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)

Q9P1W9

- PIM2_HUMAN

UniProt

Q9P1W9 - PIM2_HUMAN

Protein

Serine/threonine-protein kinase pim-2

Gene

PIM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Isoform 1 is less active in this respect. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei61 – 611ATPPROSITE-ProRule annotation
    Active sitei163 – 1631Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi38 – 469ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic mitochondrial changes Source: Ensembl
    2. cell proliferation Source: ProtInc
    3. G1/S transition of mitotic cell cycle Source: UniProtKB
    4. male meiosis Source: ProtInc
    5. negative regulation of apoptotic process Source: UniProtKB
    6. negative regulation of cell proliferation Source: UniProtKB
    7. positive regulation of autophagy Source: UniProtKB
    8. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    9. positive regulation of transcription, DNA-templated Source: UniProtKB
    10. protein phosphorylation Source: UniProtKB
    11. protein stabilization Source: UniProtKB
    12. response to virus Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9P1W9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase pim-2 (EC:2.7.11.1)
    Alternative name(s):
    Pim-2h
    Gene namesi
    Name:PIM2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8987. PIM2.

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA33319.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 311311Serine/threonine-protein kinase pim-2PRO_0000086532Add
    BLAST

    Post-translational modificationi

    Autophosphorylated.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9P1W9.
    PaxDbiQ9P1W9.
    PRIDEiQ9P1W9.

    PTM databases

    PhosphoSiteiQ9P1W9.

    Expressioni

    Tissue specificityi

    Highly expressed in hematopoietic tissues, in leukemic and lymphoma cell lines, testis, small intestine, colon and colorectal adenocarcinoma cells. Weakly expressed in normal liver, but highly expressed in hepatocellular carcinoma tissues.1 Publication

    Inductioni

    Down-regulated in response to enterovirus 71 (EV71) infection.1 Publication

    Gene expression databases

    ArrayExpressiQ9P1W9.
    BgeeiQ9P1W9.
    CleanExiHS_PIM2.
    GenevestigatoriQ9P1W9.

    Organism-specific databases

    HPAiHPA000285.

    Interactioni

    Subunit structurei

    Interacts with MYC.By similarity

    Protein-protein interaction databases

    BioGridi116228. 9 interactions.
    IntActiQ9P1W9. 9 interactions.
    MINTiMINT-1432143.
    STRINGi9606.ENSP00000365692.

    Structurei

    Secondary structure

    1
    311
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 419
    Beta strandi44 – 507
    Turni52 – 543
    Beta strandi57 – 626
    Turni66 – 683
    Helixi82 – 9110
    Beta strandi97 – 993
    Beta strandi102 – 1054
    Beta strandi113 – 1175
    Beta strandi120 – 1245
    Helixi125 – 1328
    Helixi137 – 15721
    Helixi166 – 1683
    Beta strandi169 – 1724
    Turni173 – 1764
    Beta strandi177 – 1804
    Turni201 – 2033
    Helixi206 – 2116
    Helixi216 – 23318
    Helixi241 – 2466
    Helixi257 – 26610
    Turni271 – 2733
    Helixi277 – 2826
    Turni284 – 2863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IWIX-ray2.80A/B1-311[»]
    ProteinModelPortaliQ9P1W9.
    SMRiQ9P1W9. Positions 32-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P1W9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 286255Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000231357.
    HOVERGENiHBG106681.
    InParanoidiQ9P1W9.
    KOiK08806.
    OMAiASTPCGL.
    PhylomeDBiQ9P1W9.
    TreeFamiTF320810.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9P1W9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTKPLQGPP APPGTPTPPP GGKDREAFEA EYRLGPLLGK GGFGTVFAGH    50
    RLTDRLQVAI KVIPRNRVLG WSPLSDSVTC PLEVALLWKV GAGGGHPGVI 100
    RLLDWFETQE GFMLVLERPL PAQDLFDYIT EKGPLGEGPS RCFFGQVVAA 150
    IQHCHSRGVV HRDIKDENIL IDLRRGCAKL IDFGSGALLH DEPYTDFDGT 200
    RVYSPPEWIS RHQYHALPAT VWSLGILLYD MVCGDIPFER DQEILEAELH 250
    FPAHVSPDCC ALIRRCLAPK PSSRPSLEEI LLDPWMQTPA EDVPLNPSKG 300
    GPAPLAWSLL P 311
    Length:311
    Mass (Da):34,190
    Last modified:October 1, 2000 - v1
    Checksum:i160E56C368C67A69
    GO

    Sequence cautioni

    The sequence AAC78506.1 differs from that shown. Reason: Frameshift at position 293.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661N → Y in BAF83620. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381G → D.1 Publication
    Corresponds to variant rs35044770 [ dbSNP | Ensembl ].
    VAR_041008
    Natural varianti280 – 2801I → V.1 Publication
    Corresponds to variant rs35208542 [ dbSNP | Ensembl ].
    VAR_041009

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77735 mRNA. Translation: AAC78506.1. Frameshift.
    AK290931 mRNA. Translation: BAF83620.1.
    AB042425 Genomic DNA. Translation: BAA95613.1.
    AF207550 Genomic DNA. No translation available.
    BC018111 mRNA. Translation: AAH18111.1.
    CCDSiCCDS14312.1.
    RefSeqiNP_006866.2. NM_006875.3.
    UniGeneiHs.727148.

    Genome annotation databases

    EnsembliENST00000376509; ENSP00000365692; ENSG00000102096.
    GeneIDi11040.
    KEGGihsa:11040.
    UCSCiuc004dls.3. human.

    Polymorphism databases

    DMDMi20139243.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77735 mRNA. Translation: AAC78506.1 . Frameshift.
    AK290931 mRNA. Translation: BAF83620.1 .
    AB042425 Genomic DNA. Translation: BAA95613.1 .
    AF207550 Genomic DNA. No translation available.
    BC018111 mRNA. Translation: AAH18111.1 .
    CCDSi CCDS14312.1.
    RefSeqi NP_006866.2. NM_006875.3.
    UniGenei Hs.727148.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IWI X-ray 2.80 A/B 1-311 [» ]
    ProteinModelPortali Q9P1W9.
    SMRi Q9P1W9. Positions 32-288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116228. 9 interactions.
    IntActi Q9P1W9. 9 interactions.
    MINTi MINT-1432143.
    STRINGi 9606.ENSP00000365692.

    Chemistry

    BindingDBi Q9P1W9.
    ChEMBLi CHEMBL4523.
    GuidetoPHARMACOLOGYi 2159.

    PTM databases

    PhosphoSitei Q9P1W9.

    Polymorphism databases

    DMDMi 20139243.

    Proteomic databases

    MaxQBi Q9P1W9.
    PaxDbi Q9P1W9.
    PRIDEi Q9P1W9.

    Protocols and materials databases

    DNASUi 11040.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376509 ; ENSP00000365692 ; ENSG00000102096 .
    GeneIDi 11040.
    KEGGi hsa:11040.
    UCSCi uc004dls.3. human.

    Organism-specific databases

    CTDi 11040.
    GeneCardsi GC0XM048770.
    HGNCi HGNC:8987. PIM2.
    HPAi HPA000285.
    MIMi 300295. gene.
    neXtProti NX_Q9P1W9.
    PharmGKBi PA33319.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000231357.
    HOVERGENi HBG106681.
    InParanoidi Q9P1W9.
    KOi K08806.
    OMAi ASTPCGL.
    PhylomeDBi Q9P1W9.
    TreeFami TF320810.

    Enzyme and pathway databases

    SignaLinki Q9P1W9.

    Miscellaneous databases

    ChiTaRSi PIM2. human.
    EvolutionaryTracei Q9P1W9.
    GeneWikii PIM2_(gene).
    GenomeRNAii 11040.
    NextBioi 41955.
    PROi Q9P1W9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P1W9.
    Bgeei Q9P1W9.
    CleanExi HS_PIM2.
    Genevestigatori Q9P1W9.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human Pim-2 proto-oncogene and its testicular expression."
      Baytel D., Shalom S., Madgar I., Weissenberg R., Don J.
      Biochim. Biophys. Acta 1442:274-285(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    2. "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].
    3. "Genomic organization of the human UDP-galactose transporter gene."
      Ishida N., Miura N., Yamauchi M., Kawakita M.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Uterus.
    6. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
      Leong W.F., Chow V.T.
      Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Pim kinases promote cell cycle progression by phosphorylating and down-regulating p27Kip1 at the transcriptional and posttranscriptional levels."
      Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.
      Cancer Res. 68:5076-5085(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDKN1B.
    8. "Serine/threonine kinase Pim-2 promotes liver tumorigenesis induction through mediating survival and preventing apoptosis of liver cell."
      Gong J., Wang J., Ren K., Liu C., Li B., Shi Y.
      J. Surg. Res. 153:17-22(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    9. "Pim-2 phosphorylation of p21(Cip1/WAF1) enhances its stability and inhibits cell proliferation in HCT116 cells."
      Wang Z., Zhang Y., Gu J.J., Davitt C., Reeves R., Magnuson N.S.
      Int. J. Biochem. Cell Biol. 42:1030-1038(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDKN1A.
    10. "Crystal structure of the PIM2 kinase in complex with an organoruthenium inhibitor."
      Bullock A.N., Russo S., Amos A., Pagano N., Bregman H., Debreczeni J.E., Lee W.H., von Delft F., Meggers E., Knapp S.
      PLoS ONE 4:E7112-E7112(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RUTHENIUM-PYRIDOCARBAZOLE-1.
    11. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-138 AND VAL-280.

    Entry informationi

    Entry nameiPIM2_HUMAN
    AccessioniPrimary (citable) accession number: Q9P1W9
    Secondary accession number(s): A8K4G6, Q99739
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 124 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 X
      Human chromosome X: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3