Heat shock protein SSA2

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ATPase activity Source: SGD <p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • "Molecular evolution of the HSP70 multigene family."
    Boorstein W.R., Ziegelhoffer T., Craig E.A.
    J. Mol. Evol. 38:1-17(1994) [PubMed] [Europe PMC] [Abstract]
• ATP binding Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles."
    Brown C.R., McCann J.A., Chiang H.L.
    J Cell Biol 150:65-76(2000) [PubMed] [Europe PMC] [Abstract]
• heat shock protein binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• misfolded protein binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• protein folding chaperone Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• tRNA binding Source: SGDInferred from direct assayⁱ
  • "Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus."
    Takano A., Kajita T., Mochizuki M., Endo T., Yoshihisa T.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
• unfolded protein binding Source: SGD <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins."
    Kim S., Schilke B., Craig E.A., Horwich A.L.
    Proc Natl Acad Sci U S A 95:12860-12865(1998) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• cellular response to unfolded protein Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• chaperone cofactor-dependent protein refolding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell aging Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Lifespan Control by Redox-Dependent Recruitment of Chaperones to Misfolded Proteins."
    Hanzen S., Vielfort K., Yang J., Roger F., Andersson V., Zamarbide-Fores S., Andersson R., Malm L., Palais G., Biteau B., Liu B., Toledano M.B., Molin M., Nystrom T.
    Cell 166:140-151(2016) [PubMed] [Europe PMC] [Abstract]
• proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGDInferred from genetic interactionⁱ
  • "The requirements of yeast Hsp70 of SSA family for the ubiquitin-dependent degradation of short-lived and abnormal proteins."
    Lee d.o. H., Sherman M.Y., Goldberg A.L.
    Biochem Biophys Res Commun 475:100-106(2016) [PubMed] [Europe PMC] [Abstract]
• protein folding Source: SGDInferred from direct assayⁱ
  • "Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation."
    Cyr D.M.
    FEBS Lett 359:129-132(1995) [PubMed] [Europe PMC] [Abstract]
• protein refolding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• SRP-dependent cotranslational protein targeting to membrane, translocation Source: SGDInferred from mutant phenotypeⁱ
  • "Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo."
    Becker J., Walter W., Yan W., Craig E.A.
    Mol Cell Biol 16:4378-4386(1996) [PubMed] [Europe PMC] [Abstract]
• tRNA import into nucleus Source: SGDInferred from mutant phenotypeⁱ
  • "Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus."
    Takano A., Kajita T., Mochizuki M., Endo T., Yoshihisa T.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
• vesicle-mediated transport Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• heat shock protein binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• misfolded protein binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• unfolded protein binding Source: SGDInferred from genetic interactionⁱ
  • "Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins."
    Kim S., Schilke B., Craig E.A., Horwich A.L.
    Proc Natl Acad Sci U S A 95:12860-12865(1998) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        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             

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

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