ERCC3_HUMAN
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 03-AUG-2022, entry version 232.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2111438; DOI=10.1128/mcb.10.6.2570-2581.1990;
RA Weeda G., van Ham R.C.A., Masurel R., Westerveld A., Odijk H., de Wit J.,
RA Bootsma D., van der Eb A.J., Hoeijmakers J.H.J.;
RT "Molecular cloning and biological characterization of the human excision
RT 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 repair
RT 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 DNA
RT 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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 transcription
RT 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 that
RT 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 functions
RT 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., 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., Wang X.W.,
RA Conaway J.W., Harris C.C., Conaway R.C., Reinberg D., Levens D.;
RT "Defective interplay of activators and repressors with TFIH in xeroderma
RT 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 BY
RP 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT 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 of
RT 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., Arlett C.F.,
RA 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 with
RT 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>3.0.co;2-w;
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): xeroderma
RT 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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the general
CC transcription and DNA repair factor IIH (TFIIH) core complex, which is
CC involved in general and transcription-coupled nucleotide excision
CC repair (NER) of damaged DNA and, when complexed to CAK, in RNA
CC transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA
CC around the lesion to allow the excision of the damaged oligonucleotide
CC and its replacement by a new DNA fragment. The ATPase activity of
CC XPB/ERCC3, but not its helicase activity, is required for DNA opening.
CC In transcription, TFIIH has an essential role in transcription
CC initiation (PubMed:8157004, PubMed:30894545). When the pre-initiation
CC complex (PIC) has been established, TFIIH is required for promoter
CC opening and promoter escape (PubMed:8157004). The ATP-dependent
CC helicase activity of XPB/ERCC3 is required for promoter opening and
CC promoter escape. Phosphorylation of the C-terminal tail (CTD) of the
CC largest subunit of RNA polymerase II by the kinase module CAK controls
CC the initiation of transcription. {ECO:0000269|PubMed:10024882,
CC ECO:0000269|PubMed:30894545, 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, which
CC is active in NER. The core complex associates with the 3-subunit CDK-
CC activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and
CC MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in
CC transcription (PubMed:9852112). Interacts with PUF60 (PubMed:10882074,
CC PubMed:11239393). Interacts with ATF7IP (PubMed:19106100). Interacts
CC with KAT2A; leading to KAT2A recruitment to promoters and acetylation
CC of histones (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 EBNA2.
CC {ECO:0000269|PubMed:7724549}.
CC -!- INTERACTION:
CC P19447; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1183307, EBI-10173507;
CC P19447; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-1183307, EBI-2548012;
CC P19447; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-1183307, EBI-739624;
CC P19447; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-1183307, EBI-742887;
CC P19447; P18074: ERCC2; NbExp=5; IntAct=EBI-1183307, EBI-6380590;
CC P19447; P51114-2: FXR1; NbExp=3; IntAct=EBI-1183307, EBI-11022345;
CC P19447; Q6ZYL4: GTF2H5; NbExp=4; IntAct=EBI-1183307, EBI-6380438;
CC P19447; O00505: KPNA3; NbExp=4; IntAct=EBI-1183307, EBI-358297;
CC P19447; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-1183307, EBI-716006;
CC P19447; P62195: PSMC5; NbExp=4; IntAct=EBI-1183307, EBI-357745;
CC P19447; P54727: RAD23B; NbExp=2; IntAct=EBI-1183307, EBI-954531;
CC P19447; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-1183307, EBI-1378139;
CC P19447; Q13573: SNW1; NbExp=3; IntAct=EBI-1183307, EBI-632715;
CC P19447; Q14142: TRIM14; NbExp=3; IntAct=EBI-1183307, EBI-2820256;
CC P19447; P14373: TRIM27; NbExp=4; IntAct=EBI-1183307, EBI-719493;
CC P19447; P98170: XIAP; NbExp=4; IntAct=EBI-1183307, EBI-517127;
CC P19447; Q01831: XPC; NbExp=2; IntAct=EBI-1183307, EBI-372610;
CC P19447; P62196: Psmc5; Xeno; NbExp=6; IntAct=EBI-1183307, EBI-357713;
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 and,
CC in some cases, neurological abnormalities. The skin develops marked
CC freckling and other pigmentation abnormalities. Some XP-B patients
CC present features of Cockayne syndrome, including cachectic dwarfism,
CC pigmentary retinopathy, ataxia, decreased nerve conduction velocities.
CC The phenotype combining xeroderma pigmentosum and Cockayne syndrome
CC traits is referred to as XP-CS complex. {ECO:0000269|PubMed:10447254,
CC ECO:0000269|PubMed:16947863, ECO:0000269|PubMed:8304337}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Trichothiodystrophy 2, photosensitive (TTD2) [MIM:616390]: A
CC form of trichothiodystrophy, an autosomal recessive disease
CC characterized by sulfur-deficient brittle hair and multisystem variable
CC abnormalities. The spectrum of clinical features varies from mild
CC disease with only hair involvement to severe disease with cutaneous,
CC neurologic and profound developmental defects. Ichthyosis, intellectual
CC and developmental disabilities, decreased fertility, abnormal
CC characteristics at birth, ocular abnormalities, short stature, and
CC infections are common manifestations. There are both photosensitive and
CC non-photosensitive forms of the disorder. {ECO:0000269|PubMed:9012405}.
CC Note=The disease is caused by variants affecting the gene represented
CC 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 and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/XPBID296.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ercc3/";
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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 PDB; 7AD8; EM; 3.50 A; A=1-782.
DR PDB; 7EGB; EM; 3.30 A; 6=1-782.
DR PDB; 7EGC; EM; 3.90 A; 6=1-782.
DR PDB; 7ENA; EM; 4.07 A; 6=1-782.
DR PDB; 7ENC; EM; 4.13 A; 6=1-782.
DR PDB; 7LBM; EM; 4.80 A; W=1-782.
DR PDB; 7NVR; EM; 4.50 A; 7=1-782.
DR PDB; 7NVV; EM; 2.90 A; 7=1-782.
DR PDB; 7NVW; EM; 4.30 A; 7=1-782.
DR PDB; 7NVX; EM; 3.90 A; 7=1-782.
DR PDB; 7NVY; EM; 7.30 A; 7=1-782.
DR PDB; 7NVZ; EM; 7.20 A; 7=1-782.
DR PDB; 7NW0; EM; 6.60 A; 7=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 PDBsum; 7AD8; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR PDBsum; 7NVV; -.
DR PDBsum; 7NVW; -.
DR PDBsum; 7NVX; -.
DR PDBsum; 7NVY; -.
DR PDBsum; 7NVZ; -.
DR PDBsum; 7NW0; -.
DR AlphaFoldDB; P19447; -.
DR SMR; P19447; -.
DR BioGRID; 108383; 145.
DR CORUM; P19447; -.
DR DIP; DIP-83N; -.
DR IntAct; P19447; 61.
DR MINT; P19447; -.
DR STRING; 9606.ENSP00000285398; -.
DR ChEMBL; CHEMBL4523193; -.
DR iPTMnet; P19447; -.
DR MetOSite; 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 Antibodypedia; 18449; 242 antibodies from 38 providers.
DR DNASU; 2071; -.
DR Ensembl; ENST00000285398.7; ENSP00000285398.2; ENSG00000163161.14.
DR GeneID; 2071; -.
DR KEGG; hsa:2071; -.
DR MANE-Select; ENST00000285398.7; ENSP00000285398.2; NM_000122.2; NP_000113.1.
DR UCSC; uc002toh.1; human.
DR CTD; 2071; -.
DR DisGeNET; 2071; -.
DR GeneCards; ERCC3; -.
DR GeneReviews; ERCC3; -.
DR HGNC; HGNC:3435; ERCC3.
DR HPA; ENSG00000163161; Low tissue specificity.
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 VEuPathDB; HostDB:ENSG00000163161; -.
DR eggNOG; KOG1123; Eukaryota.
DR GeneTree; ENSGT00390000002204; -.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; P19447; -.
DR OrthoDB; 100698at2759; -.
DR PhylomeDB; P19447; -.
DR TreeFam; TF101233; -.
DR PathwayCommons; P19447; -.
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 SignaLink; P19447; -.
DR SIGNOR; P19447; -.
DR BioGRID-ORCS; 2071; 670 hits in 1090 CRISPR screens.
DR ChiTaRS; ERCC3; human.
DR GeneWiki; XPB; -.
DR GenomeRNAi; 2071; -.
DR Pharos; P19447; Tbio.
DR PRO; PR:P19447; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P19447; protein.
DR Bgee; ENSG00000163161; Expressed in sural nerve and 182 other tissues.
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; IDA:UniProtKB.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:UniProtKB.
DR GO; GO:0097550; C:transcription 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:ATP hydrolysis 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:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
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: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: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; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
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:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II 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 Gene3D; 3.40.50.300; -; 2.
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; Deafness; Disease variant;
KW DNA damage; DNA repair; DNA-binding; Dwarfism; Helicase;
KW Host-virus interaction; Hydrolase; Ichthyosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Xeroderma pigmentosum.
FT CHAIN 1..782
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000101987"
FT DOMAIN 327..488
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 542..702
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..18
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 441..444
FT /note="DEVH box"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 340..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 99
FT /note="F -> S (in XP-B; combined with features of Cockayne
FT syndrome; mild; dbSNP:rs121913045)"
FT /evidence="ECO:0000269|PubMed:16947863,
FT ECO:0000269|PubMed:8304337"
FT /id="VAR_003632"
FT VARIANT 117
FT /note="K -> R (in dbSNP:rs1805161)"
FT /evidence="ECO:0000269|PubMed:10862089"
FT /id="VAR_014766"
FT VARIANT 119
FT /note="T -> P (in TTD2; mild; dbSNP:rs121913046)"
FT /evidence="ECO:0000269|PubMed:9012405"
FT /id="VAR_008186"
FT VARIANT 402
FT /note="G -> C (in dbSNP:rs1805162)"
FT /evidence="ECO:0000269|PubMed:10862089"
FT /id="VAR_014767"
FT VARIANT 418
FT /note="K -> Q (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035942"
FT VARIANT 704
FT /note="S -> L (in dbSNP:rs4150521)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_017294"
FT VARIANT 735
FT /note="S -> P (in dbSNP:rs4150522)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014344"
FT MUTAGEN 346
FT /note="K->R: No transcriptional activity of the
FT reconstituted TFIIH complex."
FT /evidence="ECO:0000269|PubMed:10024882"
FT MUTAGEN 782
FT /note="Missing: Impairs protein folding."
FT /evidence="ECO:0000269|PubMed:23385459"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:7NVV"
FT TURN 69..73
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:7NVV"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:7AD8"
FT HELIX 346..357
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 368..381
FT /evidence="ECO:0007829|PDB:7NVV"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 421..431
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 434..442
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:7NVV"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 453..457
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 480..483
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:7NVV"
FT HELIX 493..498
FT /evidence="ECO:0007829|PDB:7NVV"
FT STRAND 505..512
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 516..524
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 531..536
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 538..552
FT /evidence="ECO:0007829|PDB:4ERN"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:4ERN"
FT STRAND 558..561
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 565..574
FT /evidence="ECO:0007829|PDB:4ERN"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 586..598
FT /evidence="ECO:0007829|PDB:4ERN"
FT STRAND 604..607
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:4ERN"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:4ERN"
FT STRAND 620..626
FT /evidence="ECO:0007829|PDB:4ERN"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:7AD8"
FT HELIX 633..643
FT /evidence="ECO:0007829|PDB:4ERN"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:4ERN"
FT STRAND 656..664
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 668..670
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 671..682
FT /evidence="ECO:0007829|PDB:4ERN"
FT STRAND 686..692
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 706..718
FT /evidence="ECO:0007829|PDB:4ERN"
FT HELIX 721..724
FT /evidence="ECO:0007829|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
