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Q13526

- PIN1_HUMAN

UniProt

Q13526 - PIN1_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Gene

PIN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner.5 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. GTPase activating protein binding Source: BHF-UCL
    2. mitogen-activated protein kinase kinase binding Source: BHF-UCL
    3. peptidyl-prolyl cis-trans isomerase activity Source: BHF-UCL
    4. phosphoserine binding Source: BHF-UCL
    5. phosphothreonine binding Source: BHF-UCL
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cytokine-mediated signaling pathway Source: Reactome
    3. innate immune response Source: Reactome
    4. negative regulation of cell motility Source: BHF-UCL
    5. negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    6. negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    7. negative regulation of type I interferon production Source: Reactome
    8. positive regulation of protein phosphorylation Source: MGI
    9. positive regulation of Rho GTPase activity Source: BHF-UCL
    10. positive regulation of ubiquitin-protein transferase activity Source: BHF-UCL
    11. protein folding Source: UniProtKB-KW
    12. protein peptidyl-prolyl isomerization Source: GOC
    13. regulation of cytokinesis Source: MGI
    14. regulation of mitosis Source: ProtInc
    15. regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    Cell cycle

    Enzyme and pathway databases

    BRENDAi5.2.1.8. 2681.
    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    SignaLinkiQ13526.

    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
    Rotamase Pin1
    Gene namesi
    Name:PIN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:8988. PIN1.

    Subcellular locationi

    Nucleus. Nucleus speckle. Cytoplasm
    Note: Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. midbody Source: MGI
    3. nuclear speck Source: UniProtKB-SubCell
    4. nucleoplasm Source: Reactome
    5. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi23 – 231Y → A: Reduced affinity for KIF20B. 1 Publication
    Mutagenesisi71 – 711S → D or E: Loss of activity, nuclear localization and cellular function. 1 Publication

    Organism-specific databases

    PharmGKBiPA33320.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 163163Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1PRO_0000193435Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 461N6-acetyllysine1 Publication
    Modified residuei71 – 711Phosphoserine; by DAPK11 Publication
    Modified residuei108 – 1081Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-71 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13526.
    PaxDbiQ13526.
    PeptideAtlasiQ13526.
    PRIDEiQ13526.

    PTM databases

    PhosphoSiteiQ13526.

    Expressioni

    Tissue specificityi

    The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells.2 Publications

    Gene expression databases

    ArrayExpressiQ13526.
    BgeeiQ13526.
    CleanExiHS_PIN1.
    GenevestigatoriQ13526.

    Organism-specific databases

    HPAiCAB004528.
    CAB009326.

    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 (isoform PML-4) and BCL-6.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADARB1P7856312EBI-714158,EBI-2967304
    APPP05067-42EBI-714158,EBI-302641
    CDK10Q151315EBI-714158,EBI-1646959
    Grm5P31424-23EBI-714158,EBI-8830305From a different organism.
    Grm5Q3UVX52EBI-714158,EBI-8795045From a different organism.
    IRAK1P5161710EBI-714158,EBI-358664
    NEK6Q9HC983EBI-714158,EBI-740364
    NOTCH1P465319EBI-714158,EBI-636374
    RUNX2Q139507EBI-714158,EBI-976402
    SP140Q133424EBI-714158,EBI-2865100
    SULT4A1Q9BR014EBI-714158,EBI-6690555
    TP53P0463712EBI-714158,EBI-366083

    Protein-protein interaction databases

    BioGridi111317. 154 interactions.
    DIPiDIP-29306N.
    IntActiQ13526. 79 interactions.
    MINTiMINT-86298.
    STRINGi9606.ENSP00000247970.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 155
    Turni17 – 193
    Beta strandi22 – 265
    Turni27 – 293
    Beta strandi32 – 354
    Beta strandi39 – 413
    Beta strandi53 – 6210
    Beta strandi67 – 693
    Beta strandi75 – 773
    Helixi82 – 9817
    Beta strandi99 – 1013
    Helixi103 – 1108
    Helixi114 – 1185
    Beta strandi121 – 1266
    Helixi132 – 1409
    Beta strandi150 – 1523
    Beta strandi155 – 1639

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F8AX-ray1.84B1-163[»]
    1I6CNMR-A6-44[»]
    1I8GNMR-B6-44[»]
    1I8HNMR-B6-44[»]
    1NMVNMR-A1-163[»]
    1NMWNMR-A50-163[»]
    1PINX-ray1.35A1-163[»]
    1ZCNX-ray1.90A1-161[»]
    2F21X-ray1.50A1-162[»]
    2ITKX-ray1.45A1-163[»]
    2KBUNMR-A6-39[»]
    2KCFNMR-A6-39[»]
    2LB3NMR-A6-41[»]
    2M8INMR-A1-39[»]
    2M8JNMR-A1-39[»]
    2M9ENMR-A22-39[»]
    2M9FNMR-A6-39[»]
    2M9INMR-A6-39[»]
    2M9JNMR-A6-39[»]
    2Q5AX-ray1.50A1-163[»]
    2XP3X-ray2.00A1-163[»]
    2XP4X-ray1.80A1-163[»]
    2XP5X-ray1.90A1-163[»]
    2XP6X-ray1.90A1-163[»]
    2XP7X-ray2.00A1-163[»]
    2XP8X-ray2.10A1-163[»]
    2XP9X-ray1.90A1-163[»]
    2XPAX-ray1.90A1-163[»]
    2XPBX-ray2.00A1-163[»]
    2ZQSX-ray1.90A1-163[»]
    2ZQTX-ray1.46A1-163[»]
    2ZQUX-ray2.50A1-163[»]
    2ZQVX-ray2.50A1-163[»]
    2ZR4X-ray2.00A1-163[»]
    2ZR5X-ray2.60A1-163[»]
    2ZR6X-ray3.20A1-163[»]
    3I6CX-ray1.30A/B45-163[»]
    3IK8X-ray1.85A/B45-163[»]
    3IKDX-ray2.00A/B45-163[»]
    3IKGX-ray1.86A/B45-163[»]
    3JYJX-ray1.87A/B45-163[»]
    3KABX-ray2.19A1-163[»]
    3KACX-ray2.00A/B45-163[»]
    3KADX-ray1.95A1-163[»]
    3KAFX-ray2.30A1-163[»]
    3KAGX-ray1.90A1-163[»]
    3KAHX-ray2.30A1-163[»]
    3KAIX-ray1.90A1-163[»]
    3KCEX-ray1.90A1-163[»]
    3NTPX-ray1.76A1-163[»]
    3ODKX-ray2.30A1-163[»]
    3OOBX-ray1.89A1-163[»]
    3TC5X-ray1.40A1-163[»]
    3TCZX-ray2.10A6-163[»]
    3TDBX-ray2.27A6-163[»]
    4GWTX-ray2.25A6-39[»]
    4GWVX-ray3.05A6-39[»]
    ProteinModelPortaliQ13526.
    SMRiQ13526. Positions 1-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13526.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 3935WWPROSITE-ProRule annotationAdd
    BLAST
    Domaini52 – 163112PpiCPROSITE-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.
    HOGENOMiHOG000275331.
    HOVERGENiHBG002101.
    InParanoidiQ13526.
    KOiK09578.
    OMAiKLKHYMA.
    PhylomeDBiQ13526.
    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.

    Q13526-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG    50
    EPARVRCSHL LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE 100
    EDFESLASQF SDCSSAKARG DLGAFSRGQM QKPFEDASFA LRTGEMSGPV 150
    FTDSGIHIIL RTE 163
    Length:163
    Mass (Da):18,243
    Last modified:November 1, 1996 - v1
    Checksum:i35391AF40B7D1E13
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49070 mRNA. Translation: AAC50492.1.
    CR407654 mRNA. Translation: CAG28582.1.
    BT019331 mRNA. Translation: AAV38138.1.
    AK291074 mRNA. Translation: BAF83763.1.
    CH471106 Genomic DNA. Translation: EAW84057.1.
    BC002899 mRNA. Translation: AAH02899.1.
    CCDSiCCDS12220.1.
    PIRiS68520.
    RefSeqiNP_006212.1. NM_006221.3.
    UniGeneiHs.465849.

    Genome annotation databases

    EnsembliENST00000247970; ENSP00000247970; ENSG00000127445.
    ENST00000588695; ENSP00000466962; ENSG00000127445.
    GeneIDi5300.
    KEGGihsa:5300.
    UCSCiuc002mmk.2. human.

    Polymorphism databases

    DMDMi3024406.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49070 mRNA. Translation: AAC50492.1 .
    CR407654 mRNA. Translation: CAG28582.1 .
    BT019331 mRNA. Translation: AAV38138.1 .
    AK291074 mRNA. Translation: BAF83763.1 .
    CH471106 Genomic DNA. Translation: EAW84057.1 .
    BC002899 mRNA. Translation: AAH02899.1 .
    CCDSi CCDS12220.1.
    PIRi S68520.
    RefSeqi NP_006212.1. NM_006221.3.
    UniGenei Hs.465849.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F8A X-ray 1.84 B 1-163 [» ]
    1I6C NMR - A 6-44 [» ]
    1I8G NMR - B 6-44 [» ]
    1I8H NMR - B 6-44 [» ]
    1NMV NMR - A 1-163 [» ]
    1NMW NMR - A 50-163 [» ]
    1PIN X-ray 1.35 A 1-163 [» ]
    1ZCN X-ray 1.90 A 1-161 [» ]
    2F21 X-ray 1.50 A 1-162 [» ]
    2ITK X-ray 1.45 A 1-163 [» ]
    2KBU NMR - A 6-39 [» ]
    2KCF NMR - A 6-39 [» ]
    2LB3 NMR - A 6-41 [» ]
    2M8I NMR - A 1-39 [» ]
    2M8J NMR - A 1-39 [» ]
    2M9E NMR - A 22-39 [» ]
    2M9F NMR - A 6-39 [» ]
    2M9I NMR - A 6-39 [» ]
    2M9J NMR - A 6-39 [» ]
    2Q5A X-ray 1.50 A 1-163 [» ]
    2XP3 X-ray 2.00 A 1-163 [» ]
    2XP4 X-ray 1.80 A 1-163 [» ]
    2XP5 X-ray 1.90 A 1-163 [» ]
    2XP6 X-ray 1.90 A 1-163 [» ]
    2XP7 X-ray 2.00 A 1-163 [» ]
    2XP8 X-ray 2.10 A 1-163 [» ]
    2XP9 X-ray 1.90 A 1-163 [» ]
    2XPA X-ray 1.90 A 1-163 [» ]
    2XPB X-ray 2.00 A 1-163 [» ]
    2ZQS X-ray 1.90 A 1-163 [» ]
    2ZQT X-ray 1.46 A 1-163 [» ]
    2ZQU X-ray 2.50 A 1-163 [» ]
    2ZQV X-ray 2.50 A 1-163 [» ]
    2ZR4 X-ray 2.00 A 1-163 [» ]
    2ZR5 X-ray 2.60 A 1-163 [» ]
    2ZR6 X-ray 3.20 A 1-163 [» ]
    3I6C X-ray 1.30 A/B 45-163 [» ]
    3IK8 X-ray 1.85 A/B 45-163 [» ]
    3IKD X-ray 2.00 A/B 45-163 [» ]
    3IKG X-ray 1.86 A/B 45-163 [» ]
    3JYJ X-ray 1.87 A/B 45-163 [» ]
    3KAB X-ray 2.19 A 1-163 [» ]
    3KAC X-ray 2.00 A/B 45-163 [» ]
    3KAD X-ray 1.95 A 1-163 [» ]
    3KAF X-ray 2.30 A 1-163 [» ]
    3KAG X-ray 1.90 A 1-163 [» ]
    3KAH X-ray 2.30 A 1-163 [» ]
    3KAI X-ray 1.90 A 1-163 [» ]
    3KCE X-ray 1.90 A 1-163 [» ]
    3NTP X-ray 1.76 A 1-163 [» ]
    3ODK X-ray 2.30 A 1-163 [» ]
    3OOB X-ray 1.89 A 1-163 [» ]
    3TC5 X-ray 1.40 A 1-163 [» ]
    3TCZ X-ray 2.10 A 6-163 [» ]
    3TDB X-ray 2.27 A 6-163 [» ]
    4GWT X-ray 2.25 A 6-39 [» ]
    4GWV X-ray 3.05 A 6-39 [» ]
    ProteinModelPortali Q13526.
    SMRi Q13526. Positions 1-163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111317. 154 interactions.
    DIPi DIP-29306N.
    IntActi Q13526. 79 interactions.
    MINTi MINT-86298.
    STRINGi 9606.ENSP00000247970.

    Chemistry

    BindingDBi Q13526.
    ChEMBLi CHEMBL2288.

    PTM databases

    PhosphoSitei Q13526.

    Polymorphism databases

    DMDMi 3024406.

    Proteomic databases

    MaxQBi Q13526.
    PaxDbi Q13526.
    PeptideAtlasi Q13526.
    PRIDEi Q13526.

    Protocols and materials databases

    DNASUi 5300.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000247970 ; ENSP00000247970 ; ENSG00000127445 .
    ENST00000588695 ; ENSP00000466962 ; ENSG00000127445 .
    GeneIDi 5300.
    KEGGi hsa:5300.
    UCSCi uc002mmk.2. human.

    Organism-specific databases

    CTDi 5300.
    GeneCardsi GC19P009945.
    HGNCi HGNC:8988. PIN1.
    HPAi CAB004528.
    CAB009326.
    MIMi 601052. gene.
    neXtProti NX_Q13526.
    PharmGKBi PA33320.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0760.
    HOGENOMi HOG000275331.
    HOVERGENi HBG002101.
    InParanoidi Q13526.
    KOi K09578.
    OMAi KLKHYMA.
    PhylomeDBi Q13526.
    TreeFami TF101101.

    Enzyme and pathway databases

    BRENDAi 5.2.1.8. 2681.
    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    SignaLinki Q13526.

    Miscellaneous databases

    EvolutionaryTracei Q13526.
    GeneWikii PIN1.
    GenomeRNAii 5300.
    NextBioi 20486.
    PROi Q13526.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13526.
    Bgeei Q13526.
    CleanExi HS_PIN1.
    Genevestigatori Q13526.

    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. "A human peptidyl-prolyl isomerase essential for regulation of mitosis."
      Lu K.P., Hanes S.D., Hunter T.
      Nature 380:544-547(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Lung.
    7. "Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1."
      Kamimoto T., Zama T., Aoki R., Muro Y., Hagiwara M.
      J. Biol. Chem. 276:37520-37528(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIF20B, MUTAGENESIS OF TYR-23.
    8. Cited for: FUNCTION, INTERACTION WITH RAF1.
    9. "Interaction of Pin1 with Nek6 and characterization of their expression correlation in Chinese hepatocellular carcinoma patients."
      Chen J., Li L., Zhang Y., Yang H., Wei Y., Zhang L., Liu X., Yu L.
      Biochem. Biophys. Res. Commun. 341:1059-1065(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6.
    10. "Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1."
      Yu L., Mohamed A.J., Vargas L., Berglof A., Finn G., Lu K.P., Smith C.I.
      J. Biol. Chem. 281:18201-18207(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BTX, FUNCTION.
    11. "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 REGULATION, INTERACTION WITH BCL6, TISSUE SPECIFICITY.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    13. "Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons."
      Buschdorf J.P., Chew L.L., Soh U.J., Liou Y.C., Low B.C.
      PLoS ONE 3:E2686-E2686(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATCAY.
    14. "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.
    15. "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-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover."
      Lim J.H., Liu Y., Reineke E., Kao H.Y.
      J. Biol. Chem. 286:44403-44411(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PML.
    18. "Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function."
      Lee T.H., Chen C.H., Suizu F., Huang P., Schiene-Fischer C., Daum S., Zhang Y.J., Goate A., Chen R.H., Zhou X.Z., Lu K.P.
      Mol. Cell 42:147-159(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-71, INTERACTION WITH DAPK1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-71, TISSUE SPECIFICITY.
    19. "Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent."
      Ranganathan R., Lu K.P., Hunter T., Noel J.P.
      Cell 89:875-886(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).

    Entry informationi

    Entry nameiPIN1_HUMAN
    AccessioniPrimary (citable) accession number: Q13526
    Secondary accession number(s): A8K4V9, Q53X75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 150 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 19
      Human chromosome 19: 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