Search Results

Overview

Uniprot IDP62942
Protein NamePeptidyl-prolyl cis-trans isomerase FKBP1A
Gene NameFKBP1A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
53 PFKFMLGKQEVIRGW

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

Protein Sequence

10 MGVQVETISP 20 GDGRTFPKRG 30 QTCVVHYTGM 40 LEDGKKFDSS 50 RDRNKPFKFM 60 LGKQEVIRGW 70 EEGVAQMSVG 80 QRAKLTISPD 90 YAYGATGHPG 100 IIPPHATLVF DVELLKLE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0098562 cytoplasmic side of membrane
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016020 membrane
Cellular Component GO:1990425 ryanodine receptor complex
Cellular Component GO:0016529 sarcoplasmic reticulum
Cellular Component GO:0033017 sarcoplasmic reticulum membrane
Cellular Component GO:0014802 terminal cisterna
Cellular Component GO:0030018 Z disc
Molecular Function GO:0070697 activin receptor binding
Molecular Function GO:0005246 calcium channel regulator activity
Molecular Function GO:0005528 FK506 binding
Molecular Function GO:0070411 I-SMAD binding
Molecular Function GO:0005527 macrolide binding
Molecular Function GO:0003755 peptidyl-prolyl cis-trans isomerase activity
Molecular Function GO:0030547 signaling receptor inhibitor activity
Molecular Function GO:0005160 transforming growth factor beta receptor binding
Molecular Function GO:0044325 transmembrane transporter binding
Molecular Function GO:0034713 type I transforming growth factor beta receptor binding
Biological Process GO:0006458 'de novo' protein folding
Biological Process GO:1990000 amyloid fibril formation
Biological Process GO:0003007 heart morphogenesis
Biological Process GO:0060347 heart trabecula formation
Biological Process GO:0032926 negative regulation of activin receptor signaling pathway
Biological Process GO:0030512 negative regulation of transforming growth factor beta receptor signaling pathway
Biological Process GO:0043123 positive regulation of canonical NF-kappaB signal transduction
Biological Process GO:0006457 protein folding
Biological Process GO:0051604 protein maturation
Biological Process GO:0042026 protein refolding
Biological Process GO:1902991 regulation of amyloid precursor protein catabolic process
Biological Process GO:0010881 regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
Biological Process GO:0050776 regulation of immune response
Biological Process GO:0032880 regulation of protein localization
Biological Process GO:0014809 regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
Biological Process GO:0097435 supramolecular fiber organization
Biological Process GO:0042110 T cell activation
Biological Process GO:0055010 ventricular cardiac muscle tissue morphogenesis

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.