IWS1_HUMAN
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 03-AUG-2022, entry version 161.
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};
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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 PDB; 6ZV1; NMR; -; A=550-692.
DR PDB; 6ZV4; NMR; -; A=447-471.
DR PDBsum; 6EMR; -.
DR PDBsum; 6ZV1; -.
DR PDBsum; 6ZV4; -.
DR AlphaFoldDB; Q96ST2; -.
DR SMR; Q96ST2; -.
DR BioGRID; 120807; 133.
DR IntAct; Q96ST2; 31.
DR MINT; Q96ST2; -.
DR STRING; 9606.ENSP00000295321; -.
DR GlyGen; Q96ST2; 1 site, 1 O-linked glycan (1 site).
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; 116 antibodies from 22 providers.
DR DNASU; 55677; -.
DR Ensembl; ENST00000295321.9; ENSP00000295321.4; ENSG00000163166.15. [Q96ST2-1]
DR GeneID; 55677; -.
DR KEGG; hsa:55677; -.
DR MANE-Select; ENST00000295321.9; ENSP00000295321.4; NM_017969.3; NP_060439.2.
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; -.
DR eggNOG; KOG1793; Eukaryota.
DR GeneTree; ENSGT00720000108834; -.
DR HOGENOM; CLU_018182_0_0_1; -.
DR InParanoid; Q96ST2; -.
DR OMA; HTHKDET; -.
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 SignaLink; Q96ST2; -.
DR BioGRID-ORCS; 55677; 50 hits in 1087 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 tibialis anterior and 180 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 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 451..458
FT /evidence="ECO:0007829|PDB:6ZV4"
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"
FT HELIX 555..579
FT /evidence="ECO:0007829|PDB:6ZV1"
FT HELIX 586..598
FT /evidence="ECO:0007829|PDB:6ZV1"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:6ZV1"
FT HELIX 604..609
FT /evidence="ECO:0007829|PDB:6ZV1"
FT HELIX 612..620
FT /evidence="ECO:0007829|PDB:6ZV1"
FT HELIX 631..642
FT /evidence="ECO:0007829|PDB:6ZV1"
FT HELIX 649..655
FT /evidence="ECO:0007829|PDB:6ZV1"
FT HELIX 657..665
FT /evidence="ECO:0007829|PDB:6ZV1"
FT HELIX 672..684
FT /evidence="ECO:0007829|PDB:6ZV1"
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
