ID STKA_HUMAN STANDARD; PRT; 968 AA. AC O94804; Q9UIW4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein kinase 10 (EC 2.7.1.37) (Lymphocyte-oriented DE kinase). GN STK10 OR LOK. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99216434; PubMed=10199912; 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 SEQUENCE OF 814-968 FROM N.A. RC TISSUE=Testis; RA Bloecker H., Boecher M., Brandt P., Mewes H.-W., Gassenhuber J., RA Wiemann S.; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CAN ACT ON SUBSTRATES SUCH AS MYELIN BASIC PROTEIN AND CC HISTONE IIA 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 FAMILY OF PROTEIN KINASES. CC STE20 SUBFAMILY. 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; -. DR EMBL; AL133081; CAB61400.1; -. DR PIR; T42687; T42687. DR HSSP; P24941; 1HCL. DR Genew; HGNC:11388; STK10. DR MIM; 603919; -. DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS. DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS. 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; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Phosphorylation; Coiled coil. FT DOMAIN 36 294 PROTEIN KINASE. FT DOMAIN 573 947 COILED COIL (POTENTIAL). FT DOMAIN 750 884 GLN-RICH. FT NP_BIND 42 50 ATP (BY SIMILARITY). FT BINDING 65 65 ATP (BY SIMILARITY). FT ACT_SITE 157 157 BY SIMILARITY. SQ SEQUENCE 968 AA; 112134 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 //