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P19447

- ERCC3_HUMAN

UniProt

P19447 - ERCC3_HUMAN

Protein

TFIIH basal transcription factor complex helicase XPB subunit

Gene

ERCC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    ATP-dependent 3'-5' DNA helicase, component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Acts by opening DNA either around the RNA transcription start site or the DNA damage.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi340 – 3478ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 3'-5' DNA helicase activity Source: UniProtKB
    2. ATPase activity Source: UniProtKB
    3. ATP binding Source: UniProtKB-KW
    4. ATP-dependent DNA helicase activity Source: Ensembl
    5. damaged DNA binding Source: UniProtKB
    6. dATP binding Source: Ensembl
    7. DNA binding Source: UniProtKB
    8. GTP binding Source: Ensembl
    9. peptide binding Source: Ensembl
    10. protein binding Source: UniProtKB
    11. protein C-terminus binding Source: UniProtKB
    12. protein N-terminus binding Source: UniProtKB
    13. RNA polymerase II carboxy-terminal domain kinase activity Source: Ensembl
    14. transcription factor binding Source: MGI

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: Reactome
    2. apoptotic process Source: UniProtKB
    3. DNA repair Source: UniProtKB
    4. DNA topological change Source: UniProtKB
    5. gene expression Source: Reactome
    6. hair cell differentiation Source: UniProtKB
    7. nucleotide-excision repair Source: UniProtKB
    8. nucleotide-excision repair, DNA damage removal Source: Reactome
    9. nucleotide-excision repair, DNA duplex unwinding Source: UniProtKB
    10. nucleotide-excision repair, DNA incision Source: UniProtKB
    11. positive regulation of apoptotic process Source: UniProtKB
    12. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    13. positive regulation of viral transcription Source: Reactome
    14. protein localization Source: UniProtKB
    15. regulation of mitotic cell cycle phase transition Source: UniProtKB
    16. response to hypoxia Source: Ensembl
    17. response to oxidative stress Source: UniProtKB
    18. response to UV Source: UniProtKB
    19. termination of RNA polymerase I transcription Source: Reactome
    20. transcription-coupled nucleotide-excision repair Source: UniProtKB
    21. transcription elongation from RNA polymerase II promoter Source: Reactome
    22. transcription elongation from RNA polymerase I promoter Source: Reactome
    23. transcription from RNA polymerase II promoter Source: UniProtKB
    24. transcription from RNA polymerase I promoter Source: Reactome
    25. transcription initiation from RNA polymerase II promoter Source: Reactome
    26. transcription initiation from RNA polymerase I promoter Source: Reactome
    27. UV protection Source: Ensembl
    28. viral process Source: Reactome

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair, Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
    REACT_1470. mRNA Capping.
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1913. RNA Polymerase I Promoter Escape.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_953. RNA Polymerase I Transcription Initiation.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TFIIH basal transcription factor complex helicase XPB subunit (EC:3.6.4.12)
    Alternative name(s):
    Basic transcription factor 2 89 kDa subunit
    Short name:
    BTF2 p89
    DNA excision repair protein ERCC-3
    DNA repair protein complementing XP-B cells
    TFIIH basal transcription factor complex 89 kDa subunit
    Short name:
    TFIIH 89 kDa subunit
    Short name:
    TFIIH p89
    Xeroderma pigmentosum group B-complementing protein
    Gene namesi
    Name:ERCC3
    Synonyms:XPB, XPBC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3435. ERCC3.

    Subcellular locationi

    GO - Cellular componenti

    1. holo TFIIH complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Xeroderma pigmentosum complementation group B (XP-B) [MIM:610651]: 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. Some XP-B patients present features of Cockayne syndrome, including cachectic dwarfism, pigmentary retinopathy, ataxia, decreased nerve conduction velocities. The phenotype combining xeroderma pigmentosum and Cockayne syndrome traits is referred to as XP-CS complex.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991F → S in XP-B; combined with features of Cockayne syndrome; mild. 2 Publications
    VAR_003632
    Trichothiodystrophy photosensitive (TTDP) [MIM:601675]: TTDP is an autosomal recessive disease characterized by sulfur-deficient brittle hair and nails, ichthyosis, mental retardation, impaired sexual development, abnormal facies and cutaneous photosensitivity correlated with a nucleotide excision repair (NER) defect. Neonates with trichothiodystrophy and ichthyosis are usually born with a collodion membrane. The severity of the ichthyosis after the membrane is shed is variable, ranging from a mild to severe lamellar ichthyotic phenotype. There are no reports of skin cancer associated with TTDP.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti119 – 1191T → P in TTDP; mild. 1 Publication
    VAR_008186

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi346 – 3461K → R: No transcriptional activity of the reconstituted TFIIH complex. 1 Publication
    Mutagenesisi782 – 7821Missing: Impairs protein folding. 1 Publication

    Keywords - Diseasei

    Cockayne syndrome, Deafness, Disease mutation, Dwarfism, Ichthyosis, Xeroderma pigmentosum

    Organism-specific databases

    MIMi601675. phenotype.
    610651. phenotype.
    Orphaneti33364. Trichothiodystrophy.
    276252. Xeroderma pigmentosum complementation group B.
    PharmGKBiPA27849.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 782782TFIIH basal transcription factor complex helicase XPB subunitPRO_0000101987Add
    BLAST

    Proteomic databases

    MaxQBiP19447.
    PaxDbiP19447.
    PRIDEiP19447.

    PTM databases

    PhosphoSiteiP19447.

    Expressioni

    Gene expression databases

    ArrayExpressiP19447.
    BgeeiP19447.
    CleanExiHS_ERCC3.
    GenevestigatoriP19447.

    Organism-specific databases

    HPAiCAB037153.
    HPA046077.

    Interactioni

    Subunit structurei

    One of the 6 subunits forming the core-TFIIH basal transcription factor which associates with the CAK complex composed of CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal transcription factor. Interacts with PUF60. Interacts with ATF7IP. Interacts with Epstein-Barr virus EBNA2.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PSMC5P621954EBI-1183307,EBI-357745
    Psmc5P621966EBI-1183307,EBI-357713From a different organism.
    RAD23BP547272EBI-1183307,EBI-954531
    XPCQ018312EBI-1183307,EBI-372610

    Protein-protein interaction databases

    BioGridi108383. 39 interactions.
    DIPiDIP-83N.
    IntActiP19447. 19 interactions.
    MINTiMINT-3009064.
    STRINGi9606.ENSP00000285398.

    Structurei

    Secondary structure

    1
    782
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi505 – 5128
    Helixi516 – 5249
    Helixi528 – 5303
    Helixi531 – 5366
    Helixi538 – 55215
    Turni553 – 5553
    Beta strandi558 – 5614
    Helixi565 – 57410
    Helixi586 – 59813
    Beta strandi604 – 6074
    Helixi609 – 6113
    Turni612 – 6143
    Beta strandi620 – 6267
    Helixi633 – 64311
    Beta strandi651 – 6544
    Beta strandi656 – 6649
    Helixi668 – 6703
    Helixi671 – 68212
    Beta strandi686 – 6927
    Helixi696 – 6983
    Helixi706 – 71813
    Helixi721 – 7244

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4ERNX-ray1.80A494-782[»]
    ProteinModelPortaliP19447.
    SMRiP19447. Positions 283-730.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini327 – 488162Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini542 – 702161Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi6 – 1813Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi441 – 4444DEVH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi20 – 289Asp/Glu-rich (acidic)
    Compositional biasi256 – 26510Asp/Glu-rich (acidic)
    Compositional biasi697 – 7004Asp/Glu-rich (acidic)
    Compositional biasi721 – 7288Asp/Glu-rich (acidic)

    Sequence similaritiesi

    Belongs to the helicase family. RAD25/XPB subfamily.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1061.
    HOGENOMiHOG000160172.
    HOVERGENiHBG051499.
    InParanoidiP19447.
    KOiK10843.
    OMAiAPSKHVH.
    OrthoDBiEOG7DNNTM.
    PhylomeDBiP19447.
    TreeFamiTF101233.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR001161. Helicase_Ercc3.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF04851. ResIII. 1 hit.
    [Graphical view]
    PRINTSiPR00851. XRODRMPGMNTB.
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    TIGRFAMsiTIGR00603. rad25. 1 hit.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19447-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKRDRADRD KKKSRKRHYE DEEDDEEDAP GNDPQEAVPS AAGKQVDESG    50
    TKVDEYGAKD YRLQMPLKDD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL 100
    VAIAEPVCRP THVHEYKLTA YSLYAAVSVG LQTSDITEYL RKLSKTGVPD 150
    GIMQFIKLCT VSYGKVKLVL KHNRYFVESC HPDVIQHLLQ DPVIRECRLR 200
    NSEGEATELI TETFTSKSAI SKTAESSGGP STSRVTDPQG KSDIPMDLFD 250
    FYEQMDKDEE EEEETQTVSF EVKQEMIEEL QKRCIHLEYP LLAEYDFRND 300
    SVNPDINIDL KPTAVLRPYQ EKSLRKMFGN GRARSGVIVL PCGAGKSLVG 350
    VTAACTVRKR CLVLGNSAVS VEQWKAQFKM WSTIDDSQIC RFTSDAKDKP 400
    IGCSVAISTY SMLGHTTKRS WEAERVMEWL KTQEWGLMIL DEVHTIPAKM 450
    FRRVLTIVQA HCKLGLTATL VREDDKIVDL NFLIGPKLYE ANWMELQNNG 500
    YIAKVQCAEV WCPMSPEFYR EYVAIKTKKR ILLYTMNPNK FRACQFLIKF 550
    HERRNDKIIV FADNVFALKE YAIRLNKPYI YGPTSQGERM QILQNFKHNP 600
    KINTIFISKV GDTSFDLPEA NVLIQISSHG GSRRQEAQRL GRVLRAKKGM 650
    VAEEYNAFFY SLVSQDTQEM AYSTKRQRFL VDQGYSFKVI TKLAGMEEED 700
    LAFSTKEEQQ QLLQKVLAAT DLDAEEEVVA GEFGSRSSQA SRRFGTMSSM 750
    SGADDTVYME YHSSRSKAPS KHVHPLFKRF RK 782
    Length:782
    Mass (Da):89,278
    Last modified:February 1, 1991 - v1
    Checksum:iF5F4D3A89A7DF826
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991F → S in XP-B; combined with features of Cockayne syndrome; mild. 2 Publications
    VAR_003632
    Natural varianti117 – 1171K → R.1 Publication
    Corresponds to variant rs1805161 [ dbSNP | Ensembl ].
    VAR_014766
    Natural varianti119 – 1191T → P in TTDP; mild. 1 Publication
    VAR_008186
    Natural varianti402 – 4021G → C.1 Publication
    Corresponds to variant rs1805162 [ dbSNP | Ensembl ].
    VAR_014767
    Natural varianti418 – 4181K → Q in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035942
    Natural varianti704 – 7041S → L.1 Publication
    Corresponds to variant rs4150521 [ dbSNP | Ensembl ].
    VAR_017294
    Natural varianti735 – 7351S → P.1 Publication
    Corresponds to variant rs4150522 [ dbSNP | Ensembl ].
    VAR_014344

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31899 mRNA. Translation: AAA52396.1.
    AY163769 Genomic DNA. Translation: AAN46739.1.
    AC110926 Genomic DNA. Translation: AAY15069.1.
    CH471103 Genomic DNA. Translation: EAW95313.1.
    BC008820 mRNA. Translation: AAH08820.1.
    CCDSiCCDS2144.1.
    PIRiA35661.
    RefSeqiNP_000113.1. NM_000122.1.
    UniGeneiHs.469872.

    Genome annotation databases

    EnsembliENST00000285398; ENSP00000285398; ENSG00000163161.
    GeneIDi2071.
    KEGGihsa:2071.
    UCSCiuc002toe.1. human.

    Polymorphism databases

    DMDMi119541.

    Keywords - Coding sequence diversityi

    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
    M31899 mRNA. Translation: AAA52396.1 .
    AY163769 Genomic DNA. Translation: AAN46739.1 .
    AC110926 Genomic DNA. Translation: AAY15069.1 .
    CH471103 Genomic DNA. Translation: EAW95313.1 .
    BC008820 mRNA. Translation: AAH08820.1 .
    CCDSi CCDS2144.1.
    PIRi A35661.
    RefSeqi NP_000113.1. NM_000122.1.
    UniGenei Hs.469872.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4ERN X-ray 1.80 A 494-782 [» ]
    ProteinModelPortali P19447.
    SMRi P19447. Positions 283-730.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108383. 39 interactions.
    DIPi DIP-83N.
    IntActi P19447. 19 interactions.
    MINTi MINT-3009064.
    STRINGi 9606.ENSP00000285398.

    PTM databases

    PhosphoSitei P19447.

    Polymorphism databases

    DMDMi 119541.

    Proteomic databases

    MaxQBi P19447.
    PaxDbi P19447.
    PRIDEi P19447.

    Protocols and materials databases

    DNASUi 2071.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000285398 ; ENSP00000285398 ; ENSG00000163161 .
    GeneIDi 2071.
    KEGGi hsa:2071.
    UCSCi uc002toe.1. human.

    Organism-specific databases

    CTDi 2071.
    GeneCardsi GC02M128014.
    GeneReviewsi ERCC3.
    HGNCi HGNC:3435. ERCC3.
    HPAi CAB037153.
    HPA046077.
    MIMi 133510. gene.
    601675. phenotype.
    610651. phenotype.
    neXtProti NX_P19447.
    Orphaneti 33364. Trichothiodystrophy.
    276252. Xeroderma pigmentosum complementation group B.
    PharmGKBi PA27849.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1061.
    HOGENOMi HOG000160172.
    HOVERGENi HBG051499.
    InParanoidi P19447.
    KOi K10843.
    OMAi APSKHVH.
    OrthoDBi EOG7DNNTM.
    PhylomeDBi P19447.
    TreeFami TF101233.

    Enzyme and pathway databases

    Reactomei REACT_1074. RNA Polymerase I Transcription Termination.
    REACT_1470. mRNA Capping.
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1913. RNA Polymerase I Promoter Escape.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_953. RNA Polymerase I Transcription Initiation.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Miscellaneous databases

    ChiTaRSi ERCC3. human.
    GeneWikii XPB.
    GenomeRNAii 2071.
    NextBioi 8425.
    PROi P19447.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19447.
    Bgeei P19447.
    CleanExi HS_ERCC3.
    Genevestigatori P19447.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR006935. Helicase/UvrB_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR001161. Helicase_Ercc3.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF04851. ResIII. 1 hit.
    [Graphical view ]
    PRINTSi PR00851. XRODRMPGMNTB.
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    TIGRFAMsi TIGR00603. rad25. 1 hit.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and biological characterization of the human excision repair gene ERCC-3."
      Weeda G., van Ham R.C.A., Masurel R., Westerveld A., Odijk H., de Wit J., Bootsma D., van der Eb A.J., Hoeijmakers J.H.J.
      Mol. Cell. Biol. 10:2570-2581(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A presumed DNA helicase encoded by ERCC-3 is involved in the human repair disorders Xeroderma pigmentosum and Cockayne's syndrome."
      Weeda G., van Ham R.C.A., Vermeulen W., Bootsma D., van der Eb A.J., Hoeijmakers J.H.J.
      Cell 62:777-791(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Structure and expression of the human XPBC/ERCC-3 gene involved in DNA repair disorders xeroderma pigmentosum and Cockayne's syndrome."
      Weeda G., Ma L., van Ham R.C.A., van der Eb A.J., Hoeijmakers J.H.J.
      Nucleic Acids Res. 19:6301-6308(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. NIEHS SNPs program
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-704 AND PRO-735.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. 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].
      Tissue: Placenta.
    8. "Correction of xeroderma pigmentosum repair defect by basal transcription factor BTF2 (TFIIH)."
      van Vuuren A.J., Vermeulen W., Ma L., Weeda G., Appeldoorn E., Jaspers N.G.J., van der Eb A.J., Bootsma D., Hoeijmakers J.H.J., Humbert S., Schaeffer L., Egly J.-M.
      EMBO J. 13:1645-1653(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION.
    9. "The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2."
      Tong X., Drapkin R., Reinberg D., Kieff E.
      Proc. Natl. Acad. Sci. U.S.A. 92:3259-3263(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EBV EBNA2.
    10. "Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
      Kershnar E., Wu S.-Y., Chiang C.-M.
      J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
    11. "Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7."
      Tirode F., Busso D., Coin F., Egly J.-M.
      Mol. Cell 3:87-95(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-346, FUNCTION.
    12. "The FBP interacting repressor targets TFIIH to inhibit activated transcription."
      Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D.
      Mol. Cell 5:331-341(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PUF60.
    13. "Defective interplay of activators and repressors with TFIH in xeroderma pigmentosum."
      Liu J., Akoulitchev S., Weber A., Ge H., Chuikov S., Libutti D., Wang X.W., Conaway J.W., Harris C.C., Conaway R.C., Reinberg D., Levens D.
      Cell 104:353-363(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PUF60.
    14. "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-B.
    15. "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity."
      Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M.
      J. Biol. Chem. 284:5165-5174(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF7IP.
    16. "Structure of the C-terminal half of human XPB helicase and the impact of the disease-causing mutation XP11BE."
      Hilario E., Li Y., Nobumori Y., Liu X., Fan L.
      Acta Crystallogr. D 69:237-246(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 494-782, MUTAGENESIS OF LYS-782.
    17. "Clinical heterogeneity within xeroderma pigmentosum associated with mutations in the DNA repair and transcription gene ERCC3."
      Vermeulen W., Scott R.J., Rodgers S., Mueller H.J., Cole J., Arlett C.F., Kleijer W.J., Bootsma D., Hoeijmakers J.H.J., Weeda G.
      Am. J. Hum. Genet. 54:191-200(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XP-B SER-99.
    18. "A mutation in the XPB/ERCC3 DNA repair transcription gene, associated with trichothiodystrophy."
      Weeda G., Eveno E., Donker I., Vermeulen W., Chevallier-Lagente O., Taieb A., Stary A., Hoeijmakers J.H.J., Mezzina M., Sarasin A.
      Am. J. Hum. Genet. 60:320-329(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TTDP PRO-119.
    19. "Identification of four single nucleotide polymorphisms in DNA repair genes: XPA and XPB (ERCC3) in Polish population."
      Butkiewicz D., Rusin M., Harris C.C., Chorazy M.
      Hum. Mutat. 15:577-578(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARG-117 AND CYS-402.
    20. "Phenotypic heterogeneity in the XPB DNA helicase gene (ERCC3): xeroderma pigmentosum without and with Cockayne syndrome."
      Oh K.-S., Khan S.G., Jaspers N.G.J., Raams A., Ueda T., Lehmann A., Friedmann P.S., Emmert S., Gratchev A., Lachlan K., Lucassan A., Baker C.C., Kraemer K.H.
      Hum. Mutat. 27:1092-1103(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XP-B SER-99.
    21. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-418.

    Entry informationi

    Entry nameiERCC3_HUMAN
    AccessioniPrimary (citable) accession number: P19447
    Secondary accession number(s): Q53QM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 171 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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