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P10592 (HSP72_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 SSA2
Gene names
Name:SSA2
Ordered Locus Names:YLL024C
ORF Names:L0931
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length639 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. 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.12

Subcellular location

Cytoplasm. Secretedcell 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 processStress response
   Cellular componentCell wall
Cytoplasm
Secreted
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity PubMed 8151709. Source: GOC

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 electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 8755907. Source: SGD

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

polysome

Inferred from direct assay PubMed 16413483. Source: SGD

   Molecular_functionATP 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 639638Heat shock protein SSA2
PRO_0000078386

Amino acid modifications

Modified residue21N-acetylserine Ref.7 Ref.15
Modified residue201Phosphoserine Ref.13
Modified residue5511Phosphoserine By similarity
Modified residue6031Phosphoserine By similarity
Cross-link556Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Sequences

Sequence LengthMass (Da)Tools
P10592 [UniParc].

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

FASTA63969,470
        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' 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. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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.
Strain: SUB592.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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].
+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.
PIRS20139.
RefSeqNP_013076.1. NM_001181844.1.

3D structure databases

ProteinModelPortalP10592.
SMRP10592. Positions 3-608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31229. 348 interactions.
DIPDIP-2265N.
IntActP10592. 969 interactions.
MINTMINT-8285323.
STRING4932.YLL024C.

2D gel databases

COMPLUYEAST-2DPAGEP10592.
SWISS-2DPAGEP10592.

Proteomic databases

PaxDbP10592.
PeptideAtlasP10592.
PRIDEP10592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLL024C; YLL024C; YLL024C.
GeneID850636.
KEGGsce:YLL024C.

Organism-specific databases

SGDS000003947. SSA2.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00750000117237.
HOGENOMHOG000228135.
KOK03283.
OMATRIPRIM.
OrthoDBEOG728916.

Enzyme and pathway databases

BioCycYEAST:G3O-32128-MONOMER.

Gene expression databases

GenevestigatorP10592.

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

NextBio966561.
PROP10592.

Entry information

Entry nameHSP72_YEAST
AccessionPrimary (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: April 16, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families