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P53935

- NST1_YEAST

UniProt

P53935 - NST1_YEAST

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Protein

Stress response protein NST1

Gene
NST1, YNL091W, N2231
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

With MSL1, acts as a negative regulator of salt tolerance.1 Publication

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. response to salt stress Source: SGD
Complete GO annotation...

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciYEAST:G3O-33119-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Stress response protein NST1
Alternative name(s):
Negatively-affecting salt tolerance protein 1
Gene namesi
Name:NST1
Ordered Locus Names:YNL091W
ORF Names:N2231
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNL091w.
SGDiS000005035. NST1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12401240Stress response protein NST1PRO_0000203442Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53935.
PaxDbiP53935.
PeptideAtlasiP53935.
PRIDEiP53935.

Expressioni

Gene expression databases

GenevestigatoriP53935.

Interactioni

Subunit structurei

Interacts with MSL1.

Binary interactionsi

WithEntry#Exp.IntActNotes
CAF40P538293EBI-28788,EBI-28306

Protein-protein interaction databases

BioGridi35733. 172 interactions.
DIPiDIP-872N.
IntActiP53935. 11 interactions.
MINTiMINT-387884.
STRINGi4932.YNL091W.

Structurei

3D structure databases

ProteinModelPortaliP53935.
SMRiP53935. Positions 630-761.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili616 – 777162 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi506 – 55449His-richAdd
BLAST
Compositional biasi989 – 1115127Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the NST1 family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG121137.
HOGENOMiHOG000113867.
OMAiSHWESLS.
OrthoDBiEOG71CFWZ.

Family and domain databases

InterProiIPR025279. NST1.
[Graphical view]
PfamiPF13945. NST1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53935-1 [UniParc]FASTAAdd to Basket

« Hide

MPPNSKSKRR KNKSKQHNKK NGNSDPEQSI NPTQLVPRME PELYHTESDY     50
PTSRVIKRAP NGDVIVEPIN TDDDKKERTA NLTHNKDSMD SASSLAFTLD 100
SHWESLSPEE KKTILRIEKE EVFNVIRNYQ DDHSCSCSVC GRRHLAMDQE 150
MERIYNTLYA MDKDKDPETN PIKFHLGIIK ELQISKNQQQ NDLSSTKGEV 200
VKNFLSSSTV GSLKEEVLHF KQKQLSKQEQ AHNETADNTS LLEENLNNIH 250
INKTSSEISA NFNSVSDEEL QQKYSNFTKT FISSHPKIAE EYVQKMMMYP 300
NIRALTDDLM NSNGQGFLNA IEDFVRDGQI QASKKDDSIT EDEASSTDLT 350
DPKEFTTMLH SGKPLTEDEY ADLQRNIAER MTNAYDTASK KFKDVSQLEK 400
ELFTRFMSGR DKKSFRELII QSFKNKFDGE LGPSVLAATL SSCFSSQSKD 450
TSLDTDSIYE DEDEEDYDDY SEYAEDSEEV SEYEGIEAVE KPEHDEKSNG 500
IRETLHLSYD HDHKRQNHPH HHYHSTSTHS EDELSEEEYI SDIELPHDPH 550
KHFHRDDDIL DGDEDEPEEE DENEGDDEED TYDSGLDETD RLEEGRKLIQ 600
IAITKLLQSR IMASYHEKQA DNNRLKLLQE LEEEKRKKRE KEEKKQKKRE 650
KEKEKKRLQQ LAKEEEKRKR EEEKERLKKE LEEREMRRRE AQRKKVEEAK 700
RKKDEERKRR LEEQQRREEM QEKQRKQKEE LKRKREEEKK RIREQKRLEQ 750
EKLQKEKEEE ERQRLIAEDA LRKQKLNEEQ TSANILSAKP FTENGVGNPV 800
SSQSHPNMTN YQEDNSCSIN DEILKMVNSV AASKPVSPTG FNVHDLLLPS 850
TNNQMPAMEQ SHLPQPGNQN NHFGTTTIPN ALDLATKSSL QTENNYLMNS 900
QTLENTSLLM HNNSSPTKLL PNDFGLSSWG GLTNTMSINP TCKPPVIQTS 950
EMESQAHKSS PQATMPSFGL PNGGTHRKSF TDELNTLTSM LSSSGFADTS 1000
LSSSGFPPSQ RSVWNDQKSS FSGPSTAGNF NNSSIQSGML LAPTLGSVES 1050
FPNRTSIWDS STTPMMNKSE LSGRNITSTA QDSPAFMASN IWSSNSQYNS 1100
PYLTSNVLQS PQISSGVDES HILDSIYNTY LAISPQDSLN PYIAIGTLFQ 1150
NLVGLNLDYS TFINKLISMQ GAYNCEFFTD NNGSITHVRF ARQTPAGHSK 1200
GLLNQLFSGL NDPTATPFTS RPHTSTRASF PIASSTTQTS 1240
Length:1,240
Mass (Da):141,514
Last modified:October 1, 1996 - v1
Checksum:i3FE9D265822D5778
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti162 – 1621D → A in strain: SK1. 1 Publication
Natural varianti208 – 2081S → G in strain: SK1. 1 Publication
Natural varianti354 – 3541E → D in strain: SK1. 1 Publication
Natural varianti899 – 8991N → D in strain: SK1. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ115393 Genomic DNA. Translation: AAZ22517.1.
X85811 Genomic DNA. Translation: CAA59826.1.
Z71367 Genomic DNA. Translation: CAA95967.1.
BK006947 Genomic DNA. Translation: DAA10455.1.
PIRiS52734.
RefSeqiNP_014308.1. NM_001182929.1.

Genome annotation databases

EnsemblFungiiYNL091W; YNL091W; YNL091W.
GeneIDi855633.
KEGGisce:YNL091W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ115393 Genomic DNA. Translation: AAZ22517.1 .
X85811 Genomic DNA. Translation: CAA59826.1 .
Z71367 Genomic DNA. Translation: CAA95967.1 .
BK006947 Genomic DNA. Translation: DAA10455.1 .
PIRi S52734.
RefSeqi NP_014308.1. NM_001182929.1.

3D structure databases

ProteinModelPortali P53935.
SMRi P53935. Positions 630-761.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35733. 172 interactions.
DIPi DIP-872N.
IntActi P53935. 11 interactions.
MINTi MINT-387884.
STRINGi 4932.YNL091W.

Proteomic databases

MaxQBi P53935.
PaxDbi P53935.
PeptideAtlasi P53935.
PRIDEi P53935.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YNL091W ; YNL091W ; YNL091W .
GeneIDi 855633.
KEGGi sce:YNL091W.

Organism-specific databases

CYGDi YNL091w.
SGDi S000005035. NST1.

Phylogenomic databases

eggNOGi NOG121137.
HOGENOMi HOG000113867.
OMAi SHWESLS.
OrthoDBi EOG71CFWZ.

Enzyme and pathway databases

BioCyci YEAST:G3O-33119-MONOMER.

Miscellaneous databases

NextBioi 979848.

Gene expression databases

Genevestigatori P53935.

Family and domain databases

InterProi IPR025279. NST1.
[Graphical view ]
Pfami PF13945. NST1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Quantitative trait loci mapped to single-nucleotide resolution in yeast."
    Deutschbauer A.M., Davis R.W.
    Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-162; GLY-208; ASP-354 AND ASP-899.
    Strain: SK1.
  2. "Sequence analysis of a 14.2 kb fragment of Saccharomyces cerevisiae chromosome XIV that includes the ypt53, tRNALeu and gsr m2 genes and four new open reading frames."
    Garcia-Cantalejo J.M., Boskovic J., Jimenez A.
    Yeast 12:599-608(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Involvement of Nst1p/YNL091w and Msl1p, a U2B'' splicing factor, in Saccharomyces cerevisiae salt tolerance."
    Goossens A., Forment J., Serrano R.
    Yeast 19:193-202(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNST1_YEAST
AccessioniPrimary (citable) accession number: P53935
Secondary accession number(s): D6W189, Q45TZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 217 molecules/cell in log phase SD medium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

Similar proteinsi