Gene name: CLK2

Uniprot entry:

P49760

Protein names:

Dual specificity protein kinase CLK2 (EC 2.7.12.1) (CDC-like kinase 2)

Protein sequence:

1_MPHPR 6_ RYHSS 11_ ERGSR 16_ GSYRE 21_ HYRSR 26_ KHKRR 31_ RSRSW 36_ SSSSD 41_ RTRRR 46_ RREDS 51_ YHVRS 56_ RSSYD 61_ DRSSD 66_ RRVYD 71_ RRYCG 76_ SYRRN 81_ DYSRD 86_ RGDAY 91_ YDTDY 96_ RHSYE 101_ YQREN 106_ SSYRS 111_ QRSSR 116_ RKHRR 121_ RRRRS 126_ RTFSR 131_ SSSQH 136_ SSRRA 141_ KSVED 146_ DAEGH 151_ LIYHV 156_ GDWLQ 161_ ERYEI 166_ VSTLG 171_ EGTFG 176_ RVVQC 181_ VDHRR 186_ GGARV 191_ ALKII 196_ KNVEK 201_ YKEAA 206_ RLEIN 211_ VLEKI 216_ NEKDP 221_ DNKNL 226_ CVQMF 231_ DWFDY 236_ HGHMC 241_ ISFEL 246_ LGLST 251_ FDFLK 256_ DNNYL 261_ PYPIH 266_ QVRHM 271_ AFQLC 276_ QAVKF 281_ LHDNK 286_ LTHTD 291_ LKPEN 296_ ILFVN 301_ SDYEL 306_ TYNLE 311_ KKRDE 316_ RSVKS 321_ TAVRV 326_ VDFGS 331_ ATFDH 336_ EHHST 341_ IVSTR 346_ HYRAP 351_ EVILE 356_ LGWSQ 361_ PCDVW 366_ SIGCI 371_ IFEYY 376_ VGFTL 381_ FQTHD 386_ NREHL 391_ AMMER 396_ ILGPI 401_ PSRMI 406_ RKTRK 411_ QKYFY 416_ RGRLD 421_ WDENT 426_ SAGRY 431_ VRENC 436_ KPLRR 441_ YLTSE 446_ AEEHH 451_ QLFDL 456_ IESML 461_ EYEPA 466_ KRLTL 471_ GEALQ 476_ HPFFA 481_ RLRAE 486_ PPNKL 491_WDSSR

Protein annotations

Protein functions:

1: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Phosphorylates PAGE4 at several serine and threonine residues and this phosphorylation attenuates the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (PubMed:28289210)