DP00015: cAMP-dependent protein kinase inhibitor alphaFASTA viewXML view

General information
DisProt:DP00015
Name:cAMP-dependent protein kinase inhibitor alpha
Synonym(s):IPKA_RABIT
cAMP-dependent protein kinase inhibitor, muscle/brain isoform
PKI-alpha
First appeared in release:Release 2.0 (02/14/2005)
UniProt:P61926
UniGene: 
SwissProt: IPKA_RABIT
TrEMBL:  
NCBI (GI): 48428971
Source organism:Oryctolagus cuniculus (Rabbit)
Sequence length:76
Percent disordered:99%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MTDVETTYAD FIASGRTGRR NAIHDILVSS ASGNSNELAL KLAGLDINKT EGEEDAQRSS - 60
TEQSGEAQGE AAKSES



Functional narrative    

Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.

Region 1: 1-75

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 - 75
Length:75
Region sequence:

MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSS
TEQSGEAQGEAAKSE

Modification type: Native
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses: Phosphorylation
Substrate/ligand binding
Protein inhibitor
Detection methods:
  1. Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (pH: 7; Mattson Alpha Centaun (spectrometer); Perkin-Elmer (solution cell); protein (sample) 4.69 mg/mL; resolution 4 1/m; sodium phosphate 10 mM; teflon spacer 0.05 mm)

  2. Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7; bandwidth 1 nm; Jasca 40CS (spectropolarimeter); path length cell (Hellma) 0.01 mm; protein (sample) 4.69 mg/mL; sensitivity 5 m/cm; sodium phosphate (buffer) 10 mM)

References:
  1. Knighton DR, Zheng JH, Ten Eyck LF, Xuong NH, Taylor SS, Sowadski JM. "Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase." Science. 1991; 253(5018): 414-20. PubMed: 1862343

  2. Thomas J, Van Patten SM, Howard P, Day KH, Mitchell RD, Sosnick T, Trewhella J, Walsh DA, Maurer RA. "Expression in Escherichia coli and characterization of the heat-stable inhibitor of the cAMP-dependent protein kinase." J Biol Chem. 1991; 266(17): 10906-11. PubMed: 2040607

Comments:
 



References

  1. Knighton DR, Zheng JH, Ten Eyck LF, Xuong NH, Taylor SS, Sowadski JM. "Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase." Science. 1991; 253(5018): 414-20. PubMed: 1862343

  2. Thomas J, Van Patten SM, Howard P, Day KH, Mitchell RD, Sosnick T, Trewhella J, Walsh DA, Maurer RA. "Expression in Escherichia coli and characterization of the heat-stable inhibitor of the cAMP-dependent protein kinase." J Biol Chem. 1991; 266(17): 10906-11. PubMed: 2040607



Comments


Sent for AV (6-15-2010) PubMed: 2040607


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