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O94804

- STK10_HUMAN

UniProt

O94804 - STK10_HUMAN

Protein

Serine/threonine-protein kinase 10

Gene

STK10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    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.2 Publications

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. polo kinase kinase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. lymphocyte aggregation Source: Ensembl
    3. protein autophosphorylation Source: UniProtKB
    4. protein phosphorylation Source: ProtInc
    5. regulation of lymphocyte migration Source: UniProtKB
    6. signal transduction by phosphorylation Source: GOC

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiO94804.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:11388. STK10.

    Subcellular locationi

    Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma.1 Publication
    Note: The disease may be caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti277 – 2771K → E in TGCT; somatic mutation. 2 Publications
    VAR_023827

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651K → I: Loss of kinase activity. 1 Publication

    Organism-specific databases

    MIMi273300. phenotype.
    PharmGKBiPA36197.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 968968Serine/threonine-protein kinase 10PRO_0000086697Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131Phosphoserine1 Publication
    Modified residuei191 – 1911Phosphoserine3 Publications
    Modified residuei438 – 4381Phosphoserine7 Publications
    Modified residuei444 – 4441Phosphoserine1 Publication
    Modified residuei454 – 4541Phosphoserine1 Publication
    Modified residuei549 – 5491Phosphoserine1 Publication
    Modified residuei952 – 9521Phosphothreonine1 Publication

    Post-translational modificationi

    Autophosphorylates following homodimerization, leading to activation of the protein.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO94804.
    PaxDbiO94804.
    PRIDEiO94804.

    PTM databases

    PhosphoSiteiO94804.

    Expressioni

    Tissue specificityi

    Highly expressed in rapidly proliferating tissues (spleen, placenta, and peripheral blood leukocytes). Also expressed in brain, heart, skeletal muscle, colon, thymus, kidney, liver, small intestine and lung.1 Publication

    Gene expression databases

    BgeeiO94804.
    CleanExiHS_STK10.
    GenevestigatoriO94804.

    Organism-specific databases

    HPAiCAB020840.
    HPA015083.

    Interactioni

    Subunit structurei

    Homodimer; homodimerization is required for activation segment autophosphorylation.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-3951541,EBI-3951541

    Protein-protein interaction databases

    BioGridi112669. 2 interactions.

    Structurei

    Secondary structure

    1
    968
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 304
    Helixi32 – 343
    Beta strandi36 – 438
    Beta strandi50 – 556
    Turni56 – 583
    Beta strandi61 – 677
    Helixi75 – 8713
    Beta strandi96 – 1016
    Beta strandi106 – 1116
    Helixi118 – 1258
    Helixi131 – 15020
    Helixi160 – 1623
    Beta strandi163 – 1653
    Beta strandi171 – 1733
    Helixi177 – 18711
    Helixi196 – 1983
    Helixi201 – 2088
    Turni212 – 2165
    Helixi217 – 23216
    Turni236 – 2394
    Helixi242 – 25110
    Helixi260 – 2623
    Helixi265 – 27410
    Turni279 – 2813
    Helixi285 – 2884
    Turni292 – 2965
    Helixi301 – 31414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2J7TX-ray2.00A18-317[»]
    4AOTX-ray2.33A/B18-317[»]
    4BC6X-ray2.20A24-316[»]
    4EQUX-ray2.00A/B18-317[»]
    ProteinModelPortaliO94804.
    SMRiO94804. Positions 24-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94804.

    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 segmentAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili573 – 947375Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi750 – 884135Gln-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000236268.
    HOVERGENiHBG052712.
    InParanoidiO94804.
    KOiK08837.
    OMAiSEEAECP.
    OrthoDBiEOG7CNZF6.
    PhylomeDBiO94804.
    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.

    O94804-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFANFRRIL RLSTFEKRKS REYEHVRRDL DPNEVWEIVG ELGDGAFGKV    50
    YKAKNKETGA LAAAKVIETK SEEELEDYIV EIEILATCDH PYIVKLLGAY 100
    YHDGKLWIMI EFCPGGAVDA IMLELDRGLT EPQIQVVCRQ MLEALNFLHS 150
    KRIIHRDLKA GNVLMTLEGD IRLADFGVSA KNLKTLQKRD SFIGTPYWMA 200
    PEVVMCETMK DTPYDYKADI WSLGITLIEM AQIEPPHHEL NPMRVLLKIA 250
    KSDPPTLLTP SKWSVEFRDF LKIALDKNPE TRPSAAQLLE HPFVSSITSN 300
    KALRELVAEA KAEVMEEIED GRDEGEEEDA VDAASTLENH TQNSSEVSPP 350
    SLNADKPLEE SPSTPLAPSQ SQDSVNEPCS QPSGDRSLQT TSPPVVAPGN 400
    ENGLAVPVPL RKSRPVSMDA RIQVAQEKQV AEQGGDLSPA ANRSQKASQS 450
    RPNSSALETL GGEKLANGSL EPPAQAAPGP SKRDSDCSSL CTSESMDYGT 500
    NLSTDLSLNK EMGSLSIKDP KLYKKTLKRT RKFVVDGVEV SITTSKIISE 550
    DEKKDEEMRF LRRQELRELR LLQKEEHRNQ TQLSNKHELQ LEQMHKRFEQ 600
    EINAKKKFFD TELENLERQQ KQQVEKMEQD HAVRRREEAR RIRLEQDRDY 650
    TRFQEQLKLM KKEVKNEVEK LPRQQRKESM KQKMEEHTQK KQLLDRDFVA 700
    KQKEDLELAM KRLTTDNRRE ICDKERECLM KKQELLRDRE AALWEMEEHQ 750
    LQERHQLVKQ QLKDQYFLQR HELLRKHEKE REQMQRYNQR MIEQLKVRQQ 800
    QEKARLPKIQ RSEGKTRMAM YKKSLHINGG GSAAEQREKI KQFSQQEEKR 850
    QKSERLQQQQ KHENQMRDML AQCESNMSEL QQLQNEKCHL LVEHETQKLK 900
    ALDESHNQNL KEWRDKLRPR KKALEEDLNQ KKREQEMFFK LSEEAECPNP 950
    STPSKAAKFF PYSSADAS 968
    Length:968
    Mass (Da):112,135
    Last modified:May 1, 1999 - v1
    Checksum:i15E245193ECC553D
    GO

    Sequence cautioni

    The sequence BAG51143.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti62 – 621A → V in AAH70077. (PubMed:15489334)Curated
    Sequence conflicti136 – 1361V → E in AAH70077. (PubMed:15489334)Curated
    Sequence conflicti317 – 3171E → G in AAH70077. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti268 – 2681R → C.1 Publication
    Corresponds to variant rs35826078 [ dbSNP | Ensembl ].
    VAR_041131
    Natural varianti277 – 2771K → E in TGCT; somatic mutation. 2 Publications
    VAR_023827
    Natural varianti322 – 3221R → W.1 Publication
    Corresponds to variant rs56214442 [ dbSNP | Ensembl ].
    VAR_041132
    Natural varianti336 – 3361T → I.1 Publication
    Corresponds to variant rs55972616 [ dbSNP | Ensembl ].
    VAR_041133
    Natural varianti467 – 4671N → S.1 Publication
    Corresponds to variant rs56063773 [ dbSNP | Ensembl ].
    VAR_041134
    Natural varianti480 – 4801P → L.
    Corresponds to variant rs34505340 [ dbSNP | Ensembl ].
    VAR_051671
    Natural varianti520 – 5201P → L.
    Corresponds to variant rs17074311 [ dbSNP | Ensembl ].
    VAR_051672
    Natural varianti710 – 7101M → T.1 Publication
    Corresponds to variant rs34936670 [ dbSNP | Ensembl ].
    VAR_041135
    Natural varianti853 – 8531S → L.1 Publication
    Corresponds to variant rs56066852 [ dbSNP | Ensembl ].
    VAR_041136
    Natural varianti905 – 9051S → T.1 Publication
    Corresponds to variant rs55791916 [ dbSNP | Ensembl ].
    VAR_041137
    Natural varianti942 – 9421S → N.
    Corresponds to variant rs1128204 [ dbSNP | Ensembl ].
    VAR_051673
    Natural varianti947 – 9471C → Y.1 Publication
    Corresponds to variant rs56355550 [ dbSNP | Ensembl ].
    VAR_041138

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015718 mRNA. Translation: BAA35073.1.
    AK022960 mRNA. Translation: BAG51143.1. Different initiation.
    AK313350 mRNA. Translation: BAG36152.1.
    AC024561 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61439.1.
    BC070077 mRNA. Translation: AAH70077.1.
    AL133081 mRNA. Translation: CAB61400.1.
    CCDSiCCDS34290.1.
    PIRiT42687.
    RefSeqiNP_005981.3. NM_005990.3.
    UniGeneiHs.744005.

    Genome annotation databases

    EnsembliENST00000176763; ENSP00000176763; ENSG00000072786.
    GeneIDi6793.
    KEGGihsa:6793.
    UCSCiuc003mbo.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015718 mRNA. Translation: BAA35073.1 .
    AK022960 mRNA. Translation: BAG51143.1 . Different initiation.
    AK313350 mRNA. Translation: BAG36152.1 .
    AC024561 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61439.1 .
    BC070077 mRNA. Translation: AAH70077.1 .
    AL133081 mRNA. Translation: CAB61400.1 .
    CCDSi CCDS34290.1.
    PIRi T42687.
    RefSeqi NP_005981.3. NM_005990.3.
    UniGenei Hs.744005.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2J7T X-ray 2.00 A 18-317 [» ]
    4AOT X-ray 2.33 A/B 18-317 [» ]
    4BC6 X-ray 2.20 A 24-316 [» ]
    4EQU X-ray 2.00 A/B 18-317 [» ]
    ProteinModelPortali O94804.
    SMRi O94804. Positions 24-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112669. 2 interactions.

    Chemistry

    BindingDBi O94804.
    ChEMBLi CHEMBL3981.
    GuidetoPHARMACOLOGYi 2211.

    PTM databases

    PhosphoSitei O94804.

    Proteomic databases

    MaxQBi O94804.
    PaxDbi O94804.
    PRIDEi O94804.

    Protocols and materials databases

    DNASUi 6793.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000176763 ; ENSP00000176763 ; ENSG00000072786 .
    GeneIDi 6793.
    KEGGi hsa:6793.
    UCSCi uc003mbo.1. human.

    Organism-specific databases

    CTDi 6793.
    GeneCardsi GC05M171403.
    HGNCi HGNC:11388. STK10.
    HPAi CAB020840.
    HPA015083.
    MIMi 273300. phenotype.
    603919. gene.
    neXtProti NX_O94804.
    PharmGKBi PA36197.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000236268.
    HOVERGENi HBG052712.
    InParanoidi O94804.
    KOi K08837.
    OMAi SEEAECP.
    OrthoDBi EOG7CNZF6.
    PhylomeDBi O94804.
    TreeFami TF351445.

    Enzyme and pathway databases

    SignaLinki O94804.

    Miscellaneous databases

    ChiTaRSi STK10. human.
    EvolutionaryTracei O94804.
    GeneWikii STK10.
    GenomeRNAii 6793.
    NextBioi 26535.
    PROi O94804.
    SOURCEi Search...

    Gene expression databases

    Bgeei O94804.
    CleanExi HS_STK10.
    Genevestigatori O94804.

    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. "Molecular cloning of the human gene STK10 encoding lymphocyte-oriented kinase, and comparative chromosomal mapping of the human, mouse, and rat homologues."
      Kuramochi S., Matsuda Y., Okamoto M., Kitamura F., Yonekawa H., Karasuyama H.
      Immunogenetics 49:369-375(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Tissue: Teratocarcinoma and Testis.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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: Testis.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 814-968.
      Tissue: Testis.
    7. "Opposing roles of serine/threonine kinases MEKK1 and LOK in regulating the CD28 responsive element in T-cells."
      Tao L., Wadsworth S., Mercer J., Mueller C., Lynn K., Siekierka J., August A.
      Biochem. J. 363:175-182(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Stk10, a new member of the polo-like kinase kinase family highly expressed in hematopoietic tissue."
      Walter S.A., Cutler R.E. Jr., Martinez R., Gishizky M., Hill R.J.
      J. Biol. Chem. 278:18221-18228(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-65.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-191; SER-454 AND THR-952, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-438; SER-444 AND SER-549, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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, SUBCELLULAR LOCATION.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Off-target serine/threonine kinase 10 inhibition by erlotinib enhances lymphocytic activity leading to severe skin disorders."
      Yamamoto N., Honma M., Suzuki H.
      Mol. Pharmacol. 80:466-475(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites."
      Pike A.C., Rellos P., Niesen F.H., Turnbull A., Oliver A.W., Parker S.A., Turk B.E., Pearl L.H., Knapp S.
      EMBO J. 27:704-714(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-317 IN COMPLEX WITH PYRROLE-INDOLINONE INHIBITOR, ENZYME REGULATION, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, SUBUNIT.
    23. "Sequence analysis of the protein kinase gene family in human testicular germ-cell tumors of adolescents and adults."
      Bignell G., Smith R., Hunter C., Stephens P., Davies H., Greenman C., Teague J., Butler A., Edkins S., Stevens C., O'meara S., Parker A., Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J.
      , Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R., Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R., Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A., West S., Widaa S., Yates A., Gillis A.J.M., Stoop H.J., van Gurp R.J.H.L.M., Oosterhuis J.W., Looijenga L.H.J., Futreal P.A., Wooster R., Stratton M.R.
      Genes Chromosomes Cancer 45:42-46(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TGCT GLU-277.
    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] CYS-268; GLU-277; TRP-322; ILE-336; SER-467; THR-710; LEU-853; THR-905 AND TYR-947.

    Entry informationi

    Entry nameiSTK10_HUMAN
    AccessioniPrimary (citable) accession number: O94804
    Secondary accession number(s): A6ND35
    , B2R8F5, B3KMY1, Q6NSK0, Q9UIW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 142 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

    Miscellaneous

    Inhibition by erlotinib, an orally administered EGFR tyrosine kinase inhibitor used for treatment, enhances STK10-dependent lymphocytic responses, possibly leading to the aggravation of skin inflammation observed upon treatment by erlotinib.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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