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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

  • ATPase activity Source: SGD
  • ATP binding Source: SGD
  • tRNA binding Source: SGD
  • unfolded protein binding Source: SGD

GO - Biological processi

  • protein folding Source: SGD
  • SRP-dependent cotranslational protein targeting to membrane, translocation Source: SGD
  • tRNA import into nucleus Source: SGD
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32128-MONOMER.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLL024C.
SGDiS000003947. SSA2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: SGD
  • extracellular region Source: UniProtKB-KW
  • fungal-type cell wall Source: SGD
  • fungal-type vacuole membrane Source: SGD
  • mitochondrion Source: SGD
  • polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 639638Heat shock protein SSA2PRO_0000078386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources1 Publication
Modified residuei20 – 201PhosphoserineCombined sources
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.
PeptideAtlasiP10592.
PRIDEiP10592.

2D gel databases

COMPLUYEAST-2DPAGEP10592.
SWISS-2DPAGEP10592.

PTM databases

iPTMnetiP10592.

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
APE2P324545EBI-8603,EBI-2641
ARO4P324492EBI-8603,EBI-2915
BCH1Q050293EBI-8603,EBI-27508
BLM10P435832EBI-8603,EBI-22761
BRO1P485822EBI-8603,EBI-3768
CCL1P373663EBI-8603,EBI-4385
CDC28P005463EBI-8603,EBI-4253
CLN2P204382EBI-8603,EBI-4483
COQ1P189002EBI-8603,EBI-4912
CTI6Q089233EBI-8603,EBI-33349
CTR9P891053EBI-8603,EBI-5283
DIS3Q081623EBI-8603,EBI-1740
DJP1P405642EBI-8603,EBI-25380
DNM1P548613EBI-8603,EBI-6002
DOS2P548583EBI-8603,EBI-6042
DPH5P324693EBI-8603,EBI-6095
EAF3Q124323EBI-8603,EBI-6281
ECM16Q042173EBI-8603,EBI-1820
ERG13P548393EBI-8603,EBI-8373
ESS1P226963EBI-8603,EBI-6679
FAT1P382252EBI-8603,EBI-6819
FIP1P459763EBI-8603,EBI-6940
GDA1P326212EBI-8603,EBI-7511
GEM1P397223EBI-8603,EBI-20685
GND1P387203EBI-8603,EBI-1965
GPI8P490182EBI-8603,EBI-7822
GPP1P412772EBI-8603,EBI-7829
HHF2P023093EBI-8603,EBI-8113
HNT1Q043442EBI-8603,EBI-8416
HSP26P159923EBI-8603,EBI-8555
HSP42Q123293EBI-8603,EBI-8571
HSP82P028293EBI-8603,EBI-8659
IES1P435793EBI-8603,EBI-22775
ILV6P256052EBI-8603,EBI-9087
MCM5P294964EBI-8603,EBI-10549
MDH1P175052EBI-8603,EBI-10594
MET4P323892EBI-8603,EBI-10757
MFT1P334413EBI-8603,EBI-10841
MLP1Q024552EBI-8603,EBI-11009
MRP1P106623EBI-8603,EBI-16234
MSH3P253363EBI-8603,EBI-11362
NOG2P537423EBI-8603,EBI-28532
NUM1Q004022EBI-8603,EBI-12386
PRP40P332032EBI-8603,EBI-701
PRS5Q122652EBI-8603,EBI-9886
PTC2P399664EBI-8603,EBI-12795
RGR1P192633EBI-8603,EBI-15087
RKI1Q121892EBI-8603,EBI-15898
RPA190P109643EBI-8603,EBI-15730
RPN7Q061033EBI-8603,EBI-15940
RRP12Q127543EBI-8603,EBI-30678
RRP5Q050223EBI-8603,EBI-16011
RSC3Q066394EBI-8603,EBI-22058
RTN1Q049473EBI-8603,EBI-38020
SAM1P106593EBI-8603,EBI-10789
SEC16P484153EBI-8603,EBI-16551
SFB2P539533EBI-8603,EBI-17006
SGT2Q121183EBI-8603,EBI-31784
SIS1P252943EBI-8603,EBI-17244
SKG3Q063153EBI-8603,EBI-34508
SMI1P325663EBI-8603,EBI-17452
SSA1P105913EBI-8603,EBI-8591
SSA4P222023EBI-8603,EBI-8621
SSE1P325893EBI-8603,EBI-8648
STI1P157053EBI-8603,EBI-18418
SWH1P358453EBI-8603,EBI-12611
UBP10P538742EBI-8603,EBI-19873
URN1Q065252EBI-8603,EBI-35138
USO1P253862EBI-8603,EBI-20157
VAC14Q067083EBI-8603,EBI-27189
VIP1Q066853EBI-8603,EBI-35034
YIR035CP405792EBI-8603,EBI-1804
YMR027WQ043713EBI-8603,EBI-28049
YNR029CP537294EBI-8603,EBI-28492
YRB30P531072EBI-8603,EBI-24056
YTH1Q061023EBI-8603,EBI-38049
ZDS1P501113EBI-8603,EBI-29626

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi31229. 360 interactions.
DIPiDIP-2265N.
IntActiP10592. 2444 interactions.
MINTiMINT-8285323.

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

GeneTreeiENSGT00830000128434.
HOGENOMiHOG000228135.
InParanoidiP10592.
KOiK03283.
OMAiLERVCHP.
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. 360 interactions.
DIPiDIP-2265N.
IntActiP10592. 2444 interactions.
MINTiMINT-8285323.

PTM databases

iPTMnetiP10592.

2D gel databases

COMPLUYEAST-2DPAGEP10592.
SWISS-2DPAGEP10592.

Proteomic databases

MaxQBiP10592.
PeptideAtlasiP10592.
PRIDEiP10592.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YLL024C.
SGDiS000003947. SSA2.

Phylogenomic databases

GeneTreeiENSGT00830000128434.
HOGENOMiHOG000228135.
InParanoidiP10592.
KOiK03283.
OMAiLERVCHP.
OrthoDBiEOG728916.

Enzyme and pathway databases

BioCyciYEAST:G3O-32128-MONOMER.

Miscellaneous databases

NextBioi966561.
PROiP10592.

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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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: April 13, 2016
This is version 178 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

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 one 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.