Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Peptidyl-prolyl cis-trans isomerase FKBP1A  

UniProtKB / Swiss-Prot ID :  FKB1A_HUMAN

Gene Name (Synonyms) : 
FKBP1A, FKBP1, FKBP12  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein 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. 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. 

Protein Sequence MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVG...
Predicted Secondary Structure CCEEEEEEEECCCCCCCCCCCEEEEEEEEEECCCEEEECCCCCCCCEEEEECCCCCCHHHHHHHHCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
9PhosphoserineVETISPGDG
EEEEEECCC
30.19HPRD
Link
9PhosphoserineVETISPGDG
EEEEEECCC
30.19Phosphositeplus
Link
9Phosphoserine.VETISPGDG
EEEEEECCC
30.19UniProtKB
Link
53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FMLGKQEVI
EEECCCCCC
39.05Phosphositeplus
Link
53N6-acetyllysineFMLGKQEVI
EEECCCCCC
39.05HPRD
Link
53N6-acetyllysine.FMLGKQEVI
EEECCCCCC
39.05UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TGFR1_HUMANphysical interactionDIP:10978EDIP10025408
PP2BA_HUMANin vitroHPRD:01741HPRD7543369
DYR_HUMANin vitroHPRD:01741HPRD12812497
ITPR1_HUMANyeast 2-hybridHPRD:01741HPRD9346894
RYR1_HUMANin vitroHPRD:01741HPRD11237759
11171121
11279144
12704193
RYR3_HUMANin vitro
in vivo
HPRD:01741HPRD11171121
11598113
FRAP_HUMANin vitroHPRD:01741HPRD8662507
FKB1A_HUMANin vitroHPRD:01741HPRD8662507
11438723
10852943
9871618
9346894
8521476
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00337Pimecrolimus
DB00877Sirolimus
DB00864Tacrolimus
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures