Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P62942 (FKB1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1A

Short name=PPIase FKBP1A
EC=5.2.1.8
Alternative name(s):
12 kDa FK506-binding protein
Short name=12 kDa FKBP
Short name=FKBP-12
Calstabin-1
FK506-binding protein 1A
Short name=FKBP-1A
Immunophilin FKBP12
Rotamase
Gene names
Name:FKBP1A
Synonyms:FKBP1, FKBP12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.13 Ref.15

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulation

Inhibited by both FK506 and rapamycin.

Subunit structure

Interacts directly with RYR1, RYR2 and RYR3. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) By similarity. Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with ACVR1B and SMAD7. Ref.13 Ref.14 Ref.15 Ref.20

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP1 subfamily.

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
Rotamase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' protein folding

Traceable author statement PubMed 11322937. Source: BHF-UCL

SMAD protein complex assembly

Inferred from direct assay Ref.15. Source: BHF-UCL

T cell activation

Non-traceable author statement Ref.2. Source: BHF-UCL

amyloid fibril formation

Inferred from direct assay PubMed 18346205. Source: BHF-UCL

calcium ion transmembrane transport

Traceable author statement. Source: GOC

extracellular fibril organization

Inferred from direct assay PubMed 18346205. Source: BHF-UCL

heart morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

heart trabecula formation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of protein phosphatase type 2B activity

Inferred from direct assay PubMed 7592869. Source: BHF-UCL

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

positive regulation of protein binding

Inferred from direct assay PubMed 18346205. Source: BHF-UCL

positive regulation of protein ubiquitination

Inferred from direct assay Ref.15. Source: BHF-UCL

protein folding

Non-traceable author statement PubMed 1930186. Source: UniProtKB

protein maturation by protein folding

Traceable author statement PubMed 11322937. Source: BHF-UCL

protein peptidyl-prolyl isomerization

Inferred from mutant phenotype. Source: ParkinsonsUK-UCL

protein refolding

Traceable author statement PubMed 11322937. Source: BHF-UCL

regulation of activin receptor signaling pathway

Inferred from direct assay Ref.15. Source: BHF-UCL

regulation of amyloid precursor protein catabolic process

Inferred from genetic interaction PubMed 24499793. Source: ParkinsonsUK-UCL

regulation of immune response

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

regulation of protein localization

Inferred from genetic interaction PubMed 24499793. Source: ParkinsonsUK-UCL

regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 7592869. Source: BHF-UCL

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

ventricular cardiac muscle tissue morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentZ disc

Inferred from direct assay PubMed 20431056. Source: BHF-UCL

axon

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from direct assay PubMed 12443530. Source: BHF-UCL

cytosol

Inferred from direct assay Ref.10. Source: BHF-UCL

membrane

Inferred from direct assay PubMed 12443530. Source: BHF-UCL

terminal cisterna

Inferred from sequence or structural similarity PubMed 1374404. Source: BHF-UCL

   Molecular_functionFK506 binding

Inferred from direct assay PubMed 7592869. Source: BHF-UCL

SMAD binding

Inferred from physical interaction Ref.15. Source: BHF-UCL

activin binding

Inferred from physical interaction Ref.15. Source: BHF-UCL

ion channel binding

Inferred from sequence or structural similarity. Source: BHF-UCL

macrolide binding

Non-traceable author statement PubMed 17962721. Source: BHF-UCL

peptidyl-prolyl cis-trans isomerase activity

Inferred from direct assay Ref.2Ref.10Ref.11. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.14PubMed 12604780. Source: UniProtKB

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

transforming growth factor beta receptor binding

Inferred from sequence or structural similarity PubMed 7518616. Source: BHF-UCL

type I transforming growth factor beta receptor binding

Inferred from sequence or structural similarity PubMed 7518616. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10 Ref.11 Ref.12 Ref.16
Chain2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1A
PRO_0000075289

Regions

Domain20 – 10889PPIase FKBP-type

Amino acid modifications

Modified residue21N-acetylglycine Ref.16
Modified residue91Phosphoserine Ref.17 Ref.18
Modified residue531N6-acetyllysine; alternate By similarity
Modified residue531N6-succinyllysine; alternate By similarity

Experimental info

Sequence conflict601W → R in CAG28541. Ref.6
Sequence conflict911I → V in CAG28541. Ref.6

Secondary structure

..................... 108
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62942 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9CC8493C802540B4

FASTA10811,951
        10         20         30         40         50         60 
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFM LGKQEVIRGW 

        70         80         90        100 
EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPHATLVF DVELLKLE 

« Hide

References

« Hide 'large scale' references
[1]"Complementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin."
Maki N., Sekiguchi F., Nishimaki J., Miwa K., Hayano T., Takahashi N., Suzuki M.
Proc. Natl. Acad. Sci. U.S.A. 87:5440-5443(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and overexpression of the human FK506-binding protein FKBP."
Standaert R.F., Galat A., Verdine G.L., Schreiber S.L.
Nature 346:671-674(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Exon organization of the human FKBP-12 gene: correlation with structural and functional protein domains."
Dilella A.G., Craig R.J.
Biochemistry 30:8512-8517(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Three distinct messenger RNAs can encode the human immunosuppressant-binding protein FKBP12."
Peattie D.A., Hsiao K., Benasutti M., Lippke J.A.
Gene 150:251-257(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Placenta.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Placenta.
[10]"The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase."
Siekierka J.J., Widerrecht G., Greulich H., Boulton D., Hung S.H.Y., Cryan J., Hodges P.J., Sigal N.H.
J. Biol. Chem. 265:21011-21015(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-52.
[11]"A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase."
Harding M.W., Galat A., Uehling D.E., Schreiber S.L.
Nature 341:758-760(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-17.
[12]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14.
Tissue: Platelet.
[13]"Mechanism of TGFbeta receptor inhibition by FKBP12."
Chen Y.G., Liu F., Massague J.
EMBO J. 16:3866-3876(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TGFBR1 INHIBITION, INTERACTION WITH TGFBR1.
[14]"Further characterization of the type 3 ryanodine receptor (RyR3) purified from rabbit diaphragm."
Murayama T., Oba T., Katayama E., Oyamada H., Oguchi K., Kobayashi M., Otsuka K., Ogawa Y.
J. Biol. Chem. 274:17297-17308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RYR3.
[15]"FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type I receptor."
Yamaguchi T., Kurisaki A., Yamakawa N., Minakuchi K., Sugino H.
J. Mol. Endocrinol. 36:569-579(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACVR1B AND SMAD7, FUNCTION.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Characterization of the binding sites for the interactions between FKBP12 and intracellular calcium release channels."
Wen H., Kang S., Song Y., Song Y., Yang H.J., Kim M.H., Park S.
Arch. Biochem. Biophys. 517:37-42(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RYR3.
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein."
Rosen M.K., Michnick S.W., Karplus M., Schreiber S.L.
Biochemistry 30:4774-4789(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[23]"Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin."
Michnick S.W., Rosen M.K., Wandless T.J., Karplus M., Schreiber S.L.
Science 252:836-839(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[24]"Solution structure of FK506 bound to FKBP-12."
Lepre C.A., Thomson J.A., Moore J.M.
FEBS Lett. 302:89-96(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[25]"1H, 13C, and 15N assignments and secondary structure of the FK506 binding protein when bound to ascomycin."
Xu R.X., Nettesheim D., Olejniczak E.T., Meadows R., Gemmecker G., Fesik S.W.
Biopolymers 33:535-550(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF COMPLEX WITH ASCOMYCIN.
[26]"Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex."
van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J.
Science 252:839-842(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[27]"Atomic structure of the rapamycin human immunophilin FKBP-12 complex."
van Duyne G.D., Standaert R.F., Schreiber S.L., Clardy J.
J. Am. Chem. Soc. 113:7433-7434(1991)
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[28]"Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin."
van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J.
J. Mol. Biol. 229:105-124(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
[29]"Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12."
Huse M., Chen Y.-G., Massague J., Kuriyan J.
Cell 96:425-436(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-107 IN COMPLEX WITH TGFBR1.
[30]"X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies."
Burkhard P., Taylor P., Walkinshaw M.D.
J. Mol. Biol. 295:953-962(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34539 mRNA. Translation: AAA35844.1.
M92423, M92422 Genomic DNA. Translation: AAA58476.1.
M93060 Genomic DNA. No translation available.
X55741 Genomic DNA. Translation: CAA39272.1.
M80199 Genomic DNA. Translation: AAA58472.1.
X52220 mRNA. Translation: CAA36462.1.
BT007066 mRNA. Translation: AAP35729.1.
CR407613 mRNA. Translation: CAG28541.1.
CR542168 mRNA. Translation: CAG46965.1.
AL136531, AL109658 Genomic DNA. Translation: CAH72382.1.
AL109658, AL136531 Genomic DNA. Translation: CAI22728.1.
CH471133 Genomic DNA. Translation: EAX10633.1.
CH471133 Genomic DNA. Translation: EAX10634.1.
CH471133 Genomic DNA. Translation: EAX10635.1.
BC001925 mRNA. Translation: AAH01925.3.
BC005147 mRNA. Translation: AAH05147.1.
CCDSCCDS13014.1.
PIRA35780. I65284.
RefSeqNP_000792.1. NM_000801.4.
NP_463460.1. NM_054014.3.
UniGeneHs.471933.
Hs.700839.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7XX-ray2.00A/B2-108[»]
1B6CX-ray2.60A/C/E/G2-108[»]
1BKFX-ray1.60A2-108[»]
1BL4X-ray1.90A/B2-108[»]
1D6OX-ray1.85A/B2-108[»]
1D7HX-ray1.90A/B2-108[»]
1D7IX-ray1.90A/B2-108[»]
1D7JX-ray1.85A/B2-108[»]
1EYMX-ray2.00A/B2-108[»]
1F40NMR-A2-108[»]
1FAPX-ray2.70A2-108[»]
1FKBX-ray1.70A2-108[»]
1FKDX-ray1.72A2-108[»]
1FKFX-ray1.70A2-108[»]
1FKGX-ray2.00A2-108[»]
1FKHX-ray1.95A2-108[»]
1FKIX-ray2.20A/B2-108[»]
1FKJX-ray1.70A2-108[»]
1FKRNMR-A2-108[»]
1FKSNMR-A2-108[»]
1FKTNMR-A2-108[»]
1J4HX-ray1.80A2-108[»]
1J4IX-ray1.80A2-108[»]
1J4RX-ray1.80A/B/D2-108[»]
1NSGX-ray2.20A2-108[»]
1QPFX-ray2.50A/D2-108[»]
1QPLX-ray2.90A/C2-108[»]
2DG3X-ray1.70A2-108[»]
2DG4X-ray1.70A2-108[»]
2DG9X-ray1.70A2-108[»]
2FAPX-ray2.20A2-108[»]
2FKEX-ray1.72A2-108[»]
2PPNX-ray0.92A2-108[»]
2PPOX-ray1.29A2-108[»]
2PPPX-ray0.94A2-108[»]
2RSENMR-A2-108[»]
3FAPX-ray1.85A2-108[»]
3H9RX-ray2.35B1-108[»]
3MDYX-ray2.05B/D1-108[»]
4DH0X-ray2.10A2-108[»]
4FAPX-ray2.80A2-108[»]
4IPXX-ray1.70A2-108[»]
4N19X-ray1.20A2-108[»]
ProteinModelPortalP62942.
SMRP62942. Positions 2-108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108570. 25 interactions.
DIPDIP-29710N.
IntActP62942. 8 interactions.
MINTMINT-87893.
STRING9606.ENSP00000371138.

Chemistry

BindingDBP62942.
ChEMBLCHEMBL1902.
DrugBankDB00337. Pimecrolimus.
DB00877. Sirolimus.
DB00864. Tacrolimus.
GuidetoPHARMACOLOGY2609.

PTM databases

PhosphoSiteP62942.

Proteomic databases

MaxQBP62942.
PaxDbP62942.
PRIDEP62942.

Protocols and materials databases

DNASU2280.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381719; ENSP00000371138; ENSG00000088832.
ENST00000400137; ENSP00000383003; ENSG00000088832.
GeneID2280.
KEGGhsa:2280.
UCSCuc002wey.3. human.

Organism-specific databases

CTD2280.
GeneCardsGC20M001349.
HGNCHGNC:3711. FKBP1A.
HPACAB004639.
HPA051798.
MIM186945. gene.
neXtProtNX_P62942.
PharmGKBPA28153.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0545.
HOVERGENHBG051623.
InParanoidP62942.
KOK09568.
OMASPQKGDT.
OrthoDBEOG7ZGX5T.
PhylomeDBP62942.
TreeFamTF105291.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkP62942.

Gene expression databases

ArrayExpressP62942.
BgeeP62942.
CleanExHS_FKBP1A.
GenevestigatorP62942.

Family and domain databases

InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62942.
GeneWikiFKBP1A.
GenomeRNAi2280.
NextBio9269.
PMAP-CutDBP62942.
PROP62942.
SOURCESearch...

Entry information

Entry nameFKB1A_HUMAN
AccessionPrimary (citable) accession number: P62942
Secondary accession number(s): D3DVW6 expand/collapse secondary AC list , P20071, Q4VC47, Q6FGD9, Q6LEU3, Q9H103, Q9H566
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM