NST1_YEAST
ID NST1_YEAST Reviewed; 1240 AA.
AC P53935; D6W189; Q45TZ3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Stress response protein NST1;
DE AltName: Full=Negatively-affecting salt tolerance protein 1;
GN Name=NST1; OrderedLocusNames=YNL091W; ORFNames=N2231;
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], AND VARIANTS ALA-162; GLY-208; ASP-354
RP AND ASP-899.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8771715;
RX DOI=10.1002/(sici)1097-0061(199605)12:6<599::aid-yea938>3.0.co;2-9;
RA Garcia-Cantalejo J.M., Boskovic J., Jimenez A.;
RT "Sequence analysis of a 14.2 kb fragment of Saccharomyces cerevisiae
RT chromosome XIV that includes the ypt53, tRNALeu and gsr m2 genes and four
RT new open reading frames.";
RL Yeast 12:599-608(1996).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=11816027; DOI=10.1002/yea.815.abs;
RA Goossens A., Forment J., Serrano R.;
RT "Involvement of Nst1p/YNL091w and Msl1p, a U2B'' splicing factor, in
RT Saccharomyces cerevisiae salt tolerance.";
RL Yeast 19:193-202(2002).
RN [6]
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 [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-266, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP 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).
RN [11]
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: With MSL1, acts as a negative regulator of salt tolerance.
CC {ECO:0000269|PubMed:11816027}.
CC -!- SUBUNIT: Interacts with MSL1.
CC -!- INTERACTION:
CC P53935; P53829: CAF40; NbExp=3; IntAct=EBI-28788, EBI-28306;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NST1 family. {ECO:0000305}.
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DR EMBL; DQ115393; AAZ22517.1; -; Genomic_DNA.
DR EMBL; X85811; CAA59826.1; -; Genomic_DNA.
DR EMBL; Z71367; CAA95967.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10455.1; -; Genomic_DNA.
DR PIR; S52734; S52734.
DR RefSeq; NP_014308.1; NM_001182929.1.
DR AlphaFoldDB; P53935; -.
DR SMR; P53935; -.
DR BioGRID; 35733; 436.
DR DIP; DIP-872N; -.
DR IntAct; P53935; 16.
DR MINT; P53935; -.
DR STRING; 4932.YNL091W; -.
DR iPTMnet; P53935; -.
DR MaxQB; P53935; -.
DR PaxDb; P53935; -.
DR PRIDE; P53935; -.
DR EnsemblFungi; YNL091W_mRNA; YNL091W; YNL091W.
DR GeneID; 855633; -.
DR KEGG; sce:YNL091W; -.
DR SGD; S000005035; NST1.
DR VEuPathDB; FungiDB:YNL091W; -.
DR eggNOG; ENOG502QSSK; Eukaryota.
DR HOGENOM; CLU_267374_0_0_1; -.
DR InParanoid; P53935; -.
DR OMA; TLDSHWE; -.
DR BioCyc; YEAST:G3O-33119-MON; -.
DR PRO; PR:P53935; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53935; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0009651; P:response to salt stress; IMP:SGD.
DR InterPro; IPR025279; NST1.
DR Pfam; PF13945; NST1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome;
KW Stress response.
FT CHAIN 1..1240
FT /note="Stress response protein NST1"
FT /id="PRO_0000203442"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 616..777
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..483
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..587
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT VARIANT 162
FT /note="D -> A (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 208
FT /note="S -> G (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 354
FT /note="E -> D (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 899
FT /note="N -> D (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
SQ SEQUENCE 1240 AA; 141514 MW; 3FE9D265822D5778 CRC64;
MPPNSKSKRR KNKSKQHNKK NGNSDPEQSI NPTQLVPRME PELYHTESDY PTSRVIKRAP
NGDVIVEPIN TDDDKKERTA NLTHNKDSMD SASSLAFTLD SHWESLSPEE KKTILRIEKE
EVFNVIRNYQ DDHSCSCSVC GRRHLAMDQE MERIYNTLYA MDKDKDPETN PIKFHLGIIK
ELQISKNQQQ NDLSSTKGEV VKNFLSSSTV GSLKEEVLHF KQKQLSKQEQ AHNETADNTS
LLEENLNNIH INKTSSEISA NFNSVSDEEL QQKYSNFTKT FISSHPKIAE EYVQKMMMYP
NIRALTDDLM NSNGQGFLNA IEDFVRDGQI QASKKDDSIT EDEASSTDLT DPKEFTTMLH
SGKPLTEDEY ADLQRNIAER MTNAYDTASK KFKDVSQLEK ELFTRFMSGR DKKSFRELII
QSFKNKFDGE LGPSVLAATL SSCFSSQSKD TSLDTDSIYE DEDEEDYDDY SEYAEDSEEV
SEYEGIEAVE KPEHDEKSNG IRETLHLSYD HDHKRQNHPH HHYHSTSTHS EDELSEEEYI
SDIELPHDPH KHFHRDDDIL DGDEDEPEEE DENEGDDEED TYDSGLDETD RLEEGRKLIQ
IAITKLLQSR IMASYHEKQA DNNRLKLLQE LEEEKRKKRE KEEKKQKKRE KEKEKKRLQQ
LAKEEEKRKR EEEKERLKKE LEEREMRRRE AQRKKVEEAK RKKDEERKRR LEEQQRREEM
QEKQRKQKEE LKRKREEEKK RIREQKRLEQ EKLQKEKEEE ERQRLIAEDA LRKQKLNEEQ
TSANILSAKP FTENGVGNPV SSQSHPNMTN YQEDNSCSIN DEILKMVNSV AASKPVSPTG
FNVHDLLLPS TNNQMPAMEQ SHLPQPGNQN NHFGTTTIPN ALDLATKSSL QTENNYLMNS
QTLENTSLLM HNNSSPTKLL PNDFGLSSWG GLTNTMSINP TCKPPVIQTS EMESQAHKSS
PQATMPSFGL PNGGTHRKSF TDELNTLTSM LSSSGFADTS LSSSGFPPSQ RSVWNDQKSS
FSGPSTAGNF NNSSIQSGML LAPTLGSVES FPNRTSIWDS STTPMMNKSE LSGRNITSTA
QDSPAFMASN IWSSNSQYNS PYLTSNVLQS PQISSGVDES HILDSIYNTY LAISPQDSLN
PYIAIGTLFQ NLVGLNLDYS TFINKLISMQ GAYNCEFFTD NNGSITHVRF ARQTPAGHSK
GLLNQLFSGL NDPTATPFTS RPHTSTRASF PIASSTTQTS
