Clk2
entrez
12748
canonical
uniprot
O35491
canonical
ensembl
ENSMUSG00000068917
resolver
ensp
ENSMUSP00000088445
resolver
ensp
ENSMUSP00000113390
resolver
enst
ENSMUST00000090927
resolver
enst
ENSMUST00000121212
resolver
genesymbol
Clk2
resolver
uniprot
E9Q721
resolver
uniprot
F8WHX0
resolver
uniprot_entry
CLK2_MOUSE
resolver
uniprot_entry
F8WHX0_MOUSE
resolver
uniprot_sec
E9Q721
resolver
activity_regulation
ACTIVITY REGULATION: 5,6-dichloro-1-b-D-ribofuranosylbenzimidazole (DRB) inhibits autophosphorylation. TG003 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins. {ECO:0000269|PubMed:15010457, ECO:0000269|PubMed:9852100}.
uniprot
proteins
amino_acid_sequence
MPHPRRYHSSERGSRGSYHEHYQSRKHKRRRSRSWSSSSDRTRRRRREDSYHVRSRSSYDDHSSDRRLYDRRYCGSYRRNDYSRDRGEAYYDTDFRQSYEYHRENSSYRSQRSSRRKHRRRRRRSRTFSRSSSHSSRRAKSVEDDAEGHLIYHVGDWLQERYEIVSTLGEGTFGRVVQCVDHRRGGTQVALKIIKNVEKYKEAARLEINVLEKINEKDPDNKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKDNNYLPYPIHQVRHMAFQLCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTAVRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPVPSRMIRKTRKQKYFYRGRLDWDENTSAGRYVRENCKPLRRYLTSEAEDHHQLFDLIENMLEYEPAKRLTLGEALQHPFFACLRTEPPNTKLWDSSRDISR
uniprot
proteins
ec_number
2.7.12.1
uniprot
proteins
function
FUNCTION: 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 (By similarity). {ECO:0000250|UniProtKB:P49760, ECO:0000269|PubMed:20074525, ECO:0000269|PubMed:21329884, ECO:0000269|PubMed:9307018}.
uniprot
proteins
mass_dalton
59987
uniprot
proteins
mutagenesis
MUTAGEN 141; /note="S->A,E: Loss of phosphorylation."; /evidence="ECO:0000269|PubMed:9852100
uniprot
proteins
post_translational_modification
PTM: Autophosphorylates on all three types of residues. Phosphorylation on Ser-34 and Thr-127 by AKT1 is induced by ionizing radiation or insulin. Phosphorylation plays a critical role in cell proliferation following low dose radiation and prevents cell death following high dose radiation. Phosphorylation at Thr-343 by PKB/AKT2 induces its kinase activity which is required for its stability. The phosphorylation status at Ser-141 influences its subnuclear localization; inhibition of phosphorylation at Ser-141 results in accumulation in the nuclear speckle. {ECO:0000269|PubMed:20074525, ECO:0000269|PubMed:9852100}.
uniprot
proteins
protein_family
CMGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
Lammer subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
15010457
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20074525
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21329884
uniprot
proteins
pubmed
9307018
uniprot
proteins
pubmed
9852100
uniprot
proteins
sequence_length
499
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9307018, ECO:0000269|PubMed:9852100}. Nucleus speckle {ECO:0000269|PubMed:9852100}. Note=Inhibition of phosphorylation at Ser-141 results in accumulation in the nuclear speckle. {ECO:0000269|PubMed:9852100}.
uniprot
proteins