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P32589

- HSP7F_YEAST

UniProt

P32589 - HSP7F_YEAST

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Protein

Heat shock protein homolog SSE1

Gene

SSE1

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

Functioni

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

GO - Molecular functioni

  1. adenyl-nucleotide exchange factor activity Source: SGD
  2. ATP binding Source: SGD
  3. peptide binding Source: SGD

GO - Biological processi

  1. protein folding Source: SGD
  2. protein refolding Source: SGD
  3. regulation of catalytic activity Source: GOC
  4. response to stress Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34008-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein homolog SSE1
Alternative name(s):
Chaperone protein MSI3
Gene namesi
Name:SSE1
Synonyms:MSI3
Ordered Locus Names:YPL106C
ORF Names:LPG3C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

SGDiS000006027. SSE1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 693692Heat shock protein homolog SSE1PRO_0000078396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei242 – 2421Phosphothreonine1 Publication
Modified residuei660 – 6601Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP32589.
PaxDbiP32589.
PeptideAtlasiP32589.
PRIDEiP32589.

2D gel databases

SWISS-2DPAGEP32589.

Expressioni

Inductioni

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

Gene expression databases

GenevestigatoriP32589.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi36075. 257 interactions.
DIPiDIP-6645N.
IntActiP32589. 126 interactions.
MINTiMINT-8285491.
STRINGi4932.YPL106C.

Structurei

Secondary structure

1
693
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84
Beta strandi11 – 2010
Beta strandi23 – 275
Beta strandi34 – 374
Beta strandi40 – 423
Beta strandi44 – 496
Helixi51 – 577
Helixi61 – 633
Helixi68 – 714
Helixi81 – 855
Beta strandi90 – 945
Beta strandi98 – 1069
Beta strandi109 – 1146
Helixi115 – 13420
Beta strandi140 – 1456
Helixi151 – 16313
Beta strandi167 – 1737
Helixi174 – 18512
Beta strandi192 – 1943
Beta strandi197 – 2048
Beta strandi209 – 2179
Beta strandi220 – 22910
Helixi234 – 25219
Helixi257 – 2593
Helixi261 – 28020
Beta strandi282 – 2887
Beta strandi291 – 2944
Beta strandi297 – 3026
Helixi303 – 3097
Helixi311 – 3144
Turni315 – 3184
Helixi319 – 32810
Helixi332 – 3343
Beta strandi337 – 3426
Helixi343 – 3464
Helixi348 – 35811
Turni368 – 3703
Helixi371 – 38212
Beta strandi387 – 3893
Beta strandi393 – 3986
Beta strandi402 – 4065
Beta strandi414 – 4196
Beta strandi423 – 43715
Beta strandi439 – 4468
Helixi448 – 4503
Beta strandi457 – 4659
Beta strandi476 – 4849
Beta strandi490 – 4989
Beta strandi505 – 5073
Beta strandi520 – 5223
Beta strandi529 – 5324
Beta strandi534 – 5385
Helixi544 – 58542
Turni586 – 5894
Helixi590 – 5923
Helixi595 – 61117
Turni612 – 6143
Helixi615 – 6184
Helixi621 – 65333

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP32589.
SMRiP32589. Positions 1-649.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32589.

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00390000016919.
HOGENOMiHOG000228138.
InParanoidiP32589.
KOiK09485.
OMAiEARYKEW.
OrthoDBiEOG7B8SC7.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32589-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTPFGLDLG NNNSVLAVAR NRGIDIVVNE VSNRSTPSVV GFGPKNRYLG
60 70 80 90 100
ETGKNKQTSN IKNTVANLKR IIGLDYHHPD FEQESKHFTS KLVELDDKKT
110 120 130 140 150
GAEVRFAGEK HVFSATQLAA MFIDKVKDTV KQDTKANITD VCIAVPPWYT
160 170 180 190 200
EEQRYNIADA ARIAGLNPVR IVNDVTAAGV SYGIFKTDLP EGEEKPRIVA
210 220 230 240 250
FVDIGHSSYT CSIMAFKKGQ LKVLGTACDK HFGGRDFDLA ITEHFADEFK
260 270 280 290 300
TKYKIDIREN PKAYNRILTA AEKLKKVLSA NTNAPFSVES VMNDVDVSSQ
310 320 330 340 350
LSREELEELV KPLLERVTEP VTKALAQAKL SAEEVDFVEI IGGTTRIPTL
360 370 380 390 400
KQSISEAFGK PLSTTLNQDE AIAKGAAFIC AIHSPTLRVR PFKFEDIHPY
410 420 430 440 450
SVSYSWDKQV EDEDHMEVFP AGSSFPSTKL ITLNRTGDFS MAASYTDITQ
460 470 480 490 500
LPPNTPEQIA NWEITGVQLP EGQDSVPVKL KLRCDPSGLH TIEEAYTIED
510 520 530 540 550
IEVEEPIPLP EDAPEDAEQE FKKVTKTVKK DDLTIVAHTF GLDAKKLNEL
560 570 580 590 600
IEKENEMLAQ DKLVAETEDR KNTLEEYIYT LRGKLEEEYA PFASDAEKTK
610 620 630 640 650
LQGMLNKAEE WLYDEGFDSI KAKYIAKYEE LASLGNIIRG RYLAKEEEKK
660 670 680 690
QAIRSKQEAS QMAAMAEKLA AQRKAEAEKK EEKKDTEGDV DMD
Length:693
Mass (Da):77,366
Last modified:January 23, 2007 - v4
Checksum:i6558259111B0BC38
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2702TA → NT in BAA02576. (PubMed:8406043)Curated
Sequence conflicti269 – 2702TA → NT in BAA07449. (PubMed:8406043)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS46417.
RefSeqiNP_015219.1. NM_001183920.1.

Genome annotation databases

EnsemblFungiiYPL106C; YPL106C; YPL106C.
GeneIDi855998.
KEGGisce:YPL106C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S46417.
RefSeqi NP_015219.1. NM_001183920.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QXL X-ray 2.41 A/B 2-659 [» ]
3C7N X-ray 3.12 A 1-666 [» ]
3D2E X-ray 2.35 A/C 1-502 [» ]
A/C 525-693 [» ]
3D2F X-ray 2.30 A/C 1-502 [» ]
A/C 525-693 [» ]
ProteinModelPortali P32589.
SMRi P32589. Positions 1-649.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36075. 257 interactions.
DIPi DIP-6645N.
IntActi P32589. 126 interactions.
MINTi MINT-8285491.
STRINGi 4932.YPL106C.

2D gel databases

SWISS-2DPAGE P32589.

Proteomic databases

MaxQBi P32589.
PaxDbi P32589.
PeptideAtlasi P32589.
PRIDEi P32589.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPL106C ; YPL106C ; YPL106C .
GeneIDi 855998.
KEGGi sce:YPL106C.

Organism-specific databases

SGDi S000006027. SSE1.

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00390000016919.
HOGENOMi HOG000228138.
InParanoidi P32589.
KOi K09485.
OMAi EARYKEW.
OrthoDBi EOG7B8SC7.

Enzyme and pathway databases

BioCyci YEAST:G3O-34008-MONOMER.

Miscellaneous databases

EvolutionaryTracei P32589.
NextBioi 980863.
PROi P32589.

Gene expression databases

Genevestigatori P32589.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 2 hits.
SSF100934. SSF100934. 1 hit.
PROSITEi PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. 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].

Entry informationi

Entry nameiHSP7F_YEAST
AccessioniPrimary (citable) accession number: P32589
Secondary accession number(s): D6W3R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 71700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3