ID CLK1_HUMAN STANDARD; PRT; 484 AA. AC P49759; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 18-APR-2006, entry version 52. DE Dual specificity protein kinase CLK1 (EC 2.7.12.1) (CDC-like kinase DE 1). GN Name=CLK1; Synonyms=CLK; 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=91139618; PubMed=1704889; 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 NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95082033; PubMed=7990150; 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). RN [3] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004). 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 -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with PPIG. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P49759-1; Sequence=Displayed; CC Name=Short; CC IsoId=P49759-2; Sequence=VSP_004852, VSP_004853; CC Note=Lacks the kinase domain. May be produced at very low levels CC due to a premature stop codon in the mRNA, leading to CC nonsense-mediated mRNA decay; CC -!- PTM: Autophosphorylates on all three types of residues (By CC similarity). CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. Lammer CC 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; L29219; AAA61480.1; -; mRNA. DR EMBL; L29222; AAB59459.1; -; mRNA. DR PIR; S53641; S53641. DR UniGene; Hs.433732; -. DR PDB; 1Z57; X-ray; A=148-484. DR Ensembl; ENSG00000013441; Homo sapiens. DR H-InvDB; HIX0002728; -. DR HGNC; HGNC:2068; CLK1. DR MIM; 601951; gene. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kina...; TAS. DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS. DR GO; GO:0008283; P:cell proliferation; TAS. DR GO; GO:0000074; P:regulation of progression through cell cycle; TAS. 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; Alternative splicing; ATP-binding; Kinase; KW Nuclear protein; Nucleotide-binding; Phosphorylation; KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase. FT CHAIN 1 484 Dual specificity protein kinase CLK1. FT /FTId=PRO_0000085866. FT DOMAIN 161 477 Protein kinase. FT NP_BIND 167 175 ATP (By similarity). FT ACT_SITE 288 288 Proton acceptor (By similarity). FT BINDING 191 191 ATP (By similarity). FT VARSPLIC 131 136 KSHRRK -> MKLLIL (in isoform Short). FT /FTId=VSP_004852. FT VARSPLIC 137 484 Missing (in isoform Short). FT /FTId=VSP_004853. FT HELIX 148 149 FT TURN 150 150 FT STRAND 152 152 FT TURN 153 154 FT STRAND 156 157 FT TURN 158 160 FT STRAND 161 170 FT TURN 171 172 FT STRAND 173 180 FT TURN 181 185 FT STRAND 187 193 FT STRAND 195 196 FT HELIX 197 216 FT TURN 218 219 FT TURN 221 222 FT STRAND 224 224 FT STRAND 227 233 FT TURN 234 235 FT STRAND 236 242 FT STRAND 247 247 FT HELIX 248 254 FT TURN 255 257 FT HELIX 262 281 FT TURN 282 283 FT STRAND 284 285 FT HELIX 291 293 FT STRAND 294 297 FT STRAND 301 305 FT STRAND 312 317 FT STRAND 321 323 FT STRAND 327 328 FT STRAND 330 331 FT TURN 332 333 FT STRAND 334 334 FT STRAND 338 339 FT STRAND 341 341 FT HELIX 343 345 FT HELIX 348 351 FT TURN 352 353 FT STRAND 354 354 FT TURN 358 358 FT HELIX 359 374 FT STRAND 375 376 FT STRAND 378 378 FT STRAND 382 382 FT HELIX 384 395 FT STRAND 397 397 FT HELIX 400 405 FT STRAND 407 407 FT HELIX 409 411 FT STRAND 412 413 FT TURN 414 415 FT STRAND 416 417 FT TURN 421 422 FT STRAND 423 423 FT HELIX 424 432 FT HELIX 436 439 FT STRAND 441 441 FT STRAND 444 444 FT HELIX 445 457 FT TURN 458 458 FT STRAND 460 461 FT TURN 462 464 FT STRAND 465 465 FT HELIX 468 471 FT TURN 472 473 FT STRAND 474 474 FT HELIX 475 481 SQ SEQUENCE 484 AA; 57205 MW; 304B5B4486AD0A6B CRC64; 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 //