ID IWS1_HUMAN Reviewed; 819 AA. AC Q96ST2; Q2TB65; Q6P157; Q8N3E8; Q96MI7; Q9NV97; Q9NWH8; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 2. DT 02-JUN-2021, entry version 157. DE RecName: Full=Protein IWS1 homolog; DE AltName: Full=IWS1-like protein; GN Name=IWS1; Synonyms=IWS1L; 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] (ISOFORMS 1 AND 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-696 (ISOFORM 3). RC TISSUE=Embryo, Prostate, and Teratocarcinoma; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye; 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-235; RP SER-237; SER-261; SER-263; SER-377; SER-398 AND SER-400, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-315; SER-398; RP SER-400; SER-438 AND SER-440, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRMT5. RX PubMed=17184735; DOI=10.1016/j.bbrc.2006.11.133; RA Liu Z., Zhou Z., Chen G., Bao S.; RT "A putative transcriptional elongation factor hIws1 is essential for RT mammalian cell proliferation."; RL Biochem. Biophys. Res. Commun. 353:47-53(2007). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SUPT6H AND ALYREF. RX PubMed=17234882; DOI=10.1101/gad.1503107; RA Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.; RT "The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA RT splicing and export."; RL Genes Dev. 21:160-174(2007). RN [9] RP FUNCTION, AND INTERACTION WITH SETD2 AND SUPT6H. RX PubMed=19141475; DOI=10.1101/gad.1720008; RA Yoh S.M., Lucas J.S., Jones K.A.; RT "The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and RT HYPB/Setd2-mediated histone H3K36 methylation."; RL Genes Dev. 22:3422-3434(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-287; SER-289; RP SER-313; SER-315; SER-438 AND SER-440, AND IDENTIFICATION BY MASS RP 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398 AND SER-400, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287; SER-315; SER-398; RP SER-400; THR-435 AND SER-440, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-235; RP SER-237; SER-261; SER-263; SER-313; SER-315; SER-363; SER-365; SER-377; RP SER-400; SER-415; SER-420; SER-422; SER-438 AND SER-440, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-196; RP SER-198; SER-235; SER-237; SER-261; SER-263; SER-287; SER-289; SER-300; RP SER-302; SER-304; SER-313; SER-329; SER-333; SER-377; SER-398; SER-400; RP SER-415; SER-420; SER-438 AND SER-440, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-196; SER-198; RP SER-235; SER-237; SER-248; SER-250; SER-261; SER-263; SER-274; SER-276; RP SER-287; SER-289; SER-329; SER-377; SER-398; SER-400; SER-438; SER-440 AND RP THR-725, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-183; SER-196; RP SER-198; SER-235; SER-237; SER-250; SER-261; SER-263; SER-276; SER-287; RP SER-289; SER-313; SER-398; SER-400; SER-415; SER-420; SER-422; SER-438; RP SER-440; SER-480; SER-511 AND SER-513, AND IDENTIFICATION BY MASS RP 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 [21] RP INTERACTION WITH HDGFRP2. RX PubMed=25689719; DOI=10.1016/j.bbrc.2015.02.042; RA Gao K., Xu C., Jin X., Wumaier R., Ma J., Peng J., Wang Y., Tang Y., Yu L., RA Zhang P.; RT "HDGF-related protein-2 (HRP-2) acts as an oncogene to promote cell growth RT in hepatocellular carcinoma."; RL Biochem. Biophys. Res. Commun. 458:849-855(2015). RN [22] {ECO:0007744|PDB:6EMR} RP STRUCTURE BY NMR OF 447-548 IN COMPLEX WITH PSIP1, INTERACTION WITH PSIP1, RP DOMAIN IBM MOTIF, MUTAGENESIS OF ILE-476; PHE-477 AND SER-480, AND RP PHOSPHORYLATION AT SER-461; SER-463; SER-465; SER-480 AND THR-489. RX PubMed=29997176; DOI=10.1073/pnas.1803909115; RA Sharma S., Cermakova K., De Rijck J., Demeulemeester J., Fabry M., RA El Ashkar S., Van Belle S., Lepsik M., Tesina P., Duchoslav V., Novak P., RA Hubalek M., Srb P., Christ F., Rezacova P., Hodges H.C., Debyser Z., RA Veverka V.; RT "Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase- RT dependent phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 115:E7053-E7062(2018). CC -!- FUNCTION: Transcription factor which plays a key role in defining the CC composition of the RNA polymerase II (RNAPII) elongation complex and in CC modulating the production of mature mRNA transcripts. Acts as an CC assembly factor to recruit various factors to the RNAPII elongation CC complex and is recruited to the complex via binding to the CC transcription elongation factor SUPT6H bound to the C-terminal domain CC (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex CC recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone CC modifying enzymes (such as SETD2) to ensure proper mRNA splicing, CC efficient mRNA export and elongation-coupled H3K36 methylation, a CC signature chromatin mark of active transcription. CC {ECO:0000269|PubMed:17184735, ECO:0000269|PubMed:17234882, CC ECO:0000269|PubMed:19141475}. CC -!- SUBUNIT: Interacts with SUPT6H; binds preferentially to the POLR2A- CC bound SUPT6H. Interacts with ALYREF/THOC4, SETD2 and PRMT5. Interacts CC with HDGFRP2. Interacts (via IBM motif) with PSIP1 (via IBD domain); CC phosphorylation increases its affinity for PSIP1 (PubMed:29997176). CC {ECO:0000269|PubMed:17184735, ECO:0000269|PubMed:17234882, CC ECO:0000269|PubMed:19141475, ECO:0000269|PubMed:25689719, CC ECO:0000269|PubMed:29997176}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, CC ECO:0000269|PubMed:17184735, ECO:0000269|PubMed:17234882}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96ST2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96ST2-2; Sequence=VSP_016992; CC Name=3; CC IsoId=Q96ST2-3; Sequence=VSP_016993; CC -!- PTM: Phosphorylation increases its interaction with PSIP1. CC {ECO:0000269|PubMed:29997176}. CC -!- SIMILARITY: Belongs to the IWS1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH65279.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA91858.1; Type=Erroneous initiation; Note=Truncated 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; AK000868; BAA91402.1; -; mRNA. DR EMBL; AK001717; BAA91858.1; ALT_INIT; mRNA. DR EMBL; AK027561; BAB55198.1; -; mRNA. DR EMBL; AK056881; BAB71301.1; -; mRNA. DR EMBL; AL834178; CAD38875.1; -; mRNA. DR EMBL; BC065279; AAH65279.1; ALT_SEQ; mRNA. DR EMBL; BC110536; AAI10537.1; -; mRNA. DR EMBL; BC110537; AAI10538.1; -; mRNA. DR CCDS; CCDS2146.1; -. [Q96ST2-1] DR RefSeq; NP_060439.2; NM_017969.2. [Q96ST2-1] DR PDB; 6EMR; NMR; -; A=447-548. DR PDBsum; 6EMR; -. DR SMR; Q96ST2; -. DR BioGRID; 120807; 60. DR IntAct; Q96ST2; 29. DR MINT; Q96ST2; -. DR STRING; 9606.ENSP00000295321; -. DR iPTMnet; Q96ST2; -. DR MetOSite; Q96ST2; -. DR PhosphoSitePlus; Q96ST2; -. DR BioMuta; IWS1; -. DR DMDM; 85542184; -. DR EPD; Q96ST2; -. DR jPOST; Q96ST2; -. DR MassIVE; Q96ST2; -. DR MaxQB; Q96ST2; -. DR PaxDb; Q96ST2; -. DR PeptideAtlas; Q96ST2; -. DR PRIDE; Q96ST2; -. DR ProteomicsDB; 78143; -. [Q96ST2-1] DR ProteomicsDB; 78144; -. [Q96ST2-2] DR ProteomicsDB; 78145; -. [Q96ST2-3] DR Antibodypedia; 47563; 108 antibodies. DR DNASU; 55677; -. DR Ensembl; ENST00000295321; ENSP00000295321; ENSG00000163166. [Q96ST2-1] DR GeneID; 55677; -. DR KEGG; hsa:55677; -. DR UCSC; uc002ton.3; human. [Q96ST2-1] DR CTD; 55677; -. DR DisGeNET; 55677; -. DR GeneCards; IWS1; -. DR HGNC; HGNC:25467; IWS1. DR HPA; ENSG00000163166; Low tissue specificity. DR neXtProt; NX_Q96ST2; -. DR OpenTargets; ENSG00000163166; -. DR PharmGKB; PA144596419; -. DR VEuPathDB; HostDB:ENSG00000163166.13; -. DR eggNOG; KOG1793; Eukaryota. DR GeneTree; ENSGT00720000108834; -. DR HOGENOM; CLU_018182_0_0_1; -. DR InParanoid; Q96ST2; -. DR OMA; EDRPNQH; -. DR OrthoDB; 380765at2759; -. DR PhylomeDB; Q96ST2; -. DR TreeFam; TF315504; -. DR PathwayCommons; Q96ST2; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR BioGRID-ORCS; 55677; 45 hits in 1006 CRISPR screens. DR ChiTaRS; IWS1; human. DR GeneWiki; IWS1; -. DR GenomeRNAi; 55677; -. DR Pharos; Q96ST2; Tbio. DR PRO; PR:Q96ST2; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q96ST2; protein. DR Bgee; ENSG00000163166; Expressed in sural nerve and 215 other tissues. DR ExpressionAtlas; Q96ST2; baseline and differential. DR Genevisible; Q96ST2; HS. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central. DR GO; GO:2001253; P:regulation of histone H3-K36 trimethylation; IMP:UniProtKB. DR GO; GO:0090239; P:regulation of histone H4 acetylation; IMP:UniProtKB. DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IMP:UniProtKB. DR GO; GO:0050684; P:regulation of mRNA processing; IMP:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome. DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome. DR Gene3D; 1.20.930.10; -; 1. DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf. DR InterPro; IPR017923; TFIIS_N. DR Pfam; PF08711; Med26; 1. DR SUPFAM; SSF47676; SSF47676; 1. DR PROSITE; PS51319; TFIIS_N; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; mRNA processing; KW mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Transcription; Transcription regulation; Transport. FT CHAIN 1..819 FT /note="Protein IWS1 homolog" FT /id="PRO_0000083346" FT REPEAT 235..260 FT /note="1" FT REPEAT 261..286 FT /note="2" FT REPEAT 287..296 FT /note="3; half-length" FT DOMAIN 614..692 FT /note="TFIIS N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649" FT REGION 1..520 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 235..296 FT /note="3 X approximate tandem repeats" FT REGION 523..819 FT /note="Interaction with SUPT6H and ALYREF" FT /evidence="ECO:0000269|PubMed:17234882" FT REGION 696..728 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 469..495 FT /note="Integrase domain-binding motif (IBM)" FT /evidence="ECO:0000269|PubMed:29997176" FT COMPBIAS 30..71 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 82..303 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 315..463 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 475..493 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 494..520 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 698..714 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 27 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3SWT4" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 69 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 157 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 159 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 198 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3SWT4" FT MOD_RES 235 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 237 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 248 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 250 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 261 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 263 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 274 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 276 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 287 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 289 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 300 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 302 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 304 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 313 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 315 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT MOD_RES 329 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 333 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 351 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3SWT4" FT MOD_RES 362 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C1D8" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 365 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 377 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 398 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15302935, FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 400 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 415 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 420 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 422 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 426 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C1D8" FT MOD_RES 435 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 438 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 440 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 461 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:29997176" FT MOD_RES 463 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:29997176" FT MOD_RES 465 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:29997176" FT MOD_RES 480 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:29997176, FT ECO:0007744|PubMed:24275569" FT MOD_RES 489 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:29997176" FT MOD_RES 511 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 513 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 725 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 20..344 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016992" FT VAR_SEQ 54..260 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016993" FT VARIANT 390 FT /note="A -> V (in dbSNP:rs34377117)" FT /id="VAR_055975" FT VARIANT 425 FT /note="V -> I (in dbSNP:rs34785867)" FT /id="VAR_055976" FT MUTAGEN 476 FT /note="I->A: Loss of interaction with PSIP1; when FT associated with A-477." FT /evidence="ECO:0000269|PubMed:29997176" FT MUTAGEN 477 FT /note="F->A: Loss of interaction with PSIP1; when FT associated with A-476." FT /evidence="ECO:0000269|PubMed:29997176" FT MUTAGEN 480 FT /note="S->D: Phosphomimetic mutant. Moderate increase in FT interaction with PSIP1." FT /evidence="ECO:0000269|PubMed:29997176" FT CONFLICT 244 FT /note="K -> R (in Ref. 1; BAB55198)" FT /evidence="ECO:0000305" FT CONFLICT 530 FT /note="E -> G (in Ref. 1; BAA91402)" FT /evidence="ECO:0000305" FT CONFLICT 559 FT /note="V -> D (in Ref. 1; BAB55198)" FT /evidence="ECO:0000305" FT CONFLICT 786 FT /note="S -> G (in Ref. 1; BAB55198)" FT /evidence="ECO:0000305" FT HELIX 469..476 FT /evidence="ECO:0007829|PDB:6EMR" FT TURN 477..481 FT /evidence="ECO:0007829|PDB:6EMR" FT HELIX 482..484 FT /evidence="ECO:0007829|PDB:6EMR" FT HELIX 493..495 FT /evidence="ECO:0007829|PDB:6EMR" FT HELIX 512..515 FT /evidence="ECO:0007829|PDB:6EMR" FT HELIX 528..539 FT /evidence="ECO:0007829|PDB:6EMR" SQ SEQUENCE 819 AA; 91955 MW; C9749A2C2DC05D72 CRC64; MDSEYYSGDQ SDDGGATPVQ DERDSGSDGE DDVNEQHSGS DTGSVERHSE NETSDREDGL PKGHHVTDSE NDEPLNLNAS DSESEELHRQ KDSDSESEER AEPPASDSEN EDVNQHGSDS ESEETRKLPG SDSENEELLN GHASDSENED VGKHPASDSE IEELQKSPAS DSETEDALKP QISDSESEEP PRHQASDSEN EEPPKPRMSD SESEELPKPQ VSDSESEEPP RHQASDSENE ELPKPRISDS ESEDPPRHQA SDSENEELPK PRISDSESED PPRNQASDSE NEELPKPRVS DSESEGPQKG PASDSETEDA SRHKQKPESD DDSDRENKGE DTEMQNDSFH SDSHMDRKKF HSSDSEEEEH KKQKMDSDED EKEGEEEKVA KRKAAVLSDS EDEEKASAKK SRVVSDADDS DSDAVSDKSG KREKTIASDS EEEAGKELSD KKNEEKDLFG SDSESGNEEE NLIADIFGES GDEEEEEFTG FNQEDLEEEK GETQVKEAED SDSDDNIKRG KHMDFLSDFE MMLQRKKSMS GKRRRNRDGG TFISDADDVV SAMIVKMNEA AEEDRQLNNQ KKPALKKLTL LPAVVMHLKK QDLKETFIDS GVMSAIKEWL SPLPDRSLPA LKIREELLKI LQELPSVSQE TLKHSGIGRA VMYLYKHPKE SRSNKDMAGK LINEWSRPIF GLTSNYKGMT REEREQRDLE QMPQRRRMNS TGGQTPRRDL EKVLTGEEKA LRPGDPGFCA RARVPMPSNK DYVVRPKWNV EMESSRFQAT SKKGISRLDK QMRKFTDIRK KSRSAHAVKI SIEGNKMPL //