Annotations for this protein have been verified by the authors of the corresponding papers



DP00705: 12 kDa heat shock proteinFASTA viewXML view

General information
DisProt:DP00705
Name:12 kDa heat shock protein
Synonym(s):HSP12_YEAST
Glucose and lipid-regulated protein
First appeared in release:Release 5.6 (01/10/2011)
UniProt:P22943
UniGene: 
SwissProt: HSP12_YEAST
TrEMBL:  
NCBI (GI):  
Source organism:Saccharomyces cerevisiae (Baker\'s yeast)
Sequence length:109
Percent disordered:100%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MSDAGRKGFG EKASEALKPD SQKSYAEQGK EYITDKADKV AGKVQPEDNK GVFQGVHDSA - 60
EKGKDNAEGQ GESLADQARD YMGAAKSKLN DAVEYVSGRV HGEEDPTKK



Functional narrative    

Function: May play a role in a switch from carbohydrate utilizing metabolism to fatty acid utilizing metabolism. P31787:ACB1; NbExp=1; IntAct=EBI-8548, EBI-2060; P54113:ADE16; NbExp=1; IntAct=EBI-8548, EBI-14213; P54783:ALO1; NbExp=1; IntAct=EBI-8548, EBI-2519; P12962:CAF20; NbExp=1; IntAct=EBI-8548, EBI-9010; P14832:CPR1; NbExp=1; IntAct=EBI-8548, EBI-5463; P36156:ECM4; NbExp=1; IntAct=EBI-8548, EBI-2042717; Q07651:FMP45; NbExp=1; IntAct=EBI-8548, EBI-2051056; P33892:GCN1; NbExp=1; IntAct=EBI-8548, EBI-7442; Q05584:GLO2; NbExp=1; IntAct=EBI-8548, EBI-7672; Q07653:HBT1; NbExp=1; IntAct=EBI-8548, EBI-35419; Q6Q5K6:HUG1; NbExp=1; IntAct=EBI-8548, EBI-392766; P11986:INO1; NbExp=1; IntAct=EBI-8548, EBI-9257; P46673:NUP85; NbExp=1; IntAct=EBI-8548, EBI-12345; P10963:PCK1; NbExp=1; IntAct=EBI-8548, EBI-13770; P37012:PGM2; NbExp=1; IntAct=EBI-8548, EBI-13296; P21243:SCL1; NbExp=1; IntAct=EBI-8548, EBI-13975; P33338:SLA2; NbExp=1; IntAct=EBI-8548, EBI-17323; P33328:SNC2; NbExp=1; IntAct=EBI-8548, EBI-17512; P33315:TKL2; NbExp=1; IntAct=EBI-8548, EBI-19297; P28274:URA7; NbExp=1; IntAct=EBI-8548, EBI-20128; P41807:VMA13; NbExp=1; IntAct=EBI-8548, EBI-20281; P39111:VMA7; NbExp=1; IntAct=EBI-8548, EBI-20272; Q12402:YOP1; NbExp=1; IntAct=EBI-8548, EBI-37092;
INDUCTION: 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.
MISCELLANEOUS: Present with 4490 molecules/cell in log phase SD medium.
SIMILARITY: To S.pombe hsp9 and C.albicans WH11.
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Region 1: 1-7 Region 2: 8-18 Region 3: 19-23 Region 4: 24-43 Region 5: 44-73 Region 6: 74-98 Region 7: 99-109

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:1 - 7
Length:7
Region sequence:

MSDAGRK

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes:  
Functional subclasses: Protein-lipid interaction
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)

  2. Nuclear magnetic resonance (NMR) (310 K; pH: 7.5; Hsp12; SDS 300 mM; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts))

References:
  1. Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624

Comments:
 



Region 2
Type:Disordered w/ Residual Structure
Name:Helix 1
Location:8 - 18
Length:11
Region sequence:

GFGEKASEALK

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Protein-lipid interaction
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)

  2. Nuclear magnetic resonance (NMR) (310 K; pH: 7.5; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)

References:
  1. Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624

Comments:
 



Region 3
Type:Disordered
Name: 
Location:19 - 23
Length:5
Region sequence:

PDSQK

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes:  
Functional subclasses: Protein-lipid interaction
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)

  2. Nuclear magnetic resonance (NMR) (310 K; pH: 7.5; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)

References:
  1. Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624

Comments:
 



Region 4
Type:Disordered w/ Residual Structure
Name:Helix 2
Location:24 - 43
Length:20
Region sequence:

SYAEQGKEYITDKADKVAGK

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Protein-lipid interaction
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)

  2. Nuclear magnetic resonance (NMR) (310 K; pH: 7.5; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)

References:
  1. Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624

Comments:
 



Region 5
Type:Disordered
Name: 
Location:44 - 73
Length:30
Region sequence:

VQPEDNKGVFQGVHDSAEKGKDNAEGQGES

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes:  
Functional subclasses: Protein-lipid interaction
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (310 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)

  2. Nuclear magnetic resonance (NMR) (310 K; pH: 7.4; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)

References:
  1. Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624

Comments:
According to Welker et al (2010), Region 5 contains a predicted disorder-to-order helix (Helix 3) at aa 52-61.




Region 6
Type:Disordered w/ Residual Structure
Name:Helix 4
Location:74 - 98
Length:25
Region sequence:

LADQARDYMGAAKSKLNDAVEYVSG

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Protein-lipid interaction
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)

  2. Nuclear magnetic resonance (NMR) (310 K; pH: 7.5; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)

References:
  1. Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624

Comments:
 



Region 7
Type:Disordered
Name: 
Location:99 - 109
Length:11
Region sequence:

RVHGEEDPTKK

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes:  
Functional subclasses: Protein-lipid interaction
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)

  2. Nuclear magnetic resonance (NMR) (310 K; pH: 7.4; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)

References:
  1. Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624

Comments:
 



References

  1. Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624



Comments


AV 2/03/2011 (PubMed: 20797624)



Welker et al (2010) found that Hsp12 is a monomeric and fully disordered protein that gains structure when associating with negatively charged lipids. High concentrations of Hsp12 (such as in stress conditions) led to membrane association for the purpose of membrane stabilization.


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