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Serine/threonine-protein kinase 24 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 3) (MST-3) (STE20-like kinase MST3) [Cleaved into: Serine/threonine-protein kinase 24 35 kDa subunit (Mammalian STE20-like protein kinase 3 N-terminal) (MST3/N); Serine/threonine-protein kinase 24 12 kDa subunit (Mammalian STE20-like protein kinase 3 C-terminal) (MST3/C)]

 STK24_MOUSE             Reviewed;         431 AA.
Q99KH8;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 138.
RecName: Full=Serine/threonine-protein kinase 24;
EC=2.7.11.1;
AltName: Full=Mammalian STE20-like protein kinase 3;
Short=MST-3;
AltName: Full=STE20-like kinase MST3;
Contains:
RecName: Full=Serine/threonine-protein kinase 24 35 kDa subunit;
AltName: Full=Mammalian STE20-like protein kinase 3 N-terminal;
Short=MST3/N;
Contains:
RecName: Full=Serine/threonine-protein kinase 24 12 kDa subunit;
AltName: Full=Mammalian STE20-like protein kinase 3 C-terminal;
Short=MST3/C;
Name=Stk24; Synonyms=Mst3, Stk3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[3]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. Regulates also cellular migration with alteration of
PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and
inhibits its activity and may regulate PXN phosphorylation through
PTPN12. Acts as a key regulator of axon regeneration in the optic
nerve and radial nerve (By similarity).
{ECO:0000250|UniProtKB:Q9Y6E0}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
-!- SUBUNIT: Monomer. Interacts with CTTNBP2NL. Interacts with RIPOR1
(via C-terminus); this interaction occurs in a PDCD10-dependent
and Rho-independent manner. Interacts with PDCD10; this
interaction is required for the association of STK24 with RIPOR1.
{ECO:0000250|UniProtKB:Q9Y6E0}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Membrane {ECO:0000250}. Note=The truncated form
(MST3/N) translocates to the nucleus. Colocalizes with STK38L in
the membrane (By similarity). {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Oxidative stress induces phosphorylation. Activated by
autophosphorylation at Thr-178 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC004650; AAH04650.1; -; mRNA.
CCDS; CCDS37016.1; -.
RefSeq; NP_663440.1; NM_145465.2.
UniGene; Mm.390756; -.
UniGene; Mm.442081; -.
UniGene; Mm.472866; -.
ProteinModelPortal; Q99KH8; -.
SMR; Q99KH8; -.
BioGrid; 230135; 1.
IntAct; Q99KH8; 1.
MINT; MINT-4135908; -.
STRING; 10090.ENSMUSP00000078746; -.
iPTMnet; Q99KH8; -.
PhosphoSitePlus; Q99KH8; -.
EPD; Q99KH8; -.
MaxQB; Q99KH8; -.
PaxDb; Q99KH8; -.
PRIDE; Q99KH8; -.
Ensembl; ENSMUST00000079817; ENSMUSP00000078746; ENSMUSG00000063410.
GeneID; 223255; -.
KEGG; mmu:223255; -.
UCSC; uc007vac.1; mouse.
CTD; 8428; -.
MGI; MGI:2385007; Stk24.
eggNOG; KOG0201; Eukaryota.
eggNOG; ENOG410XP9G; LUCA.
GeneTree; ENSGT00900000140794; -.
HOGENOM; HOG000234203; -.
HOVERGEN; HBG108518; -.
InParanoid; Q99KH8; -.
KO; K08838; -.
OMA; DTDGQAS; -.
OrthoDB; EOG091G0F24; -.
PhylomeDB; Q99KH8; -.
TreeFam; TF354217; -.
Reactome; R-MMU-75153; Apoptotic execution phase.
ChiTaRS; Stk24; mouse.
PRO; PR:Q99KH8; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000063410; -.
CleanEx; MM_STK24; -.
ExpressionAtlas; Q99KH8; baseline and differential.
Genevisible; Q99KH8; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; ISO:MGI.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0048679; P:regulation of axon regeneration; ISO:MGI.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326}.
CHAIN 2 431 Serine/threonine-protein kinase 24.
/FTId=PRO_0000086712.
CHAIN 2 313 Serine/threonine-protein kinase 24 35 kDa
subunit. {ECO:0000250}.
/FTId=PRO_0000413620.
CHAIN 314 431 Serine/threonine-protein kinase 24 12 kDa
subunit. {ECO:0000250}.
/FTId=PRO_0000413621.
DOMAIN 24 274 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 30 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 100 102 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 266 280 Bipartite nuclear localization signal.
{ECO:0000250}.
MOTIF 323 374 Nuclear export signal (NES).
{ECO:0000250}.
ACT_SITE 144 144 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
METAL 149 149 Magnesium. {ECO:0000250}.
METAL 162 162 Magnesium. {ECO:0000250}.
BINDING 53 53 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 313 314 Cleavage; by caspase-3, caspase-7 and
caspase-8. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 178 178 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q9Y6E0}.
MOD_RES 308 308 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6E0}.
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


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