STK24
entrez
8428
canonical
uniprot
Q9Y6E0
canonical
ensembl
ENSG00000102572
resolver
ensp
ENSP00000365730
resolver
ensp
ENSP00000380651
resolver
ensp
ENSP00000442539
resolver
enst
ENST00000397517
resolver
genesymbol
HEL-S-95
resolver
genesymbol
STK24
resolver
genesymbol_syn
MST3
resolver
genesymbol_syn
STK24
resolver
genesymbol_syn
STK3
resolver
hgnc
HGNC:11403
resolver
uniprot
A0A0A0MS81
resolver
uniprot
B4DR80
resolver
uniprot
O14840
resolver
uniprot
Q5JV92
resolver
uniprot
Q5U0E6
resolver
uniprot
Q6P0Y1
resolver
uniprot_entry
A0A0A0MS81_HUMAN
resolver
uniprot_entry
B4DR80_HUMAN
resolver
uniprot_entry
Q5U0E6_HUMAN
resolver
uniprot_entry
Q6P0Y1_HUMAN
resolver
uniprot_entry
STK24_HUMAN
resolver
uniprot_sec
O14840
resolver
uniprot_sec
Q5JV92
resolver
amino_acid_sequence
MDSRAQLWGLALNKRRATLPHPGGSTNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRWKAEQSHDDSSSEDSDAETDGQASGGSDSGDWIFTIREKDPKNLENGALQPSDLDRNKMKDIPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQRYSLSGGGTSSH
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. In association with STK26 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation (PubMed:27807006). Also regulates cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12. May act as a key regulator of axon regeneration in the optic nerve and radial nerve. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:18782753). {ECO:0000269|PubMed:16314523, ECO:0000269|PubMed:17046825, ECO:0000269|PubMed:18782753, ECO:0000269|PubMed:19604147, ECO:0000269|PubMed:19782762, ECO:0000269|PubMed:19855390, ECO:0000269|PubMed:27807006}.
uniprot
proteins
mass_dalton
49308
uniprot
proteins
mutagenesis
MUTAGEN 18; /note="T->A: Loss of phosphorylation by PKA."; /evidence="ECO:0000269|PubMed:10644707"; MUTAGEN 65; /note="K->A: Loss of activity and autophosphorylation."; /evidence="ECO:0000269|PubMed:12107159"; MUTAGEN 190; /note="T->A: Loss of activity and autophosphorylation."; /evidence="ECO:0000269|PubMed:17046825"; MUTAGEN 321; /note="D->N: Loss of proteolytic cleavage by caspases."; /evidence="ECO:0000269|PubMed:12107159
uniprot
proteins
post_translational_modification
PTM: Proteolytically processed by caspases during apoptosis. Proteolytic cleavage results in kinase activation, nuclear translocation of the truncated form (MST3/N) and the induction of apoptosis. {ECO:0000269|PubMed:12107159}.; PTM: Isoform B is activated by phosphorylation by PKA. Oxidative stress induces phosphorylation. Activated by autophosphorylation at Thr-190 and phosphorylation at this site is essential for its function. Manganese, magnesium and cobalt-dependent autophosphorylation is mainly on threonine residues while zinc-dependent autophosphorylation is on both serine and threonine residues. {ECO:0000269|PubMed:10644707, ECO:0000269|PubMed:17046825, ECO:0000269|PubMed:19604147, ECO:0000269|PubMed:20124694}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
STE Ser/Thr protein kinase family
uniprot
proteins
protein_family
STE20 subfamily
uniprot
proteins
pubmed
10644707
uniprot
proteins
pubmed
12107159
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15304321
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15917084
uniprot
proteins
pubmed
16314523
uniprot
proteins
pubmed
17046825
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18782753
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19604147
uniprot
proteins
pubmed
19782762
uniprot
proteins
pubmed
19855390
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20124694
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
27807006
uniprot
proteins
pubmed
9353338
uniprot
proteins
sequence_length
443
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane. Note=The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane.
uniprot
proteins