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Q01831

- XPC_HUMAN

UniProt

Q01831 - XPC_HUMAN

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Protein

DNA repair protein complementing XP-C cells

Gene

XPC

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. bubble DNA binding Source: UniProtKB
  2. damaged DNA binding Source: UniProtKB
  3. heteroduplex DNA loop binding Source: UniProtKB
  4. single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: Reactome
  2. intra-S DNA damage checkpoint Source: Ensembl
  3. nucleotide-excision repair Source: UniProtKB
  4. nucleotide-excision repair, DNA damage recognition Source: UniProtKB
  5. nucleotide-excision repair, DNA damage removal Source: Reactome
  6. regulation of mitotic cell cycle phase transition Source: UniProtKB
  7. response to drug Source: Ensembl
  8. response to UV-B Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_257. Formation of incision complex in GG-NER.
REACT_311. Dual incision reaction in GG-NER.
REACT_476. DNA Damage Recognition in GG-NER.

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
ProteomesiUP000005640: 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

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. nucleolus Source: HPA
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: HPA
  7. XPC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Xeroderma pigmentosum complementation group C (XP-C) [MIM:278720]: 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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti334 – 3341P → H in XP-C; severe. 1 Publication
Corresponds to variant rs74737358 [ dbSNP | Ensembl ].
VAR_005846
Natural varianti690 – 6901W → S in XP-C; diminishes repair activity and impairs DNA binding. 1 Publication
VAR_064039
Natural varianti697 – 6971V → VV in XP-C; mild. 1 Publication
VAR_005847

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi531 – 5311W → A: Slightly diminishes repair activity and sligtly impairs DNA binding. 1 Publication
Mutagenesisi542 – 5421W → A: Slightly diminishes repair activity and sligtly impairs DNA binding. 1 Publication
Mutagenesisi733 – 7331F → A: Diminishes repair activity and impairs DNA binding. 2 Publications
Mutagenesisi754 – 7541N → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci. 1 Publication
Mutagenesisi755 – 7551E → K: Reduces nuclear mobility and impairs repair activity. 1 Publication
Mutagenesisi756 – 7561F → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci. 1 Publication
Mutagenesisi797 – 7971F → 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 Publication
Mutagenesisi799 – 7991F → 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 Publication
Mutagenesisi848 – 8481W → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-851 and A-855. 1 Publication
Mutagenesisi851 – 8511L → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-848 and A-855. 1 Publication
Mutagenesisi855 – 8551L → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-848 and A-851. 1 Publication

Keywords - Diseasei

Disease mutation, Xeroderma pigmentosum

Organism-specific databases

MIMi278720. phenotype.
Orphaneti276255. Xeroderma pigmentosum complementation group C.
PharmGKBiPA37413.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 940939DNA repair protein complementing XP-C cellsPRO_0000218293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941Phosphoserine4 Publications
Modified residuei129 – 1291Phosphoserine2 Publications
Modified residuei169 – 1691Phosphothreonine1 Publication
Modified residuei876 – 8761Phosphothreonine1 Publication
Modified residuei883 – 8831Phosphoserine3 Publications
Modified residuei884 – 8841Phosphoserine3 Publications
Modified residuei891 – 8911Phosphoserine1 Publication

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

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ01831.
PaxDbiQ01831.
PeptideAtlasiQ01831.
PRIDEiQ01831.

PTM databases

PhosphoSiteiQ01831.

Expressioni

Gene expression databases

BgeeiQ01831.
CleanExiHS_XPC.
ExpressionAtlasiQ01831. baseline and differential.
GenevestigatoriQ01831.

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.
CETN2P412083EBI-372610,EBI-1789926
ERCC3P194472EBI-372610,EBI-1183307
GTF2H1P327802EBI-372610,EBI-715539
RAD23BP547275EBI-372610,EBI-954531

Protein-protein interaction databases

BioGridi113345. 46 interactions.
DIPiDIP-31225N.
IntActiQ01831. 19 interactions.
MINTiMINT-105410.
STRINGi9606.ENSP00000285021.

Structurei

Secondary structure

1
940
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi848 – 86114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A4JNMR-B847-863[»]
2GGMX-ray2.35C/D847-863[»]
2OBHX-ray1.80C/D847-863[»]
ProteinModelPortaliQ01831.
SMRiQ01831. Positions 531-824.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01831.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni496 – 734239Interaction with RAD23BAdd
BLAST
Regioni607 – 766160Minimal sensor domain involved in damage recognitionAdd
BLAST
Regioni607 – 741135DNA-binding; preference for heteroduplex DNAAdd
BLAST
Regioni767 – 83165DNA-binding; preference for single stranded DNA; required for formation of stable nucleoprotein complexAdd
BLAST
Regioni816 – 940125Interaction with ERCC2 and GTF2H1Add
BLAST
Regioni847 – 86620Interaction with CETN2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi390 – 3956Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 177148Glu-rich (acidic)Add
BLAST
Compositional biasi30 – 345Poly-Glu
Compositional biasi124 – 1307Poly-Glu
Compositional biasi359 – 39537Lys-rich (basic)Add
BLAST
Compositional biasi408 – 43124Arg/Lys-rich (basic)Add
BLAST
Compositional biasi432 – 46130Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi466 – 49328Arg/Lys-rich (basic)Add
BLAST
Compositional biasi501 – 5077Poly-Ser

Sequence similaritiesi

Belongs to the XPC family.Curated

Phylogenomic databases

eggNOGiCOG5535.
GeneTreeiENSGT00390000005194.
HOGENOMiHOG000124671.
HOVERGENiHBG000407.
InParanoidiQ01831.
KOiK10838.
OMAiPQRTKAG.
OrthoDBiEOG7BW0J2.
PhylomeDBiQ01831.
TreeFamiTF101242.

Family and domain databases

InterProiIPR004583. DNA_repair_Rad4.
IPR018026. DNA_repair_Rad4_subgr.
IPR018325. Rad4/PNGase_transGLS-fold.
IPR018326. Rad4_beta-hairpin_dom1.
IPR018327. Rad4_beta-hairpin_dom2.
IPR018328. Rad4_beta-hairpin_dom3.
[Graphical view]
PANTHERiPTHR12135. PTHR12135. 1 hit.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351E → Q in BAG58555. (PubMed:14702039)Curated
Sequence conflicti489 – 4891G → E in BAG58555. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161L → V.1 Publication
Corresponds to variant rs1870134 [ dbSNP | Ensembl ].
VAR_018894
Natural varianti48 – 481L → F.1 Publication
Corresponds to variant rs3731062 [ dbSNP | Ensembl ].
VAR_018895
Natural varianti86 – 861K → R.1 Publication
Corresponds to variant rs3731063 [ dbSNP | Ensembl ].
VAR_018896
Natural varianti287 – 2871F → C.
Corresponds to variant rs35629274 [ dbSNP | Ensembl ].
VAR_057475
Natural varianti314 – 3141R → Q.1 Publication
Corresponds to variant rs3731126 [ dbSNP | Ensembl ].
VAR_018897
Natural varianti334 – 3341P → H in XP-C; severe. 1 Publication
Corresponds to variant rs74737358 [ dbSNP | Ensembl ].
VAR_005846
Natural varianti492 – 4921R → H.1 Publication
Corresponds to variant rs2227999 [ dbSNP | Ensembl ].
VAR_018898
Natural varianti499 – 4991A → V.3 Publications
Corresponds to variant rs2228000 [ dbSNP | Ensembl ].
VAR_018899
Natural varianti511 – 5111K → Q.
Corresponds to variant rs6413541 [ dbSNP | Ensembl ].
VAR_059963
Natural varianti513 – 5131M → I.1 Publication
Corresponds to variant rs3731130 [ dbSNP | Ensembl ].
VAR_018900
Natural varianti514 – 5141C → S.
Corresponds to variant rs3731130 [ dbSNP | Ensembl ].
VAR_057476
Natural varianti632 – 6321Q → E.1 Publication
Corresponds to variant rs3731139 [ dbSNP | Ensembl ].
VAR_018901
Natural varianti671 – 6711R → H.1 Publication
Corresponds to variant rs3731140 [ dbSNP | Ensembl ].
VAR_018902
Natural varianti689 – 6891T → M.1 Publication
Corresponds to variant rs3731152 [ dbSNP | Ensembl ].
VAR_018903
Natural varianti690 – 6901W → S in XP-C; diminishes repair activity and impairs DNA binding. 1 Publication
VAR_064039
Natural varianti697 – 6971V → VV in XP-C; mild. 1 Publication
VAR_005847
Natural varianti928 – 9281K → Q.1 Publication
Corresponds to variant rs3731177 [ dbSNP | Ensembl ].
VAR_018904
Natural varianti939 – 9391Q → K.3 Publications
Corresponds to variant rs2228001 [ dbSNP | Ensembl ].
VAR_005848

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei136 – 17237Missing in isoform 2. 1 PublicationVSP_046344Add
BLAST
Alternative sequencei138 – 1403ELS → VKR in isoform 3. 1 PublicationVSP_055890
Alternative sequencei141 – 940800Missing in isoform 3. 1 PublicationVSP_055891Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc011ave.2. human. [Q01831-1]

Polymorphism databases

DMDMi296453081.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS46763.1. [Q01831-1 ]
PIRi S44345.
RefSeqi NP_004619.3. NM_004628.4. [Q01831-1 ]
UniGenei Hs.475538.
Hs.739296.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2A4J NMR - B 847-863 [» ]
2GGM X-ray 2.35 C/D 847-863 [» ]
2OBH X-ray 1.80 C/D 847-863 [» ]
ProteinModelPortali Q01831.
SMRi Q01831. Positions 531-824.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113345. 46 interactions.
DIPi DIP-31225N.
IntActi Q01831. 19 interactions.
MINTi MINT-105410.
STRINGi 9606.ENSP00000285021.

PTM databases

PhosphoSitei Q01831.

Polymorphism databases

DMDMi 296453081.

Proteomic databases

MaxQBi Q01831.
PaxDbi Q01831.
PeptideAtlasi Q01831.
PRIDEi Q01831.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000285021 ; ENSP00000285021 ; ENSG00000154767 . [Q01831-1 ]
ENST00000476581 ; ENSP00000424548 ; ENSG00000154767 . [Q01831-3 ]
GeneIDi 7508.
KEGGi hsa:7508.
UCSCi uc011ave.2. human. [Q01831-1 ]

Organism-specific databases

CTDi 7508.
GeneCardsi GC03M014161.
GeneReviewsi XPC.
HGNCi HGNC:12816. XPC.
HPAi CAB009932.
HPA035707.
MIMi 278720. phenotype.
613208. gene.
neXtProti NX_Q01831.
Orphaneti 276255. Xeroderma pigmentosum complementation group C.
PharmGKBi PA37413.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5535.
GeneTreei ENSGT00390000005194.
HOGENOMi HOG000124671.
HOVERGENi HBG000407.
InParanoidi Q01831.
KOi K10838.
OMAi PQRTKAG.
OrthoDBi EOG7BW0J2.
PhylomeDBi Q01831.
TreeFami TF101242.

Enzyme and pathway databases

Reactomei REACT_257. Formation of incision complex in GG-NER.
REACT_311. Dual incision reaction in GG-NER.
REACT_476. DNA Damage Recognition in GG-NER.

Miscellaneous databases

ChiTaRSi XPC. human.
EvolutionaryTracei Q01831.
GeneWikii XPC_(gene).
GenomeRNAii 7508.
NextBioi 29391.
PROi Q01831.
SOURCEi Search...

Gene expression databases

Bgeei Q01831.
CleanExi HS_XPC.
ExpressionAtlasi Q01831. baseline and differential.
Genevestigatori Q01831.

Family and domain databases

InterProi IPR004583. DNA_repair_Rad4.
IPR018026. DNA_repair_Rad4_subgr.
IPR018325. Rad4/PNGase_transGLS-fold.
IPR018326. Rad4_beta-hairpin_dom1.
IPR018327. Rad4_beta-hairpin_dom2.
IPR018328. Rad4_beta-hairpin_dom3.
[Graphical view ]
PANTHERi PTHR12135. PTHR12135. 1 hit.
Pfami PF10403. BHD_1. 1 hit.
PF10404. BHD_2. 1 hit.
PF10405. BHD_3. 1 hit.
PF03835. Rad4. 1 hit.
[Graphical view ]
SMARTi SM01030. BHD_1. 1 hit.
SM01031. BHD_2. 1 hit.
SM01032. BHD_3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00605. rad4. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Purification and cloning of a nucleotide excision repair complex involving the Xeroderma pigmentosum group C protein and a human homologue of yeast RAD23."
    Masutani C., Sugasawa K., Yanagisawa J., Sonoyama T., Ui M., Enomoto T., Takio K., Tanaka K., van der Spek P.J., Bootsma D., Hoeijmakers J.H.J., Hanaoka F.
    EMBO J. 13:1831-1843(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-55, VARIANTS VAL-499 AND LYS-939.
  2. "The human XPC DNA repair gene: arrangement, splice site information content and influence of a single nucleotide polymorphism in a splice acceptor site on alternative splicing and function."
    Khan S.G., Muniz-Medina V., Shahlavi T., Baker C.C., Inui H., Ueda T., Emmert S., Schneider T.D., Kraemer K.H.
    Nucleic Acids Res. 30:3624-3631(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-499 AND LYS-939, ALTERNATIVE SPLICING.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Fetal brain.
  4. NIEHS SNPs program
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-16; PHE-48; ARG-86; GLN-314; HIS-492; VAL-499; ILE-513; GLU-632; HIS-671; MET-689; GLN-928 AND LYS-939.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Hippocampus.
  6. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Testis.
  8. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-940 (ISOFORM 1).
    Tissue: Liver.
  9. "Expression cloning of a human DNA repair gene involved in Xeroderma pigmentosum group C."
    Legerski R.J., Peterson C.A.
    Nature 359:70-73(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 119-940 (ISOFORM 1).
  10. "XPC and human homologs of RAD23: intracellular localization and relationship to other nucleotide excision repair complexes."
    van der Spek P.J., Eker A., Rademakers S., Visser C., Sugasawa K., Masutani C., Hanaoka F., Bootsma D., Hoeijmakers J.H.
    Nucleic Acids Res. 24:2551-2559(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  11. "Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity."
    Sugasawa K., Ng J.M., Masutani C., Maekawa T., Uchida A., van der Spek P.J., Eker A.P., Rademakers S., Visser C., Aboussekhra A., Wood R.D., Hanaoka F., Bootsma D., Hoeijmakers J.H.
    Mol. Cell. Biol. 17:6924-6931(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD23A.
  12. "Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair."
    Sugasawa K., Ng J.M., Masutani C., Iwai S., van der Spek P.J., Eker A.P., Hanaoka F., Bootsma D., Hoeijmakers J.H.
    Mol. Cell 2:223-232(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE XPC COMPLEX.
  13. "The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA."
    Yokoi M., Masutani C., Maekawa T., Sugasawa K., Ohkuma Y., Hanaoka F.
    J. Biol. Chem. 275:9870-9875(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CCNH; GTF2H1 AND ERCC3.
  14. "Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites."
    Batty D., Rapic'-Otrin V., Levine A.S., Wood R.D.
    J. Mol. Biol. 300:275-290(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE XPC COMPLEX.
  15. "Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair."
    Araki M., Masutani C., Takemura M., Uchida A., Sugasawa K., Kondoh J., Ohkuma Y., Hanaoka F.
    J. Biol. Chem. 276:18665-18672(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CETN2 AND RAD23B, SUBCELLULAR LOCATION, CHARACTERIZATION OF THE XPC COMPLEX.
  16. "A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex."
    Sugasawa K., Shimizu Y., Iwai S., Hanaoka F.
    DNA Repair 1:95-107(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE XPC COMPLEX.
  17. "The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH."
    Uchida A., Sugasawa K., Masutani C., Dohmae N., Araki M., Yokoi M., Ohkuma Y., Hanaoka F.
    DNA Repair 1:449-461(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, INTERACTION WITH RAD23B; ERCC2 AND GTF2H1.
  18. Cited for: FUNCTION OF THE XPC COMPLEX.
  19. "Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase."
    Shimizu Y., Iwai S., Hanaoka F., Sugasawa K.
    EMBO J. 22:164-173(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TDG.
  20. "UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex."
    Sugasawa K., Okuda Y., Saijo M., Nishi R., Matsuda N., Chu G., Mori T., Iwai S., Tanaka K., Tanaka K., Hanaoka F.
    Cell 121:387-400(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH DDB2.
  21. "Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein."
    Nishi R., Okuda Y., Watanabe E., Mori T., Iwai S., Masutani C., Sugasawa K., Hanaoka F.
    Mol. Cell. Biol. 25:5664-5674(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CETN2 AND RAD23B, MUTAGENESIS OF TRP-848; LEU-851 AND LEU-855.
  22. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  25. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; THR-169; SER-883; SER-884 AND SER-891, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  28. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  29. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-129; SER-883 AND SER-884, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; THR-876; SER-883 AND SER-884, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "In vivo destabilization and functional defects of the xeroderma pigmentosum C protein caused by a pathogenic missense mutation."
    Yasuda G., Nishi R., Watanabe E., Mori T., Iwai S., Orioli D., Stefanini M., Hanaoka F., Sugasawa K.
    Mol. Cell. Biol. 27:6606-6614(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT XP-C SER-690.
  32. "An aromatic sensor with aversion to damaged strands confers versatility to DNA repair."
    Maillard O., Solyom S., Naegeli H.
    PLoS Biol. 5:E79-E79(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT XP-C SER-690, MUTAGENESIS OF PHE-733.
  33. Cited for: SUBCELLULAR LOCATION.
  34. "Two-stage dynamic DNA quality check by xeroderma pigmentosum group C protein."
    Camenisch U., Trautlein D., Clement F.C., Fei J., Leitenstorfer A., Ferrando-May E., Naegeli H.
    EMBO J. 28:2387-2399(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF VARIANT OF VARIANT XP-C SER-690, MUTAGENESIS OF TRP-531; TRP-542; PHE-733 AND GLU-755.
  35. "Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning."
    Sugasawa K., Akagi J., Nishi R., Iwai S., Hanaoka F.
    Mol. Cell 36:642-653(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE XPC COMPLEX.
  36. "Dissection of the xeroderma pigmentosum group C protein function by site-directed mutagenesis."
    Clement F.C., Kaczmarek N., Mathieu N., Tomas M., Leitenstorfer A., Ferrando-May E., Naegeli H.
    Antioxid. Redox Signal. 14:2479-2490(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASN-754; PHE-756; PHE-797 AND PHE-799.
  37. "Photo-cross-linking of XPC-Rad23B to cisplatin-damaged DNA reveals contacts with both strands of the DNA duplex and spans the DNA adduct."
    Neher T.M., Rechkunova N.I., Lavrik O.I., Turchi J.J.
    Biochemistry 49:669-678(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE XPC COMPLEX.
  38. "Stimulation of DNA glycosylase activities by XPC Protein Complex: Roles of protein-protein interactions."
    Shimizu Y., Uchimura Y., Dohmae N., Saitoh H., Hanaoka F., Sugasawa K.
    J. Nucleic Acids 2010:455-459(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE XPC COMPLEX, INTERACTION WITH TDG AND SMUG1.
  39. "Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group C protein (XPC) from nuclear excision repair."
    Yang A., Miron S., Mouawad L., Duchambon P., Blouquit Y., Craescu C.T.
    Biochemistry 45:3653-3663(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 847-863 IN COMPLEX WITH CETN2.
  40. "The structure of the human centrin 2-xeroderma pigmentosum group C protein complex."
    Thompson J.R., Ryan Z.C., Salisbury J.L., Kumar R.
    J. Biol. Chem. 281:18746-18752(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 847-863 IN COMPLEX WITH CETN2.
  41. "Structural, thermodynamic, and cellular characterization of human centrin 2 interaction with xeroderma pigmentosum group C protein."
    Charbonnier J.B., Renaud E., Miron S., Le Du M.H., Blouquit Y., Duchambon P., Christova P., Shosheva A., Rose T., Angulo J.F., Craescu C.T.
    J. Mol. Biol. 373:1032-1046(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 847-863 IN COMPLEX WITH CETN2.
  42. "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-C.
  43. "Characterization of molecular defects in Xeroderma pigmentosum group C."
    Li L., Bales E.S., Peterson C.A., Legerski R.J.
    Nat. Genet. 5:413-417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XP-C HIS-334 AND VAL-697 INS.
  44. "Mutations in the XPC gene in families with xeroderma pigmentosum and consequences at the cell, protein, and transcript levels."
    Chavanne F., Broughton B.C., Pietra D., Nardo T., Browitt A., Lehmann A.R., Stefanini M.
    Cancer Res. 60:1974-1982(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XP-C SER-690.

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: October 29, 2014
This is version 154 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

External Data

Dasty 3