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HAL9_YEAST
ID   HAL9_YEAST              Reviewed;        1030 AA.
AC   Q12180; D6W1X9;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Halotolerance protein 9;
GN   Name=HAL9; OrderedLocusNames=YOL089C; ORFNames=O0938;
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=ATCC 96604 / S288c / FY1679;
RX   PubMed=8533473; DOI=10.1002/yea.320111009;
RA   Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT   "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT   than twice as many unknown as known open reading frames.";
RL   Yeast 11:975-986(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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   FUNCTION.
RX   PubMed=9559673; DOI=10.1016/s0014-5793(98)00249-x;
RA   Mendizabal I., Rios G., Mulet J.M., Serrano R., de Larrinoa I.F.;
RT   "Yeast putative transcription factors involved in salt tolerance.";
RL   FEBS Lett. 425:323-328(1998).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-937, AND IDENTIFICATION BY
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, 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   [9]
RP   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: Putative transcription factor involved in halotolerance.
CC       {ECO:0000269|PubMed:9559673}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X83121; CAA58190.1; -; Genomic_DNA.
DR   EMBL; Z74831; CAA99101.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10695.1; -; Genomic_DNA.
DR   PIR; S57380; S57380.
DR   RefSeq; NP_014552.1; NM_001183343.1.
DR   AlphaFoldDB; Q12180; -.
DR   SMR; Q12180; -.
DR   BioGRID; 34313; 109.
DR   IntAct; Q12180; 17.
DR   MINT; Q12180; -.
DR   STRING; 4932.YOL089C; -.
DR   iPTMnet; Q12180; -.
DR   MaxQB; Q12180; -.
DR   PaxDb; Q12180; -.
DR   PRIDE; Q12180; -.
DR   EnsemblFungi; YOL089C_mRNA; YOL089C; YOL089C.
DR   GeneID; 854064; -.
DR   KEGG; sce:YOL089C; -.
DR   SGD; S000005449; HAL9.
DR   VEuPathDB; FungiDB:YOL089C; -.
DR   eggNOG; ENOG502QZJZ; Eukaryota.
DR   GeneTree; ENSGT00940000176304; -.
DR   HOGENOM; CLU_008153_0_0_1; -.
DR   InParanoid; Q12180; -.
DR   OMA; DNMARFE; -.
DR   BioCyc; YEAST:G3O-33489-MON; -.
DR   PRO; PR:Q12180; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12180; protein.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IC:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0009651; P:response to salt stress; IMP:SGD.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..1030
FT                   /note="Halotolerance protein 9"
FT                   /id="PRO_0000233012"
FT   DNA_BIND        136..166
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          185..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         937
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
SQ   SEQUENCE   1030 AA;  117927 MW;  8C8BDE84066D2105 CRC64;
     MENQGGDYSP NGFSNSASNM NAVFNNEITG RSDISNVNHQ TGTPRLVPET QIWSMPVPDQ
     LMTMPNRENT LMTGSTIGPN IPMNVAYPNT IYSPTEHQSQ FQTQQNRDIS TMMEHTNSND
     MSGSGKNLKK RVSKACDHCR KRKIRCDEVD QQTKKCSNCI KFQLPCTFKH RDEILKKKRK
     LEIKHHATPG ESLQTSNSIS NPVASSSVPN SGRFELLNGN SPLESNIIDK VSNIQNNLNK
     KMNSKIEKLD RKMSYIIDSV ARLEWLLDKA VKKQEGKYKE KNNLPKPARK IYSTALLTAQ
     KLYWFKQSLG VKASNEEFLS PISEILSISL KWYATQMKKF MDLSSPAFFS SEIILYSLPP
     KKQAKRLLEN FHATLLSSVT GIISLKECLD LAEKYYSESG EKLTYPEHLL LNVCLCSGAS
     ATQSIIRGDS KFLRKDRYDP TSQELKKIEN VALLNAMYYY HKLSTICSGT RTLQALLLLN
     RYFQLTYDTE LANCILGTAI RLAVDMELNR KSSYKSLDFE EAIRRRRMWW HCFCTDKLYS
     LMLSRPPIVG ERDMDMLTDQ NYYEVIKTNI LPDLIDKKED LDKITDVNSA LNVVVNFCQH
     ISLFISYYVS KLVSIESKIY STCFAVRSTL DLSFDAMLDK IKDLNDSLNN WRDNLHVSMK
     LKSYKQYLSV LYAQKSQENP ALSFEIACSR VLNCHFRALY SKVILSMMTT SLLIDNERLY
     KGSRHDIPQL FILFSSQYLN ASKEMLQLFQ GINYQAHMYN EVMYQFSTAM FVLFFYVVDN
     MNDLKKKGEV KEIIDILKKS YDRLVGENDE QLLFDNVKWN TLIVFYSHFL KYVLQRYHAL
     NDSTSIFDSK PYDETITKVI MHSRKIKDET VDQLIMSLKS YGSLHSLQKG NEADLADDGL
     NTNDISSEDF AEEAPINLFG ELSVEILKLL KSHSPISNFG DLSPSSNRKG ISDDSSLYPI
     RSDLTSLVYP IHSSDTGDTL SSGLETPENS NFNSDSGIKE DFEAFRALLP LGKLIYDRDY
     SFVNTFRDYE
 
 
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