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MGP001083

UniProt Annotations

Entry Information
Gene NameFK506 binding protein 1A, 12kDa
Protein Entry
UniProt ID
SpeciesHuman
Comments
Comment typeDescription
Catalytic ActivityPeptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme RegulationInhibited by both FK506 and rapamycin.
FunctionKeeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites 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. {ECO:0000269|PubMed:16720724, ECO:0000269|PubMed:9233797}.
InteractionP36896:ACVR1B; NbExp=2; IntAct=EBI-1027571, EBI-1384128; P42345:MTOR; NbExp=2; IntAct=EBI-1027571, EBI-359260; O15105:SMAD7; NbExp=3; IntAct=EBI-1027571, EBI-3861591; P36897:TGFBR1; NbExp=2; IntAct=EBI-1027571, EBI-1027557;
SimilarityBelongs to the FKBP-type PPIase family. FKBP1 subfamily. {ECO:0000305}.
SimilarityContains 1 PPIase FKBP-type domain. {ECO:0000255|PROSITE-ProRule:PRU00277}.
Subcellular LocationCytoplasm.
SubunitInteracts directly with RYR1, RYR2 and RYR3. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) (By similarity). Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with ACVR1B and SMAD7. {ECO:0000250, ECO:0000269|PubMed:10025408, ECO:0000269|PubMed:10358090, ECO:0000269|PubMed:16720724, ECO:0000269|PubMed:22100703, ECO:0000269|PubMed:9233797}.
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