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Protein

DNA repair protein complementing XP-C cells

Gene

XPC

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

Functioni

Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity.
The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.

GO - Molecular functioni

  • bubble DNA binding Source: UniProtKB
  • damaged DNA binding Source: UniProtKB
  • heteroduplex DNA loop binding Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  • DNA repair Source: ProtInc
  • global genome nucleotide-excision repair Source: Reactome
  • intra-S DNA damage checkpoint Source: Ensembl
  • mismatch repair Source: GO_Central
  • nucleotide-excision repair Source: UniProtKB
  • nucleotide-excision repair, DNA damage recognition Source: UniProtKB
  • nucleotide-excision repair, DNA duplex unwinding Source: Reactome
  • nucleotide-excision repair, preincision complex assembly Source: Reactome
  • protein sumoylation Source: Reactome
  • regulation of mitotic cell cycle phase transition Source: UniProtKB
  • response to auditory stimulus Source: Ensembl
  • response to drug Source: Ensembl
  • response to UV-B Source: Ensembl
  • UV-damage excision repair Source: CACAO
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000154767-MONOMER.
ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
SIGNORiQ01831.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein complementing XP-C cells
Alternative name(s):
Xeroderma pigmentosum group C-complementing protein
p125
Gene namesi
Name:XPC
Synonyms:XPCC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:12816. XPC.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Omnipresent in the nucleus and consistently associates with and dissociates from DNA in the absence of DNA damage. Continuously shuttles between the cytoplasm and the nucleus, which is impeded by the presence of NER lesions.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleotide-excision repair factor 2 complex Source: GO_Central
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
  • XPC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Xeroderma pigmentosum complementation group C (XP-C)2 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.
See also OMIM:278720
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005846334P → H in XP-C; severe. 1 PublicationCorresponds to variant rs74737358dbSNPEnsembl.1
Natural variantiVAR_064039690W → S in XP-C; diminishes repair activity and impairs DNA binding. 4 Publications1
Natural variantiVAR_005847697V → VV in XP-C; mild. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi531W → A: Slightly diminishes repair activity and sligtly impairs DNA binding. 1 Publication1
Mutagenesisi542W → A: Slightly diminishes repair activity and sligtly impairs DNA binding. 1 Publication1
Mutagenesisi733F → A: Diminishes repair activity and impairs DNA binding. 2 Publications1
Mutagenesisi754N → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci. 1 Publication1
Mutagenesisi755E → K: Reduces nuclear mobility and impairs repair activity. 1 Publication1
Mutagenesisi756F → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci. 1 Publication1
Mutagenesisi797F → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci; decreases recruitment of TFIIH complex to lesion sites. 1 Publication1
Mutagenesisi799F → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; greatly reduces localization at DNA damaged foci; decreases recruitment of TFIIH complex to lesion sites. 1 Publication1
Mutagenesisi848W → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-851 and A-855. 1 Publication1
Mutagenesisi851L → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-848 and A-855. 1 Publication1
Mutagenesisi855L → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-848 and A-851. 1 Publication1

Keywords - Diseasei

Disease mutation, Xeroderma pigmentosum

Organism-specific databases

DisGeNETi7508.
MalaCardsiXPC.
MIMi278720. phenotype.
OpenTargetsiENSG00000154767.
Orphaneti276255. Xeroderma pigmentosum complementation group C.
PharmGKBiPA37413.

Polymorphism and mutation databases

BioMutaiXPC.
DMDMi296453081.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002182932 – 940DNA repair protein complementing XP-C cellsAdd BLAST939

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei94PhosphoserineCombined sources1
Modified residuei129PhosphoserineCombined sources1
Modified residuei140PhosphoserineCombined sources1
Modified residuei169PhosphothreonineCombined sources1
Modified residuei397PhosphoserineCombined sources1
Modified residuei398PhosphoserineCombined sources1
Modified residuei399PhosphoserineCombined sources1
Modified residuei453PhosphoserineCombined sources1
Modified residuei460PhosphoserineCombined sources1
Modified residuei876PhosphothreonineCombined sources1
Modified residuei883PhosphoserineCombined sources1
Modified residuei884PhosphoserineCombined sources1
Modified residuei891PhosphoserineCombined sources1
Modified residuei903PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated upon UV irradiation; the ubiquitination requires the UV-DDB complex, appears to be reversible and does not serve as a signal for degradation.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ01831.
PaxDbiQ01831.
PeptideAtlasiQ01831.
PRIDEiQ01831.

PTM databases

iPTMnetiQ01831.
PhosphoSitePlusiQ01831.
SwissPalmiQ01831.

Expressioni

Gene expression databases

BgeeiENSG00000154767.
CleanExiHS_XPC.
ExpressionAtlasiQ01831. baseline and differential.
GenevisibleiQ01831. HS.

Organism-specific databases

HPAiCAB009932.
HPA035707.

Interactioni

Subunit structurei

Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with RAD23A; the interaction is suggesting the existence of a functional equivalent variant XPC complex. Interacts with TDG; the interaction is demonstrated using the XPC:RAD23B dimer. Interacts with SMUG1; the interaction is demonstrated using the XPC:RAD23B dimer. Interacts with DDB2. Interacts with CCNH, GTF2H1 and ERCC3.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BGLF4P132889EBI-372610,EBI-1630636From a different organism.
CETN2P412084EBI-372610,EBI-1789926
ERCC3P194472EBI-372610,EBI-1183307
GTF2H1P327802EBI-372610,EBI-715539
RAD23BP547275EBI-372610,EBI-954531

Protein-protein interaction databases

BioGridi113345. 72 interactors.
DIPiDIP-31225N.
IntActiQ01831. 22 interactors.
MINTiMINT-105410.
STRINGi9606.ENSP00000285021.

Structurei

Secondary structure

1940
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni120 – 123Combined sources4
Beta strandi124 – 126Combined sources3
Beta strandi134 – 137Combined sources4
Helixi150 – 153Combined sources4
Helixi848 – 861Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A4JNMR-B847-863[»]
2GGMX-ray2.35C/D847-863[»]
2OBHX-ray1.80C/D847-863[»]
2RVBNMR-A109-156[»]
ProteinModelPortaliQ01831.
SMRiQ01831.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01831.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni496 – 734Interaction with RAD23BAdd BLAST239
Regioni607 – 766Minimal sensor domain involved in damage recognitionAdd BLAST160
Regioni607 – 741DNA-binding; preference for heteroduplex DNAAdd BLAST135
Regioni767 – 831DNA-binding; preference for single stranded DNA; required for formation of stable nucleoprotein complexAdd BLAST65
Regioni816 – 940Interaction with ERCC2 and GTF2H11 PublicationAdd BLAST125
Regioni847 – 866Interaction with CETN2Add BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi390 – 395Nuclear localization signalSequence analysis6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi30 – 177Glu-rich (acidic)Add BLAST148
Compositional biasi30 – 34Poly-Glu5
Compositional biasi124 – 130Poly-Glu7
Compositional biasi359 – 395Lys-rich (basic)Add BLAST37
Compositional biasi408 – 431Arg/Lys-rich (basic)Add BLAST24
Compositional biasi432 – 461Asp/Glu-rich (acidic)Add BLAST30
Compositional biasi466 – 493Arg/Lys-rich (basic)Add BLAST28
Compositional biasi501 – 507Poly-Ser7

Sequence similaritiesi

Belongs to the XPC family.Curated

Phylogenomic databases

eggNOGiKOG2179. Eukaryota.
COG5535. LUCA.
GeneTreeiENSGT00390000005194.
HOGENOMiHOG000124671.
HOVERGENiHBG000407.
InParanoidiQ01831.
KOiK10838.
OMAiNKEVHED.
OrthoDBiEOG091G0HLY.
PhylomeDBiQ01831.
TreeFamiTF101242.

Family and domain databases

InterProiIPR018327. BHD_2.
IPR004583. DNA_repair_Rad4.
IPR018026. DNA_repair_Rad4_subgr.
IPR018325. Rad4/PNGase_transGLS-fold.
IPR018326. Rad4_beta-hairpin_dom1.
IPR018328. Rad4_beta-hairpin_dom3.
[Graphical view]
PANTHERiPTHR12135. PTHR12135. 2 hits.
PfamiPF10403. BHD_1. 1 hit.
PF10404. BHD_2. 1 hit.
PF10405. BHD_3. 1 hit.
PF03835. Rad4. 1 hit.
[Graphical view]
SMARTiSM01030. BHD_1. 1 hit.
SM01031. BHD_2. 1 hit.
SM01032. BHD_3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00605. rad4. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q01831-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARKRAAGGE PRGRELRSQK SKAKSKARRE EEEEDAFEDE KPPKKSLLSK
60 70 80 90 100
VSQGKRKRGC SHPGGSADGP AKKKVAKVTV KSENLKVIKD EALSDGDDLR
110 120 130 140 150
DFPSDLKKAH HLKRGATMNE DSNEEEEESE NDWEEVEELS EPVLGDVRES
160 170 180 190 200
TAFSRSLLPV KPVEIEIETP EQAKTRERSE KIKLEFETYL RRAMKRFNKG
210 220 230 240 250
VHEDTHKVHL LCLLANGFYR NNICSQPDLH AIGLSIIPAR FTRVLPRDVD
260 270 280 290 300
TYYLSNLVKW FIGTFTVNAE LSASEQDNLQ TTLERRFAIY SARDDEELVH
310 320 330 340 350
IFLLILRALQ LLTRLVLSLQ PIPLKSATAK GKKPSKERLT ADPGGSSETS
360 370 380 390 400
SQVLENHTKP KTSKGTKQEE TFAKGTCRPS AKGKRNKGGR KKRSKPSSSE
410 420 430 440 450
EDEGPGDKQE KATQRRPHGR ERRVASRVSY KEESGSDEAG SGSDFELSSG
460 470 480 490 500
EASDPSDEDS EPGPPKQRKA PAPQRTKAGS KSASRTHRGS HRKDPSLPAA
510 520 530 540 550
SSSSSSSKRG KKMCSDGEKA EKRSIAGIDQ WLEVFCEQEE KWVCVDCVHG
560 570 580 590 600
VVGQPLTCYK YATKPMTYVV GIDSDGWVRD VTQRYDPVWM TVTRKCRVDA
610 620 630 640 650
EWWAETLRPY QSPFMDREKK EDLEFQAKHM DQPLPTAIGL YKNHPLYALK
660 670 680 690 700
RHLLKYEAIY PETAAILGYC RGEAVYSRDC VHTLHSRDTW LKKARVVRLG
710 720 730 740 750
EVPYKMVKGF SNRARKARLA EPQLREENDL GLFGYWQTEE YQPPVAVDGK
760 770 780 790 800
VPRNEFGNVY LFLPSMMPIG CVQLNLPNLH RVARKLDIDC VQAITGFDFH
810 820 830 840 850
GGYSHPVTDG YIVCEEFKDV LLTAWENEQA VIERKEKEKK EKRALGNWKL
860 870 880 890 900
LAKGLLIRER LKRRYGPKSE AAAPHTDAGG GLSSDEEEGT SSQAEAARIL
910 920 930 940
AASWPQNRED EEKQKLKGGP KKTKREKKAA ASHLFPFEQL
Length:940
Mass (Da):105,953
Last modified:May 18, 2010 - v4
Checksum:i2F8C80D43FAA1256
GO
Isoform 2 (identifier: Q01831-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-172: Missing.

Note: No experimental confirmation available.
Show »
Length:903
Mass (Da):101,847
Checksum:iAF2F96DDCC4DB78E
GO
Isoform 3 (identifier: Q01831-3) [UniParc]FASTAAdd to basket
Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     138-140: ELS → VKR
     141-940: Missing.

Show »
Length:140
Mass (Da):15,712
Checksum:iCA721AA7474B6D20
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti135E → Q in BAG58555 (PubMed:14702039).Curated1
Sequence conflicti489G → E in BAG58555 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01889416L → V.1 PublicationCorresponds to variant rs1870134dbSNPEnsembl.1
Natural variantiVAR_01889548L → F.1 PublicationCorresponds to variant rs3731062dbSNPEnsembl.1
Natural variantiVAR_01889686K → R.1 PublicationCorresponds to variant rs3731063dbSNPEnsembl.1
Natural variantiVAR_057475287F → C.Corresponds to variant rs35629274dbSNPEnsembl.1
Natural variantiVAR_018897314R → Q.1 PublicationCorresponds to variant rs3731126dbSNPEnsembl.1
Natural variantiVAR_005846334P → H in XP-C; severe. 1 PublicationCorresponds to variant rs74737358dbSNPEnsembl.1
Natural variantiVAR_018898492R → H.1 PublicationCorresponds to variant rs2227999dbSNPEnsembl.1
Natural variantiVAR_018899499A → V.3 PublicationsCorresponds to variant rs2228000dbSNPEnsembl.1
Natural variantiVAR_059963511K → Q.Corresponds to variant rs6413541dbSNPEnsembl.1
Natural variantiVAR_018900513M → I.1 PublicationCorresponds to variant rs3731130dbSNPEnsembl.1
Natural variantiVAR_057476514C → S.Corresponds to variant rs3731130dbSNPEnsembl.1
Natural variantiVAR_018901632Q → E.1 PublicationCorresponds to variant rs3731139dbSNPEnsembl.1
Natural variantiVAR_018902671R → H.1 PublicationCorresponds to variant rs3731140dbSNPEnsembl.1
Natural variantiVAR_018903689T → M.1 PublicationCorresponds to variant rs3731152dbSNPEnsembl.1
Natural variantiVAR_064039690W → S in XP-C; diminishes repair activity and impairs DNA binding. 4 Publications1
Natural variantiVAR_005847697V → VV in XP-C; mild. 1 Publication1
Natural variantiVAR_018904928K → Q.1 PublicationCorresponds to variant rs3731177dbSNPEnsembl.1
Natural variantiVAR_005848939Q → K.3 PublicationsCorresponds to variant rs2228001dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_046344136 – 172Missing in isoform 2. 1 PublicationAdd BLAST37
Alternative sequenceiVSP_055890138 – 140ELS → VKR in isoform 3. 1 Publication3
Alternative sequenceiVSP_055891141 – 940Missing in isoform 3. 1 PublicationAdd BLAST800

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21089 mRNA. Translation: BAA04651.1.
AF261901
, AF261892, AF261893, AF261894, AF261895, AF261896, AF261897, AF261898, AF261899, AF261900 Genomic DNA. Translation: AAF87574.1.
KJ535085 mRNA. Translation: AHW56724.1.
AY131066 Genomic DNA. Translation: AAM77801.1.
AK295711 mRNA. Translation: BAG58555.1.
AC093495 Genomic DNA. No translation available.
FJ695191 Genomic DNA. No translation available.
FJ695192 Genomic DNA. No translation available.
BC016620 mRNA. Translation: AAH16620.1.
AK222844 mRNA. Translation: BAD96564.1.
X65024 mRNA. Translation: CAA46158.1.
CCDSiCCDS46763.1. [Q01831-1]
PIRiS44345.
RefSeqiNP_004619.3. NM_004628.4. [Q01831-1]
UniGeneiHs.475538.
Hs.739296.

Genome annotation databases

EnsembliENST00000285021; ENSP00000285021; ENSG00000154767. [Q01831-1]
ENST00000476581; ENSP00000424548; ENSG00000154767. [Q01831-3]
GeneIDi7508.
KEGGihsa:7508.
UCSCiuc062gzd.1. human. [Q01831-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21089 mRNA. Translation: BAA04651.1.
AF261901
, AF261892, AF261893, AF261894, AF261895, AF261896, AF261897, AF261898, AF261899, AF261900 Genomic DNA. Translation: AAF87574.1.
KJ535085 mRNA. Translation: AHW56724.1.
AY131066 Genomic DNA. Translation: AAM77801.1.
AK295711 mRNA. Translation: BAG58555.1.
AC093495 Genomic DNA. No translation available.
FJ695191 Genomic DNA. No translation available.
FJ695192 Genomic DNA. No translation available.
BC016620 mRNA. Translation: AAH16620.1.
AK222844 mRNA. Translation: BAD96564.1.
X65024 mRNA. Translation: CAA46158.1.
CCDSiCCDS46763.1. [Q01831-1]
PIRiS44345.
RefSeqiNP_004619.3. NM_004628.4. [Q01831-1]
UniGeneiHs.475538.
Hs.739296.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A4JNMR-B847-863[»]
2GGMX-ray2.35C/D847-863[»]
2OBHX-ray1.80C/D847-863[»]
2RVBNMR-A109-156[»]
ProteinModelPortaliQ01831.
SMRiQ01831.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113345. 72 interactors.
DIPiDIP-31225N.
IntActiQ01831. 22 interactors.
MINTiMINT-105410.
STRINGi9606.ENSP00000285021.

PTM databases

iPTMnetiQ01831.
PhosphoSitePlusiQ01831.
SwissPalmiQ01831.

Polymorphism and mutation databases

BioMutaiXPC.
DMDMi296453081.

Proteomic databases

EPDiQ01831.
PaxDbiQ01831.
PeptideAtlasiQ01831.
PRIDEiQ01831.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285021; ENSP00000285021; ENSG00000154767. [Q01831-1]
ENST00000476581; ENSP00000424548; ENSG00000154767. [Q01831-3]
GeneIDi7508.
KEGGihsa:7508.
UCSCiuc062gzd.1. human. [Q01831-1]

Organism-specific databases

CTDi7508.
DisGeNETi7508.
GeneCardsiXPC.
GeneReviewsiXPC.
HGNCiHGNC:12816. XPC.
HPAiCAB009932.
HPA035707.
MalaCardsiXPC.
MIMi278720. phenotype.
613208. gene.
neXtProtiNX_Q01831.
OpenTargetsiENSG00000154767.
Orphaneti276255. Xeroderma pigmentosum complementation group C.
PharmGKBiPA37413.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2179. Eukaryota.
COG5535. LUCA.
GeneTreeiENSGT00390000005194.
HOGENOMiHOG000124671.
HOVERGENiHBG000407.
InParanoidiQ01831.
KOiK10838.
OMAiNKEVHED.
OrthoDBiEOG091G0HLY.
PhylomeDBiQ01831.
TreeFamiTF101242.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000154767-MONOMER.
ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
SIGNORiQ01831.

Miscellaneous databases

ChiTaRSiXPC. human.
EvolutionaryTraceiQ01831.
GeneWikiiXPC_(gene).
GenomeRNAii7508.
PROiQ01831.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000154767.
CleanExiHS_XPC.
ExpressionAtlasiQ01831. baseline and differential.
GenevisibleiQ01831. HS.

Family and domain databases

InterProiIPR018327. BHD_2.
IPR004583. DNA_repair_Rad4.
IPR018026. DNA_repair_Rad4_subgr.
IPR018325. Rad4/PNGase_transGLS-fold.
IPR018326. Rad4_beta-hairpin_dom1.
IPR018328. Rad4_beta-hairpin_dom3.
[Graphical view]
PANTHERiPTHR12135. PTHR12135. 2 hits.
PfamiPF10403. BHD_1. 1 hit.
PF10404. BHD_2. 1 hit.
PF10405. BHD_3. 1 hit.
PF03835. Rad4. 1 hit.
[Graphical view]
SMARTiSM01030. BHD_1. 1 hit.
SM01031. BHD_2. 1 hit.
SM01032. BHD_3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00605. rad4. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiXPC_HUMAN
AccessioniPrimary (citable) accession number: Q01831
Secondary accession number(s): B4DIP3
, E9PB96, E9PH69, Q53GT7, Q96AX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 18, 2010
Last modified: November 2, 2016
This is version 175 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. 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.