UniProt Accession

 FKB1A_HUMAN; P62942; D3DVW6; P20071; Q4VC47; Q6FGD9; Q6LEU3; Q9H103; Q9H566 

Genbank Protein ID

 M34539; M92423; M92422; M93060; X55741; M80199; X52220; BT007066; CR407613; CR542168; AL136531; AL109658; AL109658; AL136531; CH471133; CH471133; CH471133; BC001925; BC005147 

Genbank Nucleotide ID

 AAA35844.1; AAA58476.1; AAA58476.1; CAA39272.1; AAA58472.1; CAA36462.1; AAP35729.1; CAG28541.1; CAG46965.1; CAH72382.1; CAH72382.1; CAI22728.1; CAI22728.1; EAX10633.1; EAX10634.1; EAX10635.1; AAH01925.3; AAH05147.1 

Protein Name

 Peptidyl-prolyl cis-trans isomerase FKBP1A 

Protein Synonyms/Alias

 PPIase FKBP1A; 12 kDa FK506-binding protein; 12 kDa FKBP; FKBP-12; Calstabin-1; FK506-binding protein 1A; FKBP-1A; Immunophilin FKBP12; Rotamase 

Gene Name

 FKBP1A 

Gene Synonyms/Alias

 FKBP1; FKBP12 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
35	TGMLEDGKKFDSSRD	ubiquitination	[1, 2, 3]
36	GMLEDGKKFDSSRDR	ubiquitination	[2, 3]
48	RDRNKPFKFMLGKQE	ubiquitination	[2, 4]
53	PFKFMLGKQEVIRGW	acetylation	[5]
53	PFKFMLGKQEVIRGW	ubiquitination	[2, 4]

Reference

 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 20 108 PPIase FKBP-type.
 MOD_RES 2 2 N-acetylglycine.
 MOD_RES 9 9 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Isomerase; Phosphoprotein; Reference proteome; Rotamase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 108 AA 

Protein Sequence

Gene Ontology

 GO:0030424; C:axon; IBA:RefGenome.
 GO:0005829; C:cytosol; IDA:BHF-UCL.
 GO:0033017; C:sarcoplasmic reticulum membrane; IBA:RefGenome.
 GO:0014802; C:terminal cisterna; ISS:BHF-UCL.
 GO:0005528; F:FK506 binding; IDA:BHF-UCL.
 GO:0044325; F:ion channel binding; ISS:BHF-UCL.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0034713; F:type I transforming growth factor beta receptor binding; ISS:BHF-UCL.
 GO:0006458; P:'de novo' protein folding; TAS:BHF-UCL.
 GO:0034205; P:beta-amyloid formation; IDA:BHF-UCL.
 GO:0043206; P:extracellular fibril organization; IDA:BHF-UCL.
 GO:0060347; P:heart trabecula formation; ISS:BHF-UCL.
 GO:0032513; P:negative regulation of protein phosphatase type 2B activity; IDA:BHF-UCL.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
 GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
 GO:0022417; P:protein maturation by protein folding; TAS:BHF-UCL.
 GO:0042026; P:protein refolding; TAS:BHF-UCL.
 GO:0032925; P:regulation of activin receptor signaling pathway; IDA:BHF-UCL.
 GO:0050776; P:regulation of immune response; IMP:BHF-UCL.
 GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
 GO:0007183; P:SMAD protein complex assembly; IDA:BHF-UCL.
 GO:0042110; P:T cell activation; NAS:BHF-UCL.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL. 

Interpro

 IPR023566; PPIase_FKBP.
 IPR001179; PPIase_FKBP_dom. 

Pfam

 PF00254; FKBP_C 

SMART

  

PROSITE

 PS50059; FKBP_PPIASE 

PRINTS