Heat shock protein SSA1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P10591 (HSP71_YEAST)

Last modified June 16, 2009. Version 107. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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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.

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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.10
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.9
Subcellular location	Cytoplasm. Secreted › cell wall. Ref.11
Miscellaneous	Present with 269000 molecules/cell in log phase SD medium. Ref.12
Sequence similarities	Belongs to the heat shock protein 70 family.

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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	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	SRP-dependent cotranslational protein targeting to membrane, translocation Inferred from direct assay. Source: SGD protein import into nucleus, translocation Inferred from direct assay. Source: SGD protein refolding Inferred from direct assay. Source: SGD protein targeting to mitochondrion Inferred from mutant phenotype. Source: SGD translation Ref.9 Inferred from mutant phenotype. Source: SGD
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell fungal-type cell wall Inferred from direct assay. Source: SGD fungal-type vacuole membrane Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from direct assay. Source: SGD unfolded protein binding Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
	P28273	1	EBI-8591,EBI-27022
	P46992	1	EBI-8591,EBI-26156
	Q06251	1	EBI-8591,EBI-32907
ABC1	P27697	1	EBI-8591,EBI-2013
ATG2	P53855	1	EBI-8591,EBI-29212
CAR2	P07991	1	EBI-8591,EBI-12430
HPT1	Q04178	1	EBI-8591,EBI-29727
HSP78	P33416	1	EBI-8591,EBI-8680
HXK1	P04806	1	EBI-8591,EBI-8732
LCB4	Q12246	1	EBI-8591,EBI-38830
MEF2	P39677	1	EBI-8591,EBI-6361
MOD5	P07884	1	EBI-8591,EBI-11135
PAN3	P36102	1	EBI-8591,EBI-12895
PHO8	P11491	1	EBI-8591,EBI-13762
RAD9	P14737	1	EBI-8591,EBI-14788
RBK1	P25332	1	EBI-8591,EBI-14854
RIM20	Q12033	1	EBI-8591,EBI-38947
RPT6	Q01939	1	EBI-8591,EBI-13914
RUD3	Q12234	1	EBI-8591,EBI-31697
SSE1	P32589	1	EBI-8591,EBI-8648
TMP1	P06785	1	EBI-8591,EBI-19690
XDJ1	P39102	1	EBI-8591,EBI-20578
YPK2	P18961	1	EBI-8591,EBI-29484

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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.8

Modified residue

Phosphothreonine Ref.14

Modified residue

Phosphothreonine Ref.17

Modified residue

Phosphothreonine Ref.17

Modified residue

Phosphothreonine Ref.17

Modified residue

Phosphoserine Ref.17

Modified residue

131

Phosphoserine Ref.17

Modified residue

151

Phosphoserine Ref.17

Modified residue

378

Phosphothreonine Ref.17

Modified residue

459

Phosphoserine Ref.17

Modified residue

486

Phosphoserine Ref.17

Modified residue

492

Phosphothreonine Ref.17

Modified residue

495

Phosphoserine Ref.17 Ref.15

Modified residue

541

Phosphoserine Ref.17

Modified residue

545

Phosphoserine Ref.17

Modified residue

551

Phosphoserine Ref.17 Ref.15

Modified residue

603

Phosphoserine Ref.17

Cross-link

521

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13

Cross-link

536

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13

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

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Sequences

Sequence

Length

Mass (Da)

Tools

P10591-1 [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

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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: 2644626] [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: 7941740] [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: 7731988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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: 7895733] [Abstract] Cited for: PROTEIN SEQUENCE OF 92-98 AND 326-342. 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: 8935650] [Abstract] Cited for: PROTEIN SEQUENCE OF 187-196. Strain: ATCC 38531 / Y41.
[7]	"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: 6096826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 591-642.
[8]	"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: 9298649] [Abstract] Cited for: ACETYLATION AT SER-2.
[9]	"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: 11279042] [Abstract] Cited for: INTERACTION WITH PAB1 AND SIS1.
[10]	"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: 12761219] [Abstract] Cited for: FUNCTION, INTERACTION WITH HUMAN HTN3.
[11]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]	"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: 12872131] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-521 AND LYS-536, MASS SPECTROMETRY.
[14]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, MASS SPECTROMETRY.
[15]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-551, MASS SPECTROMETRY.
[16]	"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: 18086883] [Abstract] Cited for: INTERACTION WITH NAP1, MASS SPECTROMETRY.
[17]	"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: 18407956] [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.

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Cross-references

Sequence databases
	X12926 Genomic DNA. Translation: CAA31393.1. L22015 Genomic DNA. Translation: AAC04952.1.
PIR	HHBYA1. S43449.
RefSeq	NP_009396.2.
3D structure databases
HSSP	HSSP built from PDB template 3HSC based on UniProtKB P19120.
SMR	P10591. Positions 1-550.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2253N.
IntAct	P10591. 278 interactions.
2-D gel databases
SWISS-2DPAGE	P10591.
COMPLUYEAST-2DPAGE	P10591.
Proteomic databases
PeptideAtlas	P10591.
PRIDE	P10591.
Genome annotation databases
Ensembl	YAL005C. Saccharomyces cerevisiae. [Contig view]
GeneID	851259.
GenomeReviews	Gene locus YAL005C in contig U00091_GR.
KEGG	sce:YAL005C.
Organism-specific databases
CYGD	YAL005c.
SGD	S000000004. SSA1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P10591.
Gene expression databases
ArrayExpress	P10591.
GermOnline	YAL005C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR018181. Heat_shock_70_CS. IPR001023. Hsp70. IPR013126. Hsp_70. [Graphical view]
PANTHER	PTHR19375. Hsp70. 1 hit.
Pfam	PF00012. HSP70. 1 hit. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
ProDom	PD000089. Hsp70. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00297. HSP70_1. 1 hit. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	968213.

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Entry information

Entry name

HSP71_YEAST

Accession

Primary (citable) accession number: P10591

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 107 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome I

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

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

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents