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Protein

Heat shock protein 26

Gene

HSP26

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

Functioni

Not known. One of the major polypeptides produced on heat shock.

GO - Molecular functioni

  1. mRNA binding Source: SGD
  2. unfolded protein binding Source: SGD

GO - Biological processi

  1. cellular response to heat Source: SGD
  2. protein folding Source: SGD
Complete GO annotation...

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciYEAST:G3O-29041-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein 26
Alternative name(s):
26 kDa heat shock protein
Gene namesi
Name:HSP26
Ordered Locus Names:YBR072W
ORF Names:YBR0714
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

SGDiS000000276. HSP26.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. cytoplasmic stress granule Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 214213Heat shock protein 26PRO_0000126004Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei42 – 421Phosphothreonine1 Publication
Modified residuei90 – 901Phosphoserine1 Publication
Modified residuei163 – 1631Phosphothreonine1 Publication
Modified residuei208 – 2081Phosphoserine1 Publication
Modified residuei211 – 2111Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15992.
PaxDbiP15992.
PeptideAtlasiP15992.

Expressioni

Developmental stagei

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

Inductioni

By heat shock, and under other conditions of stress, such as increased salt concentration and starvation.

Gene expression databases

GenevestigatoriP15992.

Interactioni

Subunit structurei

Present in large complexes.

Protein-protein interaction databases

BioGridi32775. 57 interactions.
DIPiDIP-3988N.
IntActiP15992. 36 interactions.
MINTiMINT-536537.
STRINGi4932.YBR072W.

Structurei

3D structure databases

ProteinModelPortaliP15992.
SMRiP15992. Positions 95-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0071.
HOGENOMiHOG000112974.
InParanoidiP15992.
KOiK13993.
OMAiKLEPREN.
OrthoDBiEOG7B5X7W.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15992-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFNSPFFDF FDNINNEVDA FNRLLGEGGL RGYAPRRQLA NTPAKDSTGK
60 70 80 90 100
EVARPNNYAG ALYDPRDETL DDWFDNDLSL FPSGFGFPRS VAVPVDILDH
110 120 130 140 150
DNNYELKVVV PGVKSKKDID IEYHQNKNQI LVSGEIPSTL NEESKDKVKV
160 170 180 190 200
KESSSGKFKR VITLPDYPGV DADNIKADYA NGVLTLTVPK LKPQKDGKNH
210
VKKIEVSSQE SWGN
Length:214
Mass (Da):23,880
Last modified:January 23, 2007 - v3
Checksum:i0CB8B6BD22C5308F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321G → A in AAA79010. (PubMed:2673926)Curated
Sequence conflicti207 – 2071S → C in AAA79010. (PubMed:2673926)Curated
Sequence conflicti212 – 2121W → G in AAT92994. (PubMed:17322287)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23871 Genomic DNA. Translation: AAA66914.1.
M26942 Genomic DNA. Translation: AAA79010.1.
X76294 Genomic DNA. Translation: CAA53929.1.
Z35941 Genomic DNA. Translation: CAA85016.1.
AY692975 Genomic DNA. Translation: AAT92994.1.
BK006936 Genomic DNA. Translation: DAA07191.1.
PIRiS45465.
RefSeqiNP_009628.1. NM_001178420.1.

Genome annotation databases

EnsemblFungiiYBR072W; YBR072W; YBR072W.
GeneIDi852364.
KEGGisce:YBR072W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23871 Genomic DNA. Translation: AAA66914.1.
M26942 Genomic DNA. Translation: AAA79010.1.
X76294 Genomic DNA. Translation: CAA53929.1.
Z35941 Genomic DNA. Translation: CAA85016.1.
AY692975 Genomic DNA. Translation: AAT92994.1.
BK006936 Genomic DNA. Translation: DAA07191.1.
PIRiS45465.
RefSeqiNP_009628.1. NM_001178420.1.

3D structure databases

ProteinModelPortaliP15992.
SMRiP15992. Positions 95-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32775. 57 interactions.
DIPiDIP-3988N.
IntActiP15992. 36 interactions.
MINTiMINT-536537.
STRINGi4932.YBR072W.

Proteomic databases

MaxQBiP15992.
PaxDbiP15992.
PeptideAtlasiP15992.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR072W; YBR072W; YBR072W.
GeneIDi852364.
KEGGisce:YBR072W.

Organism-specific databases

SGDiS000000276. HSP26.

Phylogenomic databases

eggNOGiCOG0071.
HOGENOMiHOG000112974.
InParanoidiP15992.
KOiK13993.
OMAiKLEPREN.
OrthoDBiEOG7B5X7W.

Enzyme and pathway databases

BioCyciYEAST:G3O-29041-MONOMER.

Miscellaneous databases

NextBioi971137.

Gene expression databases

GenevestigatoriP15992.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "hsp26 of Saccharomyces cerevisiae is related to the superfamily of small heat shock proteins but is without a demonstrable function."
    Susek R.E., Lindquist S.L.
    Mol. Cell. Biol. 9:5265-5271(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structure and expression of a yeast gene encoding the small heat-shock protein Hsp26."
    Bossier P., Fitch I.T., Boucherie H., Tuite M.F.
    Gene 78:323-330(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CLEAVAGE OF INITIATOR METHIONINE.
  3. "Sequence analysis of a 31 kb DNA fragment from the right arm of Saccharomyces cerevisiae chromosome II."
    van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M., Steensma H.Y.
    Yeast 10:959-964(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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 THR-42; SER-90 AND THR-163, 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-208 AND SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHSP26_YEAST
AccessioniPrimary (citable) accession number: P15992
Secondary accession number(s): D6VQ71, Q6B1V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 19300 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

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 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.