DNA repair protein complementing XP-C cells

Contribute

Send feedback

Reviewed, UniProtKB/Swiss-Prot Q01831 (XPC_HUMAN)

Last modified November 25, 2008. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    DNA repair protein complementing XP-C cells
Alternative name(s):
    Xeroderma pigmentosum group C-complementing protein
    p125

Gene names

Name:	XPC
Synonyms:	XPCC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	940 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes.
Subunit structure	Heterodimer of a 125 kDa subunit (p125) and of a 58 kDa subunit (p58). Interacts with CETN2.
Subcellular location	NucleusProbable.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR.
Involvement in disease	Defects in XPC are a cause of xeroderma pigmentosum complementation group C (XP-C) [MIM:278720]; also known as xeroderma pigmentosum III (XP3). XP-C is a rare human autosomal recessive disease characterized by solar sensitivity, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities.
Sequence similarities	Belongs to the XPC family.

Hide | Top

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Disease	Disease mutation Xeroderma pigmentosum
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	nucleotide-excision repair, DNA damage removal Inferred from Experiment. Source: Reactome
Cellular component	nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	damaged DNA binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct single-stranded DNA binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BGLF4	Q777D1	7	EBI-372610,EBI-1630636	From a different organism.
LSM3	P62310	1	EBI-372610,EBI-348239

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 940

939

DNA repair protein complementing XP-C cells

PRO_0000218293

Regions

Motif

390 – 395

Nuclear localization signal Potential

Compositional bias

30 – 177

148

Glu-rich (acidic)

Compositional bias

30 – 34

Poly-Glu

Compositional bias

124 – 130

Poly-Glu

Compositional bias

359 – 395

Lys-rich (basic)

Compositional bias

408 – 431

Arg/Lys-rich (basic)

Compositional bias

432 – 461

Asp/Glu-rich (acidic)

Compositional bias

466 – 493

Arg/Lys-rich (basic)

Compositional bias

501 – 507

Poly-Ser

Amino acid modifications

Modified residue

Phosphoserine

Modified residue

169

Phosphothreonine

Modified residue

347

Phosphoserine

Modified residue

351

Phosphoserine

Modified residue

883

Phosphoserine

Modified residue

884

Phosphoserine

Modified residue

891

Phosphoserine

Modified residue

892

Phosphoserine

Natural variations

Natural variant

L → V

VAR_018894

Natural variant

L → F

VAR_018895

Natural variant

K → R

VAR_018896

Natural variant

314

R → Q

VAR_018897

Natural variant

334

P → H in XP-C; severe.

VAR_005846

Natural variant

492

R → H

VAR_018898

Natural variant

499

V → A

VAR_018899

Natural variant

513

M → I

VAR_018900

Natural variant

632

Q → E

VAR_018901

Natural variant

671

R → H

VAR_018902

Natural variant

689

T → M

VAR_018903

Natural variant

697

V → VV in XP-C; mild.

VAR_005847

Natural variant

928

K → Q

VAR_018904

Natural variant

939

K → Q

VAR_005848

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q01831-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F557E3C619C1E898
Show »

FASTA

940

105,981

        10         20         30         40         50         60 
MARKRAAGGE PRGRELRSQK SKAKSKARRE EEEEDAFEDE KPPKKSLLSK VSQGKRKRGC 

        70         80         90        100        110        120 
SHPGGSADGP AKKKVAKVTV KSENLKVIKD EALSDGDDLR DFPSDLKKAH HLKRGATMNE 

       130        140        150        160        170        180 
DSNEEEEESE NDWEEVEELS EPVLGDVRES TAFSRSLLPV KPVEIEIETP EQAKTRERSE 

       190        200        210        220        230        240 
KIKLEFETYL RRAMKRFNKG VHEDTHKVHL LCLLANGFYR NNICSQPDLH AIGLSIIPAR 

       250        260        270        280        290        300 
FTRVLPRDVD TYYLSNLVKW FIGTFTVNAE LSASEQDNLQ TTLERRFAIY SARDDEELVH 

       310        320        330        340        350        360 
IFLLILRALQ LLTRLVLSLQ PIPLKSATAK GKKPSKERLT ADPGGSSETS SQVLENHTKP 

       370        380        390        400        410        420 
KTSKGTKQEE TFAKGTCRPS AKGKRNKGGR KKRSKPSSSE EDEGPGDKQE KATQRRPHGR 

       430        440        450        460        470        480 
ERRVASRVSY KEESGSDEAG SGSDFELSSG EASDPSDEDS EPGPPKQRKA PAPQRTKAGS 

       490        500        510        520        530        540 
KSASRTHRGS HRKDPSLPVA SSSSSSSKRG KKMCSDGEKA EKRSIAGIDQ WLEVFCEQEE 

       550        560        570        580        590        600 
KWVCVDCVHG VVGQPLTCYK YATKPMTYVV GIDSDGWVRD VTQRYDPVWM TVTRKCRVDA 

       610        620        630        640        650        660 
EWWAETLRPY QSPFMDREKK EDLEFQAKHM DQPLPTAIGL YKNHPLYALK RHLLKYEAIY 

       670        680        690        700        710        720 
PETAAILGYC RGEAVYSRDC VHTLHSRDTW LKKARVVRLG EVPYKMVKGF SNRARKARLA 

       730        740        750        760        770        780 
EPQLREENDL GLFGYWQTEE YQPPVAVDGK VPRNEFGNVY LFLPSMMPIG CVQLNLPNLH 

       790        800        810        820        830        840 
RVARKLDIDC VQAITGFDFH GGYSHPVTDG YIVCEEFKDV LLTAWENEQA VIERKEKEKK 

       850        860        870        880        890        900 
EKRALGNWKL LAKGLLIRER LKRRYGPKSE AAAPHTDAGG GLSSDEEEGT SSQAEAARIL 

       910        920        930        940 
AASWPQNRED EEKQKLKGGP KKTKREKKAA ASHLFPFEKL

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8168482] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-55.
[2]	"Splicing abnormalities in the xeroderma pigmentosum group C (XPC) gene." Khan S.G., Schneider T.D., Kraemer K.H. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A. 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; ALA-499; ILE-513; GLU-632; HIS-671; MET-689; GLN-928 AND GLN-939.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-499. Tissue: Testis.
[5]	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, VARIANTS ALA-499 AND GLN-939. Tissue: Liver.
[6]	"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: 1522891] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 119-940, VARIANT ALA-499.
[7]	Erratum Legerski R.J., Peterson C.A. Nature 360:610-610(1992) [PubMed: 1461286] [Abstract]
[8]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"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: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND SER-884, MASS SPECTROMETRY.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-351; SER-883; SER-884 AND SER-892, MASS SPECTROMETRY.
[11]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND SER-884, MASS SPECTROMETRY.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; THR-169; SER-883; SER-884 AND SER-891, MASS SPECTROMETRY.
[13]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND SER-884, MASS SPECTROMETRY. Tissue: Liver.
[14]	"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: 16533048] [Abstract] Cited for: STRUCTURE BY NMR OF 847-863 IN COMPLEX WITH CETN2.
[15]	"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: 16627479] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 847-863 IN COMPLEX WITH CETN2.
[16]	"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: 10447254] [Abstract] Cited for: REVIEW ON VARIANTS XP-C.
[17]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND SER-884, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"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: 8298653] [Abstract] Cited for: VARIANTS XP-C HIS-334 AND VAL-697 INS, VARIANT GLN-939.
+	Additional computationally mapped references.

Hide | Top

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Allelic variations of the XP genes

Hide | Top

Cross-references

Sequence databases

D21089 mRNA. Translation: BAA04651.1.
AF261901

AF261900 Genomic DNA. Translation: AAF87574.1.
AY131066 Genomic DNA. Translation: AAM77801.1.
BC016620 mRNA. Translation: AAH16620.1.
AK222844 mRNA. Translation: BAD96564.1.
X65024 mRNA. Translation: CAA46158.1.

PIR

S44345.

RefSeq

NP_004619.2.

UniGene

Hs.475538

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A4J	NMR	-	B	847-863	[»]
2GGM	X-ray	2.35	C/D	847-863	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q01831.

PTM databases

PhosphoSite

Q01831.

Polymorphism databases

NIEHS-SNPs

Search...

Proteomic databases

PeptideAtlas

Q01831.

Genome annotation databases

Ensembl

ENSG00000154767. Homo sapiens. [Contig view]

GeneID

7508.

KEGG

hsa:7508.

Organism-specific databases

H-InvDB

HIX0003081.

HGNC

HGNC:12816. XPC.

HPA

CAB009932.

MIM

278720. gene+phenotype.

Orphanet

910. Xeroderma pigmentosum.

PharmGKB

PA37413.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q01831.

HOVERGEN

Q01831.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

CleanEx

HS_XPC.

GermOnline

ENSG00000154767. Homo sapiens.

Family and domain databases

InterPro

IPR004583. Rad4.
[Graphical view]

PANTHER

PTHR12135. Rad4. 1 hit.

Pfam

PF03835. Rad4. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00605. rad4. 1 hit.

ProtoNet

Search...

Other Resources

LinkHub

Q01831.

NextBio

29391.

SOURCE

Search...

Hide | Top

Entry information

Entry name

XPC_HUMAN

Accession

Primary (citable) accession number: Q01831
Secondary accession number(s): Q53GT7, Q96AX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents