ID KS61_HUMAN STANDARD; PRT; 735 AA. AC Q15418; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE RIBOSOMAL PROTEIN S6 KINASE II ALPHA 1 (EC 2.7.1.-) (S6KII-ALPHA 1) DE (P90-RSK 1) (RIBOSOMAL S6 KINASE 1) (RSK1) (PP90RSK1). GN RPS6KA1 OR RSK1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 94189676. RA Moller D.E., Xia C.-H., Tang W., Zhu A.X., Jakubowski M.; RT "Human rsk isoforms: cloning and characterization of tissue-specific RT expression."; RL Am. J. Physiol. 266:C351-C359(1994). CC -!- FUNCTION: PHOSPHORYLATES A WIDE RANGE OF SUBSTRATES INCLUDING CC RIBOSOMAL PROTEIN S6. IMPLICATED IN THE ACTIVATION OF THE MITOGEN- CC ACTIVATED KINASE CASCADE. CC -!- SIMILARITY: BELONGS TO THE PROTEIN KINASE SUPERFAMILY; SER/THR CC FAMILY. CONTAINS TWO KINASE DOMAINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; L07597; AAC82497.1; -. DR MIM; 601684; -. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR000961; -. DR INTERPRO; IPR002290; -. DR PFAM; PF00069; pkinase; 2. DR PFAM; PF00433; pkinase_C; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Repeat; Multigene family. FT DOMAIN 62 321 PROTEIN KINASE 1. FT DOMAIN 418 675 PROTEIN KINASE 2. FT NP_BIND 68 76 ATP (BY SIMILARITY). FT BINDING 94 94 ATP (BY SIMILARITY). FT ACT_SITE 187 187 BY SIMILARITY. FT NP_BIND 424 432 ATP (BY SIMILARITY). FT BINDING 447 447 ATP (BY SIMILARITY). FT ACT_SITE 535 535 BY SIMILARITY. SQ SEQUENCE 735 AA; 82695 MW; DD599F3A7EFEB506 CRC64; MPLAQLKEPW PLMELVPLDP ENGQTSGEEA GLQPSKDEGV LKEISITHHV KAGSEKADPS HFELLKVLGQ GSFGKVFLVR KVTRPDSGHL YAMKVLKKAT LKVRDRVRTK MERDILADVN HPFVVKLHYA FQTEGKLYLI LDFLRGGDLF TRLSKEVMFT EEDVKFYLAE LALGLDHLHS LGIIYRDLKP ENILLDEEGH IKLTDFGLSK EAIDHEKKAY SFCGTVEYMA PEVVNRQGHS HSADWWSYGV LMFEMLTGSL PFQGKDRKET MTLILKAKLG MPQFLSTEAQ SLLRALFKRN PANRLGSGPD GAEEIKRHVF YSTIDWNKLY RREITPPFKP AVAQPDDTFY FDTEFTSRTP KDSPGIPPSA GAHQLFRGFS FVATGLMEDD GKPRAPQAPL HSVVQQLHGK NLVFSDGYVV KETIGVGSYS ECKRCVHKAT NMEYAVKVID KSKRDPSEEI EILLRYGQHP NIITLKDVYD DGKHVYLVTE LMRGGELLDK ILRQKFFSER EASFVLHTIG KTVEYLHSQG VVHRDLKPSN ILYVDESGNP ECLRICDFGF AKQLRAENGL LMTPCYTANF VAPEVLKRQG YDEGCDIWSL GILLYTMLAG YTPFANGPSD TPEEILTRIG SGKFTLSGGN WNTVSETAKD LVSKMLHVDP HQRLTAKQVL QHPWVTQKDK LPQSQLSHQD LQLVKGAMAA TYSALNSSKP TPQLKPIESS ILAQRRVRKL PSTTL //