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P25619 (HSP30_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
30 kDa heat shock protein
Gene names
Name:HSP30
Ordered Locus Names:YCR021C
ORF Names:YCR21C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Membrane; Multi-pass membrane protein.

Developmental stage

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

Miscellaneous

Present with 7800 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the archaeal/bacterial/fungal opsin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 33233230 kDa heat shock protein
PRO_0000196284

Regions

Topological domain1 – 3434Extracellular Potential
Transmembrane35 – 5521Helical; Potential
Topological domain56 – 6510Cytoplasmic Potential
Transmembrane66 – 8621Helical; Potential
Topological domain87 – 12135Extracellular Potential
Transmembrane122 – 14221Helical; Potential
Topological domain143 – 15715Cytoplasmic Potential
Transmembrane158 – 17821Helical; Potential
Topological domain179 – 1813Extracellular Potential
Transmembrane182 – 20221Helical; Potential
Topological domain203 – 21513Cytoplasmic Potential
Transmembrane216 – 23621Helical; Potential
Topological domain237 – 24812Extracellular Potential
Transmembrane249 – 26921Helical; Potential
Topological domain270 – 33263Cytoplasmic Potential
Compositional bias290 – 33243Glu-rich (acidic)

Amino acid modifications

Modified residue3081Phosphoserine Ref.4 Ref.8 Ref.9
Modified residue3121Phosphoserine Ref.8
Modified residue3151Phosphothreonine Ref.9
Modified residue3311Phosphothreonine Ref.6 Ref.9

Sequences

Sequence LengthMass (Da)Tools
P25619 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 260474A481D29AC5

FASTA33237,045
        10         20         30         40         50         60 
MNDTLSSFLN RNEALGLNPP HGLDMHITKR GSDWLWAVFA VFGFILLCYV VMFFIAENKG 

        70         80         90        100        110        120 
SRLTRYALAP AFLITFFEFF AFFTYASDLG WTGVQAEFNH VKVSKSITGE VPGIRQIFYS 

       130        140        150        160        170        180 
KYIAWFLSWP CLLFLIELAA STTGENDDIS ALDMVHSLLI QIVGTLFWVV SLLVGSLIKS 

       190        200        210        220        230        240 
TYKWGYYTIG AVAMLVTQGV ICQRQFFNLK TRGFNALMLC TCMVIVWLYF ICWGLSDGGN 

       250        260        270        280        290        300 
RIQPDGEAIF YGVLDLCVFA IYPCYLLIAV SRDGKLPRLS LTGGFSHHHA TDDVEDAAPE 

       310        320        330 
TKEAVPESPR ASGETAIHEP EPEAEQAVED TA

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae."
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.
Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, MASS SPECTROMETRY.
Strain: 2124.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-331, MASS SPECTROMETRY.
Strain: SUB592.
[7]"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.
[8]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-312, MASS SPECTROMETRY.
[9]"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-308; THR-315 AND THR-331, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M93123 Unassigned DNA. Translation: AAA02903.1.
X59720 Genomic DNA. Translation: CAA42313.1.
BK006937 Genomic DNA. Translation: DAA07500.1.
PIRS31848.
RefSeqNP_009950.1. NM_001178735.1.

3D structure databases

ProteinModelPortalP25619.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4586N.
IntActP25619. 28 interactions.
MINTMINT-511943.
STRING4932.YCR021C.

Protein family/group databases

TCDB3.E.1.4.1. ion-translocating microbial rhodopsin (MR) family.

Proteomic databases

PaxDbP25619.
PeptideAtlasP25619.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR021C; YCR021C; YCR021C.
GeneID850385.
KEGGsce:YCR021C.

Organism-specific databases

CYGDYCR021c.
SGDS000000615. HSP30.

Phylogenomic databases

eggNOGCOG5524.
GeneTreeENSGT00390000004481.
HOGENOMHOG000248243.
OMASDWLWAV.
OrthoDBEOG4HX897.

Enzyme and pathway databases

BioCycYEAST:G3O-29337-MONOMER.

Gene expression databases

ArrayExpressP25619.
GenevestigatorP25619.
GermOnlineYCR021C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001425. Rhodopsin_arc/bac/fun.
[Graphical view]
PfamPF01036. Bac_rhodopsin. 1 hit.
[Graphical view]
SMARTSM01021. Bac_rhodopsin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio965897.

Entry information

Entry nameHSP30_YEAST
AccessionPrimary (citable) accession number: P25619
Secondary accession number(s): D6VR31, Q04556
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 29, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents