SQS1_YEAST
ID SQS1_YEAST Reviewed; 767 AA.
AC P53866; D6W0W6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein SQS1;
DE AltName: Full=Squelch of splicing suppression protein 1;
GN Name=SQS1; OrderedLocusNames=YNL224C; ORFNames=N1269;
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 [GENOMIC DNA].
RX PubMed=8896273;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT reading frames including a novel gene encoding a globin-like domain.";
RL Yeast 12:1071-1076(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-298.
RA Sun Z., Hampsey M.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=16945917; DOI=10.1073/pnas.0603188103;
RA Pandit S., Lynn B., Rymond B.C.;
RT "Inhibition of a spliceosome turnover pathway suppresses splicing
RT defects.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13700-13705(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-345, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-255 AND SER-345, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-334; SER-343 AND
RP SER-345, 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: May be involved in splicing since overexpression antagonizes
CC the suppression of splicing defects by SPP382 mutants.
CC {ECO:0000269|PubMed:16945917}.
CC -!- INTERACTION:
CC P53866; Q03532: HAS1; NbExp=3; IntAct=EBI-29168, EBI-8170;
CC P53866; P32899: IMP3; NbExp=2; IntAct=EBI-29168, EBI-9237;
CC P53866; P25586: KRR1; NbExp=2; IntAct=EBI-29168, EBI-21773;
CC P53866; P53131: PRP43; NbExp=11; IntAct=EBI-29168, EBI-505;
CC P53866; P53254: UTP22; NbExp=3; IntAct=EBI-29168, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SQS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA86499.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z69381; CAA93374.1; -; Genomic_DNA.
DR EMBL; Z71500; CAA96127.1; -; Genomic_DNA.
DR EMBL; U20390; AAA86499.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006947; DAA10332.1; -; Genomic_DNA.
DR PIR; S63182; S63182.
DR RefSeq; NP_014175.1; NM_001183062.1.
DR AlphaFoldDB; P53866; -.
DR SMR; P53866; -.
DR BioGRID; 35612; 143.
DR DIP; DIP-6728N; -.
DR IntAct; P53866; 24.
DR MINT; P53866; -.
DR STRING; 4932.YNL224C; -.
DR iPTMnet; P53866; -.
DR MaxQB; P53866; -.
DR PaxDb; P53866; -.
DR PRIDE; P53866; -.
DR EnsemblFungi; YNL224C_mRNA; YNL224C; YNL224C.
DR GeneID; 855497; -.
DR KEGG; sce:YNL224C; -.
DR SGD; S000005168; SQS1.
DR VEuPathDB; FungiDB:YNL224C; -.
DR eggNOG; KOG0154; Eukaryota.
DR HOGENOM; CLU_021974_1_0_1; -.
DR InParanoid; P53866; -.
DR OMA; PVFMRID; -.
DR BioCyc; YEAST:G3O-33227-MON; -.
DR BRENDA; 2.5.1.21; 984.
DR PRO; PR:P53866; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53866; protein.
DR GO; GO:0030686; C:90S preribosome; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IGI:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IGI:SGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:SGD.
DR GO; GO:0051096; P:positive regulation of helicase activity; IDA:SGD.
DR GO; GO:0006364; P:rRNA processing; IGI:SGD.
DR CDD; cd02646; R3H_G-patch; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034082; R3H_G-patch.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..767
FT /note="Protein SQS1"
FT /id="PRO_0000203388"
FT DOMAIN 594..656
FT /note="R3H"
FT DOMAIN 720..767
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..490
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 767 AA; 86950 MW; CE5650B8679BF8C0 CRC64;
MAKRHSHYQG SRRRHARGSN SKKAGRGNAK GIQGRKIKKK PTPTNSWHNS SIPLGEGDLD
DVGADFNPGR AFISPKTIED YYFGRDAKSR SMKMGGLRPG NRYDSSTDLQ AGRAAFRKRP
MQFVKAKEVY DPSHNMIQKL RAKNETKNSE EIVEREADVF EEPGKMTSDV EYINNEDSEN
EDDDSQNSPS TDHSLSSNES KVEDGDLFFV DEEAQQSPDL TKIKRVCIEE IARPREVAIE
FDPILTIGKV ELSVSEGNES KEISVDVPNK GNKTYHPFAG YISNVLHGMH TSDSDNDELD
YEIETENNSE PLYESSASSE VDQGFNYVGQ RHNSRADNNL LPSPSPQLTE DIKCLSINGT
KTFEGNNDNL PSPASEELEF GFKEEDFVIN TNDIVVSNIR MGGVDNSYYL RCYRLLGDYD
FHWIDQDLLT DFVVDELGLP EDRLPAYLNF IKNSLIPKIE PAEPTYSDIP ISDSSDEGDS
YEGDSYEDDE DMASSVVHSD IEEGLDDLIA YTLKHDTERF KTFETKSLET KGKGKKKKLL
IDDALALDTE TLETLQSKFS KRIETKAKKR KAKEDFIDQE NRNSNDMLKK YPYGLHIQNI
KDEFESFLSR NNDRLTFPPL DPHGNKTVMK IAKHYNMKSS KIGKANHTSV VVEKIKKTKW
SSPNYSLIDQ LMRQRPVFMR IDIRRPREEQ AAFERTKTIR GKFHVKEGEI VGQNAPEIGN
ENIGRRMLEK LGWKSGEGLG IQGNKGISEP IFAKIKKNRS GLRHSES
