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FKBP1A

Gene
FKBP1A
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Bos taurus
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.91 kDa
Sequence
MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFVLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPNATLIFDVELLKLE

Gene
FKBP1A
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Homo sapiens
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.951 kDa
Sequence
MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE

Gene
Fkbp1a
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Mus musculus
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.923 kDa
Sequence
MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISSDYAYGATGHPGIIPPHATLVFDVELLKLE

Gene
FKBP1A
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Oryctolagus cuniculus
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.951 kDa
Sequence
MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE

Gene
Fkbp1a
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Rattus norvegicus
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.923 kDa
Sequence
MGVQVETISSGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISPDYAYGATGHPGIIPPHATLVFDVELLKLE

Gene
fkbp1a
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Xenopus laevis
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.912 kDa
Sequence
MGVQVETITEGDGRTFPKKGQTVVVHYVGSLENGKKFDSSRDRNKPFKFIIGRCEVIRGWEEGVAQMSVGQRARLTCSPDFAYGATGHPGIIPPNATLTFDVELLRLE

Gene
FKBP1A
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Bos taurus
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.91 kDa
Sequence
MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFVLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPNATLIFDVELLKLE

Gene
FKBP1A
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Homo sapiens
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.951 kDa
Sequence
MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE

Gene
Fkbp1a
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Mus musculus
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.923 kDa
Sequence
MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISSDYAYGATGHPGIIPPHATLVFDVELLKLE

Gene
FKBP1A
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Oryctolagus cuniculus
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.951 kDa
Sequence
MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE

Gene
Fkbp1a
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Rattus norvegicus
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.923 kDa
Sequence
MGVQVETISSGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISPDYAYGATGHPGIIPPHATLVFDVELLKLE

Gene
fkbp1a
Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Organism
Xenopus laevis
Length
108 amino acids
Function
Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Similarity
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Mass
11.912 kDa
Sequence
MGVQVETITEGDGRTFPKKGQTVVVHYVGSLENGKKFDSSRDRNKPFKFIIGRCEVIRGWEEGVAQMSVGQRARLTCSPDFAYGATGHPGIIPPNATLTFDVELLRLE