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Protein

Heat shock protein SSA2

Gene

SSA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. ATPase activity Source: SGD
  2. ATP binding Source: SGD
  3. unfolded protein binding Source: SGD

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. protein folding Source: SGD
  3. SRP-dependent cotranslational protein targeting to membrane, translocation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32128-MONOMER.
ReactomeiREACT_205607. Regulation of HSF1-mediated heat shock response.
REACT_219346. HSF1-dependent transactivation.
REACT_271186. Attenuation phase.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein SSA2
Gene namesi
Name:SSA2
Ordered Locus Names:YLL024C
ORF Names:L0931
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

SGDiS000003947. SSA2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. cytosol Source: SGD
  3. extracellular region Source: UniProtKB-KW
  4. fungal-type cell wall Source: SGD
  5. fungal-type vacuole membrane Source: SGD
  6. mitochondrion Source: SGD
  7. polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 639638Heat shock protein SSA2PRO_0000078386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei551 – 5511PhosphoserineBy similarity
Cross-linki556 – 556Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei603 – 6031PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP10592.
PaxDbiP10592.
PeptideAtlasiP10592.
PRIDEiP10592.

2D gel databases

COMPLUYEAST-2DPAGEP10592.
SWISS-2DPAGEP10592.

Expressioni

Gene expression databases

GenevestigatoriP10592.

Interactioni

Subunit structurei

Binds human HTN3/histatin-5, a peptide from saliva, and mediates its fungicidal activity. Interacts with NAP1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COQ1P189002EBI-8603,EBI-4912
ESS1P226962EBI-8603,EBI-6679
HSP82P028292EBI-8603,EBI-8659
MDH1P175052EBI-8603,EBI-10594

Protein-protein interaction databases

BioGridi31229. 350 interactions.
DIPiDIP-2265N.
IntActiP10592. 969 interactions.
MINTiMINT-8285323.
STRINGi4932.YLL024C.

Structurei

3D structure databases

ProteinModelPortaliP10592.
SMRiP10592. Positions 4-608.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00780000122619.
HOGENOMiHOG000228135.
InParanoidiP10592.
KOiK03283.
OMAiHICSVRS.
OrthoDBiEOG728916.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10592-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKAVGIDLG TTYSCVAHFS NDRVDIIAND QGNRTTPSFV GFTDTERLIG
60 70 80 90 100
DAAKNQAAMN PANTVFDAKR LIGRNFNDPE VQGDMKHFPF KLIDVDGKPQ
110 120 130 140 150
IQVEFKGETK NFTPEQISSM VLGKMKETAE SYLGAKVNDA VVTVPAYFND
160 170 180 190 200
SQRQATKDAG TIAGLNVLRI INEPTAAAIA YGLDKKGKEE HVLIFDLGGG
210 220 230 240 250
TFDVSLLSIE DGIFEVKATA GDTHLGGEDF DNRLVNHFIQ EFKRKNKKDL
260 270 280 290 300
STNQRALRRL RTACERAKRT LSSSAQTSVE IDSLFEGIDF YTSITRARFE
310 320 330 340 350
ELCADLFRST LDPVEKVLRD AKLDKSQVDE IVLVGGSTRI PKVQKLVTDY
360 370 380 390 400
FNGKEPNRSI NPDEAVAYGA AVQAAILTGD ESSKTQDLLL LDVAPLSLGI
410 420 430 440 450
ETAGGVMTKL IPRNSTIPTK KSEVFSTYAD NQPGVLIQVF EGERAKTKDN
460 470 480 490 500
NLLGKFELSG IPPAPRGVPQ IEVTFDVDSN GILNVSAVEK GTGKSNKITI
510 520 530 540 550
TNDKGRLSKE DIEKMVAEAE KFKEEDEKES QRIASKNQLE SIAYSLKNTI
560 570 580 590 600
SEAGDKLEQA DKDAVTKKAE ETIAWLDSNT TATKEEFDDQ LKELQEVANP
610 620 630
IMSKLYQAGG APEGAAPGGF PGGAPPAPEA EGPTVEEVD
Length:639
Mass (Da):69,470
Last modified:January 23, 2007 - v3
Checksum:i129049E21C9DD1F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12927 Genomic DNA. Translation: CAA31394.1.
Z73129 Genomic DNA. Translation: CAA97472.1.
X97560 Genomic DNA. Translation: CAA66167.1.
BK006945 Genomic DNA. Translation: DAA09296.1.
PIRiS20139.
RefSeqiNP_013076.1. NM_001181844.1.

Genome annotation databases

EnsemblFungiiYLL024C; YLL024C; YLL024C.
GeneIDi850636.
KEGGisce:YLL024C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12927 Genomic DNA. Translation: CAA31394.1.
Z73129 Genomic DNA. Translation: CAA97472.1.
X97560 Genomic DNA. Translation: CAA66167.1.
BK006945 Genomic DNA. Translation: DAA09296.1.
PIRiS20139.
RefSeqiNP_013076.1. NM_001181844.1.

3D structure databases

ProteinModelPortaliP10592.
SMRiP10592. Positions 4-608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31229. 350 interactions.
DIPiDIP-2265N.
IntActiP10592. 969 interactions.
MINTiMINT-8285323.
STRINGi4932.YLL024C.

2D gel databases

COMPLUYEAST-2DPAGEP10592.
SWISS-2DPAGEP10592.

Proteomic databases

MaxQBiP10592.
PaxDbiP10592.
PeptideAtlasiP10592.
PRIDEiP10592.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLL024C; YLL024C; YLL024C.
GeneIDi850636.
KEGGisce:YLL024C.

Organism-specific databases

SGDiS000003947. SSA2.

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00780000122619.
HOGENOMiHOG000228135.
InParanoidiP10592.
KOiK03283.
OMAiHICSVRS.
OrthoDBiEOG728916.

Enzyme and pathway databases

BioCyciYEAST:G3O-32128-MONOMER.
ReactomeiREACT_205607. Regulation of HSF1-mediated heat shock response.
REACT_219346. HSF1-dependent transactivation.
REACT_271186. Attenuation phase.

Miscellaneous databases

NextBioi966561.
PROiP10592.

Gene expression databases

GenevestigatoriP10592.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. 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. 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].

Entry informationi

Entry nameiHSP72_YEAST
AccessioniPrimary (citable) accession number: P10592
Secondary accession number(s): D6VXY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 364000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.