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Q12329

- HSP42_YEAST

UniProt

Q12329 - HSP42_YEAST

Protein

Heat shock protein 42

Gene

HSP42

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. unfolded protein binding Source: SGD

    GO - Biological processi

    1. cytoskeleton organization Source: SGD
    2. response to stress Source: UniProtKB-KW

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29760-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein 42
    Alternative name(s):
    42 kDa heat shock protein
    Gene namesi
    Name:HSP42
    Ordered Locus Names:YDR171W
    ORF Names:YD9395.04
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR171w.
    SGDiS000002578. HSP42.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoskeleton Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375Heat shock protein 42PRO_0000126005Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei182 – 1821Phosphoserine1 Publication
    Modified residuei213 – 2131Phosphoserine1 Publication
    Modified residuei214 – 2141Phosphoserine1 Publication
    Modified residuei215 – 2151Phosphoserine1 Publication
    Modified residuei223 – 2231Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ12329.
    PaxDbiQ12329.
    PeptideAtlasiQ12329.

    Expressioni

    Inductioni

    By stress such as heat shock or increased salt concentration. Up-regulated by all stress conditions tested. Also expressed in unstressed cells.

    Gene expression databases

    GenevestigatoriQ12329.

    Interactioni

    Subunit structurei

    Forms oligomeric complexes. Interacts with itself.

    Protein-protein interaction databases

    BioGridi32224. 68 interactions.
    DIPiDIP-2515N.
    IntActiQ12329. 50 interactions.
    MINTiMINT-626187.
    STRINGi4932.YDR171W.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12329.
    SMRiQ12329. Positions 242-356.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0071.
    HOGENOMiHOG000065948.
    KOiK13993.
    OMAiLEFEENP.
    OrthoDBiEOG7PK992.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR002068. a-crystallin/Hsp20_dom.
    IPR008978. HSP20-like_chaperone.
    [Graphical view]
    PfamiPF00011. HSP20. 1 hit.
    [Graphical view]
    SUPFAMiSSF49764. SSF49764. 1 hit.
    PROSITEiPS01031. HSP20. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12329-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFYQPSLSL YDVLNALSNQ TGQRGQQGYP RQPQRPQRYH PHYGQVHVGG    50
    HHPRHHPLYS RYNGVPNTYY YQFPGQAYYY SPEYGYDDED GEEEDQDEDM 100
    VGDSGTTRQE DGGEDSNSRR YPSYYHCNTA RNNRTNQQAN SLNDLLTALI 150
    GVPPYEGTEP EIEANTEQEG EKGEEKDKKD KSEAPKEEAG ETNKEKPLNQ 200
    LEESSRPPLA KKSSSFAHLQ APSPIPDPLQ VSKPETRMDL PFSPEVNVYD 250
    TEDTYVVVLA LPGANSRAFH IDYHPSSHEM LIKGKIEDRV GIDEKFLKIT 300
    ELKYGAFERT VKFPVLPRIK DEEIKATYNN GLLQIKVPKI VNDTEKPKPK 350
    KRIAIEEIPD EELEFEENPN PTVEN 375
    Length:375
    Mass (Da):42,817
    Last modified:November 1, 1997 - v1
    Checksum:iDF353A76493E3CE6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41401 Genomic DNA. Translation: AAC49256.1.
    Z46727 Genomic DNA. Translation: CAA86676.1.
    AY558574 Genomic DNA. Translation: AAS56900.1.
    BK006938 Genomic DNA. Translation: DAA12013.1.
    PIRiS49767.
    RefSeqiNP_010456.1. NM_001180478.1.

    Genome annotation databases

    EnsemblFungiiYDR171W; YDR171W; YDR171W.
    GeneIDi851751.
    KEGGisce:YDR171W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41401 Genomic DNA. Translation: AAC49256.1 .
    Z46727 Genomic DNA. Translation: CAA86676.1 .
    AY558574 Genomic DNA. Translation: AAS56900.1 .
    BK006938 Genomic DNA. Translation: DAA12013.1 .
    PIRi S49767.
    RefSeqi NP_010456.1. NM_001180478.1.

    3D structure databases

    ProteinModelPortali Q12329.
    SMRi Q12329. Positions 242-356.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32224. 68 interactions.
    DIPi DIP-2515N.
    IntActi Q12329. 50 interactions.
    MINTi MINT-626187.
    STRINGi 4932.YDR171W.

    Proteomic databases

    MaxQBi Q12329.
    PaxDbi Q12329.
    PeptideAtlasi Q12329.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR171W ; YDR171W ; YDR171W .
    GeneIDi 851751.
    KEGGi sce:YDR171W.

    Organism-specific databases

    CYGDi YDR171w.
    SGDi S000002578. HSP42.

    Phylogenomic databases

    eggNOGi COG0071.
    HOGENOMi HOG000065948.
    KOi K13993.
    OMAi LEFEENP.
    OrthoDBi EOG7PK992.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29760-MONOMER.

    Miscellaneous databases

    NextBioi 969507.

    Gene expression databases

    Genevestigatori Q12329.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    InterProi IPR002068. a-crystallin/Hsp20_dom.
    IPR008978. HSP20-like_chaperone.
    [Graphical view ]
    Pfami PF00011. HSP20. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49764. SSF49764. 1 hit.
    PROSITEi PS01031. HSP20. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Multimerization of Hsp42p, a novel heat shock protein of Saccharomyces cerevisiae, is dependent on a conserved carboxyl-terminal sequence."
      Wotton D., Freeman K., Shore D.
      J. Biol. Chem. 271:2717-2723(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 200060 / W303.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    8. "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-182 AND SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-213; SER-214; SER-215 AND SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHSP42_YEAST
    AccessioniPrimary (citable) accession number: Q12329
    Secondary accession number(s): D6VSF3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1470 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3