ID CLK1_HUMAN STANDARD; PRT; 484 AA. AC P49759; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE PROTEIN KINASE CLK1 (EC 2.7.1.-) (CLK). GN CLK OR CLK1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; OC Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 91139618. RA JOHNSON K.W., SMITH K.A.; RT "Molecular cloning of a novel human cdc2/CDC28-like protein kinase."; RL J. Biol. Chem. 266:3402-3407(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 95082033. RA HANES J.J., DER KAMMER H., KLAUDINY J.J., SCHEIT K.H.; RT "Characterization by cDNA cloning of two new human protein kinases. RT Evidence by sequence comparison of a new family of mammalian protein RT kinases."; RL J. Mol. Biol. 244:665-672(1994). CC -!- FUNCTION: PHOSPHORYLATES SERINE- AND ARGININE-RICH (SR) PROTEINS CC OF THE SPLICEOSOMAL COMPLEX MAY BE A CONSTITUENT OF A NETWORK OF CC REGULATORY MECHANISMS THAT ENABLE SR PROTEINS TO CONTROL RNA CC SPLICING. PHOSPHORYLATES SERINES, THREONINES AND TYROSINES (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS ARE PRODUCED BY ALTERNATIVE CC SPLICING, THE SHORTEST FORM LACK THE KINASE DOMAIN. CC -!- PTM: AUTOPHOSPHORYLATES ON ALL THREE TYPE OF RESIDUES (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC LAMMER SUBFAMILY. 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; L29219; AAA61480.1; -. DR EMBL; L29222; AAB59459.1; -. DR HSSP; Q16539; 1WFC. DR MIM; 601951; -. DR PFAM; PF00069; pkinase; 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 Tyrosine-protein kinase; Phosphorylation; Nuclear protein; KW Alternative splicing. FT DOMAIN 161 477 PROTEIN KINASE. FT NP_BIND 167 175 ATP (BY SIMILARITY). FT BINDING 191 191 ATP (BY SIMILARITY). FT ACT_SITE 288 288 BY SIMILARITY. FT VARSPLIC 131 136 KSHRRK -> MKLLIL (IN SHORT FORM). FT VARSPLIC 137 484 MISSING (IN SHORT FORM). SQ SEQUENCE 484 AA; 57205 MW; 99B67338 CRC32; MRHSKRTYCP DWDDKDWDYG KWRSSSSHKR RKRSHSSAQE NKRCKYNHSK MCDSHYLESR SINEKDYHSR RYIDEYRNDY TQGCEPGHRQ RDHESRYQNH SSKSSGRSGR SSYKSKHRIH HSTSHRRSHG KSHRRKRTRS VEDDEEGHLI CQSGDVLSAR YEIVDTLGEG AFGKVVECID HKAGGRHVAV KIVKNVDRYC EAARSEIQVL EHLNTTDPNS TFRCVQMLEW FEHHGHICIV FELLGLSTYD FIKENGFLPF RLDHIRKMAY QICKSVNFLH SNKLTHTDLK PENILFVQSD YTEAYNPKIK RDERTLINPD IKVVDFGSAT YDDEHHSTLV STRHYRAPEV ILALGWSQPC DVWSIGCILI EYYLGFTVFP THDSKEHLAM MERILGPLPK HMIQKTRKRK YFHHDRLDWD EHSSAGRYVS RACKPLKEFM LSQDVEHERL FDLIQKMLEY DPAKRITLRE ALKHPFFDLL KKSI //