1. Heat shock protein HSP 90-beta

Pharmacological action: unknown

Molecular chaperone. Has ATPase activity

Organism class: human
UniProt ID: P08238
Gene: HSP90AB1
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report

References:

1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed

2. Endoplasmin

Pharmacological action: unknown

Molecular chaperone that functions in the processing and transport of secreted proteins

Organism class: human
UniProt ID: P14625
Gene: HSP90B1
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report

References:

1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed

3. Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Pharmacological action: unknown

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3)

Organism class: human
UniProt ID: P10515
Gene: DLAT
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report

References:

1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed

4. [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3, mitochondrial

Pharmacological action: unknown

Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism

Organism class: human
UniProt ID: Q15120
Gene: PDK3
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report

References:

1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed

5. Virulence sensor histidine kinase phoQ

Pharmacological action: unknown

Member of the two-component regulatory system phoQ/phoP which regulates the expression of genes involved in virulence, adaptation to low Mg(2+) environments and resistance to host defense antimicrobial peptides. In presence of low periplasmic Mg(2+) concentrations, phoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to phoP, which results in the expression of phoP-activated genes (PAG) and repression of phoP-repressed genes (PRG). In presence of high periplasmic Mg(2+) concentrations, acts as a protein phosphatase that dephosphorylates phospho-phoP, which results in the repression of phoP-activated genes and may lead to expression of some phoP- repressed genes. Promotes intramacrophage survival of S.typhimurium. Is essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system ssrB/spiR at transcriptional and post- transcriptional levels respectively. Promotes expression of the two-component regulatory system pmrA/pmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Also, negatively regulates prgH, which is required for invasion of epithelial cells

Organism class: bacterial
UniProt ID: P14147
Gene: phoQ
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report

References:

1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed