270.

Structurei

Secondary structure

1273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi72 – 75Combined sources4
Turni106 – 108Combined sources3
Beta strandi111 – 113Combined sources3
Beta strandi115 – 117Combined sources3
Turni118 – 121Combined sources4
Turni127 – 129Combined sources3
Beta strandi131 – 135Combined sources5
Helixi141 – 144Combined sources4
Turni145 – 149Combined sources5
Beta strandi152 – 154Combined sources3
Turni155 – 157Combined sources3
Beta strandi158 – 160Combined sources3
Beta strandi164 – 168Combined sources5
Beta strandi170 – 172Combined sources3
Beta strandi179 – 181Combined sources3
Helixi183 – 193Combined sources11
Helixi197 – 206Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D4UNMR-A98-208[»]
1XPANMR-A98-219[»]
2JNWNMR-B67-80[»]
DisProtiDP00243.
ProteinModelPortaliP23025.
SMRiP23025.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23025.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 97Interaction with CEP164 and required for UV resistance1 PublicationAdd BLAST94

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi26 – 47Nuclear localization signalSequence analysisAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi78 – 84Poly-Glu7

Sequence similaritiesi

Belongs to the XPA family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri105 – 129Add BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4017. Eukaryota.
COG5145. LUCA.
GeneTreeiENSGT00390000002721.
HOGENOMiHOG000045820.
HOVERGENiHBG009053.
InParanoidiP23025.
KOiK10847.
OMAiWKRETIV.
OrthoDBiEOG091G17K3.
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:SF0. PTHR10142:SF0. 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

        10         20         30         40         50
MAAADGALPE AAALEQPAEL PASVRASIER KRQRALMLRQ ARLAARPYSA
60 70 80 90 100
TAAAATGGMA NVKAAPKIID TGGGFILEEE EEEEQKIGKV VHQPGPVMEF
110 120 130 140 150
DYVICEECGK EFMDSYLMNH FDLPTCDNCR DADDKHKLIT KTEAKQEYLL
160 170 180 190 200
KDCDLEKREP PLKFIVKKNP HHSQWGDMKL YLKLQIVKRS LEVWGSQEAL
210 220 230 240 250
EEAKEVRQEN REKMKQKKFD KKVKELRRAV RSSVWKRETI VHQHEYGPEE
260 270
NLEDDMYRKT CTMCGHELTY EKM
Length:273
Mass (Da):31,368
Last modified:November 1, 1991 - v1
Checksum:iF89F735219A8494B
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01420378Missing .1 Publication1
Natural variantiVAR_00772794P → L in XP-A. 1
Natural variantiVAR_03790797V → I.Corresponds to variant rs10983315dbSNPEnsembl.1
Natural variantiVAR_007728108C → F in XP-A; severe form. 2 PublicationsCorresponds to variant rs104894131dbSNPEnsembl.1
Natural variantiVAR_007729130R → K in XP-A. 1
Natural variantiVAR_007730185Q → H in XP-A. Corresponds to variant rs746617574dbSNPEnsembl.1
Natural variantiVAR_014799228R → Q.Corresponds to variant rs1805160dbSNPEnsembl.1
Natural variantiVAR_029325234V → L.Corresponds to variant rs3176749dbSNPEnsembl.1
Natural variantiVAR_007731244H → R in XP-A; mild form. 1 PublicationCorresponds to variant rs144725456dbSNPEnsembl.1
Natural variantiVAR_020324252L → V.Corresponds to variant rs3176750dbSNPEnsembl.1
Natural variantiVAR_061987256M → V.Corresponds to variant rs57519506dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D4UNMR-A98-208[»]
1XPANMR-A98-219[»]
2JNWNMR-B67-80[»]
DisProtiDP00243.
ProteinModelPortaliP23025.
SMRiP23025.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113344. 29 interactors.
DIPiDIP-24191N.
IntActiP23025. 31 interactors.
MINTiMINT-192332.
STRINGi9606.ENSP00000364270.

PTM databases

iPTMnetiP23025.
PhosphoSitePlusiP23025.

Polymorphism and mutation databases

BioMutaiXPA.
DMDMi139816.

Proteomic databases

EPDiP23025.
MaxQBiP23025.
PaxDbiP23025.
PeptideAtlasiP23025.
PRIDEiP23025.

Protocols and materials databases

DNASUi7507.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375128; ENSP00000364270; ENSG00000136936.
GeneIDi7507.
KEGGihsa:7507.
UCSCiuc004axr.5. human.

Organism-specific databases

CTDi7507.
DisGeNETi7507.
GeneCardsiXPA.
GeneReviewsiXPA.
HGNCiHGNC:12814. XPA.
HPAiCAB000155.
HPA030997.
HPA056856.
MalaCardsiXPA.
MIMi278700. phenotype.
611153. gene.
neXtProtiNX_P23025.
OpenTargetsiENSG00000136936.
Orphaneti276249. Xeroderma pigmentosum complementation group A.
PharmGKBiPA368.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4017. Eukaryota.
COG5145. LUCA.
GeneTreeiENSGT00390000002721.
HOGENOMiHOG000045820.
HOVERGENiHBG009053.
InParanoidiP23025.
KOiK10847.
OMAiWKRETIV.
OrthoDBiEOG091G17K3.
PhylomeDBiP23025.
TreeFamiTF101241.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000136936-MONOMER.
ReactomeiR-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6782135. Dual incision in TC-NER.
SIGNORiP23025.

Miscellaneous databases

EvolutionaryTraceiP23025.
GeneWikiiXPA.
GenomeRNAii7507.
PROiP23025.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136936.
CleanExiHS_XPA.
ExpressionAtlasiP23025. baseline and differential.
GenevisibleiP23025. HS.

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:SF0. PTHR10142:SF0. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 184 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.