Heat shock protein SSA1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P10591 (HSP71_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 147. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Heat shock protein SSA1

Alternative name(s):
Heat shock protein YG100

Gene names

Name:	SSA1
Ordered Locus Names:	YAL005C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	642 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Secreted › cell 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 process	Stress response
Cellular component	Cell wall Cytoplasm Secreted
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SRP-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 18706386 PubMed 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_component	extracellular 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 10347213 PubMed 11914276. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD polysome Inferred from direct assay PubMed 16413483. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from direct assay PubMed 18706386 PubMed 7737974. Source: SGD unfolded protein binding Inferred from direct assay PubMed 9789005. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP82	P02829	2	EBI-8591,EBI-8659
SSE1	P32589	4	EBI-8591,EBI-8648

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 642

641

Heat shock protein SSA1

PRO_0000078385

Amino acid modifications

Modified residue

N-acetylserine Ref.9

Modified residue

Phosphothreonine Ref.15

Modified residue

Phosphothreonine Ref.18

Modified residue

Phosphothreonine Ref.18

Modified residue

Phosphothreonine Ref.18

Modified residue

Phosphoserine Ref.18

Modified residue

131

Phosphoserine Ref.18

Modified residue

151

Phosphoserine Ref.18

Modified residue

378

Phosphothreonine Ref.18

Modified residue

459

Phosphoserine Ref.18

Modified residue

486

Phosphoserine Ref.18

Modified residue

492

Phosphothreonine Ref.18

Modified residue

495

Phosphoserine Ref.16 Ref.18

Modified residue

541

Phosphoserine Ref.18

Modified residue

545

Phosphoserine Ref.18

Modified residue

551

Phosphoserine Ref.16 Ref.18

Modified residue

603

Phosphoserine Ref.18

Cross-link

521

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Cross-link

536

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Experimental info

Sequence conflict

208

S → F in AAC04952. Ref.3

Sequence conflict

418

P → S in AAC04952. Ref.3

Sequence conflict

422

S → F in AAC04952. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P10591 [UniParc].

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

642

69,657

        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' referencesShow '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.

PIR

HHBYA1. S43449.

RefSeq

NP_009396.2. NM_001178151.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LCA	X-ray	2.19	Q	631-642	[»]

ProteinModelPortal

P10591.

SMR

P10591. Positions 3-602.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2253N.

IntAct

P10591. 276 interactions.

MINT

MINT-472037.

STRING

4932.YAL005C.

2D gel databases

COMPLUYEAST-2DPAGE

P10591.

SWISS-2DPAGE

P10591.

Proteomic databases

PeptideAtlas

P10591.

PRIDE

P10591.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YAL005C; YAL005C; YAL005C.

GeneID

851259.

KEGG

sce:YAL005C.

Organism-specific databases

SGD

S000000004. SSA1.

Phylogenomic databases

GeneTree

ENSGT00700000104569.

HOGENOM

HOG000228135.

K03283.

OMA

NTTASKE.

OrthoDB

EOG476P7G.

Gene expression databases

ArrayExpress

P10591.

Genevestigator

P10591.

GermOnline

YAL005C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]

Pfam

PF00012. HSP70. 1 hit.
[Graphical view]

PRINTS

PR00301. HEATSHOCK70.

PROSITE

PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5186.

EvolutionaryTrace

P10591.

NextBio

968213.

Entry information

Entry name

HSP71_YEAST

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal 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

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents