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)

Q9QUR7

- PIN1_MOUSE

UniProt

Q9QUR7 - PIN1_MOUSE

Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Gene

Pin1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation By similarity. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation By similarity. Binds and targets BCL6 and PML for degradation in a phosphorylation-dependent manner.By similarity1 Publication

    Catalytic activityi

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

    GO - Molecular functioni

    1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. protein folding Source: UniProtKB-KW
    3. regulation of cell proliferation Source: MGI
    4. regulation of cytokinesis Source: MGI

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    Cell cycle

    Enzyme and pathway databases

    BRENDAi5.2.1.8. 3474.
    ReactomeiREACT_198532. Negative regulators of RIG-I/MDA5 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8)
    Alternative name(s):
    Peptidyl-prolyl cis-trans isomerase Pin1
    Short name:
    PPIase Pin1
    Gene namesi
    Name:Pin1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1346036. Pin1.

    Subcellular locationi

    Nucleus By similarity. Nucleus speckle By similarity. Cytoplasm By similarity
    Note: Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-73 by DAPK1 results in inhibition of its nuclear localization By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nuclear speck Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Animals display more and larger germinal centers.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 165165Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1PRO_0000193436Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481N6-acetyllysineBy similarity
    Modified residuei73 – 731Phosphoserine; by DAPK1By similarity
    Modified residuei110 – 1101PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation at Ser-73 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9QUR7.
    PaxDbiQ9QUR7.
    PRIDEiQ9QUR7.

    PTM databases

    PhosphoSiteiQ9QUR7.

    Expressioni

    Gene expression databases

    BgeeiQ9QUR7.
    GenevestigatoriQ9QUR7.

    Interactioni

    Subunit structurei

    Interacts with STIL. Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX. Interacts with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon NGF stimulation. Interacts with PML and BCL-6.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GphnQ8BUV36EBI-2432975,EBI-771218
    Tp53P023403EBI-2432975,EBI-474016

    Protein-protein interaction databases

    BioGridi204839. 9 interactions.
    DIPiDIP-44280N.
    IntActiQ9QUR7. 6 interactions.
    MINTiMINT-4107624.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QUR7.
    SMRiQ9QUR7. Positions 1-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 3935WWPROSITE-ProRule annotationAdd
    BLAST
    Domaini54 – 165112PpiCPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The WW domain is required for the interaction with STIL and KIF20B.

    Sequence similaritiesi

    Contains 1 PpiC domain.PROSITE-ProRule annotation
    Contains 1 WW domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0760.
    GeneTreeiENSGT00640000091578.
    HOGENOMiHOG000275331.
    HOVERGENiHBG002101.
    InParanoidiQ9QUR7.
    KOiK09578.
    OMAiKLKHYMA.
    OrthoDBiEOG7S4X82.
    PhylomeDBiQ9QUR7.
    TreeFamiTF101101.

    Family and domain databases

    InterProiIPR000297. PPIase_PpiC.
    IPR023058. PPIase_PpiC_CS.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00639. Rotamase. 1 hit.
    PF00397. WW. 1 hit.
    [Graphical view]
    SMARTiSM00456. WW. 1 hit.
    [Graphical view]
    SUPFAMiSSF51045. SSF51045. 1 hit.
    PROSITEiPS01096. PPIC_PPIASE_1. 1 hit.
    PS50198. PPIC_PPIASE_2. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QUR7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGG STVGGSSKNG    50
    QGEPAKVRCS HLLVKHSQSR RPSSWRQEKI TRSKEEALEL INGYIQKIKS 100
    GEEDFESLAS QFSDCSSAKA RGDLGPFSRG QMQKPFEDAS FALRTGEMSG 150
    PVFTDSGIHI ILRTE 165
    Length:165
    Mass (Da):18,370
    Last modified:May 1, 2000 - v1
    Checksum:i188E95F009176B1F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009691 mRNA. Translation: BAA87037.1.
    AB009692 Genomic DNA. Translation: BAA87038.1.
    AK002665 mRNA. Translation: BAB22270.1.
    AK003369 mRNA. Translation: BAB22743.1.
    AK054045 mRNA. Translation: BAC35631.1.
    AK150652 mRNA. Translation: BAE29739.1.
    AK160228 mRNA. Translation: BAE35702.1.
    BC038254 mRNA. Translation: AAH38254.1.
    CCDSiCCDS22882.1.
    PIRiJC7136.
    RefSeqiNP_075860.1. NM_023371.3.
    UniGeneiMm.7906.

    Genome annotation databases

    EnsembliENSMUST00000034689; ENSMUSP00000034689; ENSMUSG00000032171.
    GeneIDi23988.
    KEGGimmu:23988.
    UCSCiuc009ojd.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009691 mRNA. Translation: BAA87037.1 .
    AB009692 Genomic DNA. Translation: BAA87038.1 .
    AK002665 mRNA. Translation: BAB22270.1 .
    AK003369 mRNA. Translation: BAB22743.1 .
    AK054045 mRNA. Translation: BAC35631.1 .
    AK150652 mRNA. Translation: BAE29739.1 .
    AK160228 mRNA. Translation: BAE35702.1 .
    BC038254 mRNA. Translation: AAH38254.1 .
    CCDSi CCDS22882.1.
    PIRi JC7136.
    RefSeqi NP_075860.1. NM_023371.3.
    UniGenei Mm.7906.

    3D structure databases

    ProteinModelPortali Q9QUR7.
    SMRi Q9QUR7. Positions 1-165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204839. 9 interactions.
    DIPi DIP-44280N.
    IntActi Q9QUR7. 6 interactions.
    MINTi MINT-4107624.

    PTM databases

    PhosphoSitei Q9QUR7.

    Proteomic databases

    MaxQBi Q9QUR7.
    PaxDbi Q9QUR7.
    PRIDEi Q9QUR7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034689 ; ENSMUSP00000034689 ; ENSMUSG00000032171 .
    GeneIDi 23988.
    KEGGi mmu:23988.
    UCSCi uc009ojd.1. mouse.

    Organism-specific databases

    CTDi 5300.
    MGIi MGI:1346036. Pin1.

    Phylogenomic databases

    eggNOGi COG0760.
    GeneTreei ENSGT00640000091578.
    HOGENOMi HOG000275331.
    HOVERGENi HBG002101.
    InParanoidi Q9QUR7.
    KOi K09578.
    OMAi KLKHYMA.
    OrthoDBi EOG7S4X82.
    PhylomeDBi Q9QUR7.
    TreeFami TF101101.

    Enzyme and pathway databases

    BRENDAi 5.2.1.8. 3474.
    Reactomei REACT_198532. Negative regulators of RIG-I/MDA5 signaling.

    Miscellaneous databases

    NextBioi 303885.
    PROi Q9QUR7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9QUR7.
    Genevestigatori Q9QUR7.

    Family and domain databases

    InterProi IPR000297. PPIase_PpiC.
    IPR023058. PPIase_PpiC_CS.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00639. Rotamase. 1 hit.
    PF00397. WW. 1 hit.
    [Graphical view ]
    SMARTi SM00456. WW. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51045. SSF51045. 1 hit.
    PROSITEi PS01096. PPIC_PPIASE_1. 1 hit.
    PS50198. PPIC_PPIASE_2. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G0 arrest."
      Fujimori F., Takahashi K., Uchida C., Uchida T.
      Biochem. Biophys. Res. Commun. 265:658-663(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "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].
      Strain: C57BL/6J.
      Tissue: Bone marrow, Embryo, Kidney and Oviduct.
    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: FVB/N.
      Tissue: Kidney.
    4. "Sil phosphorylation in a Pin1 binding domain affects the duration of the spindle checkpoint."
      Campaner S., Kaldis P., Izraeli S., Kirsch I.R.
      Mol. Cell. Biol. 25:6660-6672(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STIL.
    5. "Genotoxic stress regulates expression of the proto-oncogene Bcl6 in germinal center B cells."
      Phan R.T., Saito M., Kitagawa Y., Means A.R., Dalla-Favera R.
      Nat. Immunol. 8:1132-1139(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BCL6 STABILITY, DISRUPTION PHENOTYPE.
    6. "Protein kinase-X interacts with Pin-1 and Polycystin-1 during mouse kidney development."
      Li X., Hyink D.P., Radbill B., Sudol M., Zhang H., Zheleznova N.N., Wilson P.D.
      Kidney Int. 76:54-62(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKX.

    Entry informationi

    Entry nameiPIN1_MOUSE
    AccessioniPrimary (citable) accession number: Q9QUR7
    Secondary accession number(s): Q543B3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 108 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