IWS1_YEAST
ID IWS1_YEAST Reviewed; 410 AA.
AC Q06505; D6W4C9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Transcription factor SPN1;
DE AltName: Full=Interacts with SPT6 protein 1;
DE AltName: Full=Suppresses postrecruitment functions protein 1;
GN Name=SPN1; Synonyms=IWS1; OrderedLocusNames=YPR133C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF LYS-192.
RX PubMed=12524336; DOI=10.1093/genetics/162.4.1605;
RA Fischbeck J.A., Kraemer S.M., Stargell L.A.;
RT "SPN1, a conserved gene identified by suppression of a postrecruitment-
RT defective yeast TATA-binding protein mutant.";
RL Genetics 162:1605-1616(2002).
RN [5]
RP INTERACTION WITH SPT6, AND PHOSPHORYLATION AT SER-89.
RX PubMed=12242279; DOI=10.1128/mcb.22.20.6979-6992.2002;
RA Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A.,
RA Shilatifard A., Buratowski S., Greenblatt J.F.;
RT "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a
RT targeted proteomics approach.";
RL Mol. Cell. Biol. 22:6979-6992(2002).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH ABD1;
RP RBP1; SPT5 AND SPT6.
RX PubMed=12556496; DOI=10.1128/mcb.23.4.1368-1378.2003;
RA Lindstrom D.L., Squazzo S.L., Muster N., Burckin T.A., Wachter K.C.,
RA Emigh C.A., McCleery J.A., Yates J.R. III, Hartzog G.A.;
RT "Dual roles for Spt5 in pre-mRNA processing and transcription elongation
RT revealed by identification of Spt5-associated proteins.";
RL Mol. Cell. Biol. 23:1368-1378(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15; SER-23; SER-85; THR-86
RP AND SER-89, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Transcription factor involved in RNA polymerase II
CC transcription regulation. May function in both SPT15/TBP post-
CC recruitment and recruitment steps of transcription.
CC {ECO:0000269|PubMed:12524336, ECO:0000269|PubMed:12556496}.
CC -!- SUBUNIT: Interacts with ABD1, RBP1, SPT5 and SPT6.
CC {ECO:0000269|PubMed:12242279, ECO:0000269|PubMed:12556496}.
CC -!- INTERACTION:
CC Q06505; P23615: SPT6; NbExp=7; IntAct=EBI-32596, EBI-17947;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the IWS1 family. {ECO:0000305}.
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DR EMBL; U40829; AAB68274.1; -; Genomic_DNA.
DR EMBL; AY558069; AAS56395.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11545.1; -; Genomic_DNA.
DR PIR; S69023; S69023.
DR RefSeq; NP_015458.1; NM_001184230.1.
DR PDB; 3NFQ; X-ray; 1.85 A; A/B=141-310.
DR PDB; 3O8Z; X-ray; 2.15 A; A=148-295.
DR PDB; 3OAK; X-ray; 2.15 A; A/B=148-292.
DR PDBsum; 3NFQ; -.
DR PDBsum; 3O8Z; -.
DR PDBsum; 3OAK; -.
DR AlphaFoldDB; Q06505; -.
DR SMR; Q06505; -.
DR BioGRID; 36299; 459.
DR DIP; DIP-3823N; -.
DR IntAct; Q06505; 12.
DR MINT; Q06505; -.
DR STRING; 4932.YPR133C; -.
DR iPTMnet; Q06505; -.
DR MaxQB; Q06505; -.
DR PaxDb; Q06505; -.
DR PRIDE; Q06505; -.
DR EnsemblFungi; YPR133C_mRNA; YPR133C; YPR133C.
DR GeneID; 856251; -.
DR KEGG; sce:YPR133C; -.
DR SGD; S000006337; SPN1.
DR VEuPathDB; FungiDB:YPR133C; -.
DR eggNOG; KOG1793; Eukaryota.
DR GeneTree; ENSGT00940000169144; -.
DR HOGENOM; CLU_045275_0_0_1; -.
DR InParanoid; Q06505; -.
DR OMA; VAEWTRP; -.
DR BioCyc; YEAST:G3O-34269-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR EvolutionaryTrace; Q06505; -.
DR PRO; PR:Q06505; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06505; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IPI:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR Gene3D; 1.20.930.10; -; 1.
DR IDEAL; IID50050; -.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR Pfam; PF08711; Med26; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..410
FT /note="Transcription factor SPN1"
FT /id="PRO_0000083366"
FT DOMAIN 219..296
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 23
FT /note="Phosphoserine; by ATM or ATR"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12242279,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 192
FT /note="K->N: Suppresses postrecruitment-defective SPT15/TBP
FT alleles."
FT /evidence="ECO:0000269|PubMed:12524336"
FT HELIX 150..182
FT /evidence="ECO:0007829|PDB:3NFQ"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:3NFQ"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3NFQ"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:3NFQ"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:3NFQ"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:3NFQ"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:3NFQ"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:3NFQ"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3OAK"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:3NFQ"
SQ SEQUENCE 410 AA; 46082 MW; 7BC925FC8BA80E65 CRC64;
MSTADQEQPK VVEATPEDGT ASSQKSTINA ENENTKQNQS MEPQETSKGT SNDTKDPDNG
EKNEEAAIDE NSNVEAAERK RKHISTDFSD DDLEKEEHND QSLQPTVENR ASKDRDSSAT
PSSRQELEEK LDRILKKPKV RRTRRDEDDL EQYLDEKILR LKDEMNIAAQ LDIDTLNKRI
ETGDTSLIAM QKVKLLPKVV SVLSKANLAD TILDNNLLQS VRIWLEPLPD GSLPSFEIQK
SLFAALNDLP VKTEHLKESG LGRVVIFYTK SKRVEAQLAR LAEKLIAEWT RPIIGASDNY
RDKRIMQLEF DSEKLRKKSV MDSAKNRKKK SKSGEDPTSR GSSVQTLYEQ AAARRNRAAA
PAQTTTDYKY APVSNLSAVP TNARAVGVGS TLNNSEMYKR LTSRLNKKHK
