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Protein

12 kDa heat shock protein

Gene

HSP12

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

May play a role in a switch from carbohydrate utilizing metabolism to fatty acid utilizing metabolism.

GO - Molecular functioni

  • lipid binding Source: SGD

GO - Biological processi

  • cell adhesion Source: SGD
  • cellular response to heat Source: SGD
  • cellular response to osmotic stress Source: SGD
  • cellular response to oxidative stress Source: SGD
  • plasma membrane organization Source: SGD
Complete GO annotation...

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciYEAST:G3O-30442-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
12 kDa heat shock protein
Alternative name(s):
Glucose and lipid-regulated protein
Gene namesi
Name:HSP12
Synonyms:GLP1, HOR5
Ordered Locus Names:YFL014W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFL014W.
SGDiS000001880. HSP12.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • endosome Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10910912 kDa heat shock proteinPRO_0000084081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine; by ATM or ATRCombined sources
Modified residuei24 – 241PhosphoserineCombined sources
Modified residuei59 – 591PhosphoserineCombined sources
Modified residuei73 – 731PhosphoserineCombined sources
Modified residuei97 – 971PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP22943.
PRIDEiP22943.
TopDownProteomicsiP22943.

PTM databases

iPTMnetiP22943.

Expressioni

Inductioni

Strong, by heat shock, by entry in the stationary growth phase, and by cAMP, probably via the activity of a cAMP-dependent protein kinase. By glucose starvation and by fatty acids.

Interactioni

Protein-protein interaction databases

BioGridi31132. 31 interactions.
DIPiDIP-6408N.
IntActiP22943. 1 interaction.
MINTiMINT-700216.

Structurei

Secondary structure

1
109
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 1710Combined sources
Helixi25 – 4218Combined sources
Helixi53 – 564Combined sources
Helixi58 – 614Combined sources
Beta strandi62 – 643Combined sources
Beta strandi71 – 733Combined sources
Helixi74 – 10027Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L9QNMR-A1-109[»]
2LJLNMR-A1-109[»]
4AXPNMR-A1-109[»]
DisProtiDP00705.
ProteinModelPortaliP22943.
SMRiP22943. Positions 1-109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

To S.pombe hsp9 and C.albicans WH11.Curated

Phylogenomic databases

HOGENOMiHOG000202995.
InParanoidiP22943.
OMAiPDSQKSY.
OrthoDBiEOG092C0XHN.

Family and domain databases

InterProiIPR016360. Heat_shock_protein_9/12_fun.
IPR007250. HSP9_HSP12.
[Graphical view]
PfamiPF04119. HSP9_HSP12. 1 hit.
[Graphical view]
PIRSFiPIRSF002590. HSP9/HSP12_fun. 1 hit.

Sequencei

Sequence statusi: Complete.

P22943-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDAGRKGFG EKASEALKPD SQKSYAEQGK EYITDKADKV AGKVQPEDNK
60 70 80 90 100
GVFQGVHDSA EKGKDNAEGQ GESLADQARD YMGAAKSKLN DAVEYVSGRV

HGEEDPTKK
Length:109
Mass (Da):11,693
Last modified:August 1, 1991 - v1
Checksum:i7C73862689759B4A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461P → T in strain: Ar5-H12.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60827 Genomic DNA. Translation: AAA34647.1.
X55785 mRNA. Translation: CAA39306.1.
Z46255 Genomic DNA. Translation: CAA86349.1.
D50617 Genomic DNA. Translation: BAA09224.1.
D89864 Genomic DNA. Translation: BAA14033.1.
AY046957 Genomic DNA. Translation: AAL06077.1.
AY558464 Genomic DNA. Translation: AAS56790.1.
BK006940 Genomic DNA. Translation: DAA12425.1.
PIRiS11179. HHBY12.
RefSeqiNP_116640.1. NM_001179952.1.

Genome annotation databases

EnsemblFungiiBAA09224; BAA09224; BAA09224.
YFL014W; YFL014W; YFL014W.
GeneIDi850532.
KEGGisce:YFL014W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60827 Genomic DNA. Translation: AAA34647.1.
X55785 mRNA. Translation: CAA39306.1.
Z46255 Genomic DNA. Translation: CAA86349.1.
D50617 Genomic DNA. Translation: BAA09224.1.
D89864 Genomic DNA. Translation: BAA14033.1.
AY046957 Genomic DNA. Translation: AAL06077.1.
AY558464 Genomic DNA. Translation: AAS56790.1.
BK006940 Genomic DNA. Translation: DAA12425.1.
PIRiS11179. HHBY12.
RefSeqiNP_116640.1. NM_001179952.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L9QNMR-A1-109[»]
2LJLNMR-A1-109[»]
4AXPNMR-A1-109[»]
DisProtiDP00705.
ProteinModelPortaliP22943.
SMRiP22943. Positions 1-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31132. 31 interactions.
DIPiDIP-6408N.
IntActiP22943. 1 interaction.
MINTiMINT-700216.

PTM databases

iPTMnetiP22943.

Proteomic databases

MaxQBiP22943.
PRIDEiP22943.
TopDownProteomicsiP22943.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09224; BAA09224; BAA09224.
YFL014W; YFL014W; YFL014W.
GeneIDi850532.
KEGGisce:YFL014W.

Organism-specific databases

EuPathDBiFungiDB:YFL014W.
SGDiS000001880. HSP12.

Phylogenomic databases

HOGENOMiHOG000202995.
InParanoidiP22943.
OMAiPDSQKSY.
OrthoDBiEOG092C0XHN.

Enzyme and pathway databases

BioCyciYEAST:G3O-30442-MONOMER.

Miscellaneous databases

PROiP22943.

Family and domain databases

InterProiIPR016360. Heat_shock_protein_9/12_fun.
IPR007250. HSP9_HSP12.
[Graphical view]
PfamiPF04119. HSP9_HSP12. 1 hit.
[Graphical view]
PIRSFiPIRSF002590. HSP9/HSP12_fun. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHSP12_YEAST
AccessioniPrimary (citable) accession number: P22943
Secondary accession number(s): D6VTL5, Q8X145
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: September 7, 2016
This is version 152 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 4490 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: 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.