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P11309

- PIM1_HUMAN

UniProt

P11309 - PIM1_HUMAN

Protein

Serine/threonine-protein kinase pim-1

Gene

PIM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 3 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.7 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.3 Publications

    Cofactori

    Magnesium.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei158 – 1581ATP
    Binding sitei212 – 2121ATP; via carbonyl oxygen
    Binding sitei219 – 2191ATP
    Active sitei258 – 2581Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi135 – 1439ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. manganese ion binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein serine/threonine kinase activity Source: UniProtKB
    5. ribosomal small subunit binding Source: UniProtKB
    6. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell cycle Source: UniProtKB-KW
    3. cell proliferation Source: UniProtKB
    4. hyaluronan metabolic process Source: Ensembl
    5. multicellular organismal development Source: ProtInc
    6. negative regulation of apoptotic process Source: UniProtKB
    7. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    8. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: UniProtKB
    9. protein autophosphorylation Source: UniProtKB
    10. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiP11309.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase pim-1 (EC:2.7.11.1)
    Gene namesi
    Name:PIM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:8986. PIM1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi159 – 1591H → Y: Increased kinase activity. 1 Publication
    Mutagenesisi172 – 1721P → S: Decreased kinase activity. 1 Publication
    Mutagenesisi173 – 1731N → K: Decreased kinase activity. 1 Publication
    Mutagenesisi284 – 2841L → F: Decreased kinase activity. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA33318.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 404404Serine/threonine-protein kinase pim-1PRO_0000043349Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei99 – 991Phosphoserine1 Publication
    Modified residuei114 – 1141Phosphothreonine1 Publication
    Modified residuei189 – 1891Phosphoserine1 Publication
    Modified residuei352 – 3521Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation.3 Publications
    Ubiquitinated, leading to proteasomal degradation.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP11309.
    PaxDbiP11309.
    PRIDEiP11309.

    PTM databases

    PhosphoSiteiP11309.

    Expressioni

    Tissue specificityi

    Expressed primarily in cells of the hematopoietic and germline lineages. Isoform 1 and isoform 2 are both expressed in prostate cancer cell lines.1 Publication

    Inductioni

    Strongly induced in leukocytes by the JAK/STAT pathway in response to cytokines. Induced by different cellular stresses, heat shock and cytotoxic agents.3 Publications

    Gene expression databases

    BgeeiP11309.
    CleanExiHS_PIM1.
    GenevestigatoriP11309.

    Organism-specific databases

    HPAiCAB017040.
    HPA003941.

    Interactioni

    Subunit structurei

    Isoform 2 is isolated as a monomer whereas isoform 1 complexes with other proteins By similarity. Binds to RP9 By similarity. Isoform 1, but not isoform 2, binds BMX. Isoform 2 interacts with CDKN1B and FOXO3. Interacts with BAD. Interacts with PPP2CA; this interaction promotes dephosphorylation of PIM1, ubiquitination and proteasomal degradation By similarity. Interacts with HSP90, this interaction stabilizes PIM1 protein levels. Interacts (ubiquitinated form) with HSP70 and promotes its proteosomal degradation. Interacts with CDKN1A. Interacts with CDC25C. Interacts (via N-terminal 96 residues) with CDC25A By similarity. Interacts with MAP3K5. Interacts with MYC By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABCG2Q9UNQ09EBI-1018629,EBI-1569435
    BMXP518134EBI-696621,EBI-696657
    RPS19P390197EBI-696621,EBI-354451

    Protein-protein interaction databases

    BioGridi111310. 29 interactions.
    IntActiP11309. 7 interactions.
    MINTiMINT-1412755.
    STRINGi9606.ENSP00000362608.

    Structurei

    Secondary structure

    1
    404
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni126 – 1283
    Beta strandi129 – 1346
    Beta strandi136 – 1405
    Beta strandi142 – 1487
    Turni149 – 1513
    Beta strandi154 – 1618
    Helixi162 – 1643
    Beta strandi168 – 1703
    Turni172 – 1743
    Beta strandi176 – 1783
    Helixi179 – 1879
    Beta strandi189 – 1913
    Beta strandi192 – 1943
    Beta strandi197 – 2026
    Beta strandi204 – 2129
    Beta strandi215 – 2195
    Helixi220 – 2278
    Helixi232 – 25120
    Helixi261 – 2633
    Beta strandi264 – 2674
    Turni268 – 2714
    Beta strandi272 – 2754
    Helixi278 – 2803
    Helixi296 – 2983
    Helixi301 – 3066
    Helixi311 – 32818
    Helixi336 – 3416
    Helixi352 – 36110
    Helixi366 – 3683
    Helixi372 – 3765
    Helixi379 – 3813
    Helixi387 – 3948
    Turni395 – 3984

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XQZX-ray2.10A105-404[»]
    1XR1X-ray2.10A105-404[»]
    1XWSX-ray1.80A92-404[»]
    1YHSX-ray2.15A124-396[»]
    1YI3X-ray2.50A124-396[»]
    1YI4X-ray2.40A124-396[»]
    1YWVX-ray2.00A120-404[»]
    1YXSX-ray2.20A120-404[»]
    1YXTX-ray2.00A120-404[»]
    1YXUX-ray2.24A/B/C/D120-404[»]
    1YXVX-ray2.00A120-404[»]
    1YXXX-ray2.00A120-404[»]
    2BIKX-ray1.80B92-404[»]
    2BILX-ray2.55B92-404[»]
    2BZHX-ray1.90B92-404[»]
    2BZIX-ray1.90B92-404[»]
    2BZJX-ray2.05A92-404[»]
    2BZKX-ray2.45B92-404[»]
    2C3IX-ray1.90B92-404[»]
    2J2IX-ray1.90B92-403[»]
    2O3PX-ray2.24A120-404[»]
    2O63X-ray2.00A120-404[»]
    2O64X-ray2.44A120-404[»]
    2O65X-ray2.85A120-404[»]
    2OBJX-ray2.50A92-404[»]
    2OI4X-ray2.20X92-404[»]
    2XIXX-ray2.40A105-404[»]
    2XIYX-ray2.20A105-404[»]
    2XIZX-ray2.21A105-404[»]
    2XJ0X-ray3.10A105-404[»]
    2XJ1X-ray2.13A105-404[»]
    2XJ2X-ray2.20A105-404[»]
    3A99X-ray1.60A106-404[»]
    3BGPX-ray2.80A92-404[»]
    3BGQX-ray2.00A92-404[»]
    3BGZX-ray2.40A92-404[»]
    3BWFX-ray2.35A92-404[»]
    3C4EX-ray1.98A/B/C/D124-396[»]
    3CXWX-ray2.10A92-404[»]
    3CY2X-ray2.01A92-404[»]
    3CY3X-ray2.15A92-404[»]
    3DCVX-ray2.70A93-404[»]
    3F2AX-ray1.90A105-404[»]
    3JPVX-ray2.35A92-403[»]
    3JXWX-ray2.80A120-404[»]
    3JY0X-ray2.40A120-404[»]
    3JYAX-ray2.10A120-404[»]
    3MA3X-ray2.30A93-403[»]
    3QF9X-ray2.20A92-403[»]
    3R00X-ray2.10A120-404[»]
    3R01X-ray2.60A120-404[»]
    3R02X-ray1.95A120-404[»]
    3R04X-ray1.70A120-404[»]
    3T9IX-ray2.60A93-404[»]
    3UIXX-ray2.20A120-404[»]
    3UMWX-ray2.08A120-404[»]
    3UMXX-ray2.55A120-404[»]
    3VBQX-ray1.85A120-404[»]
    3VBTX-ray2.23A120-404[»]
    3VBVX-ray2.08A120-404[»]
    3VBWX-ray2.48A120-404[»]
    3VBXX-ray2.03A120-404[»]
    3VBYX-ray2.27A120-404[»]
    3VC4X-ray2.23A120-404[»]
    3WE8X-ray1.95A124-396[»]
    4A7CX-ray2.30A121-404[»]
    4ALUX-ray2.60A93-404[»]
    4ALVX-ray2.59A93-404[»]
    4ALWX-ray1.92A93-404[»]
    4AS0X-ray2.30A124-396[»]
    4BZNX-ray1.90A93-404[»]
    4BZOX-ray2.10A93-404[»]
    4DTKX-ray1.86A121-396[»]
    4ENXX-ray2.80A120-404[»]
    4ENYX-ray2.80A120-404[»]
    4GW8X-ray2.00A92-403[»]
    4I41X-ray2.70A120-396[»]
    4IAAX-ray2.85A120-404[»]
    4JX3X-ray2.50A92-404[»]
    4JX7X-ray2.40A92-404[»]
    4K0YX-ray1.95A124-397[»]
    4K18X-ray2.05A123-399[»]
    4K1BX-ray2.08A124-396[»]
    4LL5X-ray2.00A120-404[»]
    4LM5X-ray2.25A120-404[»]
    4LMUX-ray2.38A120-404[»]
    4MBIX-ray2.30A120-404[»]
    4MBLX-ray2.60A120-404[»]
    4MEDX-ray2.80A120-404[»]
    4N6YX-ray2.60A93-404[»]
    4N6ZX-ray2.20A93-404[»]
    4N70X-ray2.10A93-404[»]
    DisProtiDP00322.
    ProteinModelPortaliP11309.
    SMRiP11309. Positions 104-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11309.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini129 – 381253Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000231357.
    HOVERGENiHBG106681.
    InParanoidiP11309.
    KOiK04702.
    OMAiFIIVMER.
    OrthoDBiEOG7NW6B0.
    PhylomeDBiP11309.
    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.
    IPR017348. Ser/Thr_kinase_Pim-1.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037993. STPK_Pim-1. 1 hit.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: P11309-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPHEPHEPLT PPFSALPDPA GAPSRRQSRQ RPQLSSDSPS AFRASRSHSR    50
    NATRSHSHSH SPRHSLRHSP GSGSCGSSSG HRPCADILEV GMLLSKINSL 100
    AHLRAAPCND LHATKLAPGK EKEPLESQYQ VGPLLGSGGF GSVYSGIRVS 150
    DNLPVAIKHV EKDRISDWGE LPNGTRVPME VVLLKKVSSG FSGVIRLLDW 200
    FERPDSFVLI LERPEPVQDL FDFITERGAL QEELARSFFW QVLEAVRHCH 250
    NCGVLHRDIK DENILIDLNR GELKLIDFGS GALLKDTVYT DFDGTRVYSP 300
    PEWIRYHRYH GRSAAVWSLG ILLYDMVCGD IPFEHDEEII RGQVFFRQRV 350
    SSECQHLIRW CLALRPSDRP TFEEIQNHPW MQDVLLPQET AEIHLHSLSP 400
    GPSK 404

    Note: Initiates from CTG codon.

    Length:404
    Mass (Da):45,412
    Last modified:December 6, 2005 - v3
    Checksum:i18C421B7CFF87818
    GO
    Isoform 2 (identifier: P11309-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-91: Missing.

    Show »
    Length:313
    Mass (Da):35,686
    Checksum:i35BA76D3668E69A3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1072AP → RA in AAA60089. (PubMed:3475233)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti144 – 1441Y → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041004
    Natural varianti215 – 2151E → Q.1 Publication
    VAR_041005
    Natural varianti226 – 2261E → K.1 Publication
    VAR_041006
    Natural varianti233 – 2331E → D.1 Publication
    VAR_041007

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9191Missing in isoform 2. 4 PublicationsVSP_016530Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27903 Genomic DNA. Translation: AAA60090.1.
    M16750 mRNA. Translation: AAA60089.1.
    M54915 mRNA. Translation: AAA36447.1.
    M24779 mRNA. Translation: AAA81553.1.
    DQ022562 mRNA. Translation: AAY87461.1.
    AL353579 Genomic DNA. Translation: CAI20316.1.
    CH471081 Genomic DNA. Translation: EAX03934.1.
    BC020224 mRNA. Translation: AAH20224.1.
    AF386792 Genomic DNA. Translation: AAK70871.1.
    CCDSiCCDS4830.1. [P11309-2]
    PIRiJU0327. TVHUP1.
    RefSeqiNP_001230115.1. NM_001243186.1. [P11309-1]
    NP_002639.1. NM_002648.3. [P11309-2]
    UniGeneiHs.81170.

    Genome annotation databases

    EnsembliENST00000373509; ENSP00000362608; ENSG00000137193. [P11309-2]
    GeneIDi5292.
    KEGGihsa:5292.
    UCSCiuc003onk.3. human. [P11309-1]

    Polymorphism databases

    DMDMi83305339.

    Keywords - Coding sequence diversityi

    Alternative initiation, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27903 Genomic DNA. Translation: AAA60090.1 .
    M16750 mRNA. Translation: AAA60089.1 .
    M54915 mRNA. Translation: AAA36447.1 .
    M24779 mRNA. Translation: AAA81553.1 .
    DQ022562 mRNA. Translation: AAY87461.1 .
    AL353579 Genomic DNA. Translation: CAI20316.1 .
    CH471081 Genomic DNA. Translation: EAX03934.1 .
    BC020224 mRNA. Translation: AAH20224.1 .
    AF386792 Genomic DNA. Translation: AAK70871.1 .
    CCDSi CCDS4830.1. [P11309-2 ]
    PIRi JU0327. TVHUP1.
    RefSeqi NP_001230115.1. NM_001243186.1. [P11309-1 ]
    NP_002639.1. NM_002648.3. [P11309-2 ]
    UniGenei Hs.81170.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XQZ X-ray 2.10 A 105-404 [» ]
    1XR1 X-ray 2.10 A 105-404 [» ]
    1XWS X-ray 1.80 A 92-404 [» ]
    1YHS X-ray 2.15 A 124-396 [» ]
    1YI3 X-ray 2.50 A 124-396 [» ]
    1YI4 X-ray 2.40 A 124-396 [» ]
    1YWV X-ray 2.00 A 120-404 [» ]
    1YXS X-ray 2.20 A 120-404 [» ]
    1YXT X-ray 2.00 A 120-404 [» ]
    1YXU X-ray 2.24 A/B/C/D 120-404 [» ]
    1YXV X-ray 2.00 A 120-404 [» ]
    1YXX X-ray 2.00 A 120-404 [» ]
    2BIK X-ray 1.80 B 92-404 [» ]
    2BIL X-ray 2.55 B 92-404 [» ]
    2BZH X-ray 1.90 B 92-404 [» ]
    2BZI X-ray 1.90 B 92-404 [» ]
    2BZJ X-ray 2.05 A 92-404 [» ]
    2BZK X-ray 2.45 B 92-404 [» ]
    2C3I X-ray 1.90 B 92-404 [» ]
    2J2I X-ray 1.90 B 92-403 [» ]
    2O3P X-ray 2.24 A 120-404 [» ]
    2O63 X-ray 2.00 A 120-404 [» ]
    2O64 X-ray 2.44 A 120-404 [» ]
    2O65 X-ray 2.85 A 120-404 [» ]
    2OBJ X-ray 2.50 A 92-404 [» ]
    2OI4 X-ray 2.20 X 92-404 [» ]
    2XIX X-ray 2.40 A 105-404 [» ]
    2XIY X-ray 2.20 A 105-404 [» ]
    2XIZ X-ray 2.21 A 105-404 [» ]
    2XJ0 X-ray 3.10 A 105-404 [» ]
    2XJ1 X-ray 2.13 A 105-404 [» ]
    2XJ2 X-ray 2.20 A 105-404 [» ]
    3A99 X-ray 1.60 A 106-404 [» ]
    3BGP X-ray 2.80 A 92-404 [» ]
    3BGQ X-ray 2.00 A 92-404 [» ]
    3BGZ X-ray 2.40 A 92-404 [» ]
    3BWF X-ray 2.35 A 92-404 [» ]
    3C4E X-ray 1.98 A/B/C/D 124-396 [» ]
    3CXW X-ray 2.10 A 92-404 [» ]
    3CY2 X-ray 2.01 A 92-404 [» ]
    3CY3 X-ray 2.15 A 92-404 [» ]
    3DCV X-ray 2.70 A 93-404 [» ]
    3F2A X-ray 1.90 A 105-404 [» ]
    3JPV X-ray 2.35 A 92-403 [» ]
    3JXW X-ray 2.80 A 120-404 [» ]
    3JY0 X-ray 2.40 A 120-404 [» ]
    3JYA X-ray 2.10 A 120-404 [» ]
    3MA3 X-ray 2.30 A 93-403 [» ]
    3QF9 X-ray 2.20 A 92-403 [» ]
    3R00 X-ray 2.10 A 120-404 [» ]
    3R01 X-ray 2.60 A 120-404 [» ]
    3R02 X-ray 1.95 A 120-404 [» ]
    3R04 X-ray 1.70 A 120-404 [» ]
    3T9I X-ray 2.60 A 93-404 [» ]
    3UIX X-ray 2.20 A 120-404 [» ]
    3UMW X-ray 2.08 A 120-404 [» ]
    3UMX X-ray 2.55 A 120-404 [» ]
    3VBQ X-ray 1.85 A 120-404 [» ]
    3VBT X-ray 2.23 A 120-404 [» ]
    3VBV X-ray 2.08 A 120-404 [» ]
    3VBW X-ray 2.48 A 120-404 [» ]
    3VBX X-ray 2.03 A 120-404 [» ]
    3VBY X-ray 2.27 A 120-404 [» ]
    3VC4 X-ray 2.23 A 120-404 [» ]
    3WE8 X-ray 1.95 A 124-396 [» ]
    4A7C X-ray 2.30 A 121-404 [» ]
    4ALU X-ray 2.60 A 93-404 [» ]
    4ALV X-ray 2.59 A 93-404 [» ]
    4ALW X-ray 1.92 A 93-404 [» ]
    4AS0 X-ray 2.30 A 124-396 [» ]
    4BZN X-ray 1.90 A 93-404 [» ]
    4BZO X-ray 2.10 A 93-404 [» ]
    4DTK X-ray 1.86 A 121-396 [» ]
    4ENX X-ray 2.80 A 120-404 [» ]
    4ENY X-ray 2.80 A 120-404 [» ]
    4GW8 X-ray 2.00 A 92-403 [» ]
    4I41 X-ray 2.70 A 120-396 [» ]
    4IAA X-ray 2.85 A 120-404 [» ]
    4JX3 X-ray 2.50 A 92-404 [» ]
    4JX7 X-ray 2.40 A 92-404 [» ]
    4K0Y X-ray 1.95 A 124-397 [» ]
    4K18 X-ray 2.05 A 123-399 [» ]
    4K1B X-ray 2.08 A 124-396 [» ]
    4LL5 X-ray 2.00 A 120-404 [» ]
    4LM5 X-ray 2.25 A 120-404 [» ]
    4LMU X-ray 2.38 A 120-404 [» ]
    4MBI X-ray 2.30 A 120-404 [» ]
    4MBL X-ray 2.60 A 120-404 [» ]
    4MED X-ray 2.80 A 120-404 [» ]
    4N6Y X-ray 2.60 A 93-404 [» ]
    4N6Z X-ray 2.20 A 93-404 [» ]
    4N70 X-ray 2.10 A 93-404 [» ]
    DisProti DP00322.
    ProteinModelPortali P11309.
    SMRi P11309. Positions 104-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111310. 29 interactions.
    IntActi P11309. 7 interactions.
    MINTi MINT-1412755.
    STRINGi 9606.ENSP00000362608.

    Chemistry

    BindingDBi P11309.
    ChEMBLi CHEMBL2147.
    DrugBanki DB00131. Adenosine monophosphate.
    GuidetoPHARMACOLOGYi 2158.

    PTM databases

    PhosphoSitei P11309.

    Polymorphism databases

    DMDMi 83305339.

    Proteomic databases

    MaxQBi P11309.
    PaxDbi P11309.
    PRIDEi P11309.

    Protocols and materials databases

    DNASUi 5292.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373509 ; ENSP00000362608 ; ENSG00000137193 . [P11309-2 ]
    GeneIDi 5292.
    KEGGi hsa:5292.
    UCSCi uc003onk.3. human. [P11309-1 ]

    Organism-specific databases

    CTDi 5292.
    GeneCardsi GC06P037137.
    HGNCi HGNC:8986. PIM1.
    HPAi CAB017040.
    HPA003941.
    MIMi 164960. gene.
    neXtProti NX_P11309.
    PharmGKBi PA33318.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000231357.
    HOVERGENi HBG106681.
    InParanoidi P11309.
    KOi K04702.
    OMAi FIIVMER.
    OrthoDBi EOG7NW6B0.
    PhylomeDBi P11309.
    TreeFami TF320810.

    Enzyme and pathway databases

    SignaLinki P11309.

    Miscellaneous databases

    ChiTaRSi PIM1. human.
    EvolutionaryTracei P11309.
    GeneWikii PIM1.
    GenomeRNAii 5292.
    NextBioi 20450.
    PROi P11309.
    SOURCEi Search...

    Gene expression databases

    Bgeei P11309.
    CleanExi HS_PIM1.
    Genevestigatori P11309.

    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.
    IPR017348. Ser/Thr_kinase_Pim-1.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037993. STPK_Pim-1. 1 hit.
    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. "Primary structure of the putative human oncogene, pim-1."
      Reeves R., Spies G.A., Kiefer M., Barr P.J., Power M.
      Gene 90:303-307(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
    2. "The cDNA sequence and gene analysis of the human pim oncogene."
      Zakut-Houri R., Hazum S., Givol D., Telerman A.
      Gene 54:105-111(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Comparison of the human and mouse PIM-1 cDNAs: nucleotide sequence and immunological identification of the in vitro synthesized PIM-1 protein."
      Domen J., von Lindern M., Hermans A., Breuer M., Grosveld G., Berns A.
      Oncogene Res. 1:103-112(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "Cloning and characterization of the human PIM-1 gene: a putative oncogene related to the protein kinases."
      Meeker T.C., Nagarajan L., Ar-Rushdi A., Croce C.M.
      J. Cell. Biochem. 35:105-112(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. "The 44 kDa Pim-1 kinase directly interacts with tyrosine kinase Etk/BMX and protects human prostate cancer cells from apoptosis induced by chemotherapeutic drugs."
      Xie Y., Xu K., Dai B., Guo Z., Jiang T., Chen H., Qiu Y.
      Oncogene 25:70-78(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE INITIATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH BMX.
    6. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 2).
      Tissue: Kidney.
    9. "Hypermutation of multiple proto-oncogenes in B-cell diffuse large-cell lymphomas."
      Pasqualucci L., Neumeister P., Goossens T., Nanjangud G., Chaganti R.S.K., Kuppers R., Dalla-Favera R.
      Nature 412:341-346(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 92-293 (ISOFORM 2).
    10. "Identification of the human pim-1 gene product as a 33-kilodalton cytoplasmic protein with tyrosine kinase activity."
      Telerman A., Amson R., Zakut-Houri R., Givol D.
      Mol. Cell. Biol. 8:1498-1503(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. "The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG."
      Saris C.J., Domen J., Berns A.
      EMBO J. 10:655-664(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE INITIATION.
    12. "Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1."
      Koike N., Maita H., Taira T., Ariga H., Iguchi-Ariga S.M.M.
      FEBS Lett. 467:17-21(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX3, FUNCTION IN PHOSPHORYLATION OF CBX3.
    13. "Phosphorylation of the cell cycle inhibitor p21Cip1/WAF1 by Pim-1 kinase."
      Wang Z., Bhattacharya N., Mixter P.F., Wei W., Sedivy J., Magnuson N.S.
      Biochim. Biophys. Acta 1593:45-55(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION IN PHOSPHORYLATION OF CDKN1A, INTERACTION WITH CDKN1A.
    14. "Pim-1 protein kinase is nuclear in Burkitt's lymphoma: nuclear localization is necessary for its biologic effects."
      Ionov Y., Le X., Tunquist B.J., Sweetenham J., Sachs T., Ryder J., Johnson T., Lilly M.B., Kraft A.S.
      Anticancer Res. 23:167-178(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. "Protein phosphatase 2A regulates the stability of Pim protein kinases."
      Losman J.A., Chen X.P., Vuong B.Q., Fay S., Rothman P.B.
      J. Biol. Chem. 278:4800-4805(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP2CA, PHOSPHORYLATION, UBIQUITINATION.
    16. "IL-5 and granulocyte-macrophage colony-stimulating factor activate STAT3 and STAT5 and promote Pim-1 and cyclin D3 protein expression in human eosinophils."
      Stout B.A., Bates M.E., Liu L.Y., Farrington N.N., Bertics P.J.
      J. Immunol. 173:6409-6417(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    17. "Pim-1 kinase stability is regulated by heat shock proteins and the ubiquitin-proteasome pathway."
      Shay K.P., Wang Z., Xing P.X., McKenzie I.F., Magnuson N.S.
      Mol. Cancer Res. 3:170-181(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH HSPCA AND HSP70, INDUCTION.
    18. "The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and activates the G2/M specific phosphatase Cdc25C."
      Bachmann M., Kosan C., Xing P.X., Montenarh M., Hoffmann I., Moroy T.
      Int. J. Biochem. Cell Biol. 38:430-443(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDC25C, INTERACTION WITH CDC25C.
    19. "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 CELL CYCLE PROGRESSION, INTERACTION WITH CDKN1B AND FOXO3, PHOSPHORYLATION OF CDKN1B AND FOXO3.
    20. "PIM1 phosphorylates and negatively regulates ASK1-mediated apoptosis."
      Gu J.J., Wang Z., Reeves R., Magnuson N.S.
      Oncogene 28:4261-4271(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAP3K5, INTERACTION WITH MAP3K5.
    21. "Pim-1 ligand-bound structures reveal the mechanism of serine/threonine kinase inhibition by LY294002."
      Jacobs M.D., Black J., Futer O., Swenson L., Hare B., Fleming M., Saxena K.
      J. Biol. Chem. 280:13728-13734(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 124-396 IN COMPLEXES WITH ADENOSINE AND INHIBITORS STAUROSPORINE AND LY294002, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-99; THR-114; SER-189 AND SER-352.
    22. "Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase."
      Qian K.C., Wang L., Hickey E.R., Studts J., Barringer K., Peng C., Kronkaitis A., Li J., White A., Mische S., Farmer B.
      J. Biol. Chem. 280:6130-6137(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 105-404 OF APOPROTEIN AND IN COMPLEX WITH AMP-PNP, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION.
    23. "Crystal structures of proto-oncogene kinase Pim1: a target of aberrant somatic hypermutations in diffuse large cell lymphoma."
      Kumar A., Mandiyan V., Suzuki Y., Zhang C., Rice J., Tsai J., Artis D.R., Ibrahim P., Bremer R.
      J. Mol. Biol. 348:183-193(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 120-404 OF APOPROTEIN AND IN COMPLEXES WITH AMP-PNP AND INHIBITORS, PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, MUTAGENESIS OF HIS-159; PRO-172; ASN-173 AND LEU-284.
    24. "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] HIS-144; GLN-215; LYS-226 AND ASP-233.

    Entry informationi

    Entry nameiPIM1_HUMAN
    AccessioniPrimary (citable) accession number: P11309
    Secondary accession number(s): Q38RT9, Q5T7H7, Q96RG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 177 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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