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Q01831 (XPC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein complementing XP-C cells
Alternative name(s):
Xeroderma pigmentosum group C-complementing protein
p125
Gene names
Name:XPC
Synonyms:XPCC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length940 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40

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. Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40

Subunit structure

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. Ref.10 Ref.11 Ref.13 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21 Ref.40

Subcellular location

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. Ref.10 Ref.15 Ref.33

Post-translational modification

Ubiquitinated upon UV irradiation; the ubiquitination requires the UV-DDB complex, appears to be reversible and does not serve as a signal for degradation. Ref.20

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.32 Ref.36 Ref.45 Ref.46

Sequence similarities

Belongs to the XPC family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Xeroderma pigmentosum
   LigandDNA-binding
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

intra-S DNA damage checkpoint

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair

Inferred from direct assay Ref.1Ref.12. Source: UniProtKB

nucleotide-excision repair, DNA damage recognition

Inferred from direct assay Ref.14Ref.37. Source: UniProtKB

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

regulation of mitotic cell cycle phase transition

Inferred from mutant phenotype PubMed 17088560. Source: UniProtKB

response to UV-B

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentXPC complex

Inferred from direct assay Ref.15. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.33. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.33. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionbubble DNA binding

Traceable author statement Ref.37. Source: UniProtKB

damaged DNA binding

Inferred from direct assay Ref.14Ref.16. Source: UniProtKB

loop DNA binding

Traceable author statement Ref.37. Source: UniProtKB

single-stranded DNA binding

Inferred from direct assay Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01831-1)

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.
Isoform 2 (identifier: Q01831-2)

The sequence of this isoform differs from the canonical sequence as follows:
     136-172: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 940939DNA repair protein complementing XP-C cells
PRO_0000218293

Regions

Region496 – 734239Interaction with RAD23B
Region607 – 766160Minimal sensor domain involved in damage recognition
Region607 – 741135DNA-binding; preference for heteroduplex DNA
Region767 – 83165DNA-binding; preference for single stranded DNA; required for formation of stable nucleoprotein complex
Region816 – 940125Interaction with ERCC2 and GTF2H1
Region847 – 86620Interaction with CETN2
Motif390 – 3956Nuclear localization signal Potential
Compositional bias30 – 177148Glu-rich (acidic)
Compositional bias30 – 345Poly-Glu
Compositional bias124 – 1307Poly-Glu
Compositional bias359 – 39537Lys-rich (basic)
Compositional bias408 – 43124Arg/Lys-rich (basic)
Compositional bias432 – 46130Asp/Glu-rich (acidic)
Compositional bias466 – 49328Arg/Lys-rich (basic)
Compositional bias501 – 5077Poly-Ser

Amino acid modifications

Modified residue941Phosphoserine Ref.22 Ref.26 Ref.29 Ref.30
Modified residue1291Phosphoserine Ref.22 Ref.29
Modified residue1691Phosphothreonine Ref.26
Modified residue8761Phosphothreonine Ref.30
Modified residue8831Phosphoserine Ref.26 Ref.29 Ref.30
Modified residue8841Phosphoserine Ref.26 Ref.29 Ref.30
Modified residue8911Phosphoserine Ref.26

Natural variations

Alternative sequence136 – 17237Missing in isoform 2.
VSP_046344
Natural variant161L → V. Ref.3
Corresponds to variant rs1870134 [ dbSNP | Ensembl ].
VAR_018894
Natural variant481L → F. Ref.3
Corresponds to variant rs3731062 [ dbSNP | Ensembl ].
VAR_018895
Natural variant861K → R. Ref.3
Corresponds to variant rs3731063 [ dbSNP | Ensembl ].
VAR_018896
Natural variant2871F → C.
Corresponds to variant rs35629274 [ dbSNP | Ensembl ].
VAR_057475
Natural variant3141R → Q. Ref.3
Corresponds to variant rs3731126 [ dbSNP | Ensembl ].
VAR_018897
Natural variant3341P → H in XP-C; severe. Ref.45
Corresponds to variant rs74737358 [ dbSNP | Ensembl ].
VAR_005846
Natural variant4921R → H. Ref.3
Corresponds to variant rs2227999 [ dbSNP | Ensembl ].
VAR_018898
Natural variant4991A → V. Ref.1 Ref.2 Ref.3
Corresponds to variant rs2228000 [ dbSNP | Ensembl ].
VAR_018899
Natural variant5111K → Q.
Corresponds to variant rs6413541 [ dbSNP | Ensembl ].
VAR_059963
Natural variant5131M → I. Ref.3
Corresponds to variant rs3731130 [ dbSNP | Ensembl ].
VAR_018900
Natural variant5141C → S.
Corresponds to variant rs3731130 [ dbSNP | Ensembl ].
VAR_057476
Natural variant6321Q → E. Ref.3
Corresponds to variant rs3731139 [ dbSNP | Ensembl ].
VAR_018901
Natural variant6711R → H. Ref.3
Corresponds to variant rs3731140 [ dbSNP | Ensembl ].
VAR_018902
Natural variant6891T → M. Ref.3
Corresponds to variant rs3731152 [ dbSNP | Ensembl ].
VAR_018903
Natural variant6901W → S in XP-C; diminishes repair activity and impairs DNA binding. Ref.31 Ref.32 Ref.36 Ref.46
VAR_064039
Natural variant6971V → VV in XP-C; mild. Ref.45
VAR_005847
Natural variant9281K → Q. Ref.3
Corresponds to variant rs3731177 [ dbSNP | Ensembl ].
VAR_018904
Natural variant9391Q → K. Ref.1 Ref.2 Ref.3
Corresponds to variant rs2228001 [ dbSNP | Ensembl ].
VAR_005848

Experimental info

Mutagenesis5311W → A: Slightly diminishes repair activity and sligtly impairs DNA binding. Ref.36
Mutagenesis5421W → A: Slightly diminishes repair activity and sligtly impairs DNA binding. Ref.36
Mutagenesis7331F → A: Diminishes repair activity and impairs DNA binding. Ref.32 Ref.36
Mutagenesis7541N → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci. Ref.38
Mutagenesis7551E → K: Reduces nuclear mobility and impairs repair activity. Ref.36
Mutagenesis7561F → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci. Ref.38
Mutagenesis7971F → 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. Ref.38
Mutagenesis7991F → 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. Ref.38
Mutagenesis8481W → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-851 and A-855. Ref.21
Mutagenesis8511L → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-848 and A-855. Ref.21
Mutagenesis8551L → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-848 and A-851. Ref.21
Sequence conflict1351E → Q in BAG58555. Ref.4
Sequence conflict4891G → E in BAG58555. Ref.4

Secondary structure

... 940
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: 2F8C80D43FAA1256

FASTA940105,953
        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 HRKDPSLPAA 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 ASHLFPFEQL 

« Hide

Isoform 2 [UniParc].

Checksum: AF2F96DDCC4DB78E
Show »

FASTA903101,847

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-55, VARIANTS VAL-499 AND LYS-939.
[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], VARIANTS VAL-499 AND LYS-939.
[3]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.
[4]"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. expand/collapse author list , 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.
[5]"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. expand/collapse author list , 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].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[7]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.
[8]"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).
[9]Erratum
Legerski R.J., Peterson C.A.
Nature 360:610-610(1992) [PubMed] [Europe PMC] [Abstract]
[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]"DNA bending by the human damage recognition complex XPC-HR23B."
Janicijevic A., Sugasawa K., Shimizu Y., Hanaoka F., Wijgers N., Djurica M., Hoeijmakers J.H., Wyman C.
DNA Repair 2:325-336(2003) [PubMed] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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]"Versatile DNA damage detection by the global genome nucleotide excision repair protein XPC."
Hoogstraten D., Bergink S., Ng J.M., Verbiest V.H., Luijsterburg M.S., Geverts B., Raams A., Dinant C., Hoeijmakers J.H., Vermeulen W., Houtsmuller A.B.
J. Cell Sci. 121:2850-2859(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[34]Erratum
Hoogstraten D., Bergink S., Ng J.M., Verbiest V.H., Luijsterburg M.S., Geverts B., Raams A., Dinant C., Hoeijmakers J.H., Vermeulen W., Houtsmuller A.B.
J. Cell Sci. 121:2972-2972(2008)
[35]Erratum
Hoogstraten D., Bergink S., Ng J.M., Verbiest V.H., Luijsterburg M.S., Geverts B., Raams A., Dinant C., Hoeijmakers J.H., Vermeulen W., Houtsmuller A.B.
J. Cell Sci. 121:3991-3991(2008)
[36]"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.
[37]"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.
[38]"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.
[39]"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.
[40]"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.
[41]"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.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D21089 mRNA. Translation: BAA04651.1.
AF261901 expand/collapse EMBL AC list , AF261892, AF261893, AF261894, AF261895, AF261896, AF261897, AF261898, AF261899, AF261900 Genomic DNA. Translation: AAF87574.1.
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.
PIRS44345.
RefSeqNP_001139241.1. NM_001145769.1.
NP_004619.3. NM_004628.4.
UniGeneHs.475538.
Hs.739296.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A4JNMR-B847-863[»]
2GGMX-ray2.35C/D847-863[»]
2OBHX-ray1.80C/D847-863[»]
ProteinModelPortalQ01831.
SMRQ01831. Positions 531-824.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113345. 33 interactions.
DIPDIP-31225N.
IntActQ01831. 19 interactions.
MINTMINT-105410.
STRING9606.ENSP00000285021.

PTM databases

PhosphoSiteQ01831.

Polymorphism databases

DMDM296453081.

Proteomic databases

PaxDbQ01831.
PeptideAtlasQ01831.
PRIDEQ01831.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285021; ENSP00000285021; ENSG00000154767. [Q01831-1]
ENST00000449060; ENSP00000404002; ENSG00000154767. [Q01831-2]
GeneID7508.
KEGGhsa:7508.
UCSCuc011ave.2. human. [Q01831-1]

Organism-specific databases

CTD7508.
GeneCardsGC03M014161.
HGNCHGNC:12816. XPC.
HPACAB009932.
HPA035707.
MIM278720. phenotype.
613208. gene.
neXtProtNX_Q01831.
Orphanet276255. Xeroderma pigmentosum complementation group C.
PharmGKBPA37413.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5535.
HOGENOMHOG000124671.
HOVERGENHBG000407.
InParanoidQ01831.
KOK10838.
OMAPQRTKAG.
OrthoDBEOG7BW0J2.
PhylomeDBQ01831.
TreeFamTF101242.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ01831.
BgeeQ01831.
CleanExHS_XPC.
GenevestigatorQ01831.

Family and domain databases

InterProIPR004583. 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]
PANTHERPTHR12135. PTHR12135. 1 hit.
PfamPF10403. BHD_1. 1 hit.
PF10404. BHD_2. 1 hit.
PF10405. BHD_3. 1 hit.
PF03835. Rad4. 1 hit.
[Graphical view]
SMARTSM01030. BHD_1. 1 hit.
SM01031. BHD_2. 1 hit.
SM01032. BHD_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00605. rad4. 1 hit.
ProtoNetSearch...

Other

ChiTaRSXPC. human.
EvolutionaryTraceQ01831.
GeneWikiXPC_(gene).
GenomeRNAi7508.
NextBio29391.
PROQ01831.
SOURCESearch...

Entry information

Entry nameXPC_HUMAN
AccessionPrimary (citable) accession number: Q01831
Secondary accession number(s): B4DIP3 expand/collapse secondary AC list , E9PH69, Q53GT7, Q96AX0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

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