ID UVSSA_HUMAN Reviewed; 709 AA. AC Q2YD98; A8K9E6; B2RU11; Q8WTX4; Q9P1Z8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 27-MAR-2024, entry version 130. DE RecName: Full=UV-stimulated scaffold protein A; GN Name=UVSSA; Synonyms=KIAA1530; 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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-620. RC TISSUE=Brain; RX PubMed=10819331; DOI=10.1093/dnares/7.2.143; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:143-150(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LEU-620. RC TISSUE=Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP LEU-620. RC TISSUE=Duodenum, Lung, and Skin; 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND SER-287, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [7] RP FUNCTION, INVOLVEMENT IN UVSS3, MUTAGENESIS OF TRP-120 AND RP 157-ARG--ARG-159, VARIANT UVSS3 ARG-32, AND CHARACTERIZATION OF VARIANT RP UVSS3 ARG-32. RX PubMed=22466610; DOI=10.1038/ng.2229; RA Nakazawa Y., Sasaki K., Mitsutake N., Matsuse M., Shimada M., Nardo T., RA Takahashi Y., Ohyama K., Ito K., Mishima H., Nomura M., Kinoshita A., RA Ono S., Takenaka K., Masuyama R., Kudo T., Slor H., Utani A., Tateishi S., RA Yamashita S., Stefanini M., Lehmann A.R., Yoshiura K.I., Ogi T.; RT "Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase RT IIo processing in transcription-coupled nucleotide-excision repair."; RL Nat. Genet. 44:586-592(2012). RN [8] RP FUNCTION, INVOLVEMENT IN UVSS3, SUBCELLULAR LOCATION, UBIQUITINATION, AND RP INTERACTION WITH USP7 AND RNA POLYMERASE II. RX PubMed=22466611; DOI=10.1038/ng.2230; RA Schwertman P., Lagarou A., Dekkers D.H., Raams A., van der Hoek A.C., RA Laffeber C., Hoeijmakers J.H., Demmers J.A., Fousteri M., Vermeulen W., RA Marteijn J.A.; RT "UV-sensitive syndrome protein UVSSA recruits USP7 to regulate RT transcription-coupled repair."; RL Nat. Genet. 44:598-602(2012). RN [9] RP FUNCTION, INVOLVEMENT IN UVSS3, SUBCELLULAR LOCATION, AND INTERACTION WITH RP ERCC6; ERCC8 AND USP7. RX PubMed=22466612; DOI=10.1038/ng.2228; RA Zhang X., Horibata K., Saijo M., Ishigami C., Ukai A., Kanno S.I., RA Tahara H., Neilan E.G., Honma M., Nohmi T., Yasui A., Tanaka K.; RT "Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in RT transcription-coupled DNA repair."; RL Nat. Genet. 44:593-597(2012). RN [10] RP IDENTIFICATION 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 [11] 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 [12] RP FUNCTION, INTERACTION WITH RNA POLYMERASE II AND THE TFIIH COMPLEX, RP UBIQUITINATION AT LYS-414, AND MUTAGENESIS OF PHE-408 AND VAL-411. RX PubMed=32142649; DOI=10.1016/j.cell.2020.02.010; RA Nakazawa Y., Hara Y., Oka Y., Komine O., van den Heuvel D., Guo C., RA Daigaku Y., Isono M., He Y., Shimada M., Kato K., Jia N., Hashimoto S., RA Kotani Y., Miyoshi Y., Tanaka M., Sobue A., Mitsutake N., Suganami T., RA Masuda A., Ohno K., Nakada S., Mashimo T., Yamanaka K., Luijsterburg M.S., RA Ogi T.; RT "Ubiquitination of DNA Damage-Stalled RNAPII Promotes Transcription-Coupled RT Repair."; RL Cell 180:1228-1244(2020). CC -!- FUNCTION: Factor involved in transcription-coupled nucleotide excision CC repair (TC-NER), a mechanism that rapidly removes RNA polymerase II- CC blocking lesions from the transcribed strand of active genes CC (PubMed:22466610, PubMed:22466611, PubMed:22466612). Facilitates the CC ubiquitination of the elongating form of RNA polymerase II (RNA pol CC IIo) at DNA damage sites, thereby promoting RNA pol IIo backtracking CC and access by the TC-NER machinery to lesion sites (PubMed:22466611, CC PubMed:32142649). Acts by promoting stabilization of ERCC6 by CC recruiting deubiquitinating enzyme USP7 to TC-NER complexes, preventing CC UV-induced degradation of ERCC6 by the proteasome (PubMed:22466611, CC PubMed:22466612). Also facilitates transfer of TFIIH to RNA polymerase CC II (PubMed:32142649). Not involved in processing oxidative damage CC (PubMed:22466612). {ECO:0000269|PubMed:22466610, CC ECO:0000269|PubMed:22466611, ECO:0000269|PubMed:22466612, CC ECO:0000269|PubMed:32142649}. CC -!- SUBUNIT: Interacts with the elongating form of RNA polymerase II (RNA CC pol IIo) during transcription stress (PubMed:22466611, CC PubMed:32142649). Interacts with the TFIIH complex during transcription CC stress (PubMed:32142649). Interacts with ERCC6 (PubMed:22466612). CC Interacts with ERCC8 (PubMed:22466612). Interacts with USP7 CC (PubMed:22466612, PubMed:22466611). {ECO:0000269|PubMed:22466611, CC ECO:0000269|PubMed:22466612, ECO:0000269|PubMed:32142649}. CC -!- INTERACTION: CC Q2YD98; O00505: KPNA3; NbExp=3; IntAct=EBI-11153331, EBI-358297; CC Q2YD98; P43358: MAGEA4; NbExp=3; IntAct=EBI-11153331, EBI-743122; CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:22466611, CC ECO:0000269|PubMed:22466612}. Note=Accumulates at UV DNA damage sites. CC {ECO:0000269|PubMed:22466611}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q2YD98-1; Sequence=Displayed; CC Name=2; CC IsoId=Q2YD98-2; Sequence=VSP_030932; CC -!- PTM: Monoubiquitinated at Lys-414 in response to transcription stress; CC this promotes efficient transfer of TFIIH to stalled RNA polymerase II. CC {ECO:0000269|PubMed:22466611, ECO:0000269|PubMed:32142649}. CC -!- DISEASE: UV-sensitive syndrome 3 (UVSS3) [MIM:614640]: An autosomal CC recessive disorder characterized by cutaneous photosensitivity and CC slight dyspigmentation, without an increased risk of skin tumors. CC {ECO:0000269|PubMed:22466610, ECO:0000269|PubMed:22466611, CC ECO:0000269|PubMed:22466612}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the UVSSA family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA96054.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AB040963; BAA96054.1; ALT_INIT; mRNA. DR EMBL; AK292661; BAF85350.1; -; mRNA. DR EMBL; AC078852; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC118281; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC021930; AAH21930.1; -; mRNA. DR EMBL; BC110331; AAI10332.1; -; mRNA. DR EMBL; BC140901; AAI40902.1; -; mRNA. DR CCDS; CCDS33938.1; -. [Q2YD98-1] DR RefSeq; NP_001304863.1; NM_001317934.1. [Q2YD98-1] DR RefSeq; NP_001304864.1; NM_001317935.1. [Q2YD98-1] DR RefSeq; NP_065945.2; NM_020894.3. [Q2YD98-1] DR RefSeq; XP_016863979.1; XM_017008490.1. [Q2YD98-1] DR RefSeq; XP_016863980.1; XM_017008491.1. DR RefSeq; XP_016863981.1; XM_017008492.1. [Q2YD98-1] DR RefSeq; XP_016863982.1; XM_017008493.1. [Q2YD98-1] DR RefSeq; XP_016863983.1; XM_017008494.1. [Q2YD98-1] DR PDB; 5XV8; NMR; -; A=390-434. DR PDB; 7OO3; EM; 2.80 A; c=1-709. DR PDB; 7OOP; EM; 2.90 A; c=1-709. DR PDB; 7OPC; EM; 3.00 A; c=1-709. DR PDB; 7OPD; EM; 3.00 A; c=1-709. DR PDB; 8B3D; EM; 2.60 A; c=1-709. DR PDBsum; 5XV8; -. DR PDBsum; 7OO3; -. DR PDBsum; 7OOP; -. DR PDBsum; 7OPC; -. DR PDBsum; 7OPD; -. DR PDBsum; 8B3D; -. DR AlphaFoldDB; Q2YD98; -. DR EMDB; EMD-13004; -. DR EMDB; EMD-13010; -. DR EMDB; EMD-13015; -. DR EMDB; EMD-13016; -. DR EMDB; EMD-15825; -. DR SMR; Q2YD98; -. DR BioGRID; 121689; 37. DR IntAct; Q2YD98; 5. DR MINT; Q2YD98; -. DR STRING; 9606.ENSP00000425130; -. DR iPTMnet; Q2YD98; -. DR PhosphoSitePlus; Q2YD98; -. DR BioMuta; UVSSA; -. DR DMDM; 296434546; -. DR EPD; Q2YD98; -. DR jPOST; Q2YD98; -. DR MassIVE; Q2YD98; -. DR MaxQB; Q2YD98; -. DR PaxDb; 9606-ENSP00000374501; -. DR PeptideAtlas; Q2YD98; -. DR ProteomicsDB; 61547; -. [Q2YD98-1] DR ProteomicsDB; 61548; -. [Q2YD98-2] DR Pumba; Q2YD98; -. DR Antibodypedia; 22237; 65 antibodies from 18 providers. DR DNASU; 57654; -. DR Ensembl; ENST00000389851.10; ENSP00000374501.4; ENSG00000163945.19. [Q2YD98-1] DR Ensembl; ENST00000507531.5; ENSP00000421741.1; ENSG00000163945.19. [Q2YD98-1] DR Ensembl; ENST00000511216.6; ENSP00000425130.1; ENSG00000163945.19. [Q2YD98-1] DR Ensembl; ENST00000512728.5; ENSP00000427701.1; ENSG00000163945.19. [Q2YD98-2] DR Ensembl; ENST00000677286.1; ENSP00000503948.1; ENSG00000163945.19. [Q2YD98-1] DR Ensembl; ENST00000679192.1; ENSP00000504544.1; ENSG00000163945.19. [Q2YD98-1] DR GeneID; 57654; -. DR KEGG; hsa:57654; -. DR MANE-Select; ENST00000389851.10; ENSP00000374501.4; NM_020894.4; NP_065945.2. DR UCSC; uc003gde.5; human. [Q2YD98-1] DR AGR; HGNC:29304; -. DR CTD; 57654; -. DR DisGeNET; 57654; -. DR GeneCards; UVSSA; -. DR HGNC; HGNC:29304; UVSSA. DR HPA; ENSG00000163945; Low tissue specificity. DR MalaCards; UVSSA; -. DR MIM; 614632; gene. DR MIM; 614640; phenotype. DR neXtProt; NX_Q2YD98; -. DR OpenTargets; ENSG00000163945; -. DR Orphanet; 178338; UV-sensitive syndrome. DR PharmGKB; PA162393105; -. DR VEuPathDB; HostDB:ENSG00000163945; -. DR eggNOG; KOG2374; Eukaryota. DR GeneTree; ENSGT00390000000377; -. DR HOGENOM; CLU_023577_0_0_1; -. DR InParanoid; Q2YD98; -. DR OMA; EEHAEMR; -. DR OrthoDB; 11574at2759; -. DR PhylomeDB; Q2YD98; -. DR TreeFam; TF321660; -. DR PathwayCommons; Q2YD98; -. 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 SignaLink; Q2YD98; -. DR BioGRID-ORCS; 57654; 26 hits in 1153 CRISPR screens. DR ChiTaRS; UVSSA; human. DR GeneWiki; KIAA1530; -. DR GenomeRNAi; 57654; -. DR Pharos; Q2YD98; Tbio. DR PRO; PR:Q2YD98; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q2YD98; Protein. DR Bgee; ENSG00000163945; Expressed in oviduct epithelium and 183 other cell types or tissues. DR ExpressionAtlas; Q2YD98; baseline and differential. DR GO; GO:0005694; C:chromosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB. DR GO; GO:0009411; P:response to UV; IMP:UniProtKB. DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:UniProtKB. DR Gene3D; 1.25.40.90; -; 1. DR InterPro; IPR008942; ENTH_VHS. DR InterPro; IPR018610; UVSSA. DR InterPro; IPR049431; UVSSA_C. DR InterPro; IPR049408; UVSSA_N_a-solenoid_rpt. DR PANTHER; PTHR28670; UV-STIMULATED SCAFFOLD PROTEIN A; 1. DR PANTHER; PTHR28670:SF1; UV-STIMULATED SCAFFOLD PROTEIN A; 1. DR Pfam; PF09740; DUF2043; 1. DR Pfam; PF20867; UVSSA_N; 1. DR Genevisible; Q2YD98; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosome; Coiled coil; KW Disease variant; DNA damage; DNA repair; Isopeptide bond; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1..709 FT /note="UV-stimulated scaffold protein A" FT /id="PRO_0000317282" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..145 FT /note="VHS-like" FT REGION 230..289 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 386..406 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 469..495 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 588..655 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 165..199 FT /evidence="ECO:0000255" FT COMPBIAS 588..628 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 281 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 287 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT CROSSLNK 414 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000305|PubMed:32142649" FT VAR_SEQ 1..449 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_030932" FT VARIANT 32 FT /note="C -> R (in UVSS3; mild phenotype; impairs FT transcription-coupled nucleotide excision repair ability; FT dbSNP:rs387907164)" FT /evidence="ECO:0000269|PubMed:22466610" FT /id="VAR_067798" FT VARIANT 391 FT /note="R -> H (in dbSNP:rs2276904)" FT /id="VAR_038499" FT VARIANT 620 FT /note="P -> L (in dbSNP:rs28522910)" FT /evidence="ECO:0000269|PubMed:10819331, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334" FT /id="VAR_038500" FT MUTAGEN 120 FT /note="W->A: Impairs transcription-coupled nucleotide FT excision repair ability." FT /evidence="ECO:0000269|PubMed:22466610" FT MUTAGEN 157..159 FT /note="RKR->EEE: Impairs transcription-coupled nucleotide FT excision repair ability." FT /evidence="ECO:0000269|PubMed:22466610" FT MUTAGEN 408 FT /note="F->A: Impairs interaction with the TFIIH complex." FT /evidence="ECO:0000269|PubMed:32142649" FT MUTAGEN 411 FT /note="V->A: Impairs interaction with the TFIIH complex." FT /evidence="ECO:0000269|PubMed:32142649" FT HELIX 2..14 FT /evidence="ECO:0007829|PDB:8B3D" FT HELIX 22..34 FT /evidence="ECO:0007829|PDB:8B3D" FT HELIX 36..51 FT /evidence="ECO:0007829|PDB:8B3D" FT HELIX 55..71 FT /evidence="ECO:0007829|PDB:8B3D" FT HELIX 74..80 FT /evidence="ECO:0007829|PDB:8B3D" FT HELIX 83..90 FT /evidence="ECO:0007829|PDB:8B3D" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:7OO3" FT HELIX 103..124 FT /evidence="ECO:0007829|PDB:8B3D" FT TURN 125..127 FT /evidence="ECO:0007829|PDB:8B3D" FT HELIX 129..140 FT /evidence="ECO:0007829|PDB:8B3D" FT TURN 392..395 FT /evidence="ECO:0007829|PDB:5XV8" FT STRAND 409..411 FT /evidence="ECO:0007829|PDB:5XV8" FT STRAND 582..585 FT /evidence="ECO:0007829|PDB:8B3D" FT TURN 586..588 FT /evidence="ECO:0007829|PDB:8B3D" FT STRAND 600..602 FT /evidence="ECO:0007829|PDB:8B3D" FT HELIX 603..618 FT /evidence="ECO:0007829|PDB:8B3D" FT HELIX 661..665 FT /evidence="ECO:0007829|PDB:8B3D" FT HELIX 668..676 FT /evidence="ECO:0007829|PDB:8B3D" FT HELIX 679..698 FT /evidence="ECO:0007829|PDB:8B3D" SQ SEQUENCE 709 AA; 80591 MW; 34698BE37A43BF2F CRC64; MDQKLSKLVE ELTTSGEPRL NPEKMKELKK ICKSSEEQLS RAYRLLIAQL TQEHAEIRLS AFQIVEELFV RSHQFRMLVV SNFQEFLELT LGTDPAQPLP PPREAAQRLR QATTRAVEGW NEKFGEAYKK LALGYHFLRH NKKVDFQDTN ARSLAERKRE EEKQKHLDKI YQERASQAER EMQEMSGEIE SCLTEVESCF RLLVPFDFDP NPETESLGMA SGMSDALRSS CAGQVGPCRS GTPDPRDGEQ PCCSRDLPAS AGHPRAGGGA QPSQTATGDP SDEDEDSDLE EFVRSHGLGS HKYTLDVELC SEGLKVQENE DNLALIHAAR DTLKLIRNKF LPAVCSWIQR FTRVGTHGGC LKRAIDLKAE LELVLRKYKE LDIEPEGGER RRTEALGDAE EDEDDEDFVE VPEKEGYEPH IPDHLRPEYG LEAAPEKDTV VRCLRTRTRM DEEVSDPTSA AAQLRQLRDH LPPPSSASPS RALPEPQEAQ KLAAERARAP VVPYGVDLHY WGQELPTAGK IVKSDSQHRF WKPSEVEEEV VNADISEMLR SRHITFAGKF EPVQHWCRAP RPDGRLCERQ DRLKCPFHGK IVPRDDEGRP LDPEDRAREQ RRQLQKQERP EWQDPELMRD VEAATGQDLG SSRYSGKGRG KKRRYPSLTN LKAQADTARA RIGRKVFAKA AVRRVVAAMN RMDQKKHEKF SNQFNYALN //