STK24_MOUSE
ID STK24_MOUSE Reviewed; 431 AA.
AC Q99KH8;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Serine/threonine-protein kinase 24;
DE EC=2.7.11.1;
DE AltName: Full=Mammalian STE20-like protein kinase 3;
DE Short=MST-3;
DE AltName: Full=STE20-like kinase MST3;
DE Contains:
DE RecName: Full=Serine/threonine-protein kinase 24 35 kDa subunit;
DE AltName: Full=Mammalian STE20-like protein kinase 3 N-terminal;
DE Short=MST3/N;
DE Contains:
DE RecName: Full=Serine/threonine-protein kinase 24 12 kDa subunit;
DE AltName: Full=Mammalian STE20-like protein kinase 3 C-terminal;
DE Short=MST3/C;
GN Name=Stk24; Synonyms=Mst3, Stk3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase that acts on both serine and
CC threonine residues and promotes apoptosis in response to stress stimuli
CC and caspase activation. Mediates oxidative-stress-induced cell death by
CC modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11,
CC MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a
CC staurosporine-induced caspase-independent apoptotic pathway by
CC regulating the nuclear translocation of AIFM1 and ENDOG and the DNase
CC activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and
CC stimulates its kinase activity. In association with STK26 negatively
CC regulates Golgi reorientation in polarized cell migration upon RHO
CC activation. Regulates also cellular migration with alteration of PTPN12
CC activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits
CC its activity and may regulate PXN phosphorylation through PTPN12. Acts
CC as a key regulator of axon regeneration in the optic nerve and radial
CC nerve (By similarity). {ECO:0000250|UniProtKB:Q9Y6E0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. Interacts with CTTNBP2NL. Interacts with RIPOR1 (via
CC C-terminus); this interaction occurs in a PDCD10-dependent and Rho-
CC independent manner. Interacts with PDCD10; this interaction is required
CC for the association of STK24 with RIPOR1.
CC {ECO:0000250|UniProtKB:Q9Y6E0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Membrane {ECO:0000250}. Note=The truncated form (MST3/N) translocates
CC to the nucleus. Colocalizes with STK38L in the membrane (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Proteolytically processed by caspases during apoptosis.
CC Proteolytic cleavage results in kinase activation, nuclear
CC translocation of the truncated form (MST3/N) and the induction of
CC apoptosis (By similarity). {ECO:0000250}.
CC -!- PTM: Oxidative stress induces phosphorylation. Activated by
CC autophosphorylation at Thr-178 and phosphorylation at this site is
CC essential for its function. Manganese, magnesium and cobalt-dependent
CC autophosphorylation is mainly on threonine residues while zinc-
CC dependent autophosphorylation is on both serine and threonine residues
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; BC004650; AAH04650.1; -; mRNA.
DR CCDS; CCDS37016.1; -.
DR RefSeq; NP_663440.1; NM_145465.2.
DR AlphaFoldDB; Q99KH8; -.
DR SMR; Q99KH8; -.
DR BioGRID; 230135; 22.
DR IntAct; Q99KH8; 1.
DR MINT; Q99KH8; -.
DR STRING; 10090.ENSMUSP00000078746; -.
DR iPTMnet; Q99KH8; -.
DR PhosphoSitePlus; Q99KH8; -.
DR EPD; Q99KH8; -.
DR jPOST; Q99KH8; -.
DR MaxQB; Q99KH8; -.
DR PaxDb; Q99KH8; -.
DR PRIDE; Q99KH8; -.
DR ProteomicsDB; 257452; -.
DR Antibodypedia; 10785; 355 antibodies from 33 providers.
DR DNASU; 223255; -.
DR Ensembl; ENSMUST00000079817; ENSMUSP00000078746; ENSMUSG00000063410.
DR GeneID; 223255; -.
DR KEGG; mmu:223255; -.
DR UCSC; uc007vac.1; mouse.
DR CTD; 8428; -.
DR MGI; MGI:2385007; Stk24.
DR VEuPathDB; HostDB:ENSMUSG00000063410; -.
DR eggNOG; KOG0201; Eukaryota.
DR GeneTree; ENSGT00940000153476; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q99KH8; -.
DR OMA; YGCFLDG; -.
DR OrthoDB; 967913at2759; -.
DR PhylomeDB; Q99KH8; -.
DR TreeFam; TF354217; -.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-MMU-75153; Apoptotic execution phase.
DR BioGRID-ORCS; 223255; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Stk24; mouse.
DR PRO; PR:Q99KH8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q99KH8; protein.
DR Bgee; ENSMUSG00000063410; Expressed in blood and 246 other tissues.
DR ExpressionAtlas; Q99KH8; baseline and differential.
DR Genevisible; Q99KH8; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0097194; P:execution phase of apoptosis; ISO:MGI.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0048680; P:positive regulation of axon regeneration; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0048679; P:regulation of axon regeneration; ISO:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR Gene3D; 1.10.12.70; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR046409; PDC10_dimerisation_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326"
FT CHAIN 2..431
FT /note="Serine/threonine-protein kinase 24"
FT /id="PRO_0000086712"
FT CHAIN 2..313
FT /note="Serine/threonine-protein kinase 24 35 kDa subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000413620"
FT CHAIN 314..431
FT /note="Serine/threonine-protein kinase 24 12 kDa subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000413621"
FT DOMAIN 24..274
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 297..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 266..280
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 323..374
FT /note="Nuclear export signal (NES)"
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 100..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 313..314
FT /note="Cleavage; by caspase-3, caspase-7 and caspase-8"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 178
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6E0"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6E0"
SQ SEQUENCE 431 AA; 47954 MW; BB0A47D9701AEB00 CRC64;
MAHSPVQSGL PGMQNLKADP EELFTKLEKI GKGSFGEVFK GIDNRTQKVV AIKIIDLEEA
EDEIEDIQQE ITVLSQCDSP YVTKYYGSYL KDTKLWIIME YLGGGSALDL LEPGPLDEIQ
IATILREILK GLDYLHSEKK IHRDIKAANV LLSEHGEVKL ADFGVAGQLT DTQIKRNTFV
GTPFWMAPEV IKQSAYDSKA DIWSLGITAI ELAKGEPPHS ELHPMKVLFL IPKNNPPTLE
GNYSKPLKEF VEACLNKEPS FRPTAKELLK HKFIIRNAKK TSYLTELIDR YKRWKAEQSH
EDSSSEDSDV ETDGQASGGS DSGDWIFTIR EKDPKNLENG TLQLSDLERN KMKDIPKRPF
SQCLSTIISP LFAELKEKSQ ACGGNLGSIE ELRGAIYLAE EACPGISDTM VAQLVQRLQR
YSLSGGGASA H
