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P19447 (ERCC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. Feed History...

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

Names and origin

Protein namesRecommended 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 names
Name:ERCC3
Synonyms:XPB, XPBC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length782 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.11

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.9 Ref.10 Ref.12 Ref.13 Ref.15

Subcellular location

Nucleus.

Involvement in disease

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. Ref.17 Ref.20

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. Ref.18

Sequence similarities

Belongs to the helicase family. RAD25/XPB subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseCockayne syndrome
Deafness
Disease mutation
Dwarfism
Ichthyosis
Xeroderma pigmentosum
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

DNA repair

Inferred from mutant phenotype Ref.2. Source: UniProtKB

DNA topological change

Inferred from mutant phenotype PubMed 8663148. Source: UniProtKB

UV protection

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from mutant phenotype PubMed 8675009. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

hair cell differentiation

Inferred from mutant phenotype PubMed 11335038. Source: UniProtKB

nucleotide-excision repair

Inferred from mutant phenotype PubMed 17509950. Source: UniProtKB

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA duplex unwinding

Inferred from mutant phenotype PubMed 17466626. Source: UniProtKB

nucleotide-excision repair, DNA incision

Inferred from mutant phenotype PubMed 17466626PubMed 8692841. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay PubMed 16914395. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 8692841. Source: UniProtKB

positive regulation of viral transcription

Traceable author statement. Source: Reactome

protein localization

Inferred from mutant phenotype PubMed 17509950. Source: UniProtKB

regulation of mitotic cell cycle phase transition

Inferred from mutant phenotype PubMed 17088560. Source: UniProtKB

response to UV

Inferred from mutant phenotype PubMed 17509950. Source: UniProtKB

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from mutant phenotype PubMed 17614221. Source: UniProtKB

termination of RNA polymerase I transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.10. Source: UniProtKB

transcription initiation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Inferred from direct assay PubMed 8663148. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentSSL2-core TFIIH complex

Inferred from electronic annotation. Source: Ensembl

holo TFIIH complex

Inferred from direct assay PubMed 8692842Ref.10. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement PubMed 8663148. Source: UniProtKB

   Molecular_function3'-5' DNA helicase activity

Inferred from direct assay PubMed 17466626. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Inferred from electronic annotation. Source: Ensembl

ATPase activity

Inferred from direct assay PubMed 17466626. Source: UniProtKB

DNA binding

Traceable author statement PubMed 8663148. Source: UniProtKB

GTP binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: Ensembl

dATP binding

Inferred from electronic annotation. Source: Ensembl

damaged DNA binding

Non-traceable author statement Ref.2. Source: UniProtKB

peptide binding

Inferred from electronic annotation. Source: Ensembl

protein C-terminus binding

Inferred from physical interaction PubMed 10801852PubMed 17466626. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 8652557. Source: UniProtKB

transcription factor binding

Inferred from direct assay PubMed 9173976. Source: MGI

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 782782TFIIH basal transcription factor complex helicase XPB subunit
PRO_0000101987

Regions

Domain327 – 488162Helicase ATP-binding
Domain542 – 702161Helicase C-terminal
Nucleotide binding340 – 3478ATP By similarity
Motif6 – 1813Nuclear localization signal Potential
Motif441 – 4444DEVH box
Compositional bias20 – 289Asp/Glu-rich (acidic)
Compositional bias256 – 26510Asp/Glu-rich (acidic)
Compositional bias697 – 7004Asp/Glu-rich (acidic)
Compositional bias721 – 7288Asp/Glu-rich (acidic)

Natural variations

Natural variant991F → S in XP-B; combined with features of Cockayne syndrome; mild. Ref.17 Ref.20
VAR_003632
Natural variant1171K → R. Ref.19
Corresponds to variant rs1805161 [ dbSNP | Ensembl ].
VAR_014766
Natural variant1191T → P in TTDP; mild. Ref.18
VAR_008186
Natural variant4021G → C. Ref.19
Corresponds to variant rs1805162 [ dbSNP | Ensembl ].
VAR_014767
Natural variant4181K → Q in a breast cancer sample; somatic mutation. Ref.21
VAR_035942
Natural variant7041S → L. Ref.4
Corresponds to variant rs4150521 [ dbSNP | Ensembl ].
VAR_017294
Natural variant7351S → P. Ref.4
Corresponds to variant rs4150522 [ dbSNP | Ensembl ].
VAR_014344

Experimental info

Mutagenesis3461K → R: No transcriptional activity of the reconstituted TFIIH complex. Ref.11
Mutagenesis7821Missing: Impairs protein folding. Ref.16

Secondary structure

......................................... 782
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19447 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: F5F4D3A89A7DF826

FASTA78289,278
        10         20         30         40         50         60 
MGKRDRADRD KKKSRKRHYE DEEDDEEDAP GNDPQEAVPS AAGKQVDESG TKVDEYGAKD 

        70         80         90        100        110        120 
YRLQMPLKDD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL VAIAEPVCRP THVHEYKLTA 

       130        140        150        160        170        180 
YSLYAAVSVG LQTSDITEYL RKLSKTGVPD GIMQFIKLCT VSYGKVKLVL KHNRYFVESC 

       190        200        210        220        230        240 
HPDVIQHLLQ DPVIRECRLR NSEGEATELI TETFTSKSAI SKTAESSGGP STSRVTDPQG 

       250        260        270        280        290        300 
KSDIPMDLFD FYEQMDKDEE EEEETQTVSF EVKQEMIEEL QKRCIHLEYP LLAEYDFRND 

       310        320        330        340        350        360 
SVNPDINIDL KPTAVLRPYQ EKSLRKMFGN GRARSGVIVL PCGAGKSLVG VTAACTVRKR 

       370        380        390        400        410        420 
CLVLGNSAVS VEQWKAQFKM WSTIDDSQIC RFTSDAKDKP IGCSVAISTY SMLGHTTKRS 

       430        440        450        460        470        480 
WEAERVMEWL KTQEWGLMIL DEVHTIPAKM FRRVLTIVQA HCKLGLTATL VREDDKIVDL 

       490        500        510        520        530        540 
NFLIGPKLYE ANWMELQNNG YIAKVQCAEV WCPMSPEFYR EYVAIKTKKR ILLYTMNPNK 

       550        560        570        580        590        600 
FRACQFLIKF HERRNDKIIV FADNVFALKE YAIRLNKPYI YGPTSQGERM QILQNFKHNP 

       610        620        630        640        650        660 
KINTIFISKV GDTSFDLPEA NVLIQISSHG GSRRQEAQRL GRVLRAKKGM VAEEYNAFFY 

       670        680        690        700        710        720 
SLVSQDTQEM AYSTKRQRFL VDQGYSFKVI TKLAGMEEED LAFSTKEEQQ QLLQKVLAAT 

       730        740        750        760        770        780 
DLDAEEEVVA GEFGSRSSQA SRRFGTMSSM SGADDTVYME YHSSRSKAPS KHVHPLFKRF 


RK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-418.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA35661.
RefSeqNP_000113.1. NM_000122.1.
UniGeneHs.469872.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4ERNX-ray1.80A494-782[»]
ProteinModelPortalP19447.
SMRP19447. Positions 283-730.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108383. 39 interactions.
DIPDIP-83N.
IntActP19447. 15 interactions.
MINTMINT-3009064.
STRING9606.ENSP00000285398.

PTM databases

PhosphoSiteP19447.

Polymorphism databases

DMDM119541.

Proteomic databases

PaxDbP19447.
PRIDEP19447.

Protocols and materials databases

DNASU2071.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285398; ENSP00000285398; ENSG00000163161.
GeneID2071.
KEGGhsa:2071.
UCSCuc002toe.1. human.

Organism-specific databases

CTD2071.
GeneCardsGC02M128014.
HGNCHGNC:3435. ERCC3.
HPACAB037153.
HPA046077.
MIM133510. gene.
601675. phenotype.
610651. phenotype.
neXtProtNX_P19447.
Orphanet33364. Trichothiodystrophy.
276252. Xeroderma pigmentosum complementation group B.
PharmGKBPA27849.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1061.
HOGENOMHOG000160172.
HOVERGENHBG051499.
InParanoidP19447.
KOK10843.
OMAKAPSKHV.
OrthoDBEOG7DNNTM.
PhylomeDBP19447.
TreeFamTF101233.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP19447.
BgeeP19447.
CleanExHS_ERCC3.
GenevestigatorP19447.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR006935. Helicase/UvrB_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR001161. Helicase_Ercc3.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
PRINTSPR00851. XRODRMPGMNTB.
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
TIGRFAMsTIGR00603. rad25. 1 hit.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSERCC3. human.
GeneWikiXPB.
GenomeRNAi2071.
NextBio8425.
PROP19447.
SOURCESearch...

Entry information

Entry nameERCC3_HUMAN
AccessionPrimary (citable) accession number: P19447
Secondary accession number(s): Q53QM0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM