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Q00688

- FKBP3_HUMAN

UniProt

Q00688 - FKBP3_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase FKBP3

Gene

FKBP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins.

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited preferentially by rapamycin over FK506.

    GO - Molecular functioni

    1. FK506 binding Source: RefGenome
    2. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. receptor activity Source: ProtInc

    GO - Biological processi

    1. chaperone-mediated protein folding Source: RefGenome
    2. protein peptidyl-prolyl isomerization Source: RefGenome

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase FKBP3 (EC:5.2.1.8)
    Short name:
    PPIase FKBP3
    Alternative name(s):
    25 kDa FK506-binding protein
    Short name:
    25 kDa FKBP
    Short name:
    FKBP-25
    FK506-binding protein 3
    Short name:
    FKBP-3
    Immunophilin FKBP25
    Rapamycin-selective 25 kDa immunophilin
    Rotamase
    Gene namesi
    Name:FKBP3
    Synonyms:FKBP25
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:3719. FKBP3.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: RefGenome
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28160.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 224223Peptidyl-prolyl cis-trans isomerase FKBP3PRO_0000075307Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei36 – 361Phosphoserine1 Publication
    Modified residuei99 – 991N6-acetyllysineBy similarity
    Modified residuei152 – 1521Phosphoserine1 Publication
    Modified residuei170 – 1701N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ00688.
    PaxDbiQ00688.
    PeptideAtlasiQ00688.
    PRIDEiQ00688.

    PTM databases

    PhosphoSiteiQ00688.

    Expressioni

    Gene expression databases

    ArrayExpressiQ00688.
    BgeeiQ00688.
    CleanExiHS_FKBP3.
    GenevestigatoriQ00688.

    Organism-specific databases

    HPAiCAB012232.
    CAB012520.
    HPA000864.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MDM2Q009872EBI-1044081,EBI-389668
    PARP2Q9UGN52EBI-1044081,EBI-2795348

    Protein-protein interaction databases

    BioGridi108577. 38 interactions.
    IntActiQ00688. 3 interactions.
    STRINGi9606.ENSP00000216330.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 165
    Helixi23 – 3210
    Helixi35 – 406
    Helixi47 – 515
    Helixi56 – 6914
    Beta strandi111 – 1177
    Beta strandi130 – 1389
    Beta strandi144 – 1474
    Turni155 – 1573
    Beta strandi162 – 1654
    Turni166 – 1694
    Helixi173 – 1797
    Beta strandi187 – 1926
    Helixi194 – 1963
    Turni197 – 2015
    Helixi204 – 2063
    Beta strandi214 – 22411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PBKX-ray2.50A109-224[»]
    2KFVNMR-A1-73[»]
    ProteinModelPortaliQ00688.
    SMRiQ00688. Positions 1-73, 109-224.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00688.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini128 – 22497PPIase FKBP-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the FKBP-type PPIase family.Curated
    Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0545.
    HOGENOMiHOG000007963.
    HOVERGENiHBG105391.
    InParanoidiQ00688.
    KOiK09570.
    OMAiAMEHINA.
    OrthoDBiEOG7BZVT6.
    PhylomeDBiQ00688.
    TreeFamiTF105293.

    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.

    Q00688-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ EHGSDSFLAE HKLLGNIKNV    50
    AKTANKDHLV TAYNHLFETK RFKGTESISK VSEQVKNVKL NEDKPKETKS 100
    EETLDEGPPK YTKSVLKKGD KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ 150
    TSAKKKKNAK PLSFKVGVGK VIRGWDEALL TMSKGEKARL EIEPEWAYGK 200
    KGQPDAKIPP NAKLTFEVEL VDID 224
    Length:224
    Mass (Da):25,177
    Last modified:April 1, 1993 - v1
    Checksum:iC144C5AAB7EA9522
    GO

    Sequence cautioni

    The sequence AAA58474.1 differs from that shown. Reason: Frameshift at position 197.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811T → A in AAA58474. (PubMed:1375932)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96256 mRNA. Translation: AAA58471.1.
    M90309 mRNA. Translation: AAA58475.1.
    M90820 mRNA. Translation: AAA58474.1. Frameshift.
    BT006904 mRNA. Translation: AAP35550.1.
    AK311915 mRNA. Translation: BAG34856.1.
    CH471078 Genomic DNA. Translation: EAW65785.1.
    BC016288 mRNA. Translation: AAH16288.1.
    BC020809 mRNA. Translation: AAH20809.1.
    CCDSiCCDS9683.1.
    PIRiJQ1522.
    RefSeqiNP_002004.1. NM_002013.3.
    UniGeneiHs.509226.

    Genome annotation databases

    EnsembliENST00000216330; ENSP00000216330; ENSG00000100442.
    ENST00000396062; ENSP00000379374; ENSG00000100442.
    GeneIDi2287.
    KEGGihsa:2287.
    UCSCiuc010tqf.2. human.

    Polymorphism databases

    DMDMi232096.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96256 mRNA. Translation: AAA58471.1 .
    M90309 mRNA. Translation: AAA58475.1 .
    M90820 mRNA. Translation: AAA58474.1 . Frameshift.
    BT006904 mRNA. Translation: AAP35550.1 .
    AK311915 mRNA. Translation: BAG34856.1 .
    CH471078 Genomic DNA. Translation: EAW65785.1 .
    BC016288 mRNA. Translation: AAH16288.1 .
    BC020809 mRNA. Translation: AAH20809.1 .
    CCDSi CCDS9683.1.
    PIRi JQ1522.
    RefSeqi NP_002004.1. NM_002013.3.
    UniGenei Hs.509226.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PBK X-ray 2.50 A 109-224 [» ]
    2KFV NMR - A 1-73 [» ]
    ProteinModelPortali Q00688.
    SMRi Q00688. Positions 1-73, 109-224.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108577. 38 interactions.
    IntActi Q00688. 3 interactions.
    STRINGi 9606.ENSP00000216330.

    Chemistry

    BindingDBi Q00688.
    ChEMBLi CHEMBL4746.

    PTM databases

    PhosphoSitei Q00688.

    Polymorphism databases

    DMDMi 232096.

    Proteomic databases

    MaxQBi Q00688.
    PaxDbi Q00688.
    PeptideAtlasi Q00688.
    PRIDEi Q00688.

    Protocols and materials databases

    DNASUi 2287.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216330 ; ENSP00000216330 ; ENSG00000100442 .
    ENST00000396062 ; ENSP00000379374 ; ENSG00000100442 .
    GeneIDi 2287.
    KEGGi hsa:2287.
    UCSCi uc010tqf.2. human.

    Organism-specific databases

    CTDi 2287.
    GeneCardsi GC14M045584.
    HGNCi HGNC:3719. FKBP3.
    HPAi CAB012232.
    CAB012520.
    HPA000864.
    MIMi 186947. gene.
    neXtProti NX_Q00688.
    PharmGKBi PA28160.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0545.
    HOGENOMi HOG000007963.
    HOVERGENi HBG105391.
    InParanoidi Q00688.
    KOi K09570.
    OMAi AMEHINA.
    OrthoDBi EOG7BZVT6.
    PhylomeDBi Q00688.
    TreeFami TF105293.

    Miscellaneous databases

    ChiTaRSi FKBP3. human.
    EvolutionaryTracei Q00688.
    GeneWikii FKBP3.
    GenomeRNAii 2287.
    NextBioi 9295.
    PROi Q00688.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00688.
    Bgeei Q00688.
    CleanExi HS_FKBP3.
    Genevestigatori Q00688.

    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. "Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin binding protein."
      Wiederrecht G., Martin M., Sigal N., Siekierka J.J.
      Biochem. Biophys. Res. Commun. 185:298-303(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein."
      Hung D.T., Schreiber S.L.
      Biochem. Biophys. Res. Commun. 184:733-738(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Molecular cloning of a 25-kDa high affinity rapamycin binding protein, FKBP25."
      Jin Y.-J., Burakoff S.J., Bierer B.E.
      J. Biol. Chem. 267:10942-10945(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Thymus.
    4. "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].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Uterus.
    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].
      Tissue: Skeletal muscle and Skin.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "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-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Structure of the human 25 kDa FK506 binding protein complexed with rapamycin."
      Liang J., Hung D.T., Schreiber S.L., Clardy J.
      J. Am. Chem. Soc. 118:1231-1232(1996)
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 109-224.

    Entry informationi

    Entry nameiFKBP3_HUMAN
    AccessioniPrimary (citable) accession number: Q00688
    Secondary accession number(s): B2R4Q9, Q14317
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 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 14
      Human chromosome 14: 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