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Protein

30 kDa heat shock protein

Gene

HSP30

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably cooperates with other heat shock proteins in the translocation of polypeptides through membranes. It may counteract the altering effect of heat shock on the plasma membrane.

GO - Biological processi

  • cellular response to DNA damage stimulus Source: SGD
  • cellular response to ethanol Source: SGD
  • cellular response to heat Source: SGD
  • cellular response to hydrogen peroxide Source: SGD
  • cellular response to osmotic stress Source: SGD
  • negative regulation of ATPase activity Source: SGD
Complete GO annotation...

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciYEAST:G3O-29337-MONOMER.

Protein family/group databases

TCDBi3.E.1.4.1. the ion-translocating microbial rhodopsin (mr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
30 kDa heat shock protein
Gene namesi
Name:HSP30
Ordered Locus Names:YCR021C
ORF Names:YCR21C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCR021C.
SGDiS000000615. HSP30.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3434ExtracellularSequence analysisAdd
BLAST
Transmembranei35 – 5521HelicalSequence analysisAdd
BLAST
Topological domaini56 – 6510CytoplasmicSequence analysis
Transmembranei66 – 8621HelicalSequence analysisAdd
BLAST
Topological domaini87 – 12135ExtracellularSequence analysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence analysisAdd
BLAST
Topological domaini143 – 15715CytoplasmicSequence analysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Topological domaini179 – 1813ExtracellularSequence analysis
Transmembranei182 – 20221HelicalSequence analysisAdd
BLAST
Topological domaini203 – 21513CytoplasmicSequence analysisAdd
BLAST
Transmembranei216 – 23621HelicalSequence analysisAdd
BLAST
Topological domaini237 – 24812ExtracellularSequence analysisAdd
BLAST
Transmembranei249 – 26921HelicalSequence analysisAdd
BLAST
Topological domaini270 – 33263CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 33233230 kDa heat shock proteinPRO_0000196284Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei308 – 3081PhosphoserineCombined sources
Modified residuei331 – 3311PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PeptideAtlasiP25619.

PTM databases

iPTMnetiP25619.

Expressioni

Developmental stagei

Expressed during the entry into stationary phase resulting from glucose limitation.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CREB3L1Q96BA83EBI-8563,EBI-6942903From a different organism.

Protein-protein interaction databases

BioGridi31004. 89 interactions.
DIPiDIP-4586N.
IntActiP25619. 31 interactions.
MINTiMINT-511943.

Structurei

3D structure databases

ProteinModelPortaliP25619.
SMRiP25619. Positions 28-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi290 – 33243Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000004481.
HOGENOMiHOG000248243.
InParanoidiP25619.
OMAiPSSEMIW.
OrthoDBiEOG754J0K.

Family and domain databases

InterProiIPR001425. Arc/bac/fun_rhod.
[Graphical view]
PfamiPF01036. Bac_rhodopsin. 1 hit.
[Graphical view]
SMARTiSM01021. Bac_rhodopsin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25619-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDTLSSFLN RNEALGLNPP HGLDMHITKR GSDWLWAVFA VFGFILLCYV
60 70 80 90 100
VMFFIAENKG SRLTRYALAP AFLITFFEFF AFFTYASDLG WTGVQAEFNH
110 120 130 140 150
VKVSKSITGE VPGIRQIFYS KYIAWFLSWP CLLFLIELAA STTGENDDIS
160 170 180 190 200
ALDMVHSLLI QIVGTLFWVV SLLVGSLIKS TYKWGYYTIG AVAMLVTQGV
210 220 230 240 250
ICQRQFFNLK TRGFNALMLC TCMVIVWLYF ICWGLSDGGN RIQPDGEAIF
260 270 280 290 300
YGVLDLCVFA IYPCYLLIAV SRDGKLPRLS LTGGFSHHHA TDDVEDAAPE
310 320 330
TKEAVPESPR ASGETAIHEP EPEAEQAVED TA
Length:332
Mass (Da):37,045
Last modified:May 1, 1992 - v1
Checksum:i260474A481D29AC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93123 Unassigned DNA. Translation: AAA02903.1.
X59720 Genomic DNA. Translation: CAA42313.1.
BK006937 Genomic DNA. Translation: DAA07500.1.
PIRiS31848.
RefSeqiNP_009950.1. NM_001178735.1.

Genome annotation databases

EnsemblFungiiCAA42313; CAA42313; CAA42313.
YCR021C; YCR021C; YCR021C.
GeneIDi850385.
KEGGisce:YCR021C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93123 Unassigned DNA. Translation: AAA02903.1.
X59720 Genomic DNA. Translation: CAA42313.1.
BK006937 Genomic DNA. Translation: DAA07500.1.
PIRiS31848.
RefSeqiNP_009950.1. NM_001178735.1.

3D structure databases

ProteinModelPortaliP25619.
SMRiP25619. Positions 28-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31004. 89 interactions.
DIPiDIP-4586N.
IntActiP25619. 31 interactions.
MINTiMINT-511943.

Protein family/group databases

TCDBi3.E.1.4.1. the ion-translocating microbial rhodopsin (mr) family.

PTM databases

iPTMnetiP25619.

Proteomic databases

PeptideAtlasiP25619.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42313; CAA42313; CAA42313.
YCR021C; YCR021C; YCR021C.
GeneIDi850385.
KEGGisce:YCR021C.

Organism-specific databases

EuPathDBiFungiDB:YCR021C.
SGDiS000000615. HSP30.

Phylogenomic databases

GeneTreeiENSGT00390000004481.
HOGENOMiHOG000248243.
InParanoidiP25619.
OMAiPSSEMIW.
OrthoDBiEOG754J0K.

Enzyme and pathway databases

BioCyciYEAST:G3O-29337-MONOMER.

Miscellaneous databases

NextBioi965897.
PROiP25619.

Family and domain databases

InterProiIPR001425. Arc/bac/fun_rhod.
[Graphical view]
PfamiPF01036. Bac_rhodopsin. 1 hit.
[Graphical view]
SMARTiSM01021. Bac_rhodopsin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence of HSP30, a yeast heat-shock gene coding for a hydrophobic membrane protein."
    Regnacq M., Boucherie H.
    Curr. Genet. 23:435-442(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 44827 / SKQ2N.
  2. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [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: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  6. "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 THR-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHSP30_YEAST
AccessioniPrimary (citable) accession number: P25619
Secondary accession number(s): D6VR31, Q04556
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 11, 2016
This is version 129 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 7800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: 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.