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UniProtKB/Swiss-Prot entry P62942


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FKB1A_HUMAN
Primary accession number P62942
Secondary accession numbers P20071 Q4VC47 Q6FGD9 Q6LEU3 Q9H103 Q9H566
Integrated into Swiss-Prot on August 31, 2004
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 61)
Name and origin of the protein
Protein name Peptidyl-prolyl cis-trans isomerase FKBP1A
Synonyms PPIase FKBP1A
EC 5.2.1.8
FK506-binding protein 1A
FKBP-1A
Rotamase
Immunophilin FKBP12
12 kDa FKBP
FKBP-12
Gene name
Name: FKBP1A
Synonyms: FKBP1, FKBP12
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.87.14.5440; PubMed=1695378 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/346671a0; PubMed=1696686 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1021/bi00099a002; PubMed=1716149 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1016/0378-1119(94)90434-0; PubMed=7529739 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
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 MRNA].
TISSUE=Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
PROTEIN SEQUENCE OF 2-52.
PubMed=1701173 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
PROTEIN SEQUENCE OF 2-17.
DOI=10.1038/341758a0; PubMed=2477715 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
PROTEIN SEQUENCE OF 2-14.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[13]
STRUCTURE BY NMR.
DOI=10.1021/bi00233a020; PubMed=1709363 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
STRUCTURE BY NMR.
DOI=10.1126/science.1709301; PubMed=1709301 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
STRUCTURE BY NMR.
DOI=10.1016/0014-5793(92)80292-O; PubMed=1375171 [NCBI, ExPASy, EBI, Israel, Japan]
Lepre C.A., Thomson J.A., Moore J.M.;
"Solution structure of FK506 bound to FKBP-12.";
FEBS Lett. 302:89-96(1992).
[16]
STRUCTURE BY NMR OF COMPLEX WITH ASCOMYCIN.
DOI=10.1002/bip.360330404; PubMed=7682113 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
DOI=10.1126/science.1709302; PubMed=1709302 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
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).
[19]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
DOI=10.1006/jmbi.1993.1012; PubMed=7678431 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
DOI=10.1006/jmbi.1999.3411; PubMed=10656803 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M34539; AAA35844.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M92423; AAA58476.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M92422; AAA58476.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M93060; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X55741; CAA39272.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M80199; AAA58472.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X52220; CAA36462.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007066; AAP35729.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR407613; CAG28541.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR542168; CAG46965.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136531; CAH72382.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109658; CAH72382.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109658; CAI22728.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136531; CAI22728.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001925; AAH01925.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005147; AAH05147.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00873810; -.
PIR I65284; A35780.
RefSeq NP_000792.1; -.
NP_463460.1; -.
UniGene Hs.471933
3D structure databases
PDB
1A7X; X-ray; 2.00 A; A/B=2-107.[ExPASy / RCSB / EBI]
1B6C; X-ray; 2.60 A; A/C/E/G=2-107.[ExPASy / RCSB / EBI]
1BKF; X-ray; 1.60 A; A=2-108.[ExPASy / RCSB / EBI]
1BL4; X-ray; 1.90 A; A/B=2-107.[ExPASy / RCSB / EBI]
1D6O; X-ray; 1.85 A; A/B=2-108.[ExPASy / RCSB / EBI]
1D7H; X-ray; 1.90 A; A/B=2-108.[ExPASy / RCSB / EBI]
1D7I; X-ray; 1.90 A; A/B=2-108.[ExPASy / RCSB / EBI]
1D7J; X-ray; 1.85 A; A/B=2-108.[ExPASy / RCSB / EBI]
1EYM; X-ray; 2.00 A; A/B=2-108.[ExPASy / RCSB / EBI]
1F40; NMR; -; A=2-108.[ExPASy / RCSB / EBI]
1FAP; X-ray; 2.70 A; A=2-107.[ExPASy / RCSB / EBI]
1FKB; X-ray; 1.70 A; A=2-108.[ExPASy / RCSB / EBI]
1FKD; X-ray; 1.72 A; A=2-107.[ExPASy / RCSB / EBI]
1FKF; X-ray; 1.70 A; A=2-108.[ExPASy / RCSB / EBI]
1FKG; X-ray; 2.00 A; A=2-108.[ExPASy / RCSB / EBI]
1FKH; X-ray; 1.95 A; A=2-108.[ExPASy / RCSB / EBI]
1FKI; X-ray; 2.20 A; A/B=2-108.[ExPASy / RCSB / EBI]
1FKJ; X-ray; 1.70 A; A=2-107.[ExPASy / RCSB / EBI]
1FKR; NMR; -; A=2-108.[ExPASy / RCSB / EBI]
1FKS; NMR; -; A=2-108.[ExPASy / RCSB / EBI]
1FKT; NMR; -; A=2-108.[ExPASy / RCSB / EBI]
1J4H; X-ray; 1.80 A; A=2-107.[ExPASy / RCSB / EBI]
1J4I; X-ray; 1.80 A; A=2-107.[ExPASy / RCSB / EBI]
1J4R; X-ray; 1.80 A; A/B/D=2-107.[ExPASy / RCSB / EBI]
1NSG; X-ray; 2.20 A; A=2-107.[ExPASy / RCSB / EBI]
1QPF; X-ray; 2.50 A; A/D=2-107.[ExPASy / RCSB / EBI]
1QPL; X-ray; 2.90 A; A/C=2-107.[ExPASy / RCSB / EBI]
1TCO; X-ray; 2.50 A; C=1-108.[ExPASy / RCSB / EBI]
2DG3; X-ray; 1.70 A; A=2-108.[ExPASy / RCSB / EBI]
2DG4; X-ray; 1.70 A; A=2-108.[ExPASy / RCSB / EBI]
2DG9; X-ray; 1.70 A; A=2-108.[ExPASy / RCSB / EBI]
2FAP; X-ray; 2.20 A; A=2-107.[ExPASy / RCSB / EBI]
2FKE; X-ray; 1.72 A; A=2-107.[ExPASy / RCSB / EBI]
2PPN; X-ray; 0.92 A; A=2-108.[ExPASy / RCSB / EBI]
2PPO; X-ray; 1.29 A; A=2-108.[ExPASy / RCSB / EBI]
2PPP; X-ray; 0.94 A; A=2-108.[ExPASy / RCSB / EBI]
3FAP; X-ray; 1.85 A; A=2-107.[ExPASy / RCSB / EBI]
4FAP; X-ray; 2.80 A; A=2-107.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A7X; -.
1B6C; -.
1BKF; -.
1BL4; -.
1D6O; -.
1D7H; -.
1D7I; -.
1D7J; -.
1EYM; -.
1F40; -.
1FAP; -.
1FKB; -.
1FKD; -.
1FKF; -.
1FKG; -.
1FKH; -.
1FKI; -.
1FKJ; -.
1FKR; -.
1FKS; -.
1FKT; -.
1J4H; -.
1J4I; -.
1J4R; -.
1NSG; -.
1QPF; -.
1QPL; -.
1TCO; -.
2DG3; -.
2DG4; -.
2DG9; -.
2FAP; -.
2FKE; -.
2PPN; -.
2PPO; -.
2PPP; -.
3FAP; -.
4FAP; -.
ModBase P62942.
Protein-protein interaction databases
IntAct P62942; 4.
Enzyme and pathway databases
BRENDA 5.2.1.8; 247.
Pathway_Interaction_DB alphasynuclein_pathway; Alpha-synuclein signaling.
tcrcalciumpathway; Calcium signaling in the CD4+ TCR pathway.
mtor_4pathway; mTOR signaling pathway.
nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
tgfbrpathway; TGF-beta receptor signaling.
Organism-specific databases
GeneCards GC20M001297; -.
H-InvDB HIX0015564; -.
HGNC HGNC:3711; FKBP1A.
GenAtlas FKBP1A.
HPA CAB004639; -.
MIM 186945; gene. [NCBI / EBI]
PharmGKB PA28153; -.
Gene expression databases
ArrayExpress P62942; -.
Bgee P62942; -.
CleanEx HS_FKBP1A; -.
GermOnline ENSG00000088832; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0014802; Cellular component: terminal cisterna (inferred from sequence or structural similarity from UniProtKB).
GO:0048185; Molecular function: activin binding (inferred from physical interaction from UniProtKB).
GO:0005528; Molecular function: FK506 binding (inferred from direct assay from UniProtKB).
GO:0003755; Molecular function: peptidyl-prolyl cis-trans isomerase activity (inferred from direct assay from UniProtKB).
GO:0004871; Molecular function: signal transducer activity (inferred from mutant phenotype from UniProtKB).
GO:0046332; Molecular function: SMAD binding (inferred from physical interaction from UniProtKB).
GO:0034713; Molecular function: type I transforming growth factor beta receptor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0006458; Biological process: 'de novo' protein folding (traceable author statement from UniProtKB).
GO:0034205; Biological process: beta-amyloid formation (inferred from direct assay from UniProtKB).
GO:0043206; Biological process: fibril organization (inferred from direct assay from UniProtKB).
GO:0060347; Biological process: heart trabecula formation (inferred from sequence or structural similarity from UniProtKB).
GO:0032513; Biological process: negative regulation of protein phosphatase type 2B activity (inferred from direct assay from UniProtKB).
GO:0043123; Biological process: positive regulation of I-kappaB kinase/NF-kappaB cascade (inferred from mutant phenotype from UniProtKB).
GO:0032092; Biological process: positive regulation of protein binding (inferred from direct assay from UniProtKB).
GO:0031398; Biological process: positive regulation of protein ubiquitination (inferred from direct assay from UniProtKB).
GO:0022417; Biological process: protein maturation by protein folding (traceable author statement from UniProtKB).
GO:0042026; Biological process: protein refolding (traceable author statement from UniProtKB).
GO:0032925; Biological process: regulation of activin receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0050776; Biological process: regulation of immune response (inferred from mutant phenotype from UniProtKB).
GO:0060314; Biological process: regulation of ryanodine-sensitive calcium-release channel activity (inferred from direct assay from UniProtKB).
GO:0007183; Biological process: SMAD protein complex assembly (inferred from direct assay from UniProtKB).
GO:0042110; Biological process: T cell activation (non-traceable author statement from UniProtKB).
GO:0055010; Biological process: ventricular cardiac muscle morphogenesis (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001179; PPIase_FKBP.
Graphical view of domain structure.
PANTHER PTHR10516; PPIase_FKBP; 1.
Pfam PF00254; FKBP_C; 1.
Pfam graphical view of domain structure.
PROSITE PS50059; FKBP_PPIASE; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P62942; -.
Genome annotation databases
Ensembl ENSG00000088832; Homo sapiens. [Contig view]
GeneID 2280; -.
KEGG hsa:2280; -.
Phylogenomic databases
HOVERGEN P62942; -.
Other
BindingDB P62942; -.
DrugBank DB00337; Pimecrolimus.
DB00877; Sirolimus.
DB00864; Tacrolimus.
NextBio 9269; -.
PMAP-CutDB P62942; -.
SOURCE FKBP1A; Homo sapiens.
ProtoNet P62942.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Isomerase; Rotamase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   108  107     Peptidyl-prolyl cis-trans isomerase FKBP1A. PRO_0000075289
DOMAIN   20   108  89     PPIase FKBP-type. 
CONFLICT   60    60        W -> R (in Ref. 6; CAG28541). 
CONFLICT   91    91        I -> V (in Ref. 6; CAG28541). 
STRAND   3     9  7      
STRAND   22    31  10      
STRAND   36    39  4      
HELIX   40    43  4      
STRAND   47    50  4      
HELIX   58    64  7      
STRAND   72    77  6      
HELIX   79    81  3      
TURN   82    86  5      
TURN   89    91  3      
Sequence information
Length: 108 AA [This is the length of the unprocessed precursor] Molecular weight: 11951 Da [This is the MW of the unprocessed precursor] CRC64: 9CC8493C802540B4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFM LGKQEVIRGW 

        70         80         90        100 
EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPHATLVF DVELLKLE 

P62942 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

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