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Q9Z247

- FKBP9_MOUSE

UniProt

Q9Z247 - FKBP9_MOUSE

Protein

Peptidyl-prolyl cis-trans isomerase FKBP9

Gene

Fkbp9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins during protein synthesis.

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by FK506.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi501 – 512121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi546 – 557122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. FK506 binding Source: RefGenome
    3. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome

    GO - Biological processi

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

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase FKBP9 (EC:5.2.1.8)
    Short name:
    PPIase FKBP9
    Alternative name(s):
    63 kDa FK506-binding protein
    Short name:
    63 kDa FKBP
    Short name:
    FKBP-63
    FK506-binding protein 9
    Short name:
    FKBP-9
    FKBP65RS
    Rotamase
    Gene namesi
    Name:Fkbp9
    Synonyms:Fkbp60, Fkbp63
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1350921. Fkbp9.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 570546Peptidyl-prolyl cis-trans isomerase FKBP9PRO_0000025516Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi174 – 1741N-linked (GlcNAc...)1 Publication
    Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylated.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z247.
    PaxDbiQ9Z247.
    PRIDEiQ9Z247.

    Expressioni

    Tissue specificityi

    Predominantly expressed in heart, skeletal muscle, lung, liver and kidney. Lower levels found in brain, spleen and testis.2 Publications

    Developmental stagei

    Expressed in all developmental stages.1 Publication

    Gene expression databases

    BgeeiQ9Z247.
    CleanExiMM_FKBP9.
    GenevestigatoriQ9Z247.

    Interactioni

    Protein-protein interaction databases

    BioGridi205110. 1 interaction.
    IntActiQ9Z247. 3 interactions.
    MINTiMINT-4095122.
    STRINGi10090.ENSMUSP00000031795.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z247.
    SMRiQ9Z247. Positions 50-564.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 14289PPIase FKBP-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini166 – 25489PPIase FKBP-type 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini278 – 36588PPIase FKBP-type 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini389 – 47789PPIase FKBP-type 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini488 – 52336EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini533 – 56836EF-hand 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi567 – 5704Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Contains 2 EF-hand domains.PROSITE-ProRule annotation
    Contains 4 PPIase FKBP-type domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0545.
    GeneTreeiENSGT00530000062784.
    HOGENOMiHOG000230960.
    HOVERGENiHBG051620.
    InParanoidiQ9Z247.
    KOiK09575.
    OMAiEMIVKNM.
    OrthoDBiEOG7T1R9S.
    PhylomeDBiQ9Z247.
    TreeFamiTF105296.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view]
    PANTHERiPTHR10516. PTHR10516. 1 hit.
    PfamiPF00254. FKBP_C. 4 hits.
    [Graphical view]
    SMARTiSM00054. EFh. 2 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 2 hits.
    PS00014. ER_TARGET. 1 hit.
    PS50059. FKBP_PPIASE. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9Z247-1 [UniParc]FASTAAdd to Basket

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    MALGARGWRR RSLLLLLLWV TGQAAPVLGL AVSSELQIQQ SFVPDECPRT    50
    VHSGDFVRYH YVGTFLDGQK FDSSYDRDST FNVFVGKGQL IAGMDQALVG 100
    MCVNERRLVT IPPNLAYGSE GVSGVIPPNS VLHFDVLLVD IWNSEDQVHI 150
    QTYFKPPSCP RTIQVSDFVR YHYNGTFLDG TLFDSSHNRM KTYDTYVGIG 200
    WLIPGMDKGL LGMCVGEKRI ITVPPFLAYG EEGDGKDIPG QASLVFDVAL 250
    LDLHNPKDTI SIENKVVPEN CERRSQSGDF LRYHYNGTLL DGTLFDSSYS 300
    RNHTFDTYIG QGYVIPGMDE GLLGVCIGER RRIVVPPHLG YGEKGRGSIP 350
    GSAVLVFDIH VIDFHNPSDS ISITSHYKPP DCSVLSKKGD YLKYHYNASL 400
    LDGTLLDSTW NLGKTYNIVL GSGQVVLGMD MGLREMCVGE KRTVIIPPHL 450
    GYGEAGVDGE VPGSAVLVFD IELLELVSGL PEGYMFIWNG EVSPNLFEEI 500
    DRDGNGEVLL EEFSEYIHAQ VATGKGKLAP GFNAEMIVKN MFTNQDRNGD 550
    GKVTAEEFKL KDQEAKHDEL 570
    Length:570
    Mass (Da):62,995
    Last modified:May 1, 1999 - v1
    Checksum:iDFE8B8F2F6A0F1DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401Q → R in AAH26133. (PubMed:15489334)Curated
    Sequence conflicti149 – 1491H → Q in AAH26133. (PubMed:15489334)Curated
    Sequence conflicti234 – 2363DGK → NGE in AAF79215. (PubMed:11710534)Curated
    Sequence conflicti321 – 3211G → S in BAB25071. (PubMed:16141072)Curated
    Sequence conflicti351 – 3511G → A in AAF79215. (PubMed:11710534)Curated
    Sequence conflicti353 – 3531A → T in BAB25071. (PubMed:16141072)Curated
    Sequence conflicti361 – 3611V → F in AAF79215. (PubMed:11710534)Curated
    Sequence conflicti364 – 3641F → V in AAF79215. (PubMed:11710534)Curated
    Sequence conflicti378 – 3781K → N in AAF79215. (PubMed:11710534)Curated
    Sequence conflicti386 – 3861S → I in AAF79215. (PubMed:11710534)Curated
    Sequence conflicti475 – 4751E → D in AAF79215. (PubMed:11710534)Curated
    Sequence conflicti548 – 5481N → S in AAH43129. (PubMed:15489334)Curated
    Sequence conflicti550 – 5501D → N in AAF79215. (PubMed:11710534)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090334 mRNA. Translation: AAC72964.1.
    AF279263 mRNA. Translation: AAF79215.1.
    BC026133 mRNA. Translation: AAH26133.1.
    BC043129 mRNA. Translation: AAH43129.1.
    AK007499 mRNA. Translation: BAB25071.1.
    CCDSiCCDS39494.1.
    RefSeqiNP_036186.2. NM_012056.2.
    UniGeneiMm.20943.

    Genome annotation databases

    EnsembliENSMUST00000031795; ENSMUSP00000031795; ENSMUSG00000029781.
    GeneIDi27055.
    KEGGimmu:27055.
    UCSCiuc009cbp.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090334 mRNA. Translation: AAC72964.1 .
    AF279263 mRNA. Translation: AAF79215.1 .
    BC026133 mRNA. Translation: AAH26133.1 .
    BC043129 mRNA. Translation: AAH43129.1 .
    AK007499 mRNA. Translation: BAB25071.1 .
    CCDSi CCDS39494.1.
    RefSeqi NP_036186.2. NM_012056.2.
    UniGenei Mm.20943.

    3D structure databases

    ProteinModelPortali Q9Z247.
    SMRi Q9Z247. Positions 50-564.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 205110. 1 interaction.
    IntActi Q9Z247. 3 interactions.
    MINTi MINT-4095122.
    STRINGi 10090.ENSMUSP00000031795.

    Proteomic databases

    MaxQBi Q9Z247.
    PaxDbi Q9Z247.
    PRIDEi Q9Z247.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031795 ; ENSMUSP00000031795 ; ENSMUSG00000029781 .
    GeneIDi 27055.
    KEGGi mmu:27055.
    UCSCi uc009cbp.2. mouse.

    Organism-specific databases

    CTDi 11328.
    MGIi MGI:1350921. Fkbp9.

    Phylogenomic databases

    eggNOGi COG0545.
    GeneTreei ENSGT00530000062784.
    HOGENOMi HOG000230960.
    HOVERGENi HBG051620.
    InParanoidi Q9Z247.
    KOi K09575.
    OMAi EMIVKNM.
    OrthoDBi EOG7T1R9S.
    PhylomeDBi Q9Z247.
    TreeFami TF105296.

    Miscellaneous databases

    ChiTaRSi FKBP9. mouse.
    NextBioi 304999.
    PROi Q9Z247.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Z247.
    CleanExi MM_FKBP9.
    Genevestigatori Q9Z247.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view ]
    PANTHERi PTHR10516. PTHR10516. 1 hit.
    Pfami PF00254. FKBP_C. 4 hits.
    [Graphical view ]
    SMARTi SM00054. EFh. 2 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 2 hits.
    PS00014. ER_TARGET. 1 hit.
    PS50059. FKBP_PPIASE. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Biochemical analysis of mouse FKBP60, a novel member of the FKBP family."
      Shadidy M., Caubit X., Olsen R., Seternes O.M., Moens U., Krauss S.
      Biochim. Biophys. Acta 1446:295-307(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, CALCIUM-BINDING.
    2. "Identification and genetic mapping of the mouse Fkbp9 gene encoding a new member of FK506-binding protein family."
      Jo D., Lyu M.S., Cho E.-G., Park D., Kozak C.A., Kim M.G.
      Mol. Cells 12:272-275(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Thymus.
    3. "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].
      Strain: C57BL/6 and Czech II.
      Tissue: Fetal brain and Mammary tumor.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-570.
      Strain: C57BL/6J.
      Tissue: Pancreas.
    5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174.

    Entry informationi

    Entry nameiFKBP9_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z247
    Secondary accession number(s): Q80ZZ6
    , Q8R386, Q9CVM0, Q9JHX5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3