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 27-MAR-2024, entry version 241. 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; DOI=10.1002/j.1460-2075.1994.tb06428.x; 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 STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), AND SUBUNIT. RX PubMed=27193682; DOI=10.1038/nature17970; RA He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.; RT "Near-atomic resolution visualization of human transcription promoter RT opening."; RL Nature 533:359-365(2016). RN [21] 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 [22] 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 [23] 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 [24] 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 [25] 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). Part of TBP-based Pol II pre-initiation CC complex (PIC), in which Pol II core assembles with general CC transcription factors and other specific initiation factors including CC GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3, CC GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit CC PIC complex mediates DNA unwinding and targets Pol II core to the CC transcription start site where the first phosphodiester bond forms. CC {ECO:0000269|PubMed:10882074, ECO:0000269|PubMed:11239393, CC ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:27193682, 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=3; 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="https://atlasgeneticsoncology.org/gene/296/XPB"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ercc3/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8BVW; EM; 4.00 A; 0=1-772. DR PDB; 8BYQ; EM; 4.10 A; 0=1-782. DR PDB; 8EBS; EM; 4.00 A; A=1-782. DR PDB; 8EBT; EM; 3.90 A; A=52-721. DR PDB; 8EBU; EM; 3.30 A; A=1-782. DR PDB; 8EBV; EM; 7.10 A; A=1-782. DR PDB; 8EBW; EM; 5.60 A; A=1-782. DR PDB; 8EBX; EM; 3.60 A; A=1-782. DR PDB; 8EBY; EM; 3.60 A; A=1-782. DR PDB; 8GXQ; EM; 5.04 A; HH=1-782. DR PDB; 8GXS; EM; 4.16 A; HH=1-782. DR PDB; 8WAK; EM; 5.47 A; 6=1-782. DR PDB; 8WAL; EM; 8.52 A; 6=1-782. DR PDB; 8WAN; EM; 6.07 A; 6=1-782. DR PDB; 8WAO; EM; 6.40 A; 6=1-782. DR PDB; 8WAP; EM; 5.85 A; 6=1-782. DR PDB; 8WAQ; EM; 6.29 A; 6=1-782. DR PDB; 8WAR; EM; 7.20 A; 6=1-782. DR PDB; 8WAS; EM; 6.13 A; 6=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 PDBsum; 8BVW; -. DR PDBsum; 8BYQ; -. DR PDBsum; 8EBS; -. DR PDBsum; 8EBT; -. DR PDBsum; 8EBU; -. DR PDBsum; 8EBV; -. DR PDBsum; 8EBW; -. DR PDBsum; 8EBX; -. DR PDBsum; 8EBY; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR PDBsum; 8WAK; -. DR PDBsum; 8WAL; -. DR PDBsum; 8WAN; -. DR PDBsum; 8WAO; -. DR PDBsum; 8WAP; -. DR PDBsum; 8WAQ; -. DR PDBsum; 8WAR; -. DR PDBsum; 8WAS; -. DR AlphaFoldDB; P19447; -. DR EMDB; EMD-0452; -. DR EMDB; EMD-12610; -. DR EMDB; EMD-12614; -. DR EMDB; EMD-12615; -. DR EMDB; EMD-12616; -. DR EMDB; EMD-12617; -. DR EMDB; EMD-12618; -. DR EMDB; EMD-12619; -. DR EMDB; EMD-16274; -. DR EMDB; EMD-16331; -. DR EMDB; EMD-23255; -. DR EMDB; EMD-27996; -. DR EMDB; EMD-27997; -. DR EMDB; EMD-27998; -. DR EMDB; EMD-27999; -. DR EMDB; EMD-28000; -. DR EMDB; EMD-28001; -. DR EMDB; EMD-28002; -. DR EMDB; EMD-29673; -. DR EMDB; EMD-29674; -. DR EMDB; EMD-31111; -. DR EMDB; EMD-31112; -. DR EMDB; EMD-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR EMDB; EMD-3802; -. DR EMDB; EMD-4970; -. DR EMDB; EMD-8131; -. DR EMDB; EMD-8132; -. DR EMDB; EMD-8133; -. DR EMDB; EMD-8134; -. DR SMR; P19447; -. DR BioGRID; 108383; 178. DR ComplexPortal; CPX-2395; General transcription factor TFIIH complex. DR CORUM; P19447; -. DR DIP; DIP-83N; -. DR IntAct; P19447; 61. DR MINT; P19447; -. DR STRING; 9606.ENSP00000285398; -. DR ChEMBL; CHEMBL4523193; -. DR MoonProt; P19447; -. 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; 9606-ENSP00000285398; -. DR PeptideAtlas; P19447; -. DR ProteomicsDB; 53665; -. DR Pumba; P19447; -. DR Antibodypedia; 18449; 279 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 AGR; HGNC:3435; -. 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; 1360679at2759; -. 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; 703 hits in 1184 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 184 other cell types or tissues. DR ExpressionAtlas; P19447; baseline and differential. 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: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: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 by RNA polymerase II; TAS:Reactome. DR GO; GO:0006367; P:transcription initiation at 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 CDD; cd18029; DEXHc_XPB; 1. DR CDD; cd18789; SF2_C_XPB; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00603; rad25; 1. DR PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1. DR PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1. DR Pfam; PF16203; ERCC3_RAD25_C; 1. DR Pfam; PF13625; Helicase_C_3; 1. DR Pfam; PF04851; ResIII; 1. DR PRINTS; PR00851; XRODRMPGMNTB. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR Genevisible; P19447; HS. 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 STRAND 55..60 FT /evidence="ECO:0007829|PDB:8EBU" 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 HELIX 200..202 FT /evidence="ECO:0007829|PDB:8EBU" 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:8EBU" 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..344 FT /evidence="ECO:0007829|PDB:8EBU" 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:8EBU" 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 //