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O55098

- STK10_MOUSE

UniProt

O55098 - STK10_MOUSE

Protein

Serine/threonine-protein kinase 10

Gene

Stk10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Inhibited by the pyrrole-indolinone inhibitor SU11274 (K00593): intercalates between the ATP-binding Lys-65 and alpha-C glutamate (Glu-81), resulting in a partial disordering of the lysine side chain. Also specifically inhibited by erlotinib. Slightly inhibited by gefitinib By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651ATPPROSITE-ProRule annotation
    Binding sitei111 – 1111InhibitorBy similarity
    Binding sitei113 – 1131InhibitorBy similarity
    Binding sitei117 – 1171Inhibitor; via amide nitrogenBy similarity
    Active sitei157 – 1571Proton acceptorPROSITE-ProRule annotation
    Binding sitei175 – 1751InhibitorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi42 – 509ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. lymphocyte aggregation Source: UniProtKB
    3. protein autophosphorylation Source: UniProtKB
    4. regulation of lymphocyte migration Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase 10 (EC:2.7.11.1)
    Alternative name(s):
    Lymphocyte-oriented kinase
    Gene namesi
    Name:Stk10
    Synonyms:Lok
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1099439. Stk10.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice do not show any obvious abnormalities. Lymphocytes develop normally but activated lymphocytes show enhanced cell adhesion. Decreased phosphorylation of ERM proteins.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 966966Serine/threonine-protein kinase 10PRO_0000086698Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131PhosphoserineBy similarity
    Modified residuei185 – 1851Phosphothreonine; by autocatalysisBy similarity
    Modified residuei191 – 1911Phosphoserine; by autocatalysisBy similarity
    Modified residuei437 – 4371PhosphoserineBy similarity
    Modified residuei443 – 4431PhosphoserineBy similarity
    Modified residuei453 – 4531PhosphoserineBy similarity
    Modified residuei548 – 5481PhosphoserineBy similarity
    Modified residuei950 – 9501Phosphothreonine1 Publication

    Post-translational modificationi

    Autophosphorylates following homodimerization, leading to activation of the protein.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO55098.
    PaxDbiO55098.
    PRIDEiO55098.

    PTM databases

    PhosphoSiteiO55098.

    Expressioni

    Tissue specificityi

    Expressed predominantly in lymphoid organs such as spleen, thymus, and bone marrow.

    Gene expression databases

    BgeeiO55098.
    CleanExiMM_STK10.
    GenevestigatoriO55098.

    Interactioni

    Subunit structurei

    Homodimer; homodimerization is required for activation segment autophosphorylation.By similarity

    Protein-protein interaction databases

    IntActiO55098. 2 interactions.
    MINTiMINT-4135895.
    STRINGi10090.ENSMUSP00000099885.

    Structurei

    3D structure databases

    ProteinModelPortaliO55098.
    SMRiO55098. Positions 24-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 294259Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni175 – 22450Activation segmentBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili588 – 936349Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi749 – 883135Gln-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000114927.
    HOVERGENiHBG052712.
    InParanoidiB1ATW8.
    KOiK08837.
    OMAiSEEAECP.
    OrthoDBiEOG7CNZF6.
    TreeFamiTF351445.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR022165. PKK.
    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.
    PF12474. PKK. 2 hits.
    [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.

    O55098-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFANFRRIL RLSTFEKRKS REYEHVRRDL DPNDVWEIVG ELGDGAFGKV    50
    YKAKNKETGA LAAAKVIETK SEEELEDYIV EIEILATCDH PYIVKLLGAY 100
    YYDGKLWIMI EFCPGGAVDA IMLELDRGLT EPQIQVVCRQ MLEALNFLHG 150
    KRIIHRDLKA GNVLMTLEGD IRLADFGVSA KNLKTLQKRD SFIGTPYWMA 200
    PEVVLCETMK DAPYDYKADI WSLGITLIEM AQIEPPHHEL NPMRVLLKIA 250
    KSDPPTLLTP SKWSVEFRDF LKIALDKNPE TRPSAAQLLQ HPFVSRVTSN 300
    KALRELVAEA KAEVMEEIED GREDGEEEDA VDAVPPLVNH TQDSANVTQP 350
    SLDSNKLLQD SSTPLPPSQP QEPVSGSCSQ PSGDGPLQTT SPADGLSKND 400
    NDLKVPVPLR KSRPLSMDAR IQMDEEKQIP DQDENPSPAA SKSQKANQSR 450
    PNSSALETLG GEALTNGGLE LPSSVTPSHS KRASDCSNLS TSESMDYGTS 500
    LSADLSLNKE TGSLSLKGSK LHNKTLKRTR RFVVDGVEVS ITTSKIISED 550
    EKKDEEMRFL RRQELRELRL LQKEEHRNQT QLSSKHELQL EQMHKRFEQE 600
    INAKKKFYDV ELENLERQQK QQVEKMEQDH SVRRKEEAKR IRLEQDRDYA 650
    KFQEQLKQMK KEVKSEVEKL PRQQRKESMK QKMEEHSQKK QRLDRDFVAK 700
    QKEDLELAMR KLTTENRREI CDKERDCLSK KQELLRDREA ALWEMEEHQL 750
    QERHQLVKQQ LKDQYFLQRH DLLRKHEKER EQMQRYNQRM MEQLKVRQQQ 800
    EKARLPKIQR SDGKTRMAMY KKSLHINGAG SASEQREKIK QFSQQEEKRQ 850
    KAERLQQQQK HENQMRDMVA QCESNMSELQ QLQNEKCHLL VEHETQKLKA 900
    LDESHNQSLK EWRDKLRPRK KALEEDLNQK KREQEMFFKL SEEAEPRPTT 950
    PSKASNFFPY SSGDAS 966
    Length:966
    Mass (Da):111,906
    Last modified:July 27, 2011 - v2
    Checksum:i7A95ABF9D58C8699
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti375 – 3773SGS → NGP in BAA24073. (PubMed:9278426)Curated
    Sequence conflicti814 – 8141K → E in BAA24073. (PubMed:9278426)Curated
    Sequence conflicti863 – 8631N → H in BAA24073. (PubMed:9278426)Curated
    Sequence conflicti888 – 8881H → Y in BAA24073. (PubMed:9278426)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89728 mRNA. Translation: BAA24073.1.
    AL669844 Genomic DNA. Translation: CAI25517.1.
    CCDSiCCDS24529.1.
    RefSeqiNP_033314.2. NM_009288.2.
    UniGeneiMm.8235.

    Genome annotation databases

    EnsembliENSMUST00000102821; ENSMUSP00000099885; ENSMUSG00000020272.
    GeneIDi20868.
    KEGGimmu:20868.
    UCSCiuc007ijt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89728 mRNA. Translation: BAA24073.1 .
    AL669844 Genomic DNA. Translation: CAI25517.1 .
    CCDSi CCDS24529.1.
    RefSeqi NP_033314.2. NM_009288.2.
    UniGenei Mm.8235.

    3D structure databases

    ProteinModelPortali O55098.
    SMRi O55098. Positions 24-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O55098. 2 interactions.
    MINTi MINT-4135895.
    STRINGi 10090.ENSMUSP00000099885.

    PTM databases

    PhosphoSitei O55098.

    Proteomic databases

    MaxQBi O55098.
    PaxDbi O55098.
    PRIDEi O55098.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102821 ; ENSMUSP00000099885 ; ENSMUSG00000020272 .
    GeneIDi 20868.
    KEGGi mmu:20868.
    UCSCi uc007ijt.1. mouse.

    Organism-specific databases

    CTDi 6793.
    MGIi MGI:1099439. Stk10.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000114927.
    HOVERGENi HBG052712.
    InParanoidi B1ATW8.
    KOi K08837.
    OMAi SEEAECP.
    OrthoDBi EOG7CNZF6.
    TreeFami TF351445.

    Miscellaneous databases

    ChiTaRSi STK10. mouse.
    NextBioi 299697.
    PROi O55098.
    SOURCEi Search...

    Gene expression databases

    Bgeei O55098.
    CleanExi MM_STK10.
    Genevestigatori O55098.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR022165. PKK.
    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.
    PF12474. PKK. 2 hits.
    [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. "LOK is a novel mouse STE20-like protein kinase that is expressed predominantly in lymphocytes."
      Kuramochi S., Moriguchi T., Kuida K., Endo J., Semba K., Nishida E., Karasuyama H.
      J. Biol. Chem. 272:22679-22684(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Thymus.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Deficiency of a STE20/PAK family kinase LOK leads to the acceleration of LFA-1 clustering and cell adhesion of activated lymphocytes."
      Endo J., Toyama-Sorimachi N., Taya C., Kuramochi-Miyagawa S., Nagata K., Kuida K., Takashi T., Yonekawa H., Yoshizawa Y., Miyasaka N., Karasuyama H.
      FEBS Lett. 468:234-238(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    4. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-950, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    6. "LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation."
      Belkina N.V., Liu Y., Hao J.J., Karasuyama H., Shaw S.
      Proc. Natl. Acad. Sci. U.S.A. 106:4707-4712(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiSTK10_MOUSE
    AccessioniPrimary (citable) accession number: O55098
    Secondary accession number(s): B1ATW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3