Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32589 (HSP7F_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock protein homolog SSE1
Alternative name(s):
Chaperone protein MSI3
Gene names
Name:SSE1
Synonyms:MSI3
Ordered Locus Names:YPL106C
ORF Names:LPG3C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.

Subcellular location

Cytoplasm Ref.8.

Induction

Increases a few-fold upon upshift to 37 degrees Celsius.

Miscellaneous

Present with 71700 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the heat shock protein 70 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSP82P028293EBI-8648,EBI-8659
HSPA1BP081072EBI-8648,EBI-629985From a different organism.
SSA1P105918EBI-8648,EBI-8591
SSB1P114842EBI-8648,EBI-8627

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 693692Heat shock protein homolog SSE1
PRO_0000078396

Amino acid modifications

Modified residue21N-acetylserine Ref.7
Modified residue2421Phosphothreonine Ref.10
Modified residue6601Phosphoserine Ref.11

Experimental info

Sequence conflict269 – 2702TA → NT in BAA02576. Ref.1
Sequence conflict269 – 2702TA → NT in BAA07449. Ref.1

Secondary structure

............................................................................................................ 693
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32589 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 6558259111B0BC38

FASTA69377,366
        10         20         30         40         50         60 
MSTPFGLDLG NNNSVLAVAR NRGIDIVVNE VSNRSTPSVV GFGPKNRYLG ETGKNKQTSN 

        70         80         90        100        110        120 
IKNTVANLKR IIGLDYHHPD FEQESKHFTS KLVELDDKKT GAEVRFAGEK HVFSATQLAA 

       130        140        150        160        170        180 
MFIDKVKDTV KQDTKANITD VCIAVPPWYT EEQRYNIADA ARIAGLNPVR IVNDVTAAGV 

       190        200        210        220        230        240 
SYGIFKTDLP EGEEKPRIVA FVDIGHSSYT CSIMAFKKGQ LKVLGTACDK HFGGRDFDLA 

       250        260        270        280        290        300 
ITEHFADEFK TKYKIDIREN PKAYNRILTA AEKLKKVLSA NTNAPFSVES VMNDVDVSSQ 

       310        320        330        340        350        360 
LSREELEELV KPLLERVTEP VTKALAQAKL SAEEVDFVEI IGGTTRIPTL KQSISEAFGK 

       370        380        390        400        410        420 
PLSTTLNQDE AIAKGAAFIC AIHSPTLRVR PFKFEDIHPY SVSYSWDKQV EDEDHMEVFP 

       430        440        450        460        470        480 
AGSSFPSTKL ITLNRTGDFS MAASYTDITQ LPPNTPEQIA NWEITGVQLP EGQDSVPVKL 

       490        500        510        520        530        540 
KLRCDPSGLH TIEEAYTIED IEVEEPIPLP EDAPEDAEQE FKKVTKTVKK DDLTIVAHTF 

       550        560        570        580        590        600 
GLDAKKLNEL IEKENEMLAQ DKLVAETEDR KNTLEEYIYT LRGKLEEEYA PFASDAEKTK 

       610        620        630        640        650        660 
LQGMLNKAEE WLYDEGFDSI KAKYIAKYEE LASLGNIIRG RYLAKEEEKK QAIRSKQEAS 

       670        680        690 
QMAAMAEKLA AQRKAEAEKK EEKKDTEGDV DMD 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family."
Mukai H., Kuno T., Tanaka H., Hirata D., Miyakawa T., Tanaka C.
Gene 132:57-66(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 204626 / S288c / A364A.
[2]"MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae."
Shirayama M., Kawakami K., Matsui Y., Tanaka K., Toh-e A.
Mol. Gen. Genet. 240:323-332(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Protein identifications for a Saccharomyces cerevisiae protein database."
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.
Electrophoresis 15:1466-1486(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 100-110.
Strain: ATCC 204508 / S288c.
[6]"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
Norbeck J., Blomberg A.
FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 330-339.
Strain: ATCC 38531 / Y41.
[7]"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT SER-2.
[8]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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-660, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13319 mRNA. Translation: BAA02576.1.
D38368 mRNA. Translation: BAA07449.1.
D38370 Genomic DNA. Translation: BAA07451.1.
D13743 Genomic DNA. Translation: BAA02888.1.
U43281 Genomic DNA. Translation: AAB68194.1.
BK006949 Genomic DNA. Translation: DAA11327.1.
PIRS46417.
RefSeqNP_015219.1. NM_001183920.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QXLX-ray2.41A/B2-659[»]
3C7NX-ray3.12A1-666[»]
3D2EX-ray2.35A/C1-502[»]
A/C525-693[»]
3D2FX-ray2.30A/C1-502[»]
A/C525-693[»]
ProteinModelPortalP32589.
SMRP32589. Positions 1-649.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36075. 255 interactions.
DIPDIP-6645N.
IntActP32589. 126 interactions.
MINTMINT-8285491.
STRING4932.YPL106C.

2D gel databases

SWISS-2DPAGEP32589.

Proteomic databases

MaxQBP32589.
PaxDbP32589.
PeptideAtlasP32589.
PRIDEP32589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL106C; YPL106C; YPL106C.
GeneID855998.
KEGGsce:YPL106C.

Organism-specific databases

SGDS000006027. SSE1.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00390000016919.
HOGENOMHOG000228138.
KOK09485.
OMAEARYKEW.
OrthoDBEOG7B8SC7.

Enzyme and pathway databases

BioCycYEAST:G3O-34008-MONOMER.

Gene expression databases

GenevestigatorP32589.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 1 hit.
PROSITEPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32589.
NextBio980863.
PROP32589.

Entry information

Entry nameHSP7F_YEAST
AccessionPrimary (citable) accession number: P32589
Secondary accession number(s): D6W3R1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 143 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references