ID STK10_HUMAN Reviewed; 968 AA. AC O94804; Q9UIW4; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 03-APR-2007, entry version 63. DE Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented DE kinase). GN Name=STK10; Synonyms=LOK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=99216434; PubMed=10199912; DOI=10.1007/s002510050509; RA Kuramochi S., Matsuda Y., Okamoto M., Kitamura F., Yonekawa H., RA Karasuyama H.; RT "Molecular cloning of the human gene STK10 encoding lymphocyte- RT oriented kinase, and comparative chromosomal mapping of the human, RT mouse, and rat homologues."; RL Immunogenetics 49:369-375(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 814-968. RC TISSUE=Testis; RG The German cDNA consortium; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASS RP SPECTROMETRY. RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASS RP SPECTROMETRY. RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASS RP SPECTROMETRY. RX PubMed=17192257; DOI=10.1074/mcp.T600062-MCP200; RA Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., RA Keri G., Wehland J., Daub H.; RT "Proteomic analysis of protein kinases by target class-selective pre- RT fractionation and tandem mass spectrometry."; RL Mol. Cell. Proteomics 0:0-0(2007). RN [6] RP VARIANT TGCT GLU-277. RX PubMed=16175573; DOI=10.1002/gcc.20265; RA Bignell G., Smith R., Hunter C., Stephens P., Davies H., Greenman C., RA Teague J., Butler A., Edkins S., Stevens C., O'meara S., Parker A., RA Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J., RA Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K., RA Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R., RA Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R., RA Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A., RA West S., Widaa S., Yates A., Gillis A.J.M., Stoop H.J., RA van Gurp R.J.H.L.M., Oosterhuis J.W., Looijenga L.H.J., Futreal P.A., RA Wooster R., Stratton M.R.; RT "Sequence analysis of the protein kinase gene family in human RT testicular germ-cell tumors of adolescents and adults."; RL Genes Chromosomes Cancer 45:42-46(2006). CC -!- FUNCTION: Can act on substrates such as myelin basic protein and CC histone 2A on serine and threonine residues (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- TISSUE SPECIFICITY: Expressed predominantly in lymphoid organs. CC -!- PTM: Autophosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. STE20 CC subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB015718; BAA35073.1; -; mRNA. DR EMBL; AL133081; CAB61400.1; -; mRNA. DR PIR; T42687; T42687. DR UniGene; Hs.519756; -. DR UniGene; Hs.594403; -. DR PDB; 2J7T; X-ray; A=18-317. DR Ensembl; ENSG00000072786; Homo sapiens. DR KEGG; hsa:6793; -. DR HGNC; HGNC:11388; STK10. DR MIM; 603919; gene. DR ArrayExpress; O94804; -. DR GermOnline; ENSG00000072786; Homo sapiens. DR RZPD-ProtExp; IOH13994; -. DR RZPD-ProtExp; T2295; -. DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc. DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS:ProtInc. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW 3D-structure; ATP-binding; Coiled coil; Disease mutation; Kinase; KW Nucleotide-binding; Phosphorylation; Serine/threonine-protein kinase; KW Transferase. FT CHAIN 1 968 Serine/threonine-protein kinase 10. FT /FTId=PRO_0000086697. FT DOMAIN 36 294 Protein kinase. FT NP_BIND 42 50 ATP (By similarity). FT COILED 573 947 Potential. FT COMPBIAS 750 884 Gln-rich. FT ACT_SITE 157 157 Proton acceptor (By similarity). FT BINDING 65 65 ATP (By similarity). FT MOD_RES 438 438 Phosphoserine. FT VARIANT 277 277 K -> E (in a testicular germ cell tumor FT (TGCT); somatic mutation). FT /FTId=VAR_023827. FT STRAND 27 30 FT HELIX 32 34 FT STRAND 36 43 FT STRAND 50 55 FT TURN 56 58 FT STRAND 61 67 FT HELIX 75 87 FT STRAND 96 101 FT STRAND 106 111 FT HELIX 118 125 FT HELIX 131 150 FT HELIX 160 162 FT STRAND 163 165 FT STRAND 171 173 FT HELIX 177 187 FT HELIX 196 198 FT HELIX 201 208 FT TURN 212 216 FT HELIX 217 232 FT TURN 236 239 FT HELIX 242 251 FT HELIX 260 262 FT HELIX 265 274 FT TURN 279 281 FT HELIX 285 288 FT TURN 292 296 FT HELIX 301 314 SQ SEQUENCE 968 AA; 112135 MW; 15E245193ECC553D CRC64; MAFANFRRIL RLSTFEKRKS REYEHVRRDL DPNEVWEIVG ELGDGAFGKV YKAKNKETGA LAAAKVIETK SEEELEDYIV EIEILATCDH PYIVKLLGAY YHDGKLWIMI EFCPGGAVDA IMLELDRGLT EPQIQVVCRQ MLEALNFLHS KRIIHRDLKA GNVLMTLEGD IRLADFGVSA KNLKTLQKRD SFIGTPYWMA PEVVMCETMK DTPYDYKADI WSLGITLIEM AQIEPPHHEL NPMRVLLKIA KSDPPTLLTP SKWSVEFRDF LKIALDKNPE TRPSAAQLLE HPFVSSITSN KALRELVAEA KAEVMEEIED GRDEGEEEDA VDAASTLENH TQNSSEVSPP SLNADKPLEE SPSTPLAPSQ SQDSVNEPCS QPSGDRSLQT TSPPVVAPGN ENGLAVPVPL RKSRPVSMDA RIQVAQEKQV AEQGGDLSPA ANRSQKASQS RPNSSALETL GGEKLANGSL EPPAQAAPGP SKRDSDCSSL CTSESMDYGT NLSTDLSLNK EMGSLSIKDP KLYKKTLKRT RKFVVDGVEV SITTSKIISE DEKKDEEMRF LRRQELRELR LLQKEEHRNQ TQLSNKHELQ LEQMHKRFEQ EINAKKKFFD TELENLERQQ KQQVEKMEQD HAVRRREEAR RIRLEQDRDY TRFQEQLKLM KKEVKNEVEK LPRQQRKESM KQKMEEHTQK KQLLDRDFVA KQKEDLELAM KRLTTDNRRE ICDKERECLM KKQELLRDRE AALWEMEEHQ LQERHQLVKQ QLKDQYFLQR HELLRKHEKE REQMQRYNQR MIEQLKVRQQ QEKARLPKIQ RSEGKTRMAM YKKSLHINGG GSAAEQREKI KQFSQQEEKR QKSERLQQQQ KHENQMRDML AQCESNMSEL QQLQNEKCHL LVEHETQKLK ALDESHNQNL KEWRDKLRPR KKALEEDLNQ KKREQEMFFK LSEEAECPNP STPSKAAKFF PYSSADAS //