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Protein

Heat shock protein 42

Gene

HSP42

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. unfolded protein binding Source: SGD

GO - Biological processi

  1. cytoskeleton organization Source: SGD
Complete GO annotation...

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 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR171w.
EuPathDBiFungiDB:YDR171W.
SGDiS000002578. HSP42.

Subcellular locationi

GO - Cellular componenti

  1. cytoskeleton Source: SGD
Complete GO annotation...

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. 71 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.
InParanoidiQ12329.
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

        10         20         30         40         50
MSFYQPSLSL YDVLNALSNQ TGQRGQQGYP RQPQRPQRYH PHYGQVHVGG
60 70 80 90 100
HHPRHHPLYS RYNGVPNTYY YQFPGQAYYY SPEYGYDDED GEEEDQDEDM
110 120 130 140 150
VGDSGTTRQE DGGEDSNSRR YPSYYHCNTA RNNRTNQQAN SLNDLLTALI
160 170 180 190 200
GVPPYEGTEP EIEANTEQEG EKGEEKDKKD KSEAPKEEAG ETNKEKPLNQ
210 220 230 240 250
LEESSRPPLA KKSSSFAHLQ APSPIPDPLQ VSKPETRMDL PFSPEVNVYD
260 270 280 290 300
TEDTYVVVLA LPGANSRAFH IDYHPSSHEM LIKGKIEDRV GIDEKFLKIT
310 320 330 340 350
ELKYGAFERT VKFPVLPRIK DEEIKATYNN GLLQIKVPKI VNDTEKPKPK
360 370
KRIAIEEIPD EELEFEENPN PTVEN
Length:375
Mass (Da):42,817
Last modified:November 1, 1997 - v1
Checksum:iDF353A76493E3CE6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi32224. 71 interactions.
DIPiDIP-2515N.
IntActiQ12329. 50 interactions.
MINTiMINT-626187.
STRINGi4932.YDR171W.

Proteomic databases

MaxQBiQ12329.
PaxDbiQ12329.
PeptideAtlasiQ12329.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYDR171w.
EuPathDBiFungiDB:YDR171W.
SGDiS000002578. HSP42.

Phylogenomic databases

eggNOGiCOG0071.
HOGENOMiHOG000065948.
InParanoidiQ12329.
KOiK13993.
OMAiLEFEENP.
OrthoDBiEOG7PK992.

Enzyme and pathway databases

BioCyciYEAST:G3O-29760-MONOMER.

Miscellaneous databases

NextBioi969507.
PROiQ12329.

Gene expression databases

GenevestigatoriQ12329.

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. "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: April 29, 2015
This is version 128 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

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.