GenomeNet

Database: UniProt
Entry: P62942
LinkDB: P62942
Original site: P62942 
ID   FKB1A_HUMAN             Reviewed;         108 AA.
AC   P62942; D3DVW6; P20071; Q4VC47; Q6FGD9; Q6LEU3; Q9H103; Q9H566;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-DEC-2019, entry version 172.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A;
DE            Short=PPIase FKBP1A;
DE            EC=5.2.1.8 {ECO:0000269|PubMed:1696686, ECO:0000269|PubMed:1701173};
DE   AltName: Full=12 kDa FK506-binding protein;
DE            Short=12 kDa FKBP;
DE            Short=FKBP-12;
DE   AltName: Full=Calstabin-1;
DE   AltName: Full=FK506-binding protein 1A;
DE            Short=FKBP-1A;
DE   AltName: Full=Immunophilin FKBP12;
DE   AltName: Full=Rotamase;
GN   Name=FKBP1A; Synonyms=FKBP1, FKBP12;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1695378; DOI=10.1073/pnas.87.14.5440;
RA   Maki N., Sekiguchi F., Nishimaki J., Miwa K., Hayano T., Takahashi N.,
RA   Suzuki M.;
RT   "Complementary DNA encoding the human T-cell FK506-binding protein, a
RT   peptidylprolyl cis-trans isomerase distinct from cyclophilin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5440-5443(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=1696686; DOI=10.1038/346671a0;
RA   Standaert R.F., Galat A., Verdine G.L., Schreiber S.L.;
RT   "Molecular cloning and overexpression of the human FK506-binding protein
RT   FKBP.";
RL   Nature 346:671-674(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1716149; DOI=10.1021/bi00099a002;
RA   Dilella A.G., Craig R.J.;
RT   "Exon organization of the human FKBP-12 gene: correlation with structural
RT   and functional protein domains.";
RL   Biochemistry 30:8512-8517(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Placenta;
RX   PubMed=7529739; DOI=10.1016/0378-1119(94)90434-0;
RA   Peattie D.A., Hsiao K., Benasutti M., Lippke J.A.;
RT   "Three distinct messenger RNAs can encode the human immunosuppressant-
RT   binding protein FKBP12.";
RL   Gene 150:251-257(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-52, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=1701173;
RA   Siekierka J.J., Widerrecht G., Greulich H., Boulton D., Hung S.H.Y.,
RA   Cryan J., Hodges P.J., Sigal N.H.;
RT   "The cytosolic-binding protein for the immunosuppressant FK-506 is both a
RT   ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase.";
RL   J. Biol. Chem. 265:21011-21015(1990).
RN   [11]
RP   PROTEIN SEQUENCE OF 2-17.
RX   PubMed=2477715; DOI=10.1038/341758a0;
RA   Harding M.W., Galat A., Uehling D.E., Schreiber S.L.;
RT   "A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl
RT   isomerase.";
RL   Nature 341:758-760(1989).
RN   [12]
RP   PROTEIN SEQUENCE OF 2-14.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [13]
RP   INTERACTION WITH GLMN.
RX   PubMed=8955134; DOI=10.1074/jbc.271.51.32923;
RA   Chambraud B., Radanyi C., Camonis J.H., Shazand K., Rajkowski K.,
RA   Baulieu E.-E.;
RT   "FAP48, a new protein that forms specific complexes with both immunophilins
RT   FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and
RT   rapamycin.";
RL   J. Biol. Chem. 271:32923-32929(1996).
RN   [14]
RP   FUNCTION IN TGFBR1 INHIBITION, AND INTERACTION WITH TGFBR1.
RX   PubMed=9233797; DOI=10.1093/emboj/16.13.3866;
RA   Chen Y.G., Liu F., Massague J.;
RT   "Mechanism of TGFbeta receptor inhibition by FKBP12.";
RL   EMBO J. 16:3866-3876(1997).
RN   [15]
RP   INTERACTION WITH RYR3.
RX   PubMed=10358090; DOI=10.1074/jbc.274.24.17297;
RA   Murayama T., Oba T., Katayama E., Oyamada H., Oguchi K., Kobayashi M.,
RA   Otsuka K., Ogawa Y.;
RT   "Further characterization of the type 3 ryanodine receptor (RyR3) purified
RT   from rabbit diaphragm.";
RL   J. Biol. Chem. 274:17297-17308(1999).
RN   [16]
RP   INTERACTION WITH ACVR1B AND SMAD7, AND FUNCTION.
RX   PubMed=16720724; DOI=10.1677/jme.1.01966;
RA   Yamaguchi T., Kurisaki A., Yamakawa N., Minakuchi K., Sugino H.;
RT   "FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type
RT   I receptor.";
RL   J. Mol. Endocrinol. 36:569-579(2006).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [18]
RP   INTERACTION WITH RYR3.
RX   PubMed=22100703; DOI=10.1016/j.abb.2011.11.004;
RA   Wen H., Kang S., Song Y., Song Y., Yang H.J., Kim M.H., Park S.;
RT   "Characterization of the binding sites for the interactions between FKBP12
RT   and intracellular calcium release channels.";
RL   Arch. Biochem. Biophys. 517:37-42(2012).
RN   [19]
RP   STRUCTURE BY NMR.
RX   PubMed=1709363; DOI=10.1021/bi00233a020;
RA   Rosen M.K., Michnick S.W., Karplus M., Schreiber S.L.;
RT   "Proton and nitrogen sequential assignments and secondary structure
RT   determination of the human FK506 and rapamycin binding protein.";
RL   Biochemistry 30:4774-4789(1991).
RN   [20]
RP   STRUCTURE BY NMR.
RX   PubMed=1709301; DOI=10.1126/science.1709301;
RA   Michnick S.W., Rosen M.K., Wandless T.J., Karplus M., Schreiber S.L.;
RT   "Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and
RT   rapamycin.";
RL   Science 252:836-839(1991).
RN   [21]
RP   STRUCTURE BY NMR.
RX   PubMed=1375171; DOI=10.1016/0014-5793(92)80292-o;
RA   Lepre C.A., Thomson J.A., Moore J.M.;
RT   "Solution structure of FK506 bound to FKBP-12.";
RL   FEBS Lett. 302:89-96(1992).
RN   [22]
RP   STRUCTURE BY NMR OF COMPLEX WITH ASCOMYCIN.
RX   PubMed=7682113; DOI=10.1002/bip.360330404;
RA   Xu R.X., Nettesheim D., Olejniczak E.T., Meadows R., Gemmecker G.,
RA   Fesik S.W.;
RT   "1H, 13C, and 15N assignments and secondary structure of the FK506 binding
RT   protein when bound to ascomycin.";
RL   Biopolymers 33:535-550(1993).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=1709302; DOI=10.1126/science.1709302;
RA   van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J.;
RT   "Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant
RT   complex.";
RL   Science 252:839-842(1991).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RA   van Duyne G.D., Standaert R.F., Schreiber S.L., Clardy J.;
RT   "Atomic structure of the rapamycin human immunophilin FKBP-12 complex.";
RL   J. Am. Chem. Soc. 113:7433-7434(1991).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX   PubMed=7678431; DOI=10.1006/jmbi.1993.1012;
RA   van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J.;
RT   "Atomic structures of the human immunophilin FKBP-12 complexes with FK506
RT   and rapamycin.";
RL   J. Mol. Biol. 229:105-124(1993).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-107 IN COMPLEX WITH TGFBR1.
RX   PubMed=10025408; DOI=10.1016/s0092-8674(00)80555-3;
RA   Huse M., Chen Y.-G., Massague J., Kuriyan J.;
RT   "Crystal structure of the cytoplasmic domain of the type I TGF beta
RT   receptor in complex with FKBP12.";
RL   Cell 96:425-436(1999).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX   PubMed=10656803; DOI=10.1006/jmbi.1999.3411;
RA   Burkhard P., Taylor P., Walkinshaw M.D.;
RT   "X-ray structures of small ligand-FKBP complexes provide an estimate for
RT   hydrophobic interaction energies.";
RL   J. Mol. Biol. 295:953-962(2000).
CC   -!- FUNCTION: Keeps in an inactive conformation TGFBR1, the TGF-beta type I
CC       serine/threonine kinase receptor, preventing TGF-beta receptor
CC       activation in absence of ligand. Recruits SMAD7 to ACVR1B which
CC       prevents the association of SMAD2 and SMAD3 with the activin receptor
CC       complex, thereby blocking the activin signal. May modulate the RYR1
CC       calcium channel activity. PPIases accelerate the folding of proteins.
CC       It catalyzes the cis-trans isomerization of proline imidic peptide
CC       bonds in oligopeptides. {ECO:0000269|PubMed:16720724,
CC       ECO:0000269|PubMed:1696686, ECO:0000269|PubMed:1701173,
CC       ECO:0000269|PubMed:9233797}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:1696686,
CC         ECO:0000269|PubMed:1701173};
CC   -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC   -!- SUBUNIT: Interacts with TGFBR1; prevents TGFBR1 phosphorylation by
CC       TGFBR2 and stabilizes it in the inactive conformation (PubMed:9233797).
CC       Interacts with ACVR1B and SMAD7 (PubMed:16720724). Identified in a
CC       complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1
CC       (PP1) (By similarity). Interacts directly with RYR2 and RYR3
CC       (PubMed:10358090, PubMed:22100703). Interacts with GLMN; rapamycin and
CC       FK506 abolish the interaction with GLMN in a dose dependent manner
CC       (PubMed:8955134). Interacts directly with RYR1 (By similarity).
CC       {ECO:0000250|UniProtKB:P26883, ECO:0000250|UniProtKB:P62943,
CC       ECO:0000269|PubMed:10025408, ECO:0000269|PubMed:10358090,
CC       ECO:0000269|PubMed:16720724, ECO:0000269|PubMed:22100703,
CC       ECO:0000269|PubMed:8955134, ECO:0000269|PubMed:9233797}.
CC   -!- INTERACTION:
CC       P36896:ACVR1B; NbExp=2; IntAct=EBI-1027571, EBI-1384128;
CC       Q9NZD4:AHSP; NbExp=3; IntAct=EBI-1027571, EBI-720250;
CC       P42345:MTOR; NbExp=5; IntAct=EBI-1027571, EBI-359260;
CC       P11716:RYR1 (xeno); NbExp=2; IntAct=EBI-1027571, EBI-6477441;
CC       Q92736:RYR2; NbExp=2; IntAct=EBI-1027571, EBI-1170425;
CC       O15105:SMAD7; NbExp=3; IntAct=EBI-1027571, EBI-3861591;
CC       P36897:TGFBR1; NbExp=2; IntAct=EBI-1027571, EBI-1027557;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1701173}.
CC       Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P62943};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P62943}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:P62943}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC       {ECO:0000305}.
DR   EMBL; M34539; AAA35844.1; -; mRNA.
DR   EMBL; M92423; AAA58476.1; -; Genomic_DNA.
DR   EMBL; M92422; AAA58476.1; JOINED; Genomic_DNA.
DR   EMBL; M93060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X55741; CAA39272.1; -; Genomic_DNA.
DR   EMBL; M80199; AAA58472.1; -; Genomic_DNA.
DR   EMBL; X52220; CAA36462.1; -; mRNA.
DR   EMBL; BT007066; AAP35729.1; -; mRNA.
DR   EMBL; CR407613; CAG28541.1; -; mRNA.
DR   EMBL; CR542168; CAG46965.1; -; mRNA.
DR   EMBL; AL136531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL109658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471133; EAX10633.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10634.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10635.1; -; Genomic_DNA.
DR   EMBL; BC001925; AAH01925.3; -; mRNA.
DR   EMBL; BC005147; AAH05147.1; -; mRNA.
DR   CCDS; CCDS13014.1; -.
DR   PIR; I65284; A35780.
DR   RefSeq; NP_000792.1; NM_000801.4.
DR   RefSeq; NP_463460.1; NM_054014.3.
DR   PDB; 1A7X; X-ray; 2.00 A; A/B=2-108.
DR   PDB; 1B6C; X-ray; 2.60 A; A/C/E/G=2-108.
DR   PDB; 1BKF; X-ray; 1.60 A; A=2-108.
DR   PDB; 1BL4; X-ray; 1.90 A; A/B=2-108.
DR   PDB; 1D6O; X-ray; 1.85 A; A/B=2-108.
DR   PDB; 1D7H; X-ray; 1.90 A; A/B=2-108.
DR   PDB; 1D7I; X-ray; 1.90 A; A/B=2-108.
DR   PDB; 1D7J; X-ray; 1.85 A; A/B=2-108.
DR   PDB; 1EYM; X-ray; 2.00 A; A/B=2-108.
DR   PDB; 1F40; NMR; -; A=2-108.
DR   PDB; 1FAP; X-ray; 2.70 A; A=2-108.
DR   PDB; 1FKB; X-ray; 1.70 A; A=2-108.
DR   PDB; 1FKD; X-ray; 1.72 A; A=2-108.
DR   PDB; 1FKF; X-ray; 1.70 A; A=2-108.
DR   PDB; 1FKG; X-ray; 2.00 A; A=2-108.
DR   PDB; 1FKH; X-ray; 1.95 A; A=2-108.
DR   PDB; 1FKI; X-ray; 2.20 A; A/B=2-108.
DR   PDB; 1FKJ; X-ray; 1.70 A; A=2-108.
DR   PDB; 1FKR; NMR; -; A=2-108.
DR   PDB; 1FKS; NMR; -; A=2-108.
DR   PDB; 1FKT; NMR; -; A=2-108.
DR   PDB; 1J4H; X-ray; 1.80 A; A=2-108.
DR   PDB; 1J4I; X-ray; 1.80 A; A=2-108.
DR   PDB; 1J4R; X-ray; 1.80 A; A/B/D=2-108.
DR   PDB; 1NSG; X-ray; 2.20 A; A=2-108.
DR   PDB; 1QPF; X-ray; 2.50 A; A/D=2-108.
DR   PDB; 1QPL; X-ray; 2.90 A; A/C=2-108.
DR   PDB; 2DG3; X-ray; 1.70 A; A=2-108.
DR   PDB; 2DG4; X-ray; 1.70 A; A=2-108.
DR   PDB; 2DG9; X-ray; 1.70 A; A=2-108.
DR   PDB; 2FAP; X-ray; 2.20 A; A=2-108.
DR   PDB; 2FKE; X-ray; 1.72 A; A=2-108.
DR   PDB; 2ND5; NMR; -; A=1-108.
DR   PDB; 2PPN; X-ray; 0.92 A; A=2-108.
DR   PDB; 2PPO; X-ray; 1.29 A; A=2-108.
DR   PDB; 2PPP; X-ray; 0.94 A; A=2-108.
DR   PDB; 2RSE; NMR; -; A=2-108.
DR   PDB; 3FAP; X-ray; 1.85 A; A=2-108.
DR   PDB; 3H9R; X-ray; 2.35 A; B=1-108.
DR   PDB; 3MDY; X-ray; 2.05 A; B/D=1-108.
DR   PDB; 4DH0; X-ray; 2.10 A; A=2-108.
DR   PDB; 4FAP; X-ray; 2.80 A; A=2-108.
DR   PDB; 4IPX; X-ray; 1.70 A; A=2-108.
DR   PDB; 4N19; X-ray; 1.20 A; A=2-108.
DR   PDB; 4ODP; X-ray; 1.75 A; A=85-97.
DR   PDB; 4ODQ; X-ray; 2.00 A; A=85-97.
DR   PDB; 4ODR; X-ray; 1.93 A; A/B=85-97.
DR   PDB; 5I7P; X-ray; 2.00 A; A=2-84, A=98-108.
DR   PDB; 5I7Q; X-ray; 1.90 A; A=2-84, A=97-108.
DR   PDB; 6I1S; X-ray; 1.52 A; B=1-108.
DR   PDBsum; 1A7X; -.
DR   PDBsum; 1B6C; -.
DR   PDBsum; 1BKF; -.
DR   PDBsum; 1BL4; -.
DR   PDBsum; 1D6O; -.
DR   PDBsum; 1D7H; -.
DR   PDBsum; 1D7I; -.
DR   PDBsum; 1D7J; -.
DR   PDBsum; 1EYM; -.
DR   PDBsum; 1F40; -.
DR   PDBsum; 1FAP; -.
DR   PDBsum; 1FKB; -.
DR   PDBsum; 1FKD; -.
DR   PDBsum; 1FKF; -.
DR   PDBsum; 1FKG; -.
DR   PDBsum; 1FKH; -.
DR   PDBsum; 1FKI; -.
DR   PDBsum; 1FKJ; -.
DR   PDBsum; 1FKR; -.
DR   PDBsum; 1FKS; -.
DR   PDBsum; 1FKT; -.
DR   PDBsum; 1J4H; -.
DR   PDBsum; 1J4I; -.
DR   PDBsum; 1J4R; -.
DR   PDBsum; 1NSG; -.
DR   PDBsum; 1QPF; -.
DR   PDBsum; 1QPL; -.
DR   PDBsum; 2DG3; -.
DR   PDBsum; 2DG4; -.
DR   PDBsum; 2DG9; -.
DR   PDBsum; 2FAP; -.
DR   PDBsum; 2FKE; -.
DR   PDBsum; 2ND5; -.
DR   PDBsum; 2PPN; -.
DR   PDBsum; 2PPO; -.
DR   PDBsum; 2PPP; -.
DR   PDBsum; 2RSE; -.
DR   PDBsum; 3FAP; -.
DR   PDBsum; 3H9R; -.
DR   PDBsum; 3MDY; -.
DR   PDBsum; 4DH0; -.
DR   PDBsum; 4FAP; -.
DR   PDBsum; 4IPX; -.
DR   PDBsum; 4N19; -.
DR   PDBsum; 4ODP; -.
DR   PDBsum; 4ODQ; -.
DR   PDBsum; 4ODR; -.
DR   PDBsum; 5I7P; -.
DR   PDBsum; 5I7Q; -.
DR   PDBsum; 6I1S; -.
DR   SMR; P62942; -.
DR   BioGrid; 108570; 65.
DR   CORUM; P62942; -.
DR   DIP; DIP-29710N; -.
DR   IntAct; P62942; 19.
DR   MINT; P62942; -.
DR   STRING; 9606.ENSP00000383003; -.
DR   BindingDB; P62942; -.
DR   ChEMBL; CHEMBL1902; -.
DR   DrugBank; DB08520; (21S)-1AZA-4,4-DIMETHYL-6,19-DIOXA-2,3,7,20-TETRAOXOBICYCLO[19.4.0] PENTACOSANE.
DR   DrugBank; DB04012; (3r)-4-(P-Toluenesulfonyl)-1,4-Thiazane-3-Carboxylicacid-L-Leucine.
DR   DrugBank; DB01712; (3r)-4-(P-Toluenesulfonyl)-1,4-Thiazane-3-Carboxylicacid-L-Phenylalanine Ethyl Ester.
DR   DrugBank; DB04094; 4-Hydroxy-2-Butanone.
DR   DrugBank; DB08597; 6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-ylpyrazolo[1,5-a]pyrimidine.
DR   DrugBank; DB02888; FKB-001.
DR   DrugBank; DB01951; Gpi-1046.
DR   DrugBank; DB05814; GPI-1485.
DR   DrugBank; DB03338; Heptyl-Beta-D-Glucopyranoside.
DR   DrugBank; DB03621; L-709,587.
DR   DrugBank; DB02311; Methyl Methylsulfinylmethyl Sulfide.
DR   DrugBank; DB08231; Myristic acid.
DR   DrugBank; DB00337; Pimecrolimus.
DR   DrugBank; DB00877; Sirolimus.
DR   DrugBank; DB00864; Tacrolimus.
DR   DrugBank; DB01723; {3-[3-(3,4-Dimethoxy-Phenyl)-1-(1-{1-[2-(3,4,5-Trimethoxy-Phenyl)-Butyryl]-Piperidin-2yl}-Vinyloxy)-Propyl]-Phenoxy}-Acetic Acid.
DR   DrugCentral; P62942; -.
DR   GuidetoPHARMACOLOGY; 2609; -.
DR   TCDB; 8.A.11.1.2; the immunophilin-like prolyl:peptidyl isomerase regulator (i-ppi) family.
DR   iPTMnet; P62942; -.
DR   PhosphoSitePlus; P62942; -.
DR   BioMuta; FKBP1A; -.
DR   EPD; P62942; -.
DR   jPOST; P62942; -.
DR   MassIVE; P62942; -.
DR   MaxQB; P62942; -.
DR   PaxDb; P62942; -.
DR   PeptideAtlas; P62942; -.
DR   PRIDE; P62942; -.
DR   ProteomicsDB; 57456; -.
DR   TopDownProteomics; P62942; -.
DR   DNASU; 2280; -.
DR   Ensembl; ENST00000381719; ENSP00000371138; ENSG00000088832.
DR   Ensembl; ENST00000400137; ENSP00000383003; ENSG00000088832.
DR   GeneID; 2280; -.
DR   KEGG; hsa:2280; -.
DR   UCSC; uc002wey.4; human.
DR   CTD; 2280; -.
DR   DisGeNET; 2280; -.
DR   EuPathDB; HostDB:ENSG00000088832.14; -.
DR   GeneCards; FKBP1A; -.
DR   HGNC; HGNC:3711; FKBP1A.
DR   HPA; CAB004639; -.
DR   HPA; HPA051798; -.
DR   MIM; 186945; gene.
DR   neXtProt; NX_P62942; -.
DR   OpenTargets; ENSG00000088832; -.
DR   PharmGKB; PA28153; -.
DR   eggNOG; KOG0544; Eukaryota.
DR   eggNOG; COG0545; LUCA.
DR   GeneTree; ENSGT00940000153311; -.
DR   InParanoid; P62942; -.
DR   KO; K09568; -.
DR   OMA; WGIMPNS; -.
DR   OrthoDB; 1328688at2759; -.
DR   PhylomeDB; P62942; -.
DR   TreeFam; TF105291; -.
DR   BRENDA; 5.2.1.8; 2681.
DR   Reactome; R-HSA-2025928; Calcineurin activates NFAT.
DR   Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR   Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR   Reactome; R-HSA-3656535; TGFBR1 LBD Mutants in Cancer.
DR   SignaLink; P62942; -.
DR   SIGNOR; P62942; -.
DR   ChiTaRS; FKBP1A; human.
DR   EvolutionaryTrace; P62942; -.
DR   GeneWiki; FKBP1A; -.
DR   GenomeRNAi; 2280; -.
DR   Pharos; P62942; Tclin.
DR   PRO; PR:P62942; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P62942; protein.
DR   Bgee; ENSG00000088832; Expressed in 231 organ(s), highest expression level in caudate nucleus.
DR   ExpressionAtlas; P62942; baseline and differential.
DR   Genevisible; P62942; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0098562; C:cytoplasmic side of membrane; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR   GO; GO:0031312; C:extrinsic component of organelle membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR   GO; GO:1990425; C:ryanodine receptor complex; ISS:UniProtKB.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0014802; C:terminal cisterna; ISS:BHF-UCL.
DR   GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR   GO; GO:0048185; F:activin binding; IPI:BHF-UCL.
DR   GO; GO:0005528; F:FK506 binding; IDA:BHF-UCL.
DR   GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL.
DR   GO; GO:0005527; F:macrolide binding; NAS:BHF-UCL.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL.
DR   GO; GO:0046332; F:SMAD binding; IPI:BHF-UCL.
DR   GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:BHF-UCL.
DR   GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISS:BHF-UCL.
DR   GO; GO:0006458; P:'de novo' protein folding; TAS:BHF-UCL.
DR   GO; GO:1990000; P:amyloid fibril formation; IDA:BHF-UCL.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; NAS:BHF-UCL.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR   GO; GO:0003007; P:heart morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060347; P:heart trabecula formation; ISS:BHF-UCL.
DR   GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR   GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
DR   GO; GO:0006457; P:protein folding; NAS:UniProtKB.
DR   GO; GO:0022417; P:protein maturation by protein folding; TAS:BHF-UCL.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:BHF-UCL.
DR   GO; GO:0042026; P:protein refolding; TAS:BHF-UCL.
DR   GO; GO:0032925; P:regulation of activin receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0050776; P:regulation of immune response; IMP:BHF-UCL.
DR   GO; GO:0032880; P:regulation of protein localization; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR   GO; GO:0007183; P:SMAD protein complex assembly; IDA:BHF-UCL.
DR   GO; GO:0097435; P:supramolecular fiber organization; IDA:BHF-UCL.
DR   GO; GO:0042110; P:T cell activation; NAS:BHF-UCL.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
DR   InterPro; IPR023566; PPIase_FKBP.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR10516; PTHR10516; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Isomerase;
KW   Membrane; Reference proteome; Rotamase; Sarcoplasmic reticulum.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0000269|PubMed:1701173, ECO:0000269|PubMed:2477715"
FT   CHAIN           2..108
FT                   /note="Peptidyl-prolyl cis-trans isomerase FKBP1A"
FT                   /id="PRO_0000075289"
FT   DOMAIN          20..108
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   MOD_RES         53
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26883"
FT   MOD_RES         53
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26883"
FT   CONFLICT        60
FT                   /note="W -> R (in Ref. 6; CAG28541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="I -> V (in Ref. 6; CAG28541)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..9
FT                   /evidence="ECO:0000244|PDB:2PPN"
FT   STRAND          22..31
FT                   /evidence="ECO:0000244|PDB:2PPN"
FT   STRAND          36..39
FT                   /evidence="ECO:0000244|PDB:2PPN"
FT   HELIX           40..43
FT                   /evidence="ECO:0000244|PDB:2PPN"
FT   STRAND          47..50
FT                   /evidence="ECO:0000244|PDB:2PPN"
FT   TURN            51..54
FT                   /evidence="ECO:0000244|PDB:6I1S"
FT   HELIX           58..64
FT                   /evidence="ECO:0000244|PDB:2PPN"
FT   STRAND          72..77
FT                   /evidence="ECO:0000244|PDB:2PPN"
FT   HELIX           79..81
FT                   /evidence="ECO:0000244|PDB:2PPN"
FT   TURN            82..86
FT                   /evidence="ECO:0000244|PDB:2PPN"
FT   TURN            89..91
FT                   /evidence="ECO:0000244|PDB:2PPN"
FT   STRAND          98..108
FT                   /evidence="ECO:0000244|PDB:2PPN"
SQ   SEQUENCE   108 AA;  11951 MW;  9CC8493C802540B4 CRC64;
     MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFM LGKQEVIRGW
     EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPHATLVF DVELLKLE
//
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