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Q01831

- XPC_HUMAN

UniProt

Q01831 - XPC_HUMAN

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
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 4 (18 May 2010)
      Previous versions | rss
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    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. protein binding Source: IntAct
    5. 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

    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

    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

    ArrayExpressiQ01831.
    BgeeiQ01831.
    CleanExiHS_XPC.
    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. 35 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.
    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

    MARKRAAGGE PRGRELRSQK SKAKSKARRE EEEEDAFEDE KPPKKSLLSK    50
    VSQGKRKRGC SHPGGSADGP AKKKVAKVTV KSENLKVIKD EALSDGDDLR 100
    DFPSDLKKAH HLKRGATMNE DSNEEEEESE NDWEEVEELS EPVLGDVRES 150
    TAFSRSLLPV KPVEIEIETP EQAKTRERSE KIKLEFETYL RRAMKRFNKG 200
    VHEDTHKVHL LCLLANGFYR NNICSQPDLH AIGLSIIPAR FTRVLPRDVD 250
    TYYLSNLVKW FIGTFTVNAE LSASEQDNLQ TTLERRFAIY SARDDEELVH 300
    IFLLILRALQ LLTRLVLSLQ PIPLKSATAK GKKPSKERLT ADPGGSSETS 350
    SQVLENHTKP KTSKGTKQEE TFAKGTCRPS AKGKRNKGGR KKRSKPSSSE 400
    EDEGPGDKQE KATQRRPHGR ERRVASRVSY KEESGSDEAG SGSDFELSSG 450
    EASDPSDEDS EPGPPKQRKA PAPQRTKAGS KSASRTHRGS HRKDPSLPAA 500
    SSSSSSSKRG KKMCSDGEKA EKRSIAGIDQ WLEVFCEQEE KWVCVDCVHG 550
    VVGQPLTCYK YATKPMTYVV GIDSDGWVRD VTQRYDPVWM TVTRKCRVDA 600
    EWWAETLRPY QSPFMDREKK EDLEFQAKHM DQPLPTAIGL YKNHPLYALK 650
    RHLLKYEAIY PETAAILGYC RGEAVYSRDC VHTLHSRDTW LKKARVVRLG 700
    EVPYKMVKGF SNRARKARLA EPQLREENDL GLFGYWQTEE YQPPVAVDGK 750
    VPRNEFGNVY LFLPSMMPIG CVQLNLPNLH RVARKLDIDC VQAITGFDFH 800
    GGYSHPVTDG YIVCEEFKDV LLTAWENEQA VIERKEKEKK EKRALGNWKL 850
    LAKGLLIRER LKRRYGPKSE AAAPHTDAGG GLSSDEEEGT SSQAEAARIL 900
    AASWPQNRED EEKQKLKGGP KKTKREKKAA ASHLFPFEQL 940
    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]
    CCDS46764.1. [Q01831-2]
    PIRiS44345.
    RefSeqiNP_001139241.1. NM_001145769.1. [Q01831-2]
    NP_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 ]
    CCDS46764.1. [Q01831-2 ]
    PIRi S44345.
    RefSeqi NP_001139241.1. NM_001145769.1. [Q01831-2 ]
    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. 35 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.
    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

    ArrayExpressi Q01831.
    Bgeei Q01831.
    CleanExi HS_XPC.
    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

    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. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
      Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.
      , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
      Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
      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 1, 2014
    This is version 153 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