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Protein

Heat shock protein SSA1

Gene

SSA1

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. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.1 Publication

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • tRNA binding Source: SGD
  • unfolded protein binding Source: SGD

GO - Biological processi

  • clathrin coat disassembly Source: SGD
  • cytoplasmic translation Source: SGD
  • protein folding Source: SGD
  • protein import into nucleus, translocation Source: SGD
  • protein polyubiquitination Source: SGD
  • protein refolding Source: SGD
  • protein targeting to mitochondrion Source: SGD
  • SRP-dependent cotranslational protein targeting to membrane, translocation Source: SGD
  • stress granule disassembly Source: SGD
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-28819-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein SSA1
Alternative name(s):
Heat shock protein YG100
Gene namesi
Name:SSA1
Ordered Locus Names:YAL005C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAL005C.
SGDiS000000004. SSA1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell wall, Cytoplasm, Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 642641Heat shock protein SSA1PRO_0000078385Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei62 – 621PhosphoserineCombined sources
Cross-linki521 – 521Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki536 – 536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei551 – 5511PhosphoserineCombined sources
Cross-linki556 – 556Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei603 – 6031PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP10591.
PRIDEiP10591.

2D gel databases

COMPLUYEAST-2DPAGEP10591.
SWISS-2DPAGEP10591.

PTM databases

iPTMnetiP10591.

Interactioni

Subunit structurei

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 NAP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CLG1P351903EBI-8591,EBI-4762
FES1P382603EBI-8591,EBI-21563
HSC82P151082EBI-8591,EBI-8666
HSP78P334162EBI-8591,EBI-8680
HSP82P028293EBI-8591,EBI-8659
PCL2P256933EBI-8591,EBI-4499
PHO85P171572EBI-8591,EBI-13327
RPT6Q019392EBI-8591,EBI-13914
SIS1P252943EBI-8591,EBI-17244
SSE1P325898EBI-8591,EBI-8648

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi31786. 711 interactions.
DIPiDIP-2253N.
IntActiP10591. 577 interactions.
MINTiMINT-8285515.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LCAX-ray2.19Q631-642[»]
ProteinModelPortaliP10591.
SMRiP10591. Positions 4-608.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10591.

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

GeneTreeiENSGT00840000129996.
HOGENOMiHOG000228135.
InParanoidiP10591.
KOiK03283.
OMAiAEETISW.
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.

P10591-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKAVGIDLG TTYSCVAHFA NDRVDIIAND QGNRTTPSFV AFTDTERLIG
60 70 80 90 100
DAAKNQAAMN PSNTVFDAKR LIGRNFNDPE VQADMKHFPF 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 KSEIFSTYAD 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 DKDTVTKKAE ETISWLDSNT TASKEEFDDK LKELQDIANP
610 620 630 640
IMSKLYQAGG APGGAAGGAP GGFPGGAPPA PEAEGPTVEE VD
Length:642
Mass (Da):69,657
Last modified:January 23, 2007 - v4
Checksum:i249D8A3BC42527CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081S → F in AAC04952 (PubMed:7941740).Curated
Sequence conflicti418 – 4181P → S in AAC04952 (PubMed:7941740).Curated
Sequence conflicti422 – 4221S → F in AAC04952 (PubMed:7941740).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12926 Genomic DNA. Translation: CAA31393.1.
L22015 Genomic DNA. Translation: AAC04952.1.
BK006935 Genomic DNA. Translation: DAA06982.1.
PIRiS43449. HHBYA1.
RefSeqiNP_009396.2. NM_001178151.1.

Genome annotation databases

EnsemblFungiiYAL005C; YAL005C; YAL005C.
GeneIDi851259.
KEGGisce:YAL005C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12926 Genomic DNA. Translation: CAA31393.1.
L22015 Genomic DNA. Translation: AAC04952.1.
BK006935 Genomic DNA. Translation: DAA06982.1.
PIRiS43449. HHBYA1.
RefSeqiNP_009396.2. NM_001178151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LCAX-ray2.19Q631-642[»]
ProteinModelPortaliP10591.
SMRiP10591. Positions 4-608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31786. 711 interactions.
DIPiDIP-2253N.
IntActiP10591. 577 interactions.
MINTiMINT-8285515.

Chemistry

ChEMBLiCHEMBL5186.

PTM databases

iPTMnetiP10591.

2D gel databases

COMPLUYEAST-2DPAGEP10591.
SWISS-2DPAGEP10591.

Proteomic databases

MaxQBiP10591.
PRIDEiP10591.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL005C; YAL005C; YAL005C.
GeneIDi851259.
KEGGisce:YAL005C.

Organism-specific databases

EuPathDBiFungiDB:YAL005C.
SGDiS000000004. SSA1.

Phylogenomic databases

GeneTreeiENSGT00840000129996.
HOGENOMiHOG000228135.
InParanoidiP10591.
KOiK03283.
OMAiAEETISW.
OrthoDBiEOG728916.

Enzyme and pathway databases

BioCyciYEAST:G3O-28819-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP10591.
PROiP10591.

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. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: PROTEIN SEQUENCE OF 92-98 AND 326-342.
    Strain: ATCC 204508 / S288c.
  7. "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.
  8. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 591-642.
  9. "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.
  10. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAB1 AND SIS1.
  11. "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.
  12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-521 AND LYS-536.
    Strain: SUB592.
  15. "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].
  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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHSP71_YEAST
AccessioniPrimary (citable) accession number: P10591
Secondary accession number(s): D6VPL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 181 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 269000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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