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P68106

- FKB1B_HUMAN

UniProt

P68106 - FKB1B_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase FKBP1B

Gene

FKBP1B

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

    Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by both FK506 and rapamycin.

    GO - Molecular functioni

    1. calcium channel inhibitor activity Source: BHF-UCL
    2. cyclic nucleotide binding Source: Ensembl
    3. FK506 binding Source: BHF-UCL
    4. ion channel binding Source: BHF-UCL
    5. peptidyl-prolyl cis-trans isomerase activity Source: BHF-UCL
    6. protein binding Source: IntAct
    7. receptor binding Source: BHF-UCL

    GO - Biological processi

    1. 'de novo' protein folding Source: BHF-UCL
    2. calcium ion transmembrane transport Source: GOC
    3. calcium-mediated signaling using intracellular calcium source Source: BHF-UCL
    4. cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
    5. chaperone-mediated protein folding Source: RefGenome
    6. cytosolic calcium ion homeostasis Source: BHF-UCL
    7. insulin secretion Source: Ensembl
    8. negative regulation of heart rate Source: BHF-UCL
    9. negative regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
    10. negative regulation of protein phosphatase type 2B activity Source: BHF-UCL
    11. negative regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
    12. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    13. neuronal action potential propagation Source: Ensembl
    14. positive regulation of axon regeneration Source: Ensembl
    15. positive regulation of sequestering of calcium ion Source: BHF-UCL
    16. protein maturation by protein folding Source: BHF-UCL
    17. protein peptidyl-prolyl isomerization Source: BHF-UCL
    18. protein refolding Source: BHF-UCL
    19. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
    20. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    21. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    22. release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: Ensembl
    23. response to glucose Source: Ensembl
    24. response to hydrogen peroxide Source: Ensembl
    25. response to redox state Source: BHF-UCL
    26. response to vitamin E Source: Ensembl
    27. smooth muscle contraction Source: Ensembl
    28. T cell proliferation Source: Ensembl

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase FKBP1B (EC:5.2.1.8)
    Short name:
    PPIase FKBP1B
    Alternative name(s):
    12.6 kDa FK506-binding protein
    Short name:
    12.6 kDa FKBP
    Short name:
    FKBP-12.6
    FK506-binding protein 1B
    Short name:
    FKBP-1B
    Immunophilin FKBP12.6
    Rotamase
    h-FKBP-12
    Gene namesi
    Name:FKBP1B
    Synonyms:FKBP12.6, FKBP1L, FKBP9, OTK4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3712. FKBP1B.

    Subcellular locationi

    Cytoplasm By similarity. Sarcoplasmic reticulum By similarity

    GO - Cellular componenti

    1. calcium channel complex Source: BHF-UCL
    2. cytoplasm Source: BHF-UCL
    3. cytosol Source: BHF-UCL
    4. membrane Source: BHF-UCL
    5. sarcoplasmic reticulum membrane Source: RefGenome
    6. Z disc Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Sarcoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28154.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1BPRO_0000075295Add
    BLAST

    Proteomic databases

    PaxDbiP68106.
    PRIDEiP68106.

    PTM databases

    PhosphoSiteiP68106.

    Expressioni

    Tissue specificityi

    Detected in heart muscle (at protein level). Isoform 1 and isoform 2 are ubiquitous with highest levels in brain and thymus.1 Publication

    Gene expression databases

    BgeeiP68106.
    CleanExiHS_FKBP1B.
    HS_FKBP9.
    GenevestigatoriP68106.

    Organism-specific databases

    HPAiHPA051798.

    Interactioni

    Subunit structurei

    Identified in a complex composed of RYR2, FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and PP1. Interacts directly with RYR2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RYR2Q927362EBI-6693977,EBI-1170425

    Protein-protein interaction databases

    BioGridi108571. 2 interactions.
    DIPiDIP-48796N.
    IntActiP68106. 4 interactions.
    STRINGi9606.ENSP00000370373.

    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 – 405
    Turni41 – 444
    Beta strandi47 – 504
    Turni51 – 544
    Helixi58 – 647
    Beta strandi72 – 776
    Helixi79 – 813
    Turni82 – 865
    Beta strandi89 – 913
    Beta strandi98 – 10811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C9HX-ray2.00A2-108[»]
    4C02X-ray2.17B1-108[»]
    4IQ2X-ray1.70A/B2-108[»]
    4IQCX-ray1.90A/B2-108[»]
    ProteinModelPortaliP68106.
    SMRiP68106. Positions 2-108.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68106.

    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.
    HOGENOMiHOG000154887.
    HOVERGENiHBG051623.
    InParanoidiP68106.
    KOiK09568.
    OMAiCWIGSWR.
    OrthoDBiEOG7ZGX5T.
    PhylomeDBiP68106.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P68106-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGVEIETISP GDGRTFPKKG QTCVVHYTGM LQNGKKFDSS RDRNKPFKFR    50
    IGKQEVIKGF EEGAAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF 100
    DVELLNLE 108
    Length:108
    Mass (Da):11,783
    Last modified:January 23, 2007 - v2
    Checksum:iBAC2A25945F63AC4
    GO
    Isoform 2 (identifier: P68106-2) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         67-108: MSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE → LGPLSPLPICPHPC

    Show »
    Length:80
    Mass (Da):8,802
    Checksum:i99C0A9C743984BA2
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei67 – 10842MSLGQ…LLNLE → LGPLSPLPICPHPC in isoform 2. 3 PublicationsVSP_005184Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S69815 mRNA. Translation: AAB30684.1.
    D38037 mRNA. Translation: BAA07232.1.
    L37086 mRNA. Translation: AAC37581.1.
    S69800 mRNA. Translation: AAB30685.1.
    AF322070 mRNA. Translation: AAK11191.1.
    AB190793 Genomic DNA. Translation: BAE44300.1.
    AC008073 Genomic DNA. Translation: AAY14663.1.
    CH471053 Genomic DNA. Translation: EAX00769.1.
    BC002614 mRNA. Translation: AAH02614.1.
    CCDSiCCDS1706.1.
    CCDS33153.1. [P68106-2]
    PIRiJC2188.
    RefSeqiNP_004107.1. NM_004116.3. [P68106-1]
    NP_473374.1. NM_054033.2. [P68106-2]
    UniGeneiHs.709461.

    Genome annotation databases

    EnsembliENST00000380986; ENSP00000370373; ENSG00000119782. [P68106-1]
    ENST00000380991; ENSP00000370379; ENSG00000119782. [P68106-2]
    GeneIDi2281.
    KEGGihsa:2281.
    UCSCiuc002rer.3. human.
    uc002res.3. human. [P68106-2]

    Polymorphism databases

    DMDMi61224185.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S69815 mRNA. Translation: AAB30684.1 .
    D38037 mRNA. Translation: BAA07232.1 .
    L37086 mRNA. Translation: AAC37581.1 .
    S69800 mRNA. Translation: AAB30685.1 .
    AF322070 mRNA. Translation: AAK11191.1 .
    AB190793 Genomic DNA. Translation: BAE44300.1 .
    AC008073 Genomic DNA. Translation: AAY14663.1 .
    CH471053 Genomic DNA. Translation: EAX00769.1 .
    BC002614 mRNA. Translation: AAH02614.1 .
    CCDSi CCDS1706.1.
    CCDS33153.1. [P68106-2 ]
    PIRi JC2188.
    RefSeqi NP_004107.1. NM_004116.3. [P68106-1 ]
    NP_473374.1. NM_054033.2. [P68106-2 ]
    UniGenei Hs.709461.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C9H X-ray 2.00 A 2-108 [» ]
    4C02 X-ray 2.17 B 1-108 [» ]
    4IQ2 X-ray 1.70 A/B 2-108 [» ]
    4IQC X-ray 1.90 A/B 2-108 [» ]
    ProteinModelPortali P68106.
    SMRi P68106. Positions 2-108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108571. 2 interactions.
    DIPi DIP-48796N.
    IntActi P68106. 4 interactions.
    STRINGi 9606.ENSP00000370373.

    Chemistry

    BindingDBi P68106.
    ChEMBLi CHEMBL2430.

    PTM databases

    PhosphoSitei P68106.

    Polymorphism databases

    DMDMi 61224185.

    Proteomic databases

    PaxDbi P68106.
    PRIDEi P68106.

    Protocols and materials databases

    DNASUi 2281.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380986 ; ENSP00000370373 ; ENSG00000119782 . [P68106-1 ]
    ENST00000380991 ; ENSP00000370379 ; ENSG00000119782 . [P68106-2 ]
    GeneIDi 2281.
    KEGGi hsa:2281.
    UCSCi uc002rer.3. human.
    uc002res.3. human. [P68106-2 ]

    Organism-specific databases

    CTDi 2281.
    GeneCardsi GC02P024272.
    HGNCi HGNC:3712. FKBP1B.
    HPAi HPA051798.
    MIMi 600620. gene.
    neXtProti NX_P68106.
    PharmGKBi PA28154.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0545.
    HOGENOMi HOG000154887.
    HOVERGENi HBG051623.
    InParanoidi P68106.
    KOi K09568.
    OMAi CWIGSWR.
    OrthoDBi EOG7ZGX5T.
    PhylomeDBi P68106.
    TreeFami TF105291.

    Miscellaneous databases

    EvolutionaryTracei P68106.
    GeneWikii FKBP1B.
    GenomeRNAii 2281.
    NextBioi 9275.
    PROi P68106.
    SOURCEi Search...

    Gene expression databases

    Bgeei P68106.
    CleanExi HS_FKBP1B.
    HS_FKBP9.
    Genevestigatori P68106.

    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. "Molecular cloning and expression of a novel human gene that is highly homologous to human FK506-binding protein 12kDa (hFKBP-12) and characterization of two alternatively spliced transcripts."
      Arakawa H., Nagase H., Hayashi N., Fujiwara T., Ogawa M., Shin S., Nakamura Y.
      Biochem. Biophys. Res. Commun. 200:836-843(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Fetal brain.
    2. "A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor."
      Lam E., Martin M.M., Timerman A.P., Sabers C., Fleischer S., Lukas T., Abraham R.T., O'Keefe S.J., O'Neill E.A., Wiederrecht G.J.
      J. Biol. Chem. 270:26511-26522(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain and Heart muscle.
    3. "FKBP9: an alternative splice variant of the FK506-binding protein FKBP12.6 expressed in the human heart."
      Seidler T., Kussebi N., Prestle J.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "Genomic organization, chromosomal localization, and promoter of human gene for FK506-binding protein 12.6."
      Nakazawa T., Takasawa S., Noguchi N., Nata K., Tohgo A., Mori M., Nakagawara K., Akiyama T., Ikeda T., Yamauchi A., Takahashi I., Yoshikawa T., Okamoto H.
      Gene 360:55-64(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 2).
      Tissue: Brain.
    8. "PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts."
      Marx S.O., Reiken S., Hisamatsu Y., Jayaraman T., Burkhoff D., Rosemblit N., Marks A.R.
      Cell 101:365-376(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH RYR2; PP1; PP2A AKAP6 AND PKA, INTERACTION WITH RYR2, TISSUE SPECIFICITY.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiFKB1B_HUMAN
    AccessioniPrimary (citable) accession number: P68106
    Secondary accession number(s): Q13664
    , Q16645, Q53TM2, Q9BQ40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 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, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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