Heat shock protein SSA2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P10592 (HSP72_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 148. History...

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

Documents (3) |

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 SSA2

Gene names

Name:	SSA2
Ordered Locus Names:	YLL024C
ORF Names:	L0931

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	639 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. SSA2 can participate in the ATP-dependent disassembly of clathrin-coated vesicles. Ref.8
Subunit structure	Binds human HTN3/histatin-5, a peptide from saliva, and mediates its fungicidal activity. Interacts with NAP1. Ref.8 Ref.14
Subcellular location	Cytoplasm. Secreted › cell wall.
Miscellaneous	Present with 364000 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	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane, translocation Inferred from mutant phenotype PubMed 8754838. Source: SGD protein folding Inferred from direct assay PubMed 7867784. Source: SGD response to stress Inferred from mutant phenotype PubMed 3302682. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 16806052. Source: SGD 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 mitochondrion Inferred from direct assay PubMed 16806052. 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 direct assay PubMed 10893257. Source: SGD ATPase activity Inferred from sequence or structural similarity PubMed 8151709. Source: SGD unfolded protein binding Inferred from genetic interaction PubMed 9789005. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
COQ1	P18900	2	EBI-8603,EBI-4912
ESS1	P22696	2	EBI-8603,EBI-6679
HSP82	P02829	2	EBI-8603,EBI-8659
MDH1	P17505	2	EBI-8603,EBI-10594

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 639

638

Heat shock protein SSA2

PRO_0000078386

Amino acid modifications

Modified residue

N-acetylserine Ref.7

Modified residue

Phosphoserine Ref.15

Modified residue

Phosphothreonine Ref.15

Modified residue

Phosphothreonine Ref.15

Modified residue

426

Phosphoserine Ref.12

Modified residue

551

Phosphoserine Ref.11 Ref.13 Ref.15

Cross-link

556

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Sequences

Sequence

Length

Mass (Da)

Tools

P10592 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 129049E21C9DD1F3
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FASTA

639

69,470

        10         20         30         40         50         60 
MSKAVGIDLG TTYSCVAHFS NDRVDIIAND QGNRTTPSFV GFTDTERLIG DAAKNQAAMN 

        70         80         90        100        110        120 
PANTVFDAKR LIGRNFNDPE VQGDMKHFPF 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 
KSEVFSTYAD 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 DKDAVTKKAE ETIAWLDSNT TATKEEFDDQ LKELQEVANP 

       610        620        630 
IMSKLYQAGG APEGAAPGGF PGGAPPAPEA EGPTVEEVD

« 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]	"The sequence of 32kb on the left arm of yeast chromosome XII reveals six known genes, a new member of the seripauperins family and a new ABC transporter homologous to the human multidrug resistance protein." Purnelle B., Goffeau A. Yeast 13:183-188(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 187-196. 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, PHOSPHORYLATION.
[8]	"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.
[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]	"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-556, MASS SPECTROMETRY. Strain: SUB592.
[11]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, MASS SPECTROMETRY. Strain: YAL6B.
[12]	"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 SER-426, MASS SPECTROMETRY.
[13]	"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-551, MASS SPECTROMETRY.
[14]	"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.
[15]	"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-20; THR-35; THR-36 AND SER-551, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X12927 Genomic DNA. Translation: CAA31394.1. Z73129 Genomic DNA. Translation: CAA97472.1. X97560 Genomic DNA. Translation: CAA66167.1. BK006945 Genomic DNA. Translation: DAA09296.1.
PIR	S20139.
RefSeq	NP_013076.1. NM_001181844.1.
3D structure databases
ProteinModelPortal	P10592.
SMR	P10592. Positions 3-608.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2265N.
IntAct	P10592. 963 interactions.
MINT	MINT-8285323.
STRING	4932.YLL024C.
2D gel databases
COMPLUYEAST-2DPAGE	P10592.
SWISS-2DPAGE	P10592.
Proteomic databases
PaxDb	P10592.
PeptideAtlas	P10592.
PRIDE	P10592.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLL024C; YLL024C; YLL024C.
GeneID	850636.
KEGG	sce:YLL024C.
Organism-specific databases
SGD	S000003947. SSA2.
Phylogenomic databases
eggNOG	COG0443.
GeneTree	ENSGT00550000074467.
HOGENOM	HOG000228135.
KO	K03283.
OMA	CFDIDSN.
OrthoDB	EOG476P7G.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32128-MONOMER.
Gene expression databases
Genevestigator	P10592.
GermOnline	YLL024C. 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
NextBio	966561.

Entry information

Entry name

HSP72_YEAST

Accession

Primary (citable) accession number: P10592
Secondary accession number(s): D6VXY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 148 of the entry and version 3 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 XII

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

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

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents