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Peptidyl-prolyl cis-trans isomerase FKBP1A (PPIase FKBP1A) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FKBP-12) (Calstabin-1) (FK506-binding protein 1A) (FKBP-1A) (Immunophilin FKBP12) (Rotamase)

 FKB1A_HUMAN             Reviewed;         108 AA.
P62942; D3DVW6; P20071; Q4VC47; Q6FGD9; Q6LEU3; Q9H103; Q9H566;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-JUL-2017, entry version 149.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A;
Short=PPIase FKBP1A;
EC=5.2.1.8 {ECO:0000269|PubMed:1696686, ECO:0000269|PubMed:1701173};
AltName: Full=12 kDa FK506-binding protein;
Short=12 kDa FKBP;
Short=FKBP-12;
AltName: Full=Calstabin-1;
AltName: Full=FK506-binding protein 1A;
Short=FKBP-1A;
AltName: Full=Immunophilin FKBP12;
AltName: Full=Rotamase;
Name=FKBP1A; Synonyms=FKBP1, FKBP12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1695378; DOI=10.1073/pnas.87.14.5440;
Maki N., Sekiguchi F., Nishimaki J., Miwa K., Hayano T., Takahashi N.,
Suzuki M.;
"Complementary DNA encoding the human T-cell FK506-binding protein, a
peptidylprolyl cis-trans isomerase distinct from cyclophilin.";
Proc. Natl. Acad. Sci. U.S.A. 87:5440-5443(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=1696686; DOI=10.1038/346671a0;
Standaert R.F., Galat A., Verdine G.L., Schreiber S.L.;
"Molecular cloning and overexpression of the human FK506-binding
protein FKBP.";
Nature 346:671-674(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1716149; DOI=10.1021/bi00099a002;
Dilella A.G., Craig R.J.;
"Exon organization of the human FKBP-12 gene: correlation with
structural and functional protein domains.";
Biochemistry 30:8512-8517(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Placenta;
PubMed=7529739; DOI=10.1016/0378-1119(94)90434-0;
Peattie D.A., Hsiao K., Benasutti M., Lippke J.A.;
"Three distinct messenger RNAs can encode the human immunosuppressant-
binding protein FKBP12.";
Gene 150:251-257(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 2-52, FUNCTION, CATALYTIC ACTIVITY, AND
SUBCELLULAR LOCATION.
PubMed=1701173;
Siekierka J.J., Widerrecht G., Greulich H., Boulton D., Hung S.H.Y.,
Cryan J., Hodges P.J., Sigal N.H.;
"The cytosolic-binding protein for the immunosuppressant FK-506 is
both a ubiquitous and highly conserved peptidyl-prolyl cis-trans
isomerase.";
J. Biol. Chem. 265:21011-21015(1990).
[11]
PROTEIN SEQUENCE OF 2-17.
PubMed=2477715; DOI=10.1038/341758a0;
Harding M.W., Galat A., Uehling D.E., Schreiber S.L.;
"A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-
prolyl isomerase.";
Nature 341:758-760(1989).
[12]
PROTEIN SEQUENCE OF 2-14.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[13]
FUNCTION IN TGFBR1 INHIBITION, AND INTERACTION WITH TGFBR1.
PubMed=9233797; DOI=10.1093/emboj/16.13.3866;
Chen Y.G., Liu F., Massague J.;
"Mechanism of TGFbeta receptor inhibition by FKBP12.";
EMBO J. 16:3866-3876(1997).
[14]
INTERACTION WITH RYR3.
PubMed=10358090; DOI=10.1074/jbc.274.24.17297;
Murayama T., Oba T., Katayama E., Oyamada H., Oguchi K., Kobayashi M.,
Otsuka K., Ogawa Y.;
"Further characterization of the type 3 ryanodine receptor (RyR3)
purified from rabbit diaphragm.";
J. Biol. Chem. 274:17297-17308(1999).
[15]
INTERACTION WITH ACVR1B AND SMAD7, AND FUNCTION.
PubMed=16720724; DOI=10.1677/jme.1.01966;
Yamaguchi T., Kurisaki A., Yamakawa N., Minakuchi K., Sugino H.;
"FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin
type I receptor.";
J. Mol. Endocrinol. 36:569-579(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
INTERACTION WITH RYR3.
PubMed=22100703; DOI=10.1016/j.abb.2011.11.004;
Wen H., Kang S., Song Y., Song Y., Yang H.J., Kim M.H., Park S.;
"Characterization of the binding sites for the interactions between
FKBP12 and intracellular calcium release channels.";
Arch. Biochem. Biophys. 517:37-42(2012).
[18]
STRUCTURE BY NMR.
PubMed=1709363; DOI=10.1021/bi00233a020;
Rosen M.K., Michnick S.W., Karplus M., Schreiber S.L.;
"Proton and nitrogen sequential assignments and secondary structure
determination of the human FK506 and rapamycin binding protein.";
Biochemistry 30:4774-4789(1991).
[19]
STRUCTURE BY NMR.
PubMed=1709301; DOI=10.1126/science.1709301;
Michnick S.W., Rosen M.K., Wandless T.J., Karplus M., Schreiber S.L.;
"Solution structure of FKBP, a rotamase enzyme and receptor for FK506
and rapamycin.";
Science 252:836-839(1991).
[20]
STRUCTURE BY NMR.
PubMed=1375171; DOI=10.1016/0014-5793(92)80292-O;
Lepre C.A., Thomson J.A., Moore J.M.;
"Solution structure of FK506 bound to FKBP-12.";
FEBS Lett. 302:89-96(1992).
[21]
STRUCTURE BY NMR OF COMPLEX WITH ASCOMYCIN.
PubMed=7682113; DOI=10.1002/bip.360330404;
Xu R.X., Nettesheim D., Olejniczak E.T., Meadows R., Gemmecker G.,
Fesik S.W.;
"1H, 13C, and 15N assignments and secondary structure of the FK506
binding protein when bound to ascomycin.";
Biopolymers 33:535-550(1993).
[22]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
PubMed=1709302; DOI=10.1126/science.1709302;
van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L.,
Clardy J.;
"Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant
complex.";
Science 252:839-842(1991).
[23]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
van Duyne G.D., Standaert R.F., Schreiber S.L., Clardy J.;
"Atomic structure of the rapamycin human immunophilin FKBP-12
complex.";
J. Am. Chem. Soc. 113:7433-7434(1991).
[24]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
PubMed=7678431; DOI=10.1006/jmbi.1993.1012;
van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L.,
Clardy J.;
"Atomic structures of the human immunophilin FKBP-12 complexes with
FK506 and rapamycin.";
J. Mol. Biol. 229:105-124(1993).
[25]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-107 IN COMPLEX WITH
TGFBR1.
PubMed=10025408; DOI=10.1016/S0092-8674(00)80555-3;
Huse M., Chen Y.-G., Massague J., Kuriyan J.;
"Crystal structure of the cytoplasmic domain of the type I TGF beta
receptor in complex with FKBP12.";
Cell 96:425-436(1999).
[26]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
PubMed=10656803; DOI=10.1006/jmbi.1999.3411;
Burkhard P., Taylor P., Walkinshaw M.D.;
"X-ray structures of small ligand-FKBP complexes provide an estimate
for hydrophobic interaction energies.";
J. Mol. Biol. 295:953-962(2000).
-!- 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.
{ECO:0000269|PubMed:16720724, ECO:0000269|PubMed:1696686,
ECO:0000269|PubMed:1701173, ECO:0000269|PubMed:9233797}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0). {ECO:0000269|PubMed:1696686,
ECO:0000269|PubMed:1701173}.
-!- ENZYME REGULATION: Inhibited by both FK506 and rapamycin.
-!- SUBUNIT: Interacts with TGFBR1; prevents TGFBR1 phosphorylation by
TGFBR2 and stabilizes it in the inactive conformation
(PubMed:9233797). Interacts with ACVR1B and SMAD7
(PubMed:16720724). Identified in a complex composed of RYR1,
PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) (By
similarity). Interacts directly with RYR2 and RYR3
(PubMed:10358090, PubMed:22100703). Interacts directly with RYR1
(By similarity). {ECO:0000250|UniProtKB:P26883,
ECO:0000250|UniProtKB:P62943, ECO:0000269|PubMed:10025408,
ECO:0000269|PubMed:10358090, ECO:0000269|PubMed:16720724,
ECO:0000269|PubMed:22100703, ECO:0000269|PubMed:9233797}.
-!- INTERACTION:
P36896:ACVR1B; NbExp=2; IntAct=EBI-1027571, EBI-1384128;
Q9NZD4:AHSP; NbExp=3; IntAct=EBI-1027571, EBI-720250;
P42345:MTOR; NbExp=2; IntAct=EBI-1027571, EBI-359260;
Q92736:RYR2; NbExp=2; IntAct=EBI-1027571, EBI-1170425;
O15105:SMAD7; NbExp=3; IntAct=EBI-1027571, EBI-3861591;
P36897:TGFBR1; NbExp=2; IntAct=EBI-1027571, EBI-1027557;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:1701173}. Sarcoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P62943}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P62943}; Cytoplasmic side
{ECO:0000250|UniProtKB:P62943}.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1
subfamily. {ECO:0000305}.
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EMBL; M34539; AAA35844.1; -; mRNA.
EMBL; M92423; AAA58476.1; -; Genomic_DNA.
EMBL; M92422; AAA58476.1; JOINED; Genomic_DNA.
EMBL; M93060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X55741; CAA39272.1; -; Genomic_DNA.
EMBL; M80199; AAA58472.1; -; Genomic_DNA.
EMBL; X52220; CAA36462.1; -; mRNA.
EMBL; BT007066; AAP35729.1; -; mRNA.
EMBL; CR407613; CAG28541.1; -; mRNA.
EMBL; CR542168; CAG46965.1; -; mRNA.
EMBL; AL136531; CAH72382.1; -; Genomic_DNA.
EMBL; AL109658; CAH72382.1; JOINED; Genomic_DNA.
EMBL; AL109658; CAI22728.1; -; Genomic_DNA.
EMBL; AL136531; CAI22728.1; JOINED; Genomic_DNA.
EMBL; CH471133; EAX10633.1; -; Genomic_DNA.
EMBL; CH471133; EAX10634.1; -; Genomic_DNA.
EMBL; CH471133; EAX10635.1; -; Genomic_DNA.
EMBL; BC001925; AAH01925.3; -; mRNA.
EMBL; BC005147; AAH05147.1; -; mRNA.
CCDS; CCDS13014.1; -.
PIR; I65284; A35780.
RefSeq; NP_000792.1; NM_000801.4.
RefSeq; NP_463460.1; NM_054014.3.
UniGene; Hs.471933; -.
UniGene; Hs.700839; -.
PDB; 1A7X; X-ray; 2.00 A; A/B=2-108.
PDB; 1B6C; X-ray; 2.60 A; A/C/E/G=2-108.
PDB; 1BKF; X-ray; 1.60 A; A=2-108.
PDB; 1BL4; X-ray; 1.90 A; A/B=2-108.
PDB; 1D6O; X-ray; 1.85 A; A/B=2-108.
PDB; 1D7H; X-ray; 1.90 A; A/B=2-108.
PDB; 1D7I; X-ray; 1.90 A; A/B=2-108.
PDB; 1D7J; X-ray; 1.85 A; A/B=2-108.
PDB; 1EYM; X-ray; 2.00 A; A/B=2-108.
PDB; 1F40; NMR; -; A=2-108.
PDB; 1FAP; X-ray; 2.70 A; A=2-108.
PDB; 1FKB; X-ray; 1.70 A; A=2-108.
PDB; 1FKD; X-ray; 1.72 A; A=2-108.
PDB; 1FKF; X-ray; 1.70 A; A=2-108.
PDB; 1FKG; X-ray; 2.00 A; A=2-108.
PDB; 1FKH; X-ray; 1.95 A; A=2-108.
PDB; 1FKI; X-ray; 2.20 A; A/B=2-108.
PDB; 1FKJ; X-ray; 1.70 A; A=2-108.
PDB; 1FKR; NMR; -; A=2-108.
PDB; 1FKS; NMR; -; A=2-108.
PDB; 1FKT; NMR; -; A=2-108.
PDB; 1J4H; X-ray; 1.80 A; A=2-108.
PDB; 1J4I; X-ray; 1.80 A; A=2-108.
PDB; 1J4R; X-ray; 1.80 A; A/B/D=2-108.
PDB; 1NSG; X-ray; 2.20 A; A=2-108.
PDB; 1QPF; X-ray; 2.50 A; A/D=2-108.
PDB; 1QPL; X-ray; 2.90 A; A/C=2-108.
PDB; 2DG3; X-ray; 1.70 A; A=2-108.
PDB; 2DG4; X-ray; 1.70 A; A=2-108.
PDB; 2DG9; X-ray; 1.70 A; A=2-108.
PDB; 2FAP; X-ray; 2.20 A; A=2-108.
PDB; 2FKE; X-ray; 1.72 A; A=2-108.
PDB; 2ND5; NMR; -; A=1-108.
PDB; 2PPN; X-ray; 0.92 A; A=2-108.
PDB; 2PPO; X-ray; 1.29 A; A=2-108.
PDB; 2PPP; X-ray; 0.94 A; A=2-108.
PDB; 2RSE; NMR; -; A=2-108.
PDB; 3FAP; X-ray; 1.85 A; A=2-108.
PDB; 3H9R; X-ray; 2.35 A; B=1-108.
PDB; 3MDY; X-ray; 2.05 A; B/D=1-108.
PDB; 4DH0; X-ray; 2.10 A; A=2-108.
PDB; 4FAP; X-ray; 2.80 A; A=2-108.
PDB; 4IPX; X-ray; 1.70 A; A=2-108.
PDB; 4N19; X-ray; 1.20 A; A=2-108.
PDB; 4ODP; X-ray; 1.75 A; A=85-97.
PDB; 4ODQ; X-ray; 2.00 A; A=85-97.
PDB; 4ODR; X-ray; 1.93 A; A/B=85-97.
PDB; 5I7P; X-ray; 2.00 A; A=2-84, A=98-108.
PDB; 5I7Q; X-ray; 1.90 A; A=2-84, A=97-108.
PDBsum; 1A7X; -.
PDBsum; 1B6C; -.
PDBsum; 1BKF; -.
PDBsum; 1BL4; -.
PDBsum; 1D6O; -.
PDBsum; 1D7H; -.
PDBsum; 1D7I; -.
PDBsum; 1D7J; -.
PDBsum; 1EYM; -.
PDBsum; 1F40; -.
PDBsum; 1FAP; -.
PDBsum; 1FKB; -.
PDBsum; 1FKD; -.
PDBsum; 1FKF; -.
PDBsum; 1FKG; -.
PDBsum; 1FKH; -.
PDBsum; 1FKI; -.
PDBsum; 1FKJ; -.
PDBsum; 1FKR; -.
PDBsum; 1FKS; -.
PDBsum; 1FKT; -.
PDBsum; 1J4H; -.
PDBsum; 1J4I; -.
PDBsum; 1J4R; -.
PDBsum; 1NSG; -.
PDBsum; 1QPF; -.
PDBsum; 1QPL; -.
PDBsum; 2DG3; -.
PDBsum; 2DG4; -.
PDBsum; 2DG9; -.
PDBsum; 2FAP; -.
PDBsum; 2FKE; -.
PDBsum; 2ND5; -.
PDBsum; 2PPN; -.
PDBsum; 2PPO; -.
PDBsum; 2PPP; -.
PDBsum; 2RSE; -.
PDBsum; 3FAP; -.
PDBsum; 3H9R; -.
PDBsum; 3MDY; -.
PDBsum; 4DH0; -.
PDBsum; 4FAP; -.
PDBsum; 4IPX; -.
PDBsum; 4N19; -.
PDBsum; 4ODP; -.
PDBsum; 4ODQ; -.
PDBsum; 4ODR; -.
PDBsum; 5I7P; -.
PDBsum; 5I7Q; -.
ProteinModelPortal; P62942; -.
SMR; P62942; -.
BioGrid; 108570; 62.
DIP; DIP-29710N; -.
IntAct; P62942; 15.
MINT; MINT-87893; -.
STRING; 9606.ENSP00000371138; -.
BindingDB; P62942; -.
ChEMBL; CHEMBL1902; -.
DrugBank; DB04094; 4-Hydroxy-2-Butanone.
DrugBank; DB02888; FKB-001.
DrugBank; DB01951; Gpi-1046.
DrugBank; DB05814; GPI-1485.
DrugBank; DB03338; Heptyl-Beta-D-Glucopyranoside.
DrugBank; DB02311; Methyl Methylsulfinylmethyl Sulfide.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB00337; Pimecrolimus.
DrugBank; DB00877; Sirolimus.
DrugBank; DB00864; Tacrolimus.
GuidetoPHARMACOLOGY; 2609; -.
iPTMnet; P62942; -.
PhosphoSitePlus; P62942; -.
BioMuta; FKBP1A; -.
EPD; P62942; -.
MaxQB; P62942; -.
PaxDb; P62942; -.
PeptideAtlas; P62942; -.
PRIDE; P62942; -.
TopDownProteomics; P62942; -.
DNASU; 2280; -.
Ensembl; ENST00000381719; ENSP00000371138; ENSG00000088832.
Ensembl; ENST00000400137; ENSP00000383003; ENSG00000088832.
GeneID; 2280; -.
KEGG; hsa:2280; -.
UCSC; uc002wey.4; human.
CTD; 2280; -.
DisGeNET; 2280; -.
GeneCards; FKBP1A; -.
GeneCards; MIR6869; -.
HGNC; HGNC:3711; FKBP1A.
HPA; CAB004639; -.
HPA; HPA051798; -.
HPA; HPA057830; -.
MIM; 186945; gene.
neXtProt; NX_P62942; -.
OpenTargets; ENSG00000088832; -.
PharmGKB; PA28153; -.
eggNOG; KOG0544; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00760000119159; -.
HOVERGEN; HBG051623; -.
InParanoid; P62942; -.
KO; K09568; -.
OMA; RVIAGWD; -.
PhylomeDB; P62942; -.
TreeFam; TF105291; -.
BRENDA; 5.2.1.8; 2681.
Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-HSA-3645790; TGFBR2 Kinase Domain Mutants in Cancer.
Reactome; R-HSA-3656532; TGFBR1 KD Mutants in Cancer.
Reactome; R-HSA-3656535; TGFBR1 LBD Mutants in Cancer.
SignaLink; P62942; -.
SIGNOR; P62942; -.
EvolutionaryTrace; P62942; -.
GeneWiki; FKBP1A; -.
GenomeRNAi; 2280; -.
PMAP-CutDB; P62942; -.
PRO; PR:P62942; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000088832; -.
CleanEx; HS_FKBP1A; -.
ExpressionAtlas; P62942; baseline and differential.
Genevisible; P62942; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0098562; C:cytoplasmic side of membrane; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031312; C:extrinsic component of organelle membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:1990425; C:ryanodine receptor complex; ISS:UniProtKB.
GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
GO; GO:0014802; C:terminal cisterna; ISS:BHF-UCL.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0048185; F:activin binding; IPI:BHF-UCL.
GO; GO:0005528; F:FK506 binding; IDA:BHF-UCL.
GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL.
GO; GO:0005527; F:macrolide binding; NAS:BHF-UCL.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL.
GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
GO; GO:0046332; F:SMAD binding; IPI:BHF-UCL.
GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:BHF-UCL.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISS:BHF-UCL.
GO; GO:0006458; P:'de novo' protein folding; TAS:BHF-UCL.
GO; GO:1990000; P:amyloid fibril formation; IDA:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; NAS:BHF-UCL.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0003007; P:heart morphogenesis; ISS:BHF-UCL.
GO; GO:0060347; P:heart trabecula formation; ISS:BHF-UCL.
GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:0006457; P:protein folding; NAS:UniProtKB.
GO; GO:0022417; P:protein maturation by protein folding; TAS:BHF-UCL.
GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:BHF-UCL.
GO; GO:0042026; P:protein refolding; TAS:BHF-UCL.
GO; GO:0032925; P:regulation of activin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; IGI:ParkinsonsUK-UCL.
GO; GO:0050776; P:regulation of immune response; IMP:BHF-UCL.
GO; GO:0032880; P:regulation of protein localization; IGI:ParkinsonsUK-UCL.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0007183; P:SMAD protein complex assembly; IDA:BHF-UCL.
GO; GO:0097435; P:supramolecular fiber organization; IDA:BHF-UCL.
GO; GO:0042110; P:T cell activation; NAS:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Isomerase; Membrane; Reference proteome;
Rotamase; Sarcoplasmic reticulum.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:1701173,
ECO:0000269|PubMed:2477715}.
CHAIN 2 108 Peptidyl-prolyl cis-trans isomerase
FKBP1A.
/FTId=PRO_0000075289.
DOMAIN 20 108 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
MOD_RES 53 53 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P26883}.
MOD_RES 53 53 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26883}.
CONFLICT 60 60 W -> R (in Ref. 6; CAG28541).
{ECO:0000305}.
CONFLICT 91 91 I -> V (in Ref. 6; CAG28541).
{ECO:0000305}.
STRAND 3 9 {ECO:0000244|PDB:2PPN}.
STRAND 22 31 {ECO:0000244|PDB:2PPN}.
STRAND 36 39 {ECO:0000244|PDB:2PPN}.
HELIX 40 43 {ECO:0000244|PDB:2PPN}.
STRAND 47 50 {ECO:0000244|PDB:2PPN}.
TURN 51 54 {ECO:0000244|PDB:2DG3}.
HELIX 58 64 {ECO:0000244|PDB:2PPN}.
STRAND 72 77 {ECO:0000244|PDB:2PPN}.
HELIX 79 81 {ECO:0000244|PDB:2PPN}.
TURN 82 86 {ECO:0000244|PDB:2PPN}.
TURN 89 91 {ECO:0000244|PDB:2PPN}.
STRAND 98 108 {ECO:0000244|PDB:2PPN}.
SEQUENCE 108 AA; 11951 MW; 9CC8493C802540B4 CRC64;
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFM LGKQEVIRGW
EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPHATLVF DVELLKLE


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