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GTS1_YEAST
ID   GTS1_YEAST              Reviewed;         396 AA.
AC   P40956; D6VTX2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 186.
DE   RecName: Full=Protein GTS1;
DE   AltName: Full=Protein LSR1;
GN   Name=GTS1; Synonyms=LSR1; OrderedLocusNames=YGL181W;
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].
RC   STRAIN=IFO 10151 / YNN140;
RX   PubMed=8035831; DOI=10.1128/mcb.14.8.5569-5578.1994;
RA   Mitsui K., Yaguchi S., Tsurugi K.;
RT   "The GTS1 gene, which contains a Gly-Thr repeat, affects the timing of
RT   budding and cell size of the yeast Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 14:5569-5578(1994).
RN   [2]
RP   SEQUENCE REVISION.
RA   Mitsui K.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 44827 / SKQ2N;
RX   PubMed=9219336;
RX   DOI=10.1002/(sici)1097-0061(19970630)13:8<717::aid-yea132>3.0.co;2-2;
RA   Bossier P.G.M., Goethal P., Rodrigues-Pousada C.;
RT   "Constitutive flocculation in Saccharomyces cerevisiae through
RT   overexpression of the GTS1 gene, coding for a 'Glo'-type Zn-finger-
RT   containing protein.";
RL   Yeast 13:717-725(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9046087;
RX   DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA   Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT   "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT   from Saccharomyces cerevisiae.";
RL   Yeast 13:55-64(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [6]
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   [7]
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   [8]
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-184, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION BY
RP   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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; TYR-181; SER-187;
RP   SER-240 AND THR-249, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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: Appears to modulate the timing of budding to obtain an
CC       appropriate cell size independent of the DNA replication cycle.
CC       Transcription factor involved in both heat resistance and flocculation.
CC   -!- INTERACTION:
CC       P40956; P43603: LSB3; NbExp=4; IntAct=EBI-7968, EBI-22980;
CC       P40956; P39743: RVS167; NbExp=4; IntAct=EBI-7968, EBI-14500;
CC       P40956; P32793: YSC84; NbExp=4; IntAct=EBI-7968, EBI-24460;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; D31853; BAA06637.1; -; Genomic_DNA.
DR   EMBL; X85806; CAA59801.1; -; Genomic_DNA.
DR   EMBL; X91489; CAA62793.1; -; Genomic_DNA.
DR   EMBL; Z72703; CAA96893.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07933.1; -; Genomic_DNA.
DR   PIR; S58223; S58223.
DR   RefSeq; NP_011334.1; NM_001181046.1.
DR   AlphaFoldDB; P40956; -.
DR   SMR; P40956; -.
DR   BioGRID; 33073; 102.
DR   DIP; DIP-2746N; -.
DR   IntAct; P40956; 33.
DR   MINT; P40956; -.
DR   STRING; 4932.YGL181W; -.
DR   iPTMnet; P40956; -.
DR   MaxQB; P40956; -.
DR   PaxDb; P40956; -.
DR   PRIDE; P40956; -.
DR   EnsemblFungi; YGL181W_mRNA; YGL181W; YGL181W.
DR   GeneID; 852694; -.
DR   KEGG; sce:YGL181W; -.
DR   SGD; S000003149; GTS1.
DR   VEuPathDB; FungiDB:YGL181W; -.
DR   eggNOG; KOG0703; Eukaryota.
DR   HOGENOM; CLU_031494_1_0_1; -.
DR   InParanoid; P40956; -.
DR   OMA; ANKCGEC; -.
DR   BioCyc; YEAST:G3O-30668-MON; -.
DR   ChiTaRS; LSR1; yeast.
DR   PRO; PR:P40956; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P40956; protein.
DR   GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR   GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:SGD.
DR   GO; GO:0005096; F:GTPase activator activity; IMP:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IMP:SGD.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0010512; P:negative regulation of phosphatidylinositol biosynthetic process; IMP:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IPI:SGD.
DR   Gene3D; 1.10.220.150; -; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00627; UBA; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF57863; SSF57863; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..396
FT                   /note="Protein GTS1"
FT                   /id="PRO_0000074226"
FT   DOMAIN          14..141
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   DOMAIN          193..234
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   ZN_FING         30..53
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          148..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         181
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         249
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   396 AA;  44407 MW;  D687E3BF6B620795 CRC64;
     MRFRSSSHSL KHVDRELKEL INSSENANKC GECGNFYPTW CSVNLGVFLC GRCASVHRKV
     FGSRDDDAFS NVKSLSMDRW TREDIDELVS LGGNKGNARF WNPKNVPFPF DGDDDKAIVE
     HYIRDKYILG KFRYDEIKPE DFGSRMDDFD GESDRFDERN RSRSRSRSHS FYKGGHNRSD
     YGGSRDSFQS SGSRYSRQLA ELKDMGFGDT NKNLDALSSA HGNINRAIDY LEKSSSSRNS
     VSAAATTSTP PLPRRRATTS GPQPAIFDGT NVITPDFTSN SASFVQAKPA VFDGTLQQYY
     DPATGMIYVD QQQYAMAMQQ QQQQQQQLAV AQAQAQAQAQ AQAQVQAQAQ AQAQAQAQAQ
     QIQMQQLQMQ QQQQAPLSFQ QMSQGGNLPQ GYFYTQ
 
 
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