Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q14318

- FKBP8_HUMAN

UniProt

Q14318 - FKBP8_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase FKBP8

Gene

FKBP8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 Jul 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.3 Publications

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).1 Publication

    Cofactori

    Calcium.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi149 – 1491Calcium
    Metal bindingi151 – 1511Calcium

    GO - Molecular functioni

    1. FK506 binding Source: RefGenome
    2. identical protein binding Source: IntAct
    3. metal ion binding Source: UniProtKB-KW
    4. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome
    5. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. chaperone-mediated protein folding Source: RefGenome
    3. intracellular signal transduction Source: ProtInc
    4. protein peptidyl-prolyl isomerization Source: RefGenome
    5. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    Apoptosis, Host-virus interaction

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase FKBP8 (EC:5.2.1.8)
    Short name:
    PPIase FKBP8
    Alternative name(s):
    38 kDa FK506-binding protein
    Short name:
    38 kDa FKBP
    Short name:
    FKBP-38
    Short name:
    hFKBP38
    FK506-binding protein 8
    Short name:
    FKBP-8
    FKBPR38
    Rotamase
    Gene namesi
    Name:FKBP8
    Synonyms:FKBP38
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3724. FKBP8.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: RefGenome
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB
    4. mitochondrial membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi149 – 1491D → N: Abolishes calcium-binding and reduces affinity for BCL2; when associated with Asn-151. 1 Publication
    Mutagenesisi151 – 1511D → N: Abolishes calcium-binding and reduces affinity for BCL2; when associated with Asn-149. 1 Publication

    Organism-specific databases

    PharmGKBiPA28165.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 412412Peptidyl-prolyl cis-trans isomerase FKBP8PRO_0000075331Add
    BLAST

    Proteomic databases

    MaxQBiQ14318.
    PaxDbiQ14318.
    PRIDEiQ14318.

    PTM databases

    PhosphoSiteiQ14318.

    Expressioni

    Tissue specificityi

    Widely expressed. Highest levels seen in the brain. Highly abundant in the retina.1 Publication

    Gene expression databases

    ArrayExpressiQ14318.
    BgeeiQ14318.
    CleanExiHS_FKBP8.
    GenevestigatoriQ14318.

    Organism-specific databases

    HPAiCAB025346.
    HPA045177.

    Interactioni

    Subunit structurei

    Homomultimers or heteromultimers Potential. Forms heterodimer with calmodulin. When activated by calmodulin and calcium, interacts with the BH4 domain of BCL2 and weakly with BCL2L1/BCLX isoform Bcl-X(L). Does not bind and inhibit calcineurin. Interacts with HCV NS5A. Interacts with ZFYVE27; may negatively regulate ZFYVE27 phosphorylation.6 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-724839,EBI-724839
    Q9WMX28EBI-724839,EBI-6863748From a different organism.
    EGFRP005333EBI-724839,EBI-297353
    EGLN1Q9GZT96EBI-724839,EBI-1174818
    HSP90AA1P079007EBI-724839,EBI-296047
    NS5AO3947416EBI-724839,EBI-7016711From a different organism.
    ZFYVE27Q5T4F44EBI-724839,EBI-3892947

    Protein-protein interaction databases

    BioGridi117270. 67 interactions.
    DIPiDIP-42200N.
    IntActiQ14318. 32 interactions.
    MINTiMINT-1338555.
    STRINGi9606.ENSP00000222308.

    Structurei

    Secondary structure

    1
    412
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi94 – 10815
    Beta strandi111 – 1133
    Beta strandi121 – 13111
    Beta strandi136 – 14611
    Turni147 – 1504
    Helixi154 – 1574
    Helixi160 – 1623
    Beta strandi168 – 1736
    Helixi175 – 1773
    Helixi180 – 1823
    Turni185 – 1873
    Beta strandi190 – 1923
    Beta strandi194 – 20411
    Beta strandi208 – 2114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AWGX-ray1.60A90-205[»]
    2D9FNMR-A91-211[»]
    2F2DNMR-A92-210[»]
    2MF9NMR-A58-205[»]
    3EY6X-ray1.05A92-210[»]
    ProteinModelPortaliQ14318.
    SMRiQ14318. Positions 58-368.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14318.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei390 – 41021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini120 – 20485PPIase FKBP-typePROSITE-ProRule annotationAdd
    BLAST
    Repeati221 – 25434TPR 1Add
    BLAST
    Repeati272 – 30534TPR 2Add
    BLAST
    Repeati306 – 33934TPR 3Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi22 – 9271Glu-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation
    Contains 3 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG256105.
    HOVERGENiHBG051626.
    InParanoidiQ14318.
    KOiK09574.
    OrthoDBiEOG70S75T.
    PhylomeDBiQ14318.
    TreeFamiTF105295.

    Family and domain databases

    Gene3Di1.10.150.160. 1 hit.
    1.25.40.10. 1 hit.
    InterProiIPR023114. Elongated_TPR_rpt_dom.
    IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR10516. PTHR10516. 1 hit.
    PfamiPF00254. FKBP_C. 1 hit.
    PF00515. TPR_1. 2 hits.
    [Graphical view]
    PROSITEiPS50059. FKBP_PPIASE. 1 hit.
    PS50005. TPR. 2 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14318-1) [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

    MASCAEPSEP SAPLPAGVPP LEDFEVLDGV EDAEGEEEEE EEEEEEDDLS    50
    ELPPLEDMGQ PPAEEAEQPG ALAREFLAAM EPEPAPAPAP EEWLDILGNG 100
    LLRKKTLVPG PPGSSRPVKG QVVTVHLQTS LENGTRVQEE PELVFTLGDC 150
    DVIQALDLSV PLMDVGETAM VTADSKYCYG PQGRSPYIPP HAALCLEVTL 200
    KTAVDGPDLE MLTGQERVAL ANRKRECGNA HYQRADFVLA ANSYDLAIKA 250
    ITSSAKVDMT FEEEAQLLQL KVKCLNNLAA SQLKLDHYRA ALRSCSLVLE 300
    HQPDNIKALF RKGKVLAQQG EYSEAIPILR AALKLEPSNK TIHAELSKLV 350
    KKHAAQRSTE TALYRKMLGN PSRLPAKCPG KGAWSIPWKW LFGATAVALG 400
    GVALSVVIAA RN 412
    Length:412
    Mass (Da):44,562
    Last modified:July 1, 2008 - v2
    Checksum:i887C25ADE71EBA8D
    GO
    Isoform 2 (identifier: Q14318-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         183-183: G → GS

    Show »
    Length:413
    Mass (Da):44,649
    Checksum:i0C32331CCBE5E4D9
    GO
    Isoform 3 (identifier: Q14318-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         98-256: Missing.

    Note: Interacts with BCL2L1/BCLX.

    Show »
    Length:253
    Mass (Da):27,545
    Checksum:iF899112DC6BF5118
    GO

    Sequence cautioni

    The sequence AAB00102.1 differs from that shown. Reason: The first part of the cDNA maps to the same locus, but in opposite orientation.
    The sequence AAH09966.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAD98028.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441V → A in CAD98028. (PubMed:17974005)Curated
    Sequence conflicti191 – 1911H → R in CAD98028. (PubMed:17974005)Curated
    Sequence conflicti206 – 2061G → R in BAD96558. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti87 – 871A → V.
    Corresponds to variant rs11574806 [ dbSNP | Ensembl ].
    VAR_044225

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei98 – 256159Missing in isoform 3. 1 PublicationVSP_047717Add
    BLAST
    Alternative sequencei183 – 1831G → GS in isoform 2. 2 PublicationsVSP_034486

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY225339 mRNA. Translation: AAO39020.1.
    AY278607 mRNA. Translation: AAQ84561.1.
    GQ372970 mRNA. Translation: ACU65096.1.
    BX538124 mRNA. Translation: CAD98028.1. Different initiation.
    BX647405 mRNA. No translation available.
    AC005387 Genomic DNA. Translation: AAC28753.1.
    CH471106 Genomic DNA. Translation: EAW84709.1.
    L37033 mRNA. Translation: AAB00102.1. Sequence problems.
    AK222838 mRNA. Translation: BAD96558.1.
    BC009966 mRNA. Translation: AAH09966.1. Different initiation.
    CCDSiCCDS32961.1. [Q14318-2]
    RefSeqiNP_036313.3. NM_012181.3. [Q14318-2]
    UniGeneiHs.173464.

    Genome annotation databases

    EnsembliENST00000222308; ENSP00000222308; ENSG00000105701. [Q14318-1]
    ENST00000596558; ENSP00000472302; ENSG00000105701. [Q14318-1]
    ENST00000597960; ENSP00000471700; ENSG00000105701. [Q14318-2]
    ENST00000608443; ENSP00000476767; ENSG00000105701. [Q14318-2]
    GeneIDi23770.
    KEGGihsa:23770.
    UCSCiuc002njj.1. human. [Q14318-2]
    uc002njk.1. human. [Q14318-1]

    Polymorphism databases

    DMDMi193806337.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY225339 mRNA. Translation: AAO39020.1 .
    AY278607 mRNA. Translation: AAQ84561.1 .
    GQ372970 mRNA. Translation: ACU65096.1 .
    BX538124 mRNA. Translation: CAD98028.1 . Different initiation.
    BX647405 mRNA. No translation available.
    AC005387 Genomic DNA. Translation: AAC28753.1 .
    CH471106 Genomic DNA. Translation: EAW84709.1 .
    L37033 mRNA. Translation: AAB00102.1 . Sequence problems.
    AK222838 mRNA. Translation: BAD96558.1 .
    BC009966 mRNA. Translation: AAH09966.1 . Different initiation.
    CCDSi CCDS32961.1. [Q14318-2 ]
    RefSeqi NP_036313.3. NM_012181.3. [Q14318-2 ]
    UniGenei Hs.173464.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AWG X-ray 1.60 A 90-205 [» ]
    2D9F NMR - A 91-211 [» ]
    2F2D NMR - A 92-210 [» ]
    2MF9 NMR - A 58-205 [» ]
    3EY6 X-ray 1.05 A 92-210 [» ]
    ProteinModelPortali Q14318.
    SMRi Q14318. Positions 58-368.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117270. 67 interactions.
    DIPi DIP-42200N.
    IntActi Q14318. 32 interactions.
    MINTi MINT-1338555.
    STRINGi 9606.ENSP00000222308.

    PTM databases

    PhosphoSitei Q14318.

    Polymorphism databases

    DMDMi 193806337.

    Proteomic databases

    MaxQBi Q14318.
    PaxDbi Q14318.
    PRIDEi Q14318.

    Protocols and materials databases

    DNASUi 23770.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222308 ; ENSP00000222308 ; ENSG00000105701 . [Q14318-1 ]
    ENST00000596558 ; ENSP00000472302 ; ENSG00000105701 . [Q14318-1 ]
    ENST00000597960 ; ENSP00000471700 ; ENSG00000105701 . [Q14318-2 ]
    ENST00000608443 ; ENSP00000476767 ; ENSG00000105701 . [Q14318-2 ]
    GeneIDi 23770.
    KEGGi hsa:23770.
    UCSCi uc002njj.1. human. [Q14318-2 ]
    uc002njk.1. human. [Q14318-1 ]

    Organism-specific databases

    CTDi 23770.
    GeneCardsi GC19M018642.
    HGNCi HGNC:3724. FKBP8.
    HPAi CAB025346.
    HPA045177.
    MIMi 604840. gene.
    neXtProti NX_Q14318.
    PharmGKBi PA28165.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG256105.
    HOVERGENi HBG051626.
    InParanoidi Q14318.
    KOi K09574.
    OrthoDBi EOG70S75T.
    PhylomeDBi Q14318.
    TreeFami TF105295.

    Miscellaneous databases

    ChiTaRSi FKBP8. human.
    EvolutionaryTracei Q14318.
    GeneWikii FKBP8.
    GenomeRNAii 23770.
    NextBioi 35483698.
    PROi Q14318.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14318.
    Bgeei Q14318.
    CleanExi HS_FKBP8.
    Genevestigatori Q14318.

    Family and domain databases

    Gene3Di 1.10.150.160. 1 hit.
    1.25.40.10. 1 hit.
    InterProi IPR023114. Elongated_TPR_rpt_dom.
    IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    PANTHERi PTHR10516. PTHR10516. 1 hit.
    Pfami PF00254. FKBP_C. 1 hit.
    PF00515. TPR_1. 2 hits.
    [Graphical view ]
    PROSITEi PS50059. FKBP_PPIASE. 1 hit.
    PS50005. TPR. 2 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis."
      Shirane M., Nakayama K.I.
      Nat. Cell Biol. 5:28-37(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH BCL2 AND BCL2L1/BCLXL, SUBCELLULAR LOCATION.
    2. "FKBP8 is a negative regulator of mouse sonic hedgehog signaling in neural tissues."
      Bulgakov O.V., Eggenschwiler J.T., Hong D.-H., Anderson K.V., Li T.
      Development 131:2149-2159(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Characterization of a Bcl-XL-interacting protein FKBP8 and its splice variant in human RPE cells."
      Chen Y., Sternberg P., Cai J.
      Invest. Ophthalmol. Vis. Sci. 49:1721-1727(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, INTERACTION WITH BCL2L1, TISSUE SPECIFICITY.
      Tissue: Retinal pigment epithelium.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Colon endothelium.
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs."
      Lam E., Martin M., Wiederrecht G.
      Gene 160:297-302(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-412 (ISOFORM 1).
    8. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-412 (ISOFORM 2).
      Tissue: Liver.
    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] OF 54-412 (ISOFORM 1).
      Tissue: Pancreas.
    10. "Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2."
      Kang C.B., Feng L., Chia J., Yoon H.S.
      Biochem. Biophys. Res. Commun. 337:30-38(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. Cited for: CATALYTIC ACTIVITY, COFACTOR.
    12. "A reassessment of the inhibitory capacity of human FKBP38 on calcineurin."
      Weiwad M., Edlich F., Erdmann F., Jarczowski F., Kilka S., Dorn M., Pechstein A., Fischer G.
      FEBS Lett. 579:1591-1596(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ABSENCE OF DIRECT INTERACTION WITH CALCINEURIN.
    13. "The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)."
      Kang C.B., Tai J., Chia J., Yoon H.S.
      FEBS Lett. 579:1469-1476(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCL2.
    14. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Bcl-2 localized at the nuclear compartment induces apoptosis after transient overexpression."
      Portier B.P., Taglialatela G.
      J. Biol. Chem. 281:40493-40502(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCL2.
    16. "Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells."
      Wang J., Tong W., Zhang X., Chen L., Yi Z., Pan T., Hu Y., Xiang L., Yuan Z.
      FEBS Lett. 580:4392-4400(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCV NS5A.
    17. "Regulation of apoptosis and neurite extension by FKBP38 is required for neural tube formation in the mouse."
      Shirane M., Ogawa M., Motoyama J., Nakayama K.I.
      Genes Cells 13:635-651(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZFYVE27.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Solution structure of the FK506-binding domain of human FKBP38."
      Maestre-Martinez M., Edlich F., Jarczowski F., Weiwad M., Fischer G., Luecke C.
      J. Biomol. NMR 34:197-202(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 92-210.
    20. "Solution structure of RSGI RUH-047, an FKBP domain from human cDNA."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 91-205.
    21. "Structure of the human FK-506 binding protein 8."
      Structural genomics consortium (SGC)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 90-205.
    22. "A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-2 binding."
      Maestre-Martinez M., Haupt K., Edlich F., Neumann P., Parthier C., Stubbs M.T., Fischer G., Lucke C.
      J. Mol. Recognit. 24:23-34(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 92-210, METAL-BINDING SITES, MUTAGENESIS OF ASP-149 AND ASP-151.

    Entry informationi

    Entry nameiFKBP8_HUMAN
    AccessioniPrimary (citable) accession number: Q14318
    Secondary accession number(s): C8C9T5
    , Q53GU3, Q7Z349, Q86YK6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 150 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

    Miscellaneous

    Binds the immunosuppressant FK506 only in its calmodulin/calcium activated form.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3