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P62942

- FKB1A_HUMAN

UniProt

P62942 - FKB1A_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase FKBP1A

Gene

FKBP1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.2 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by both FK506 and rapamycin.

    GO - Molecular functioni

    1. activin binding Source: BHF-UCL
    2. FK506 binding Source: BHF-UCL
    3. ion channel binding Source: BHF-UCL
    4. macrolide binding Source: BHF-UCL
    5. peptidyl-prolyl cis-trans isomerase activity Source: BHF-UCL
    6. protein binding Source: UniProtKB
    7. signal transducer activity Source: UniProtKB
    8. SMAD binding Source: BHF-UCL
    9. transforming growth factor beta receptor binding Source: BHF-UCL
    10. type I transforming growth factor beta receptor binding Source: BHF-UCL

    GO - Biological processi

    1. 'de novo' protein folding Source: BHF-UCL
    2. amyloid fibril formation Source: BHF-UCL
    3. calcium ion transmembrane transport Source: BHF-UCL
    4. chaperone-mediated protein folding Source: RefGenome
    5. extracellular fibril organization Source: BHF-UCL
    6. heart morphogenesis Source: BHF-UCL
    7. heart trabecula formation Source: BHF-UCL
    8. negative regulation of protein phosphatase type 2B activity Source: BHF-UCL
    9. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    10. positive regulation of protein binding Source: BHF-UCL
    11. positive regulation of protein ubiquitination Source: BHF-UCL
    12. protein folding Source: UniProtKB
    13. protein maturation by protein folding Source: BHF-UCL
    14. protein peptidyl-prolyl isomerization Source: BHF-UCL
    15. protein refolding Source: BHF-UCL
    16. regulation of activin receptor signaling pathway Source: BHF-UCL
    17. regulation of amyloid precursor protein catabolic process Source: ParkinsonsUK-UCL
    18. regulation of immune response Source: BHF-UCL
    19. regulation of protein localization Source: ParkinsonsUK-UCL
    20. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    21. SMAD protein complex assembly Source: BHF-UCL
    22. T cell activation Source: BHF-UCL
    23. transforming growth factor beta receptor signaling pathway Source: Reactome
    24. ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Enzyme and pathway databases

    ReactomeiREACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_120850. TGF-beta receptor signaling activates SMADs.
    REACT_169263. TGFBR1 KD Mutants in Cancer.
    REACT_169440. TGFBR2 Kinase Domain Mutants in Cancer.
    REACT_169445. TGFBR1 LBD Mutants in Cancer.
    SignaLinkiP62942.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase FKBP1A (EC:5.2.1.8)
    Short name:
    PPIase FKBP1A
    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 namesi
    Name:FKBP1A
    Synonyms:FKBP1, FKBP12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:3711. FKBP1A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: BHF-UCL
    3. endoplasmic reticulum membrane Source: RefGenome
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: BHF-UCL
    6. terminal cisterna Source: BHF-UCL
    7. Z disc Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28153.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1APRO_0000075289Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication
    Modified residuei9 – 91Phosphoserine2 Publications
    Modified residuei53 – 531N6-acetyllysine; alternateBy similarity
    Modified residuei53 – 531N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP62942.
    PaxDbiP62942.
    PRIDEiP62942.

    PTM databases

    PhosphoSiteiP62942.

    Miscellaneous databases

    PMAP-CutDBP62942.

    Expressioni

    Gene expression databases

    ArrayExpressiP62942.
    BgeeiP62942.
    CleanExiHS_FKBP1A.
    GenevestigatoriP62942.

    Organism-specific databases

    HPAiCAB004639.
    HPA051798.

    Interactioni

    Subunit structurei

    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.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACVR1BP368962EBI-1027571,EBI-1384128
    MTORP423452EBI-1027571,EBI-359260
    SMAD7O151053EBI-1027571,EBI-3861591

    Protein-protein interaction databases

    BioGridi108570. 25 interactions.
    DIPiDIP-29710N.
    IntActiP62942. 8 interactions.
    MINTiMINT-87893.
    STRINGi9606.ENSP00000371138.

    Structurei

    Secondary structure

    1
    108
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 97
    Beta strandi22 – 3110
    Beta strandi36 – 394
    Helixi40 – 434
    Beta strandi47 – 504
    Turni51 – 544
    Helixi58 – 647
    Beta strandi72 – 776
    Helixi79 – 813
    Turni82 – 865
    Turni89 – 913
    Beta strandi98 – 10811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP62942.
    SMRiP62942. Positions 2-108.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62942.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 10889PPIase FKBP-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0545.
    HOVERGENiHBG051623.
    InParanoidiP62942.
    KOiK09568.
    OMAiSPQKGDT.
    OrthoDBiEOG7ZGX5T.
    PhylomeDBiP62942.
    TreeFamiTF105291.

    Family and domain databases

    InterProiIPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view]
    PANTHERiPTHR10516. PTHR10516. 1 hit.
    PfamiPF00254. FKBP_C. 1 hit.
    [Graphical view]
    PROSITEiPS50059. FKBP_PPIASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P62942-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFM    50
    LGKQEVIRGW EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPHATLVF 100
    DVELLKLE 108
    Length:108
    Mass (Da):11,951
    Last modified:January 23, 2007 - v2
    Checksum:i9CC8493C802540B4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601W → R in CAG28541. 1 PublicationCurated
    Sequence conflicti91 – 911I → V in CAG28541. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13014.1.
    PIRiI65284. A35780.
    RefSeqiNP_000792.1. NM_000801.4.
    NP_463460.1. NM_054014.3.
    UniGeneiHs.471933.
    Hs.700839.

    Genome annotation databases

    EnsembliENST00000381719; ENSP00000371138; ENSG00000088832.
    ENST00000400137; ENSP00000383003; ENSG00000088832.
    GeneIDi2280.
    KEGGihsa:2280.
    UCSCiuc002wey.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13014.1.
    PIRi I65284. A35780.
    RefSeqi NP_000792.1. NM_000801.4.
    NP_463460.1. NM_054014.3.
    UniGenei Hs.471933.
    Hs.700839.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A7X X-ray 2.00 A/B 2-108 [» ]
    1B6C X-ray 2.60 A/C/E/G 2-108 [» ]
    1BKF X-ray 1.60 A 2-108 [» ]
    1BL4 X-ray 1.90 A/B 2-108 [» ]
    1D6O X-ray 1.85 A/B 2-108 [» ]
    1D7H X-ray 1.90 A/B 2-108 [» ]
    1D7I X-ray 1.90 A/B 2-108 [» ]
    1D7J X-ray 1.85 A/B 2-108 [» ]
    1EYM X-ray 2.00 A/B 2-108 [» ]
    1F40 NMR - A 2-108 [» ]
    1FAP X-ray 2.70 A 2-108 [» ]
    1FKB X-ray 1.70 A 2-108 [» ]
    1FKD X-ray 1.72 A 2-108 [» ]
    1FKF X-ray 1.70 A 2-108 [» ]
    1FKG X-ray 2.00 A 2-108 [» ]
    1FKH X-ray 1.95 A 2-108 [» ]
    1FKI X-ray 2.20 A/B 2-108 [» ]
    1FKJ X-ray 1.70 A 2-108 [» ]
    1FKR NMR - A 2-108 [» ]
    1FKS NMR - A 2-108 [» ]
    1FKT NMR - A 2-108 [» ]
    1J4H X-ray 1.80 A 2-108 [» ]
    1J4I X-ray 1.80 A 2-108 [» ]
    1J4R X-ray 1.80 A/B/D 2-108 [» ]
    1NSG X-ray 2.20 A 2-108 [» ]
    1QPF X-ray 2.50 A/D 2-108 [» ]
    1QPL X-ray 2.90 A/C 2-108 [» ]
    2DG3 X-ray 1.70 A 2-108 [» ]
    2DG4 X-ray 1.70 A 2-108 [» ]
    2DG9 X-ray 1.70 A 2-108 [» ]
    2FAP X-ray 2.20 A 2-108 [» ]
    2FKE X-ray 1.72 A 2-108 [» ]
    2PPN X-ray 0.92 A 2-108 [» ]
    2PPO X-ray 1.29 A 2-108 [» ]
    2PPP X-ray 0.94 A 2-108 [» ]
    2RSE NMR - A 2-108 [» ]
    3FAP X-ray 1.85 A 2-108 [» ]
    3H9R X-ray 2.35 B 1-108 [» ]
    3MDY X-ray 2.05 B/D 1-108 [» ]
    4DH0 X-ray 2.10 A 2-108 [» ]
    4FAP X-ray 2.80 A 2-108 [» ]
    4IPX X-ray 1.70 A 2-108 [» ]
    4N19 X-ray 1.20 A 2-108 [» ]
    ProteinModelPortali P62942.
    SMRi P62942. Positions 2-108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108570. 25 interactions.
    DIPi DIP-29710N.
    IntActi P62942. 8 interactions.
    MINTi MINT-87893.
    STRINGi 9606.ENSP00000371138.

    Chemistry

    BindingDBi P62942.
    ChEMBLi CHEMBL1902.
    DrugBanki DB00337. Pimecrolimus.
    DB00877. Sirolimus.
    DB00864. Tacrolimus.
    GuidetoPHARMACOLOGYi 2609.

    PTM databases

    PhosphoSitei P62942.

    Proteomic databases

    MaxQBi P62942.
    PaxDbi P62942.
    PRIDEi P62942.

    Protocols and materials databases

    DNASUi 2280.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381719 ; ENSP00000371138 ; ENSG00000088832 .
    ENST00000400137 ; ENSP00000383003 ; ENSG00000088832 .
    GeneIDi 2280.
    KEGGi hsa:2280.
    UCSCi uc002wey.3. human.

    Organism-specific databases

    CTDi 2280.
    GeneCardsi GC20M001349.
    HGNCi HGNC:3711. FKBP1A.
    HPAi CAB004639.
    HPA051798.
    MIMi 186945. gene.
    neXtProti NX_P62942.
    PharmGKBi PA28153.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0545.
    HOVERGENi HBG051623.
    InParanoidi P62942.
    KOi K09568.
    OMAi SPQKGDT.
    OrthoDBi EOG7ZGX5T.
    PhylomeDBi P62942.
    TreeFami TF105291.

    Enzyme and pathway databases

    Reactomei REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_120850. TGF-beta receptor signaling activates SMADs.
    REACT_169263. TGFBR1 KD Mutants in Cancer.
    REACT_169440. TGFBR2 Kinase Domain Mutants in Cancer.
    REACT_169445. TGFBR1 LBD Mutants in Cancer.
    SignaLinki P62942.

    Miscellaneous databases

    EvolutionaryTracei P62942.
    GeneWikii FKBP1A.
    GenomeRNAii 2280.
    NextBioi 9269.
    PMAP-CutDB P62942.
    PROi P62942.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62942.
    Bgeei P62942.
    CleanExi HS_FKBP1A.
    Genevestigatori P62942.

    Family and domain databases

    InterProi IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view ]
    PANTHERi PTHR10516. PTHR10516. 1 hit.
    Pfami PF00254. FKBP_C. 1 hit.
    [Graphical view ]
    PROSITEi PS50059. FKBP_PPIASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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).

    Entry informationi

    Entry nameiFKB1A_HUMAN
    AccessioniPrimary (citable) accession number: P62942
    Secondary accession number(s): D3DVW6
    , P20071, Q4VC47, Q6FGD9, Q6LEU3, Q9H103, Q9H566
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3