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Q02790

- FKBP4_HUMAN

UniProt

Q02790 - FKBP4_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase FKBP4

Gene

FKBP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.5 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by FK506.1 Publication

    GO - Molecular functioni

    1. ATP binding Source: Ensembl
    2. FK506 binding Source: UniProtKB
    3. GTP binding Source: Ensembl
    4. heat shock protein binding Source: UniProtKB
    5. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
    6. poly(A) RNA binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein binding, bridging Source: ProtInc

    GO - Biological processi

    1. androgen receptor signaling pathway Source: Ensembl
    2. chaperone-mediated protein folding Source: UniProtKB
    3. copper ion transport Source: Ensembl
    4. embryo implantation Source: Ensembl
    5. male sex differentiation Source: Ensembl
    6. negative regulation of microtubule polymerization Source: Ensembl
    7. negative regulation of microtubule polymerization or depolymerization Source: UniProtKB
    8. negative regulation of neuron projection development Source: UniProtKB
    9. prostate gland development Source: Ensembl
    10. protein complex localization Source: Ensembl
    11. protein folding Source: ProtInc
    12. protein peptidyl-prolyl isomerization Source: GOC
    13. steroid hormone receptor complex assembly Source: Ensembl

    Keywords - Molecular functioni

    Chaperone, Isomerase, Rotamase

    Enzyme and pathway databases

    ReactomeiREACT_200624. Attenuation phase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase FKBP4 (EC:5.2.1.8)
    Short name:
    PPIase FKBP4
    Alternative name(s):
    51 kDa FK506-binding protein
    Short name:
    FKBP51
    52 kDa FK506-binding protein
    Short name:
    52 kDa FKBP
    Short name:
    FKBP-52
    59 kDa immunophilin
    Short name:
    p59
    FK506-binding protein 4
    Short name:
    FKBP-4
    FKBP59
    HSP-binding immunophilin
    Short name:
    HBI
    Immunophilin FKBP52
    Rotamase
    Cleaved into the following chain:
    Gene namesi
    Name:FKBP4
    Synonyms:FKBP52
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:3720. FKBP4.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Mitochondrion. Nucleus. Cytoplasmcytoskeleton By similarity
    Note: Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor.

    GO - Cellular componenti

    1. axonal growth cone Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytosol Source: UniProtKB
    4. endoplasmic reticulum membrane Source: RefGenome
    5. extracellular vesicular exosome Source: UniProt
    6. microtubule Source: UniProtKB-KW
    7. mitochondrion Source: UniProtKB-SubCell
    8. neuronal cell body Source: Ensembl
    9. nucleus Source: HPA
    10. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 682FD → DV: Decreased catalytic activity toward TRPC1. 1 Publication

    Organism-specific databases

    PharmGKBiPA28161.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 459459Peptidyl-prolyl cis-trans isomerase FKBP4PRO_0000391468Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate4 Publications
    Chaini2 – 459458Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processedPRO_0000075318Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine; in peptidyl-prolyl cis-trans isomerase FKBP4; alternate1 Publication
    Modified residuei2 – 21N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partial1 Publication
    Modified residuei143 – 1431Phosphothreonine; by CK2By similarity
    Modified residuei282 – 2821N6-acetyllysine1 Publication
    Modified residuei451 – 4511Phosphoserine3 Publications
    Modified residuei453 – 4531Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylation by CK2 results in loss of HSP90 binding activity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ02790.
    PaxDbiQ02790.
    PeptideAtlasiQ02790.
    PRIDEiQ02790.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00219005.

    PTM databases

    PhosphoSiteiQ02790.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ02790.
    BgeeiQ02790.
    CleanExiHS_FKBP4.
    GenevestigatoriQ02790.

    Organism-specific databases

    HPAiCAB017441.
    HPA006148.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Associates with HSP90AA1 and HSP70 in steroid hormone receptor complexes. Also interacts with peroxisomal phytanoyl-CoA alpha-hydroxylase (PHYH). Interacts with NR3C1 and dynein. Interacts with HSF1 in the HSP90 complex. Associates with tubulin. Interacts with MAPT/TAU. Interacts (via TPR domain) with S100A1, S100A2 and S100A6; the interaction is Ca2+ dependent. Interaction with S100A1 and S100A2 (but not with S100A6) leads to inhibition of FKBP4-HSP90 interaction. Interacts with dynein; causes partially NR3C1 transport to the nucleus.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGO2Q9UKV82EBI-1047444,EBI-528269
    CDC37Q165433EBI-1047444,EBI-295634
    HSP90AA1P079008EBI-1047444,EBI-296047
    S100a1P354677EBI-1047444,EBI-6477109From a different organism.
    S100A2P290343EBI-1047444,EBI-752230
    S100A6P067033EBI-1047444,EBI-352877

    Protein-protein interaction databases

    BioGridi108578. 49 interactions.
    DIPiDIP-50866N.
    IntActiQ02790. 42 interactions.
    MINTiMINT-3024864.
    STRINGi9606.ENSP00000001008.

    Structurei

    Secondary structure

    1
    459
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 243
    Beta strandi30 – 3910
    Beta strandi42 – 443
    Beta strandi52 – 6110
    Beta strandi66 – 694
    Helixi70 – 723
    Beta strandi73 – 753
    Beta strandi77 – 804
    Beta strandi83 – 864
    Helixi88 – 947
    Beta strandi102 – 1076
    Helixi109 – 1113
    Turni112 – 1165
    Turni119 – 1213
    Beta strandi128 – 13811
    Beta strandi147 – 15610
    Beta strandi159 – 1613
    Beta strandi169 – 17810
    Beta strandi181 – 19111
    Turni192 – 1943
    Helixi195 – 1984
    Helixi202 – 2087
    Beta strandi216 – 2216
    Helixi223 – 2253
    Turni226 – 2305
    Helixi233 – 2353
    Beta strandi243 – 25311
    Helixi258 – 2603
    Helixi263 – 28321
    Helixi286 – 29914
    Turni300 – 3023
    Helixi309 – 33123
    Helixi335 – 34814
    Helixi353 – 36513
    Helixi369 – 38214
    Helixi387 – 42438

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N1AX-ray2.40A/B1-140[»]
    1P5QX-ray2.80A/B/C146-459[»]
    1Q1CX-ray1.90A2-260[»]
    1QZ2X-ray3.00A/B/C145-459[»]
    4DRJX-ray1.80A1-140[»]
    4LAVX-ray1.80A/B16-260[»]
    4LAWX-ray2.40A/B16-260[»]
    4LAXX-ray2.01A16-260[»]
    4LAYX-ray1.70A1-260[»]
    ProteinModelPortaliQ02790.
    SMRiQ02790. Positions 22-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02790.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 13889PPIase FKBP-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini167 – 25387PPIase FKBP-type 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati270 – 30334TPR 1Add
    BLAST
    Repeati319 – 35234TPR 2Add
    BLAST
    Repeati353 – 38634TPR 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni267 – 400134Interaction with tubulinBy similarityAdd
    BLAST

    Domaini

    The PPIase activity is mainly due to the fisrt PPIase FKBP-type domain (1-138 AA).By similarity
    The C-terminal region (AA 375-458) is required to prevent tubulin polymerization.By similarity
    The chaperone activity resides in the C-terminal region, mainly between amino acids 264 and 400.By similarity
    The TPR repeats mediate mitochondrial localization.

    Sequence similaritiesi

    Contains 2 PPIase FKBP-type domains.PROSITE-ProRule annotation
    Contains 3 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0545.
    HOGENOMiHOG000256916.
    HOVERGENiHBG051624.
    InParanoidiQ02790.
    KOiK09571.
    OMAiNAELKYE.
    PhylomeDBiQ02790.
    TreeFamiTF354214.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    InterProiIPR023566. 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. 2 hits.
    PF00515. TPR_1. 3 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 3 hits.
    [Graphical view]
    PROSITEiPS50059. FKBP_PPIASE. 2 hits.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q02790-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAEEMKATE SGAQSAPLPM EGVDISPKQD EGVLKVIKRE GTGTEMPMIG    50
    DRVFVHYTGW LLDGTKFDSS LDRKDKFSFD LGKGEVIKAW DIAIATMKVG 100
    EVCHITCKPE YAYGSAGSPP KIPPNATLVF EVELFEFKGE DLTEEEDGGI 150
    IRRIQTRGEG YAKPNEGAIV EVALEGYYKD KLFDQRELRF EIGEGENLDL 200
    PYGLERAIQR MEKGEHSIVY LKPSYAFGSV GKEKFQIPPN AELKYELHLK 250
    SFEKAKESWE MNSEEKLEQS TIVKERGTVY FKEGKYKQAL LQYKKIVSWL 300
    EYESSFSNEE AQKAQALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS 350
    NNEKGLFRRG EAHLAVNDFE LARADFQKVL QLYPNNKAAK TQLAVCQQRI 400
    RRQLAREKKL YANMFERLAE EENKAKAEAS SGDHPTDTEM KEEQKSNTAG 450
    SQSQVETEA 459
    Length:459
    Mass (Da):51,805
    Last modified:January 23, 2007 - v3
    Checksum:i6A498105418D9435
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti436 – 4361T → P.
    Corresponds to variant rs1042228 [ dbSNP | Ensembl ].
    VAR_050624

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88279 mRNA. Translation: AAA36111.1.
    AC005841 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88889.1.
    CH471116 Genomic DNA. Translation: EAW88890.1.
    BC001786 mRNA. Translation: AAH01786.1.
    BC007924 mRNA. Translation: AAH07924.1.
    CCDSiCCDS8512.1.
    PIRiA46372.
    RefSeqiNP_002005.1. NM_002014.3.
    UniGeneiHs.524183.
    Hs.713721.

    Genome annotation databases

    EnsembliENST00000001008; ENSP00000001008; ENSG00000004478.
    GeneIDi2288.
    KEGGihsa:2288.
    UCSCiuc001qkz.3. human.

    Polymorphism databases

    DMDMi399866.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    A mind astray - Issue 118 of June 2010

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88279 mRNA. Translation: AAA36111.1 .
    AC005841 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88889.1 .
    CH471116 Genomic DNA. Translation: EAW88890.1 .
    BC001786 mRNA. Translation: AAH01786.1 .
    BC007924 mRNA. Translation: AAH07924.1 .
    CCDSi CCDS8512.1.
    PIRi A46372.
    RefSeqi NP_002005.1. NM_002014.3.
    UniGenei Hs.524183.
    Hs.713721.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N1A X-ray 2.40 A/B 1-140 [» ]
    1P5Q X-ray 2.80 A/B/C 146-459 [» ]
    1Q1C X-ray 1.90 A 2-260 [» ]
    1QZ2 X-ray 3.00 A/B/C 145-459 [» ]
    4DRJ X-ray 1.80 A 1-140 [» ]
    4LAV X-ray 1.80 A/B 16-260 [» ]
    4LAW X-ray 2.40 A/B 16-260 [» ]
    4LAX X-ray 2.01 A 16-260 [» ]
    4LAY X-ray 1.70 A 1-260 [» ]
    ProteinModelPortali Q02790.
    SMRi Q02790. Positions 22-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108578. 49 interactions.
    DIPi DIP-50866N.
    IntActi Q02790. 42 interactions.
    MINTi MINT-3024864.
    STRINGi 9606.ENSP00000001008.

    Chemistry

    BindingDBi Q02790.
    ChEMBLi CHEMBL4050.
    DrugBanki DB01093. Dimethyl sulfoxide.

    PTM databases

    PhosphoSitei Q02790.

    Polymorphism databases

    DMDMi 399866.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00219005.

    Proteomic databases

    MaxQBi Q02790.
    PaxDbi Q02790.
    PeptideAtlasi Q02790.
    PRIDEi Q02790.

    Protocols and materials databases

    DNASUi 2288.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000001008 ; ENSP00000001008 ; ENSG00000004478 .
    GeneIDi 2288.
    KEGGi hsa:2288.
    UCSCi uc001qkz.3. human.

    Organism-specific databases

    CTDi 2288.
    GeneCardsi GC12P002904.
    H-InvDB HIX0010330.
    HGNCi HGNC:3720. FKBP4.
    HPAi CAB017441.
    HPA006148.
    MIMi 600611. gene.
    neXtProti NX_Q02790.
    PharmGKBi PA28161.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0545.
    HOGENOMi HOG000256916.
    HOVERGENi HBG051624.
    InParanoidi Q02790.
    KOi K09571.
    OMAi NAELKYE.
    PhylomeDBi Q02790.
    TreeFami TF354214.

    Enzyme and pathway databases

    Reactomei REACT_200624. Attenuation phase.

    Miscellaneous databases

    ChiTaRSi FKBP4. human.
    EvolutionaryTracei Q02790.
    GeneWikii FKBP52.
    GenomeRNAii 2288.
    NextBioi 9299.
    PROi Q02790.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02790.
    Bgeei Q02790.
    CleanExi HS_FKBP4.
    Genevestigatori Q02790.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    InterProi 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. 2 hits.
    PF00515. TPR_1. 3 hits.
    [Graphical view ]
    SMARTi SM00028. TPR. 3 hits.
    [Graphical view ]
    PROSITEi PS50059. FKBP_PPIASE. 2 hits.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes."
      Peattie D.A., Harding M.W., Fleming M.A., Decenzo M.T., Lippke J.A., Livingston D.J., Benasutti M.
      Proc. Natl. Acad. Sci. U.S.A. 89:10974-10978(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Lymph and Uterus.
    5. Bienvenut W.V., Lourenco F., Olson M.F.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-28; 40-73; 75-121; 139-152; 158-179; 187-206; 211-250; 257-274; 277-313; 319-354; 359-399; 409-426 AND 446-459, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Mammary carcinoma and Ovarian carcinoma.
    6. "Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex."
      Tai P.-K.K., Albers M.W., Chang H., Faber L.E., Schreiber S.L.
      Science 256:1315-1318(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-25, SUBUNIT, FUNCTION.
      Tissue: Thymus.
    7. "The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins."
      Sanchez E.R., Faber L.E., Henzel W.J., Pratt W.B.
      Biochemistry 29:5145-5152(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
      Tissue: Lymphocyte.
    8. "The Hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13."
      Yem A.W., Tomasselli A.G., Heinrikson R.L., Zurcher-Neely H., Ruff V.A., Johnson R.A., Deibel M.R. Jr.
      J. Biol. Chem. 267:2868-2871(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-18.
      Tissue: T-cell.
    9. "Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex."
      Wiederrecht G., Hung S., Chan H.K., Marcy A., Martin M., Calaycay J., Boulton D., Sigal N., Kincaid R.L., Siekierka J.J.
      J. Biol. Chem. 267:21753-21760(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-32, SUBUNIT.
    10. "The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52."
      Bruner K.L., Derfoul A., Robertson N.M., Guerriero G., Fernandes-Alnemri T., Alnemri E.S., Litwack G.
      Recept. Signal Transduct. 7:85-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TERNARY COMPLEX WITH HSP90; HSP70 AND NR3C2, DISSOCIATION UPON ALDOSTERONE BINDING.
    11. "Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex."
      Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W.B., Toft D.O., Smith D.F., Voellmy R.
      J. Biol. Chem. 276:45791-45799(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSF1.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Peptidyl-prolyl isomerase FKBP52 controls chemotropic guidance of neuronal growth cones via regulation of TRPC1 channel opening."
      Shim S., Yuan J.P., Kim J.Y., Zeng W., Huang G., Milshteyn A., Kern D., Muallem S., Ming G.L., Worley P.F.
      Neuron 64:471-483(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRPC1, FUNCTION, MUTAGENESIS OF 67-PHE-ASP-68.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "S100 proteins regulate the interaction of Hsp90 with cyclophilin 40 and FKBP52 through their tetratricopeptide repeats."
      Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.
      FEBS Lett. 584:1119-1125(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH S100A1; S100A2 AND S100A6.
    19. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress."
      Gallo L.I., Lagadari M., Piwien-Pilipuk G., Galigniana M.D.
      J. Biol. Chem. 286:30152-30160(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH GLUCOCORTICOID RECEPTOR.
    22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Structure of the N-terminal domain of human FKBP52."
      Li P., Ding Y., Wu B., Shu C., Shen B., Rao Z.
      Acta Crystallogr. D 59:16-22(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-139.
    24. "3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex."
      Wu B., Li P., Liu Y., Lou Z., Ding Y., Shu C., Ye S., Bartlam M., Shen B., Rao Z.
      Proc. Natl. Acad. Sci. U.S.A. 101:8348-8353(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-458 IN COMPLEX WITH HSP90, SUBUNIT.

    Entry informationi

    Entry nameiFKBP4_HUMAN
    AccessioniPrimary (citable) accession number: Q02790
    Secondary accession number(s): D3DUQ1, Q9UCP1, Q9UCV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 167 of the entry and version 3 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 12
      Human chromosome 12: 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

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