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P10591 (HSP71_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 147. 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 SSA1
Alternative name(s):
Heat shock protein YG100
Gene names
Name:SSA1
Ordered Locus Names:YAL005C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles. Ref.11

Subunit structure

Binds human HTN3/histatin-5, a peptide from saliva, and mediates its fungicidal activity. Interacts with polyadenylate-binding protein PAB1 and Hsp70 chaperone SSA1 on translating ribosomes. Interacts with NAP1. Ref.10 Ref.11 Ref.17

Subcellular location

Cytoplasm. Secretedcell wall Ref.12.

Miscellaneous

Present with 269000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCell wall
Cytoplasm
Secreted
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processSRP-dependent cotranslational protein targeting to membrane, translocation

Inferred from direct assay PubMed 8754838. Source: SGD

cytoplasmic translation

Inferred from mutant phenotype Ref.10. Source: SGD

protein import into nucleus, translocation

Inferred from direct assay PubMed 10347213. Source: SGD

protein refolding

Inferred from direct assay PubMed 18706386PubMed 9674429. Source: SGD

protein targeting to mitochondrion

Inferred from mutant phenotype PubMed 8754838. Source: SGD

response to stress

Inferred from mutant phenotype PubMed 3302682. Source: SGD

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

fungal-type cell wall

Inferred from direct assay PubMed 8755907. Source: SGD

fungal-type vacuole membrane

Inferred from direct assay PubMed 10745074. Source: SGD

nucleus

Inferred from direct assay PubMed 10347213PubMed 11914276. Source: SGD

plasma membrane

Inferred from direct assay PubMed 16622836. Source: SGD

polysome

Inferred from direct assay PubMed 16413483. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay PubMed 18706386PubMed 7737974. Source: SGD

unfolded protein binding

Inferred from direct assay PubMed 9789005. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSP82P028292EBI-8591,EBI-8659
SSE1P325894EBI-8591,EBI-8648

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 642641Heat shock protein SSA1
PRO_0000078385

Amino acid modifications

Modified residue21N-acetylserine Ref.9
Modified residue121Phosphothreonine Ref.15
Modified residue351Phosphothreonine Ref.18
Modified residue361Phosphothreonine Ref.18
Modified residue431Phosphothreonine Ref.18
Modified residue621Phosphoserine Ref.18
Modified residue1311Phosphoserine Ref.18
Modified residue1511Phosphoserine Ref.18
Modified residue3781Phosphothreonine Ref.18
Modified residue4591Phosphoserine Ref.18
Modified residue4861Phosphoserine Ref.18
Modified residue4921Phosphothreonine Ref.18
Modified residue4951Phosphoserine Ref.16 Ref.18
Modified residue5411Phosphoserine Ref.18
Modified residue5451Phosphoserine Ref.18
Modified residue5511Phosphoserine Ref.16 Ref.18
Modified residue6031Phosphoserine Ref.18
Cross-link521Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14
Cross-link536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Experimental info

Sequence conflict2081S → F in AAC04952. Ref.3
Sequence conflict4181P → S in AAC04952. Ref.3
Sequence conflict4221S → F in AAC04952. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P10591 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 249D8A3BC42527CA

FASTA64269,657
        10         20         30         40         50         60 
MSKAVGIDLG TTYSCVAHFA NDRVDIIAND QGNRTTPSFV AFTDTERLIG DAAKNQAAMN 

        70         80         90        100        110        120 
PSNTVFDAKR LIGRNFNDPE VQADMKHFPF KLIDVDGKPQ IQVEFKGETK NFTPEQISSM 

       130        140        150        160        170        180 
VLGKMKETAE SYLGAKVNDA VVTVPAYFND SQRQATKDAG TIAGLNVLRI INEPTAAAIA 

       190        200        210        220        230        240 
YGLDKKGKEE HVLIFDLGGG TFDVSLLSIE DGIFEVKATA GDTHLGGEDF DNRLVNHFIQ 

       250        260        270        280        290        300 
EFKRKNKKDL STNQRALRRL RTACERAKRT LSSSAQTSVE IDSLFEGIDF YTSITRARFE 

       310        320        330        340        350        360 
ELCADLFRST LDPVEKVLRD AKLDKSQVDE IVLVGGSTRI PKVQKLVTDY FNGKEPNRSI 

       370        380        390        400        410        420 
NPDEAVAYGA AVQAAILTGD ESSKTQDLLL LDVAPLSLGI ETAGGVMTKL IPRNSTIPTK 

       430        440        450        460        470        480 
KSEIFSTYAD NQPGVLIQVF EGERAKTKDN NLLGKFELSG IPPAPRGVPQ IEVTFDVDSN 

       490        500        510        520        530        540 
GILNVSAVEK GTGKSNKITI TNDKGRLSKE DIEKMVAEAE KFKEEDEKES QRIASKNQLE 

       550        560        570        580        590        600 
SIAYSLKNTI SEAGDKLEQA DKDTVTKKAE ETISWLDSNT TASKEEFDDK LKELQDIANP 

       610        620        630        640 
IMSKLYQAGG APGGAAGGAP GGFPGGAPPA PEAEGPTVEE VD 

« Hide

References

« Hide 'large scale' references
[1]"The SSA1 and SSA2 genes of the yeast Saccharomyces cerevisiae."
Slater M.R., Craig E.A.
Nucleic Acids Res. 17:805-806(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Slater M.R.
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 208; 418 AND 422.
[3]"Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region."
Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.
Yeast 10:535-541(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"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 92-98 AND 326-342.
Strain: ATCC 204508 / S288c.
[7]"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 187-196.
Strain: ATCC 38531 / Y41.
[8]"Transfer RNA splicing in Saccharomyces cerevisiae: defining the substrates."
Ogden R.C., Lee M.-C., Knapp G.
Nucleic Acids Res. 12:9367-9382(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 591-642.
[9]"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.
[10]"The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes."
Horton L.E., James P., Craig E.A., Hensold J.O.
J. Biol. Chem. 276:14426-14433(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAB1 AND SIS1.
[11]"Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5."
Li X.S., Reddy M.S., Baev D., Edgerton M.
J. Biol. Chem. 278:28553-28561(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HUMAN HTN3.
[12]"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].
[13]"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].
[14]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-521 AND LYS-536, MASS SPECTROMETRY.
Strain: SUB592.
[15]"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-12, MASS SPECTROMETRY.
[16]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-551, MASS SPECTROMETRY.
[17]"Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAP1, MASS SPECTROMETRY.
[18]"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 THR-35; THR-36; THR-43; SER-62; SER-131; SER-151; THR-378; SER-459; SER-486; THR-492; SER-495; SER-541; SER-545; SER-551 AND SER-603, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12926 Genomic DNA. Translation: CAA31393.1.
L22015 Genomic DNA. Translation: AAC04952.1.
BK006935 Genomic DNA. Translation: DAA06982.1.
PIRHHBYA1. S43449.
RefSeqNP_009396.2. NM_001178151.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LCAX-ray2.19Q631-642[»]
ProteinModelPortalP10591.
SMRP10591. Positions 3-602.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2253N.
IntActP10591. 276 interactions.
MINTMINT-472037.
STRING4932.YAL005C.

2D gel databases

COMPLUYEAST-2DPAGEP10591.
SWISS-2DPAGEP10591.

Proteomic databases

PeptideAtlasP10591.
PRIDEP10591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL005C; YAL005C; YAL005C.
GeneID851259.
KEGGsce:YAL005C.

Organism-specific databases

SGDS000000004. SSA1.

Phylogenomic databases

GeneTreeENSGT00700000104569.
HOGENOMHOG000228135.
KOK03283.
OMANTTASKE.
OrthoDBEOG476P7G.

Gene expression databases

ArrayExpressP10591.
GenevestigatorP10591.
GermOnlineYAL005C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL5186.
EvolutionaryTraceP10591.
NextBio968213.

Entry information

Entry nameHSP71_YEAST
AccessionPrimary (citable) accession number: P10591
Secondary accession number(s): D6VPL2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome I

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families