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TFIIH basal transcription factor complex helicase XPB subunit (EC 3.6.4.12) (Basic transcription factor 2 89 kDa subunit) (BTF2 p89) (DNA excision repair protein ERCC-3) (DNA repair protein complementing XP-B cells) (TFIIH basal transcription factor complex 89 kDa subunit) (TFIIH 89 kDa subunit) (TFIIH p89) (Xeroderma pigmentosum group B-complementing protein)

 ERCC3_HUMAN             Reviewed;         782 AA.
P19447; Q53QM0;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
05-DEC-2018, entry version 211.
RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPB;
Short=TFIIH subunit XPB;
EC=3.6.4.12;
AltName: Full=Basic transcription factor 2 89 kDa subunit;
Short=BTF2 p89;
AltName: Full=DNA excision repair protein ERCC-3;
AltName: Full=DNA repair protein complementing XP-B cells;
AltName: Full=TFIIH basal transcription factor complex 89 kDa subunit;
Short=TFIIH 89 kDa subunit;
Short=TFIIH p89;
AltName: Full=Xeroderma pigmentosum group B-complementing protein;
Name=ERCC3; Synonyms=XPB, XPBC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2111438; DOI=10.1128/MCB.10.6.2570;
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.;
"Molecular cloning and biological characterization of the human
excision repair gene ERCC-3.";
Mol. Cell. Biol. 10:2570-2581(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2167179; DOI=10.1016/0092-8674(90)90122-U;
Weeda G., van Ham R.C.A., Vermeulen W., Bootsma D., van der Eb A.J.,
Hoeijmakers J.H.J.;
"A presumed DNA helicase encoded by ERCC-3 is involved in the human
repair disorders Xeroderma pigmentosum and Cockayne's syndrome.";
Cell 62:777-791(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1956789; DOI=10.1093/nar/19.22.6301;
Weeda G., Ma L., van Ham R.C.A., van der Eb A.J., Hoeijmakers J.H.J.;
"Structure and expression of the human XPBC/ERCC-3 gene involved in
DNA repair disorders xeroderma pigmentosum and Cockayne's syndrome.";
Nucleic Acids Res. 19:6301-6308(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-704 AND PRO-735.
NIEHS SNPs program;
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION IN TRANSCRIPTION.
PubMed=8157004;
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.;
"Correction of xeroderma pigmentosum repair defect by basal
transcription factor BTF2 (TFIIH).";
EMBO J. 13:1645-1653(1994).
[9]
INTERACTION WITH EBV EBNA2 (MICROBIAL INFECTION).
PubMed=7724549; DOI=10.1073/pnas.92.8.3259;
Tong X., Drapkin R., Reinberg D., Kieff E.;
"The 62- and 80-kDa subunits of transcription factor IIH mediate the
interaction with Epstein-Barr virus nuclear protein 2.";
Proc. Natl. Acad. Sci. U.S.A. 92:3259-3263(1995).
[10]
IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
Kershnar E., Wu S.-Y., Chiang C.-M.;
"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.";
J. Biol. Chem. 273:34444-34453(1998).
[11]
MUTAGENESIS OF LYS-346, AND FUNCTION.
PubMed=10024882; DOI=10.1016/S1097-2765(00)80177-X;
Tirode F., Busso D., Coin F., Egly J.-M.;
"Reconstitution of the transcription factor TFIIH: assignment of
functions for the three enzymatic subunits, XPB, XPD, and cdk7.";
Mol. Cell 3:87-95(1999).
[12]
INTERACTION WITH PUF60.
PubMed=10882074; DOI=10.1016/S1097-2765(00)80428-1;
Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M.,
Levens D.;
"The FBP interacting repressor targets TFIIH to inhibit activated
transcription.";
Mol. Cell 5:331-341(2000).
[13]
INTERACTION WITH PUF60.
PubMed=11239393; DOI=10.1016/S0092-8674(01)00223-9;
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.;
"Defective interplay of activators and repressors with TFIH in
xeroderma pigmentosum.";
Cell 104:353-363(2001).
[14]
REVIEW ON VARIANTS XP-B.
PubMed=10447254;
DOI=10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6;
Cleaver J.E., Thompson L.H., Richardson A.S., States J.C.;
"A summary of mutations in the UV-sensitive disorders: xeroderma
pigmentosum, Cockayne syndrome, and trichothiodystrophy.";
Hum. Mutat. 14:9-22(1999).
[15]
INTERACTION WITH ATF7IP.
PubMed=19106100; DOI=10.1074/jbc.M807098200;
Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S.,
Watanabe S., Saitoh N., Ito T., Nakao M.;
"MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated
telomerase activity.";
J. Biol. Chem. 284:5165-5174(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 494-782, AND MUTAGENESIS OF
LYS-782.
PubMed=23385459; DOI=10.1107/S0907444912045040;
Hilario E., Li Y., Nobumori Y., Liu X., Fan L.;
"Structure of the C-terminal half of human XPB helicase and the impact
of the disease-causing mutation XP11BE.";
Acta Crystallogr. D 69:237-246(2013).
[19]
VARIANT XP-B SER-99.
PubMed=8304337;
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.;
"Clinical heterogeneity within xeroderma pigmentosum associated with
mutations in the DNA repair and transcription gene ERCC3.";
Am. J. Hum. Genet. 54:191-200(1994).
[20]
VARIANT TTD2 PRO-119.
PubMed=9012405;
Weeda G., Eveno E., Donker I., Vermeulen W., Chevallier-Lagente O.,
Taieb A., Stary A., Hoeijmakers J.H.J., Mezzina M., Sarasin A.;
"A mutation in the XPB/ERCC3 DNA repair transcription gene, associated
with trichothiodystrophy.";
Am. J. Hum. Genet. 60:320-329(1997).
[21]
VARIANTS ARG-117 AND CYS-402.
PubMed=10862089;
DOI=10.1002/1098-1004(200006)15:6<577::AID-HUMU11>3.3.CO;2-N;
Butkiewicz D., Rusin M., Harris C.C., Chorazy M.;
"Identification of four single nucleotide polymorphisms in DNA repair
genes: XPA and XPB (ERCC3) in Polish population.";
Hum. Mutat. 15:577-578(2000).
[22]
VARIANT XP-B SER-99.
PubMed=16947863; DOI=10.1002/humu.20392;
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.;
"Phenotypic heterogeneity in the XPB DNA helicase gene (ERCC3):
xeroderma pigmentosum without and with Cockayne syndrome.";
Hum. Mutat. 27:1092-1103(2006).
[23]
VARIANT [LARGE SCALE ANALYSIS] GLN-418.
PubMed=16959974; DOI=10.1126/science.1133427;
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., 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.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the
general transcription and DNA repair factor IIH (TFIIH) core
complex, which is involved in general and transcription-coupled
nucleotide excision repair (NER) of damaged DNA and, when
complexed to CAK, in RNA transcription by RNA polymerase II. In
NER, TFIIH acts by opening DNA around the lesion to allow the
excision of the damaged oligonucleotide and its replacement by a
new DNA fragment. The ATPase activity of XPB/ERCC3, but not its
helicase activity, is required for DNA opening. In transcription,
TFIIH has an essential role in transcription initiation. When the
pre-initiation complex (PIC) has been established, TFIIH is
required for promoter opening and promoter escape. The ATP-
dependent helicase activity of XPB/ERCC3 is required for promoter
opening and promoter escape. Phosphorylation of the C-terminal
tail (CTD) of the largest subunit of RNA polymerase II by the
kinase module CAK controls the initiation of transcription.
{ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:8157004}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
-!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5,
which is active in NER. The core complex associates with the 3-
subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin
H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH)
active in transcription. Interacts with PUF60. Interacts with
ATF7IP. {ECO:0000269|PubMed:10882074, ECO:0000269|PubMed:11239393,
ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:9852112}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
EBNA2. {ECO:0000269|PubMed:7724549}.
-!- INTERACTION:
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-1183307, EBI-739624;
P18074:ERCC2; NbExp=4; IntAct=EBI-1183307, EBI-6380590;
Q6ZYL4:GTF2H5; NbExp=3; IntAct=EBI-1183307, EBI-6380438;
O00505:KPNA3; NbExp=3; IntAct=EBI-1183307, EBI-358297;
P62195:PSMC5; NbExp=4; IntAct=EBI-1183307, EBI-357745;
P62196:Psmc5 (xeno); NbExp=6; IntAct=EBI-1183307, EBI-357713;
P54727:RAD23B; NbExp=2; IntAct=EBI-1183307, EBI-954531;
P98170:XIAP; NbExp=3; IntAct=EBI-1183307, EBI-517127;
Q01831:XPC; NbExp=2; IntAct=EBI-1183307, EBI-372610;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- 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. {ECO:0000269|PubMed:10447254,
ECO:0000269|PubMed:16947863, ECO:0000269|PubMed:8304337}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Trichothiodystrophy 2, photosensitive (TTD2)
[MIM:616390]: A form of trichothiodystrophy, an autosomal
recessive disease characterized by sulfur-deficient brittle hair
and multisystem variable abnormalities. The spectrum of clinical
features varies from mild disease with only hair involvement to
severe disease with cutaneous, neurologic and profound
developmental defects. Ichthyosis, intellectual and developmental
disabilities, decreased fertility, abnormal characteristics at
birth, ocular abnormalities, short stature, and infections are
common manifestations. There are both photosensitive and non-
photosensitive forms of the disorder.
{ECO:0000269|PubMed:9012405}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/XPBID296.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ercc3/";
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EMBL; M31899; AAA52396.1; -; mRNA.
EMBL; AY163769; AAN46739.1; -; Genomic_DNA.
EMBL; AC110926; AAY15069.1; -; Genomic_DNA.
EMBL; CH471103; EAW95313.1; -; Genomic_DNA.
EMBL; BC008820; AAH08820.1; -; mRNA.
CCDS; CCDS2144.1; -.
PIR; A35661; A35661.
RefSeq; NP_000113.1; NM_000122.1.
UniGene; Hs.469872; -.
PDB; 4ERN; X-ray; 1.80 A; A=494-782.
PDB; 5IVW; EM; 10.00 A; V=1-782.
PDB; 5IY6; EM; 7.20 A; V=1-782.
PDB; 5IY7; EM; 8.60 A; V=1-782.
PDB; 5IY8; EM; 7.90 A; V=1-782.
PDB; 5IY9; EM; 6.30 A; V=1-782.
PDB; 5OF4; EM; 4.40 A; A=265-782.
PDBsum; 4ERN; -.
PDBsum; 5IVW; -.
PDBsum; 5IY6; -.
PDBsum; 5IY7; -.
PDBsum; 5IY8; -.
PDBsum; 5IY9; -.
PDBsum; 5OF4; -.
ProteinModelPortal; P19447; -.
SMR; P19447; -.
BioGrid; 108383; 62.
CORUM; P19447; -.
DIP; DIP-83N; -.
IntAct; P19447; 39.
MINT; P19447; -.
STRING; 9606.ENSP00000285398; -.
iPTMnet; P19447; -.
PhosphoSitePlus; P19447; -.
BioMuta; ERCC3; -.
DMDM; 119541; -.
EPD; P19447; -.
MaxQB; P19447; -.
PaxDb; P19447; -.
PeptideAtlas; P19447; -.
PRIDE; P19447; -.
ProteomicsDB; 53665; -.
DNASU; 2071; -.
Ensembl; ENST00000285398; ENSP00000285398; ENSG00000163161.
GeneID; 2071; -.
KEGG; hsa:2071; -.
UCSC; uc002toh.1; human.
CTD; 2071; -.
DisGeNET; 2071; -.
EuPathDB; HostDB:ENSG00000163161.12; -.
GeneCards; ERCC3; -.
GeneReviews; ERCC3; -.
HGNC; HGNC:3435; ERCC3.
HPA; CAB037153; -.
HPA; HPA046077; -.
MalaCards; ERCC3; -.
MIM; 133510; gene.
MIM; 610651; phenotype.
MIM; 616390; phenotype.
neXtProt; NX_P19447; -.
OpenTargets; ENSG00000163161; -.
Orphanet; 33364; Trichothiodystrophy.
Orphanet; 910; Xeroderma pigmentosum.
Orphanet; 220295; Xeroderma pigmentosum-Cockayne syndrome complex.
PharmGKB; PA27849; -.
eggNOG; KOG1123; Eukaryota.
eggNOG; COG1061; LUCA.
GeneTree; ENSGT00390000002204; -.
HOGENOM; HOG000160172; -.
HOVERGEN; HBG051499; -.
InParanoid; P19447; -.
KO; K10843; -.
OMA; TKHVHPL; -.
OrthoDB; EOG091G0291; -.
PhylomeDB; P19447; -.
TreeFam; TF101233; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-72086; mRNA Capping.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
SIGNOR; P19447; -.
ChiTaRS; ERCC3; human.
GeneWiki; XPB; -.
GenomeRNAi; 2071; -.
PRO; PR:P19447; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163161; Expressed in 216 organ(s), highest expression level in testis.
CleanEx; HS_ERCC3; -.
ExpressionAtlas; P19447; baseline and differential.
Genevisible; P19447; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:Ensembl.
GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:UniProtKB.
GO; GO:0097550; C:transcriptional preinitiation complex; IBA:GO_Central.
GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; IBA:GO_Central.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; NAS:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
GO; GO:0004386; F:helicase activity; TAS:Reactome.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:MGI.
GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0006265; P:DNA topological change; IMP:UniProtKB.
GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0035315; P:hair cell differentiation; IMP:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; IMP:UniProtKB.
GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; IMP:UniProtKB.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IMP:UniProtKB.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome.
GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0001111; P:promoter clearance from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0008104; P:protein localization; IMP:UniProtKB.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
GO; GO:0000019; P:regulation of mitotic recombination; IBA:GO_Central.
GO; GO:1903025; P:regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0010525; P:regulation of transposition, RNA-mediated; IBA:GO_Central.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
GO; GO:0009411; P:response to UV; IMP:UniProtKB.
GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IDA:UniProtKB.
GO; GO:0001113; P:transcriptional open complex formation at RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0009650; P:UV protection; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00079; HELICc; 1.
InterPro; IPR032438; ERCC3_RAD25_C.
InterPro; IPR006935; Helicase/UvrB_N.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001161; XPB/Ssl2.
InterPro; IPR032830; XPB/Ssl2_N.
Pfam; PF16203; ERCC3_RAD25_C; 1.
Pfam; PF13625; Helicase_C_3; 1.
Pfam; PF04851; ResIII; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 2.
TIGRFAMs; TIGR00603; rad25; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cockayne syndrome; Complete proteome;
Deafness; Disease mutation; DNA damage; DNA repair; DNA-binding;
Dwarfism; Helicase; Host-virus interaction; Hydrolase; Ichthyosis;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Xeroderma pigmentosum.
CHAIN 1 782 General transcription and DNA repair
factor IIH helicase subunit XPB.
/FTId=PRO_0000101987.
DOMAIN 327 488 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 542 702 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 340 347 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 6 18 Nuclear localization signal.
{ECO:0000255}.
MOTIF 441 444 DEVH box.
COMPBIAS 20 28 Asp/Glu-rich (acidic).
COMPBIAS 256 265 Asp/Glu-rich (acidic).
COMPBIAS 697 700 Asp/Glu-rich (acidic).
COMPBIAS 721 728 Asp/Glu-rich (acidic).
MOD_RES 686 686 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 99 99 F -> S (in XP-B; combined with features
of Cockayne syndrome; mild;
dbSNP:rs121913045).
{ECO:0000269|PubMed:16947863,
ECO:0000269|PubMed:8304337}.
/FTId=VAR_003632.
VARIANT 117 117 K -> R (in dbSNP:rs1805161).
{ECO:0000269|PubMed:10862089}.
/FTId=VAR_014766.
VARIANT 119 119 T -> P (in TTD2; mild;
dbSNP:rs121913046).
{ECO:0000269|PubMed:9012405}.
/FTId=VAR_008186.
VARIANT 402 402 G -> C (in dbSNP:rs1805162).
{ECO:0000269|PubMed:10862089}.
/FTId=VAR_014767.
VARIANT 418 418 K -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035942.
VARIANT 704 704 S -> L (in dbSNP:rs4150521).
{ECO:0000269|Ref.4}.
/FTId=VAR_017294.
VARIANT 735 735 S -> P (in dbSNP:rs4150522).
{ECO:0000269|Ref.4}.
/FTId=VAR_014344.
MUTAGEN 346 346 K->R: No transcriptional activity of the
reconstituted TFIIH complex.
{ECO:0000269|PubMed:10024882}.
MUTAGEN 782 782 Missing: Impairs protein folding.
{ECO:0000269|PubMed:23385459}.
STRAND 505 512 {ECO:0000244|PDB:4ERN}.
HELIX 516 524 {ECO:0000244|PDB:4ERN}.
HELIX 528 530 {ECO:0000244|PDB:4ERN}.
HELIX 531 536 {ECO:0000244|PDB:4ERN}.
HELIX 538 552 {ECO:0000244|PDB:4ERN}.
TURN 553 555 {ECO:0000244|PDB:4ERN}.
STRAND 558 561 {ECO:0000244|PDB:4ERN}.
HELIX 565 574 {ECO:0000244|PDB:4ERN}.
HELIX 586 598 {ECO:0000244|PDB:4ERN}.
STRAND 604 607 {ECO:0000244|PDB:4ERN}.
HELIX 609 611 {ECO:0000244|PDB:4ERN}.
TURN 612 614 {ECO:0000244|PDB:4ERN}.
STRAND 620 626 {ECO:0000244|PDB:4ERN}.
HELIX 633 643 {ECO:0000244|PDB:4ERN}.
STRAND 651 654 {ECO:0000244|PDB:4ERN}.
STRAND 656 664 {ECO:0000244|PDB:4ERN}.
HELIX 668 670 {ECO:0000244|PDB:4ERN}.
HELIX 671 682 {ECO:0000244|PDB:4ERN}.
STRAND 686 692 {ECO:0000244|PDB:4ERN}.
HELIX 696 698 {ECO:0000244|PDB:4ERN}.
HELIX 706 718 {ECO:0000244|PDB:4ERN}.
HELIX 721 724 {ECO:0000244|PDB:4ERN}.
SEQUENCE 782 AA; 89278 MW; F5F4D3A89A7DF826 CRC64;
MGKRDRADRD KKKSRKRHYE DEEDDEEDAP GNDPQEAVPS AAGKQVDESG TKVDEYGAKD
YRLQMPLKDD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL VAIAEPVCRP THVHEYKLTA
YSLYAAVSVG LQTSDITEYL RKLSKTGVPD GIMQFIKLCT VSYGKVKLVL KHNRYFVESC
HPDVIQHLLQ DPVIRECRLR NSEGEATELI TETFTSKSAI SKTAESSGGP STSRVTDPQG
KSDIPMDLFD FYEQMDKDEE EEEETQTVSF EVKQEMIEEL QKRCIHLEYP LLAEYDFRND
SVNPDINIDL KPTAVLRPYQ EKSLRKMFGN GRARSGVIVL PCGAGKSLVG VTAACTVRKR
CLVLGNSAVS VEQWKAQFKM WSTIDDSQIC RFTSDAKDKP IGCSVAISTY SMLGHTTKRS
WEAERVMEWL KTQEWGLMIL DEVHTIPAKM FRRVLTIVQA HCKLGLTATL VREDDKIVDL
NFLIGPKLYE ANWMELQNNG YIAKVQCAEV WCPMSPEFYR EYVAIKTKKR ILLYTMNPNK
FRACQFLIKF HERRNDKIIV FADNVFALKE YAIRLNKPYI YGPTSQGERM QILQNFKHNP
KINTIFISKV GDTSFDLPEA NVLIQISSHG GSRRQEAQRL GRVLRAKKGM VAEEYNAFFY
SLVSQDTQEM AYSTKRQRFL VDQGYSFKVI TKLAGMEEED LAFSTKEEQQ QLLQKVLAAT
DLDAEEEVVA GEFGSRSSQA SRRFGTMSSM SGADDTVYME YHSSRSKAPS KHVHPLFKRF
RK


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