Heat shock protein STI1

<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 inhibitor activity 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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle."
    Li J., Richter K., Buchner J.
    Nat. Struct. Mol. Biol. 18:61-66(2011) [PubMed] [Europe PMC] [Abstract]
• Hsp70 protein binding Source: SGDInferred from direct assayⁱ
  • "Sti1 is a novel activator of the Ssa proteins."
    Wegele H., Haslbeck M., Reinstein J., Buchner J.
    J. Biol. Chem. 278:25970-25976(2003) [PubMed] [Europe PMC] [Abstract]
• Hsp90 protein binding Source: SGDInferred from direct assayⁱ
  • "Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle."
    Richter K., Muschler P., Hainzl O., Reinstein J., Buchner J.
    J. Biol. Chem. 278:10328-10333(2003) [PubMed] [Europe PMC] [Abstract]
  • "Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones."
    Prodromou C., Siligardi G., O'Brien R., Woolfson D.N., Regan L., Panaretou B., Ladbury J.E., Piper P.W., Pearl L.H.
    EMBO J. 18:754-762(1999) [PubMed] [Europe PMC] [Abstract]
• mRNA binding Source: SGDInferred from direct assayⁱ
  • "A screen for RNA-binding proteins in yeast indicates dual functions for many enzymes."
    Scherrer T., Mittal N., Janga S.C., Gerber A.P.
    PLoS ONE 5:e15499-e15499(2010) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• protein folding 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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "In vivo analysis of the Hsp90 cochaperone Sti1 (p60)."
    Chang H.C., Nathan D.F., Lindquist S.
    Mol. Cell. Biol. 17:318-325(1997) [PubMed] [Europe PMC] [Abstract]
• protein localization Source: SGDInferred from mutant phenotypeⁱ
  • "The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins."
    Wolfe K.J., Ren H.Y., Trepte P., Cyr D.M.
    Mol. Biol. Cell 24:3588-3602(2013) [PubMed] [Europe PMC] [Abstract]
• protein targeting to mitochondrion Source: SGDInferred from mutant phenotypeⁱ
  • "The cytosolic cochaperone Sti1 is relevant for mitochondrial biogenesis and morphology."
    Hoseini H., Pandey S., Jores T., Schmitt A., Franz-Wachtel M., Macek B., Buchner J., Dimmer K.S., Rapaport D.
    FEBS J. 283:3338-3352(2016) [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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

<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_section">'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_section">'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_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• Hsp70 protein binding Source: SGDInferred from direct assayⁱ
  • "Sti1 is a novel activator of the Ssa proteins."
    Wegele H., Haslbeck M., Reinstein J., Buchner J.
    J. Biol. Chem. 278:25970-25976(2003) [PubMed] [Europe PMC] [Abstract]
• Hsp90 protein binding Source: SGDInferred from direct assayⁱ
  • "Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle."
    Richter K., Muschler P., Hainzl O., Reinstein J., Buchner J.
    J. Biol. Chem. 278:10328-10333(2003) [PubMed] [Europe PMC] [Abstract]
  • "Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones."
    Prodromou C., Siligardi G., O'Brien R., Woolfson D.N., Regan L., Panaretou B., Ladbury J.E., Piper P.W., Pearl L.H.
    EMBO J. 18:754-762(1999) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction 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

Secondary structure

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

Domains and Repeats

Keywords - Domainⁱ

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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

        10         20         30         40         50
MSLTADEYKQ QGNAAFTAKD YDKAIELFTK AIEVSETPNH VLYSNRSACY 
        60         70         80         90        100
TSLKKFSDAL NDANECVKIN PSWSKGYNRL GAAHLGLGDL DEAESNYKKA 
       110        120        130        140        150
LELDASNKAA KEGLDQVHRT QQARQAQPDL GLTQLFADPN LIENLKKNPK 
       160        170        180        190        200
TSEMMKDPQL VAKLIGYKQN PQAIGQDLFT DPRLMTIMAT LMGVDLNMDD 
       210        220        230        240        250
INQSNSMPKE PETSKSTEQK KDAEPQSDST TSKENSSKAP QKEESKESEP 
       260        270        280        290        300
MEVDEDDSKI EADKEKAEGN KFYKARQFDE AIEHYNKAWE LHKDITYLNN 
       310        320        330        340        350
RAAAEYEKGE YETAISTLND AVEQGREMRA DYKVISKSFA RIGNAYHKLG 
       360        370        380        390        400
DLKKTIEYYQ KSLTEHRTAD ILTKLRNAEK ELKKAEAEAY VNPEKAEEAR 
       410        420        430        440        450
LEGKEYFTKS DWPNAVKAYT EMIKRAPEDA RGYSNRAAAL AKLMSFPEAI 
       460        470        480        490        500
ADCNKAIEKD PNFVRAYIRK ATAQIAVKEY ASALETLDAA RTKDAEVNNG 
       510        520        530        540        550
SSAREIDQLY YKASQQRFQP GTSNETPEET YQRAMKDPEV AAIMQDPVMQ 
       560        570        580 
SILQQAQQNP AALQEHMKNP EVFKKIQTLI AAGIIRTGR             

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

• 100% Identity
• 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

Protocols and materials 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. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. Yeast chromosome XV
   Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
3. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD