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Database: UniProt
Entry: P19447
LinkDB: P19447
Original site: P19447 
ID   ERCC3_HUMAN             Reviewed;         782 AA.
AC   P19447; Q53QM0;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   13-NOV-2019, entry version 218.
DE   RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPB;
DE            Short=TFIIH subunit XPB;
DE            EC=3.6.4.12;
DE   AltName: Full=Basic transcription factor 2 89 kDa subunit;
DE            Short=BTF2 p89;
DE   AltName: Full=DNA excision repair protein ERCC-3;
DE   AltName: Full=DNA repair protein complementing XP-B cells;
DE   AltName: Full=TFIIH basal transcription factor complex 89 kDa subunit;
DE            Short=TFIIH 89 kDa subunit;
DE            Short=TFIIH p89;
DE   AltName: Full=Xeroderma pigmentosum group B-complementing protein;
GN   Name=ERCC3; Synonyms=XPB, XPBC;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2111438; DOI=10.1128/mcb.10.6.2570;
RA   Weeda G., van Ham R.C.A., Masurel R., Westerveld A., Odijk H.,
RA   de Wit J., Bootsma D., van der Eb A.J., Hoeijmakers J.H.J.;
RT   "Molecular cloning and biological characterization of the human
RT   excision repair gene ERCC-3.";
RL   Mol. Cell. Biol. 10:2570-2581(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2167179; DOI=10.1016/0092-8674(90)90122-u;
RA   Weeda G., van Ham R.C.A., Vermeulen W., Bootsma D., van der Eb A.J.,
RA   Hoeijmakers J.H.J.;
RT   "A presumed DNA helicase encoded by ERCC-3 is involved in the human
RT   repair disorders Xeroderma pigmentosum and Cockayne's syndrome.";
RL   Cell 62:777-791(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1956789; DOI=10.1093/nar/19.22.6301;
RA   Weeda G., Ma L., van Ham R.C.A., van der Eb A.J., Hoeijmakers J.H.J.;
RT   "Structure and expression of the human XPBC/ERCC-3 gene involved in
RT   DNA repair disorders xeroderma pigmentosum and Cockayne's syndrome.";
RL   Nucleic Acids Res. 19:6301-6308(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-704 AND PRO-735.
RG   NIEHS SNPs program;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION IN TRANSCRIPTION.
RX   PubMed=8157004;
RA   van Vuuren A.J., Vermeulen W., Ma L., Weeda G., Appeldoorn E.,
RA   Jaspers N.G.J., van der Eb A.J., Bootsma D., Hoeijmakers J.H.J.,
RA   Humbert S., Schaeffer L., Egly J.-M.;
RT   "Correction of xeroderma pigmentosum repair defect by basal
RT   transcription factor BTF2 (TFIIH).";
RL   EMBO J. 13:1645-1653(1994).
RN   [9]
RP   INTERACTION WITH EBV EBNA2 (MICROBIAL INFECTION).
RX   PubMed=7724549; DOI=10.1073/pnas.92.8.3259;
RA   Tong X., Drapkin R., Reinberg D., Kieff E.;
RT   "The 62- and 80-kDa subunits of transcription factor IIH mediate the
RT   interaction with Epstein-Barr virus nuclear protein 2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3259-3263(1995).
RN   [10]
RP   IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
RX   PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
RA   Kershnar E., Wu S.-Y., Chiang C.-M.;
RT   "Immunoaffinity purification and functional characterization of human
RT   transcription factor IIH and RNA polymerase II from clonal cell lines
RT   that conditionally express epitope-tagged subunits of the multiprotein
RT   complexes.";
RL   J. Biol. Chem. 273:34444-34453(1998).
RN   [11]
RP   MUTAGENESIS OF LYS-346, AND FUNCTION.
RX   PubMed=10024882; DOI=10.1016/s1097-2765(00)80177-x;
RA   Tirode F., Busso D., Coin F., Egly J.-M.;
RT   "Reconstitution of the transcription factor TFIIH: assignment of
RT   functions for the three enzymatic subunits, XPB, XPD, and cdk7.";
RL   Mol. Cell 3:87-95(1999).
RN   [12]
RP   INTERACTION WITH PUF60.
RX   PubMed=10882074; DOI=10.1016/s1097-2765(00)80428-1;
RA   Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M.,
RA   Levens D.;
RT   "The FBP interacting repressor targets TFIIH to inhibit activated
RT   transcription.";
RL   Mol. Cell 5:331-341(2000).
RN   [13]
RP   INTERACTION WITH PUF60.
RX   PubMed=11239393; DOI=10.1016/s0092-8674(01)00223-9;
RA   Liu J., Akoulitchev S., Weber A., Ge H., Chuikov S., Libutti D.,
RA   Wang X.W., Conaway J.W., Harris C.C., Conaway R.C., Reinberg D.,
RA   Levens D.;
RT   "Defective interplay of activators and repressors with TFIH in
RT   xeroderma pigmentosum.";
RL   Cell 104:353-363(2001).
RN   [14]
RP   REVIEW ON VARIANTS XP-B.
RX   PubMed=10447254;
RX   DOI=10.1002/(sici)1098-1004(1999)14:1<9::aid-humu2>3.0.co;2-6;
RA   Cleaver J.E., Thompson L.H., Richardson A.S., States J.C.;
RT   "A summary of mutations in the UV-sensitive disorders: xeroderma
RT   pigmentosum, Cockayne syndrome, and trichothiodystrophy.";
RL   Hum. Mutat. 14:9-22(1999).
RN   [15]
RP   INTERACTION WITH ATF7IP.
RX   PubMed=19106100; DOI=10.1074/jbc.m807098200;
RA   Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S.,
RA   Watanabe S., Saitoh N., Ito T., Nakao M.;
RT   "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated
RT   telomerase activity.";
RL   J. Biol. Chem. 284:5165-5174(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   FUNCTION, AND INTERACTION WITH KAT2A.
RX   PubMed=30894545; DOI=10.1038/s41467-019-09270-2;
RA   Sandoz J., Nagy Z., Catez P., Caliskan G., Geny S., Renaud J.B.,
RA   Concordet J.P., Poterszman A., Tora L., Egly J.M., Le May N., Coin F.;
RT   "Functional interplay between TFIIH and KAT2A regulates higher-order
RT   chromatin structure and class II gene expression.";
RL   Nat. Commun. 10:1288-1288(2019).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 494-782, AND MUTAGENESIS OF
RP   LYS-782.
RX   PubMed=23385459; DOI=10.1107/s0907444912045040;
RA   Hilario E., Li Y., Nobumori Y., Liu X., Fan L.;
RT   "Structure of the C-terminal half of human XPB helicase and the impact
RT   of the disease-causing mutation XP11BE.";
RL   Acta Crystallogr. D 69:237-246(2013).
RN   [20]
RP   VARIANT XP-B SER-99.
RX   PubMed=8304337;
RA   Vermeulen W., Scott R.J., Rodgers S., Mueller H.J., Cole J.,
RA   Arlett C.F., Kleijer W.J., Bootsma D., Hoeijmakers J.H.J., Weeda G.;
RT   "Clinical heterogeneity within xeroderma pigmentosum associated with
RT   mutations in the DNA repair and transcription gene ERCC3.";
RL   Am. J. Hum. Genet. 54:191-200(1994).
RN   [21]
RP   VARIANT TTD2 PRO-119.
RX   PubMed=9012405;
RA   Weeda G., Eveno E., Donker I., Vermeulen W., Chevallier-Lagente O.,
RA   Taieb A., Stary A., Hoeijmakers J.H.J., Mezzina M., Sarasin A.;
RT   "A mutation in the XPB/ERCC3 DNA repair transcription gene, associated
RT   with trichothiodystrophy.";
RL   Am. J. Hum. Genet. 60:320-329(1997).
RN   [22]
RP   VARIANTS ARG-117 AND CYS-402.
RX   PubMed=10862089;
RX   DOI=10.1002/1098-1004(200006)15:6<577::AID-HUMU11>3.3.CO;2-N;
RA   Butkiewicz D., Rusin M., Harris C.C., Chorazy M.;
RT   "Identification of four single nucleotide polymorphisms in DNA repair
RT   genes: XPA and XPB (ERCC3) in Polish population.";
RL   Hum. Mutat. 15:577-578(2000).
RN   [23]
RP   VARIANT XP-B SER-99.
RX   PubMed=16947863; DOI=10.1002/humu.20392;
RA   Oh K.-S., Khan S.G., Jaspers N.G.J., Raams A., Ueda T., Lehmann A.,
RA   Friedmann P.S., Emmert S., Gratchev A., Lachlan K., Lucassan A.,
RA   Baker C.C., Kraemer K.H.;
RT   "Phenotypic heterogeneity in the XPB DNA helicase gene (ERCC3):
RT   xeroderma pigmentosum without and with Cockayne syndrome.";
RL   Hum. Mutat. 27:1092-1103(2006).
RN   [24]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-418.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the
CC       general transcription and DNA repair factor IIH (TFIIH) core
CC       complex, which is involved in general and transcription-coupled
CC       nucleotide excision repair (NER) of damaged DNA and, when
CC       complexed to CAK, in RNA transcription by RNA polymerase II. In
CC       NER, TFIIH acts by opening DNA around the lesion to allow the
CC       excision of the damaged oligonucleotide and its replacement by a
CC       new DNA fragment. The ATPase activity of XPB/ERCC3, but not its
CC       helicase activity, is required for DNA opening. In transcription,
CC       TFIIH has an essential role in transcription initiation
CC       (PubMed:8157004, PubMed:30894545). When the pre-initiation complex
CC       (PIC) has been established, TFIIH is required for promoter opening
CC       and promoter escape (PubMed:8157004). The ATP-dependent helicase
CC       activity of XPB/ERCC3 is required for promoter opening and
CC       promoter escape. Phosphorylation of the C-terminal tail (CTD) of
CC       the largest subunit of RNA polymerase II by the kinase module CAK
CC       controls the initiation of transcription.
CC       {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:30894545,
CC       ECO:0000269|PubMed:8157004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC       XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5,
CC       which is active in NER. The core complex associates with the 3-
CC       subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin
CC       H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH)
CC       active in transcription (PubMed:9852112). Interacts with PUF60
CC       (PubMed:10882074, PubMed:11239393). Interacts with ATF7IP
CC       (PubMed:19106100). Interacts with KAT2A; leading to KAT2A
CC       recruitment to promoters and acetylation of histones
CC       (PubMed:30894545). {ECO:0000269|PubMed:10882074,
CC       ECO:0000269|PubMed:11239393, ECO:0000269|PubMed:19106100,
CC       ECO:0000269|PubMed:30894545, ECO:0000269|PubMed:9852112}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
CC       EBNA2. {ECO:0000269|PubMed:7724549}.
CC   -!- INTERACTION:
CC       Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-1183307, EBI-739624;
CC       P18074:ERCC2; NbExp=4; IntAct=EBI-1183307, EBI-6380590;
CC       Q6ZYL4:GTF2H5; NbExp=4; IntAct=EBI-1183307, EBI-6380438;
CC       O00505:KPNA3; NbExp=3; IntAct=EBI-1183307, EBI-358297;
CC       P62195:PSMC5; NbExp=4; IntAct=EBI-1183307, EBI-357745;
CC       P62196:Psmc5 (xeno); NbExp=6; IntAct=EBI-1183307, EBI-357713;
CC       P54727:RAD23B; NbExp=2; IntAct=EBI-1183307, EBI-954531;
CC       P98170:XIAP; NbExp=3; IntAct=EBI-1183307, EBI-517127;
CC       Q01831:XPC; NbExp=2; IntAct=EBI-1183307, EBI-372610;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DISEASE: Xeroderma pigmentosum complementation group B (XP-B)
CC       [MIM:610651]: An autosomal recessive pigmentary skin disorder
CC       characterized by solar hypersensitivity of the skin, high
CC       predisposition for developing cancers on areas exposed to sunlight
CC       and, in some cases, neurological abnormalities. The skin develops
CC       marked freckling and other pigmentation abnormalities. Some XP-B
CC       patients present features of Cockayne syndrome, including
CC       cachectic dwarfism, pigmentary retinopathy, ataxia, decreased
CC       nerve conduction velocities. The phenotype combining xeroderma
CC       pigmentosum and Cockayne syndrome traits is referred to as XP-CS
CC       complex. {ECO:0000269|PubMed:10447254,
CC       ECO:0000269|PubMed:16947863, ECO:0000269|PubMed:8304337}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Trichothiodystrophy 2, photosensitive (TTD2)
CC       [MIM:616390]: A form of trichothiodystrophy, an autosomal
CC       recessive disease characterized by sulfur-deficient brittle hair
CC       and multisystem variable abnormalities. The spectrum of clinical
CC       features varies from mild disease with only hair involvement to
CC       severe disease with cutaneous, neurologic and profound
CC       developmental defects. Ichthyosis, intellectual and developmental
CC       disabilities, decreased fertility, abnormal characteristics at
CC       birth, ocular abnormalities, short stature, and infections are
CC       common manifestations. There are both photosensitive and non-
CC       photosensitive forms of the disorder.
CC       {ECO:0000269|PubMed:9012405}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/XPBID296.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ercc3/";
DR   EMBL; M31899; AAA52396.1; -; mRNA.
DR   EMBL; AY163769; AAN46739.1; -; Genomic_DNA.
DR   EMBL; AC110926; AAY15069.1; -; Genomic_DNA.
DR   EMBL; CH471103; EAW95313.1; -; Genomic_DNA.
DR   EMBL; BC008820; AAH08820.1; -; mRNA.
DR   CCDS; CCDS2144.1; -.
DR   PIR; A35661; A35661.
DR   RefSeq; NP_000113.1; NM_000122.1.
DR   PDB; 4ERN; X-ray; 1.80 A; A=494-782.
DR   PDB; 5IVW; EM; 10.00 A; V=1-782.
DR   PDB; 5IY6; EM; 7.20 A; V=1-782.
DR   PDB; 5IY7; EM; 8.60 A; V=1-782.
DR   PDB; 5IY8; EM; 7.90 A; V=1-782.
DR   PDB; 5IY9; EM; 6.30 A; V=1-782.
DR   PDB; 5OF4; EM; 4.40 A; A=265-782.
DR   PDB; 6NMI; EM; 3.70 A; A=34-730.
DR   PDB; 6O9L; EM; 7.20 A; 7=1-782.
DR   PDB; 6O9M; EM; 4.40 A; 7=1-782.
DR   PDB; 6RO4; EM; 3.50 A; A=1-782.
DR   PDBsum; 4ERN; -.
DR   PDBsum; 5IVW; -.
DR   PDBsum; 5IY6; -.
DR   PDBsum; 5IY7; -.
DR   PDBsum; 5IY8; -.
DR   PDBsum; 5IY9; -.
DR   PDBsum; 5OF4; -.
DR   PDBsum; 6NMI; -.
DR   PDBsum; 6O9L; -.
DR   PDBsum; 6O9M; -.
DR   PDBsum; 6RO4; -.
DR   SMR; P19447; -.
DR   BioGrid; 108383; 65.
DR   CORUM; P19447; -.
DR   DIP; DIP-83N; -.
DR   IntAct; P19447; 53.
DR   MINT; P19447; -.
DR   STRING; 9606.ENSP00000285398; -.
DR   iPTMnet; P19447; -.
DR   PhosphoSitePlus; P19447; -.
DR   BioMuta; ERCC3; -.
DR   DMDM; 119541; -.
DR   EPD; P19447; -.
DR   jPOST; P19447; -.
DR   MassIVE; P19447; -.
DR   MaxQB; P19447; -.
DR   PaxDb; P19447; -.
DR   PeptideAtlas; P19447; -.
DR   PRIDE; P19447; -.
DR   ProteomicsDB; 53665; -.
DR   DNASU; 2071; -.
DR   Ensembl; ENST00000285398; ENSP00000285398; ENSG00000163161.
DR   GeneID; 2071; -.
DR   KEGG; hsa:2071; -.
DR   UCSC; uc002toh.1; human.
DR   CTD; 2071; -.
DR   DisGeNET; 2071; -.
DR   GeneCards; ERCC3; -.
DR   GeneReviews; ERCC3; -.
DR   HGNC; HGNC:3435; ERCC3.
DR   HPA; CAB037153; -.
DR   HPA; HPA046077; -.
DR   MalaCards; ERCC3; -.
DR   MIM; 133510; gene.
DR   MIM; 610651; phenotype.
DR   MIM; 616390; phenotype.
DR   neXtProt; NX_P19447; -.
DR   OpenTargets; ENSG00000163161; -.
DR   Orphanet; 33364; Trichothiodystrophy.
DR   Orphanet; 910; Xeroderma pigmentosum.
DR   Orphanet; 220295; Xeroderma pigmentosum-Cockayne syndrome complex.
DR   PharmGKB; PA27849; -.
DR   eggNOG; KOG1123; Eukaryota.
DR   eggNOG; COG1061; LUCA.
DR   GeneTree; ENSGT00390000002204; -.
DR   HOGENOM; HOG000160172; -.
DR   InParanoid; P19447; -.
DR   KO; K10843; -.
DR   OMA; PKKFQAC; -.
DR   OrthoDB; 100698at2759; -.
DR   PhylomeDB; P19447; -.
DR   TreeFam; TF101233; -.
DR   Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR   Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR   Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR   Reactome; R-HSA-167161; HIV Transcription Initiation.
DR   Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR   Reactome; R-HSA-167172; Transcription of the HIV genome.
DR   Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR   Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR   Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR   Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR   Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR   Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-HSA-72086; mRNA Capping.
DR   Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR   Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   SIGNOR; P19447; -.
DR   ChiTaRS; ERCC3; human.
DR   GeneWiki; XPB; -.
DR   GenomeRNAi; 2071; -.
DR   Pharos; P19447; -.
DR   PRO; PR:P19447; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000163161; Expressed in 216 organ(s), highest expression level in testis.
DR   ExpressionAtlas; P19447; baseline and differential.
DR   Genevisible; P19447; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR   GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:Ensembl.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:UniProtKB.
DR   GO; GO:0097550; C:transcriptional preinitiation complex; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; NAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
DR   GO; GO:0004386; F:helicase activity; TAS:Reactome.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IDA:MGI.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
DR   GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR   GO; GO:0006265; P:DNA topological change; IMP:UniProtKB.
DR   GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR   GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0035315; P:hair cell differentiation; IMP:UniProtKB.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:UniProtKB.
DR   GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; IMP:UniProtKB.
DR   GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IMP:UniProtKB.
DR   GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; TAS:Reactome.
DR   GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
DR   GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
DR   GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:GOC.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR   GO; GO:0009411; P:response to UV; IMP:UniProtKB.
DR   GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IDA:UniProtKB.
DR   GO; GO:0009650; P:UV protection; IEA:Ensembl.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   InterPro; IPR032438; ERCC3_RAD25_C.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001161; XPB/Ssl2.
DR   InterPro; IPR032830; XPB/Ssl2_N.
DR   Pfam; PF16203; ERCC3_RAD25_C; 1.
DR   Pfam; PF13625; Helicase_C_3; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00603; rad25; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cockayne syndrome; Complete proteome;
KW   Deafness; Disease mutation; DNA damage; DNA repair; DNA-binding;
KW   Dwarfism; Helicase; Host-virus interaction; Hydrolase; Ichthyosis;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Xeroderma pigmentosum.
FT   CHAIN         1    782       General transcription and DNA repair
FT                                factor IIH helicase subunit XPB.
FT                                /FTId=PRO_0000101987.
FT   DOMAIN      327    488       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      542    702       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     340    347       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF         6     18       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       441    444       DEVH box.
FT   COMPBIAS     20     28       Asp/Glu-rich (acidic).
FT   COMPBIAS    256    265       Asp/Glu-rich (acidic).
FT   COMPBIAS    697    700       Asp/Glu-rich (acidic).
FT   COMPBIAS    721    728       Asp/Glu-rich (acidic).
FT   MOD_RES     686    686       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VARIANT      99     99       F -> S (in XP-B; combined with features
FT                                of Cockayne syndrome; mild;
FT                                dbSNP:rs121913045).
FT                                {ECO:0000269|PubMed:16947863,
FT                                ECO:0000269|PubMed:8304337}.
FT                                /FTId=VAR_003632.
FT   VARIANT     117    117       K -> R (in dbSNP:rs1805161).
FT                                {ECO:0000269|PubMed:10862089}.
FT                                /FTId=VAR_014766.
FT   VARIANT     119    119       T -> P (in TTD2; mild;
FT                                dbSNP:rs121913046).
FT                                {ECO:0000269|PubMed:9012405}.
FT                                /FTId=VAR_008186.
FT   VARIANT     402    402       G -> C (in dbSNP:rs1805162).
FT                                {ECO:0000269|PubMed:10862089}.
FT                                /FTId=VAR_014767.
FT   VARIANT     418    418       K -> Q (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035942.
FT   VARIANT     704    704       S -> L (in dbSNP:rs4150521).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_017294.
FT   VARIANT     735    735       S -> P (in dbSNP:rs4150522).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_014344.
FT   MUTAGEN     346    346       K->R: No transcriptional activity of the
FT                                reconstituted TFIIH complex.
FT                                {ECO:0000269|PubMed:10024882}.
FT   MUTAGEN     782    782       Missing: Impairs protein folding.
FT                                {ECO:0000269|PubMed:23385459}.
FT   STRAND       80     82       {ECO:0000244|PDB:6RO4}.
FT   STRAND       84     87       {ECO:0000244|PDB:6RO4}.
FT   HELIX        94    100       {ECO:0000244|PDB:6RO4}.
FT   TURN        101    103       {ECO:0000244|PDB:6RO4}.
FT   STRAND      105    108       {ECO:0000244|PDB:6RO4}.
FT   STRAND      111    117       {ECO:0000244|PDB:6RO4}.
FT   HELIX       120    128       {ECO:0000244|PDB:6RO4}.
FT   HELIX       133    139       {ECO:0000244|PDB:6RO4}.
FT   HELIX       141    143       {ECO:0000244|PDB:6RO4}.
FT   STRAND      150    152       {ECO:0000244|PDB:6RO4}.
FT   HELIX       153    158       {ECO:0000244|PDB:6RO4}.
FT   TURN        159    162       {ECO:0000244|PDB:6RO4}.
FT   STRAND      166    170       {ECO:0000244|PDB:6RO4}.
FT   STRAND      175    180       {ECO:0000244|PDB:6RO4}.
FT   TURN        182    184       {ECO:0000244|PDB:6RO4}.
FT   HELIX       185    188       {ECO:0000244|PDB:6RO4}.
FT   TURN        192    196       {ECO:0000244|PDB:6RO4}.
FT   STRAND      268    272       {ECO:0000244|PDB:6RO4}.
FT   HELIX       278    286       {ECO:0000244|PDB:6RO4}.
FT   STRAND      301    303       {ECO:0000244|PDB:6RO4}.
FT   HELIX       320    327       {ECO:0000244|PDB:6RO4}.
FT   STRAND      330    333       {ECO:0000244|PDB:6RO4}.
FT   STRAND      337    339       {ECO:0000244|PDB:6RO4}.
FT   HELIX       348    357       {ECO:0000244|PDB:6RO4}.
FT   STRAND      361    364       {ECO:0000244|PDB:6RO4}.
FT   HELIX       370    381       {ECO:0000244|PDB:6RO4}.
FT   TURN        386    388       {ECO:0000244|PDB:6RO4}.
FT   STRAND      389    391       {ECO:0000244|PDB:6RO4}.
FT   STRAND      393    395       {ECO:0000244|PDB:6RO4}.
FT   STRAND      404    407       {ECO:0000244|PDB:6RO4}.
FT   TURN        410    412       {ECO:0000244|PDB:6RO4}.
FT   HELIX       421    430       {ECO:0000244|PDB:6RO4}.
FT   STRAND      438    442       {ECO:0000244|PDB:6RO4}.
FT   HELIX       443    445       {ECO:0000244|PDB:6RO4}.
FT   TURN        449    451       {ECO:0000244|PDB:6RO4}.
FT   HELIX       454    457       {ECO:0000244|PDB:6RO4}.
FT   STRAND      463    468       {ECO:0000244|PDB:6RO4}.
FT   HELIX       480    483       {ECO:0000244|PDB:6RO4}.
FT   STRAND      487    490       {ECO:0000244|PDB:6RO4}.
FT   HELIX       495    498       {ECO:0000244|PDB:6RO4}.
FT   STRAND      505    512       {ECO:0000244|PDB:4ERN}.
FT   HELIX       516    524       {ECO:0000244|PDB:4ERN}.
FT   HELIX       528    530       {ECO:0000244|PDB:4ERN}.
FT   HELIX       531    536       {ECO:0000244|PDB:4ERN}.
FT   HELIX       538    552       {ECO:0000244|PDB:4ERN}.
FT   TURN        553    555       {ECO:0000244|PDB:4ERN}.
FT   STRAND      558    561       {ECO:0000244|PDB:4ERN}.
FT   HELIX       565    574       {ECO:0000244|PDB:4ERN}.
FT   STRAND      582    584       {ECO:0000244|PDB:6RO4}.
FT   HELIX       586    598       {ECO:0000244|PDB:4ERN}.
FT   STRAND      604    607       {ECO:0000244|PDB:4ERN}.
FT   HELIX       609    611       {ECO:0000244|PDB:4ERN}.
FT   TURN        612    614       {ECO:0000244|PDB:4ERN}.
FT   STRAND      620    626       {ECO:0000244|PDB:4ERN}.
FT   HELIX       633    643       {ECO:0000244|PDB:4ERN}.
FT   STRAND      651    654       {ECO:0000244|PDB:4ERN}.
FT   STRAND      656    664       {ECO:0000244|PDB:4ERN}.
FT   HELIX       668    670       {ECO:0000244|PDB:4ERN}.
FT   HELIX       671    682       {ECO:0000244|PDB:4ERN}.
FT   STRAND      686    692       {ECO:0000244|PDB:4ERN}.
FT   HELIX       696    698       {ECO:0000244|PDB:4ERN}.
FT   HELIX       706    718       {ECO:0000244|PDB:4ERN}.
FT   HELIX       721    724       {ECO:0000244|PDB:4ERN}.
SQ   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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