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P19447

- ERCC3_HUMAN

UniProt

P19447 - ERCC3_HUMAN

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Protein
TFIIH basal transcription factor complex helicase XPB subunit
Gene
ERCC3, XPB, XPBC
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 3478ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 subunit
PRO_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. 15 interactions.
MINTiMINT-3009064.
STRINGi9606.ENSP00000285398.

Structurei

Secondary structure

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini327 – 488162Helicase ATP-binding
Add
BLAST
Domaini542 – 702161Helicase C-terminal
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi6 – 1813Nuclear localization signal Reviewed prediction
Add
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

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. 15 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 170 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

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