ID STK24_HUMAN Reviewed; 443 AA. AC Q9Y6E0; O14840; Q5JV92; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 212. 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 36 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RX PubMed=9353338; DOI=10.1074/jbc.272.45.28695; RA Schinkmann K., Blenis J.; RT "Cloning and characterization of a human STE20-like protein kinase with RT unusual cofactor requirements."; RL J. Biol. Chem. 272:28695-28703(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), PHOSPHORYLATION AT THR-18, RP MUTAGENESIS OF THR-18, AND VARIANT VAL-414. RC TISSUE=Brain; RX PubMed=10644707; DOI=10.1074/jbc.275.4.2513; RA Zhou T.-H., Ling K., Guo J., Zhou H., Wu Y.-L., Jing Q., Ma L., Pei G.; RT "Identification of a human brain-specific isoform of mammalian STE20-like RT kinase 3 that is regulated by cAMP-dependent protein kinase."; RL J. Biol. Chem. 275:2513-2519(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Skin; 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 [6] RP PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-65 AND RP ASP-321. RX PubMed=12107159; DOI=10.1074/jbc.m202468200; RA Huang C.Y., Wu Y.M., Hsu C.Y., Lee W.S., Lai M.D., Lu T.J., Huang C.L., RA Leu T.H., Shih H.M., Fang H.I., Robinson D.R., Kung H.J., Yuan C.J.; RT "Caspase activation of mammalian sterile 20-like kinase 3 (Mst3)."; RL J. Biol. Chem. 277:34367-34374(2002). RN [7] RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND NUCLEAR EXPORT RP SIGNAL. RX PubMed=15304321; DOI=10.1016/j.febslet.2004.07.007; RA Lee W.S., Hsu C.Y., Wang P.L., Huang C.Y., Chang C.H., Yuan C.J.; RT "Identification and characterization of the nuclear import and export RT signals of the mammalian Ste20-like protein kinase 3."; RL FEBS Lett. 572:41-45(2004). RN [8] RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15917084; DOI=10.1016/j.jinorgbio.2005.03.003; RA Lu T.J., Huang C.Y., Yuan C.J., Lee Y.C., Leu T.H., Chang W.C., Lu T.L., RA Jeng W.Y., Lai M.D.; RT "Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has a RT distinct role in autophosphorylation of MST3."; RL J. Inorg. Biochem. 99:1306-1313(2005). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16314523; DOI=10.1128/mcb.25.24.11019-11029.2005; RA Stegert M.R., Hergovich A., Tamaskovic R., Bichsel S.J., Hemmings B.A.; RT "Regulation of NDR protein kinase by hydrophobic motif phosphorylation RT mediated by the mammalian Ste20-like kinase MST3."; RL Mol. Cell. Biol. 25:11019-11029(2005). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP FUNCTION, PHOSPHORYLATION AT THR-190, AND MUTAGENESIS OF THR-190. RX PubMed=17046825; DOI=10.1074/jbc.m605035200; RA Lu T.J., Lai W.Y., Huang C.Y., Hsieh W.J., Yu J.S., Hsieh Y.J., Chang W.T., RA Leu T.H., Chang W.C., Chuang W.J., Tang M.J., Chen T.Y., Lu T.L., Lai M.D.; RT "Inhibition of cell migration by autophosphorylated mammalian sterile 20- RT like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase- RT PEST."; RL J. Biol. Chem. 281:38405-38417(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] RP FUNCTION, AND PHOSPHORYLATION AT THR-190. RX PubMed=19604147; DOI=10.1042/bsr20090096; RA Chen C.B., Ng J.K., Choo P.H., Wu W., Porter A.G.; RT "Mammalian sterile 20-like kinase 3 (MST3) mediates oxidative-stress- RT induced cell death by modulating JNK activation."; RL Biosci. Rep. 29:405-415(2009). RN [14] RP INTERACTION WITH CTTNBP2NL. RX PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200; RA Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., RA Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., RA Aebersold R., Raught B., Gingras A.C.; RT "A PP2A phosphatase high density interaction network identifies a novel RT striatin-interacting phosphatase and kinase complex linked to the cerebral RT cavernous malformation 3 (CCM3) protein."; RL Mol. Cell. Proteomics 8:157-171(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM A), PHOSPHORYLATION RP [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM A), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [16] RP FUNCTION. RX PubMed=19855390; DOI=10.1038/nn.2414; RA Lorber B., Howe M.L., Benowitz L.I., Irwin N.; RT "Mst3b, an Ste20-like kinase, regulates axon regeneration in mature CNS and RT PNS pathways."; RL Nat. Neurosci. 12:1407-1414(2009). RN [17] RP FUNCTION. RX PubMed=19782762; DOI=10.1016/j.biocel.2009.09.012; RA Lin C.Y., Wu H.Y., Wang P.L., Yuan C.J.; RT "Mammalian Ste20-like protein kinase 3 induces a caspase-independent RT apoptotic pathway."; RL Int. J. Biochem. Cell Biol. 42:98-105(2010). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM A), PHOSPHORYLATION RP [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM A), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM A), PHOSPHORYLATION RP [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM A), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-190, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP FUNCTION, AND INTERACTION WITH PDCD10 AND RIPOR1. RX PubMed=27807006; DOI=10.1242/jcs.198614; RA Mardakheh F.K., Self A., Marshall C.J.; RT "RHO binding to FAM65A regulates Golgi reorientation during cell RT migration."; RL J. Cell Sci. 129:4466-4479(2016). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 27-315 IN COMPLEX WITH ADENINE; RP ADP AND MANGANESE IONS, SUBUNIT, AND PHOSPHORYLATION AT THR-190. RX PubMed=20124694; DOI=10.1107/s0907444909047507; RA Ko T.P., Jeng W.Y., Liu C.I., Lai M.D., Wu C.L., Chang W.J., Shr H.L., RA Lu T.J., Wang A.H.; RT "Structures of human MST3 kinase in complex with adenine, ADP and Mn2+."; RL Acta Crystallogr. D 66:145-154(2010). RN [24] RP VARIANTS [LARGE SCALE ANALYSIS] VAL-414 AND ILE-426. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). 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 (PubMed:27807006). Regulates also cellular migration with CC alteration of PTPN12 activity and PXN phosphorylation: phosphorylates CC PTPN12 and inhibits its activity and may regulate PXN phosphorylation CC through PTPN12. May act as a key regulator of axon regeneration in the CC optic nerve and radial nerve. {ECO:0000269|PubMed:16314523, CC ECO:0000269|PubMed:17046825, ECO:0000269|PubMed:19604147, CC ECO:0000269|PubMed:19782762, ECO:0000269|PubMed:19855390, CC ECO:0000269|PubMed:27807006}. 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; CC Evidence={ECO:0000269|PubMed:15917084}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:15917084}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:15917084}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:15917084}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=12.8 uM for manganese ions {ECO:0000269|PubMed:15917084}; CC KM=34.9 uM for cobalt ions {ECO:0000269|PubMed:15917084}; CC KM=22.7 uM for magnesium ions {ECO:0000269|PubMed:15917084}; CC KM=4.1 uM for zinc ions {ECO:0000269|PubMed:15917084}; CC Vmax=2623.1 pmol/min/mg enzyme for manganese ions CC {ECO:0000269|PubMed:15917084}; CC Vmax=1746.1 pmol/min/mg enzyme for cobalt ions CC {ECO:0000269|PubMed:15917084}; CC Vmax=129.1 pmol/min/mg enzyme for magnesium ions CC {ECO:0000269|PubMed:15917084}; CC Vmax=22.3 pmol/min/mg enzyme for zinc ions CC {ECO:0000269|PubMed:15917084}; CC -!- SUBUNIT: Monomer (PubMed:20124694). Interacts with CTTNBP2NL CC (PubMed:18782753). Interacts with RIPOR1 (via C-terminus); this CC interaction occurs in a PDCD10-dependent and Rho-independent manner CC (PubMed:27807006). Interacts with PDCD10; this interaction is required CC for the association of STK24 with RIPOR1 (PubMed:27807006). CC {ECO:0000269|PubMed:18782753, ECO:0000269|PubMed:20124694, CC ECO:0000269|PubMed:27807006}. CC -!- INTERACTION: CC Q9Y6E0; Q9P2B4: CTTNBP2NL; NbExp=5; IntAct=EBI-740175, EBI-1774273; CC Q9Y6E0; Q9BUL8: PDCD10; NbExp=11; IntAct=EBI-740175, EBI-740195; CC Q9Y6E0; Q5VSL9: STRIP1; NbExp=4; IntAct=EBI-740175, EBI-1773588; CC Q9Y6E0; O43815: STRN; NbExp=4; IntAct=EBI-740175, EBI-1046642; CC Q9Y6E0; Q9Y228: TRAF3IP3; NbExp=2; IntAct=EBI-740175, EBI-765817; CC Q9Y6E0-2; Q9Y376: CAB39; NbExp=3; IntAct=EBI-10299018, EBI-306905; CC Q9Y6E0-2; Q9BUL8: PDCD10; NbExp=9; IntAct=EBI-10299018, EBI-740195; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane. Note=The truncated CC form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in CC the membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=B; CC IsoId=Q9Y6E0-1; Sequence=Displayed; CC Name=A; CC IsoId=Q9Y6E0-2; Sequence=VSP_004874; CC -!- TISSUE SPECIFICITY: Isoform A is ubiquitous. Isoform B is expressed in CC brain with high expression in hippocampus and cerebral cortex. 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. {ECO:0000269|PubMed:12107159}. CC -!- PTM: Isoform B is activated by phosphorylation by PKA. Oxidative stress CC induces phosphorylation. Activated by autophosphorylation at Thr-190 CC and phosphorylation at this site is essential for its function. CC Manganese, magnesium and cobalt-dependent autophosphorylation is mainly CC on threonine residues while zinc-dependent autophosphorylation is on CC both serine and threonine residues. {ECO:0000269|PubMed:10644707, CC ECO:0000269|PubMed:17046825, ECO:0000269|PubMed:19604147, CC ECO:0000269|PubMed:20124694}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. STE20 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF024636; AAB82560.1; -; mRNA. DR EMBL; AF083420; AAD42039.1; -; mRNA. DR EMBL; AL356423; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137249; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471085; EAX08986.1; -; Genomic_DNA. DR EMBL; BC035578; AAH35578.1; -; mRNA. DR CCDS; CCDS32001.1; -. [Q9Y6E0-2] DR CCDS; CCDS9488.1; -. [Q9Y6E0-1] DR RefSeq; NP_001027467.2; NM_001032296.3. [Q9Y6E0-2] DR RefSeq; NP_003567.2; NM_003576.4. [Q9Y6E0-1] DR PDB; 3A7F; X-ray; 1.55 A; A=27-315. DR PDB; 3A7G; X-ray; 2.00 A; A/B=27-315. DR PDB; 3A7H; X-ray; 1.96 A; A/B=27-315. DR PDB; 3A7I; X-ray; 1.45 A; A=27-315. DR PDB; 3A7J; X-ray; 1.50 A; A=27-315. DR PDB; 3CKW; X-ray; 1.96 A; A=31-323. DR PDB; 3CKX; X-ray; 2.70 A; A=31-323. DR PDB; 3ZHP; X-ray; 2.90 A; C/D=31-301. DR PDB; 4O27; X-ray; 3.19 A; B=30-309. DR PDB; 4QML; X-ray; 1.88 A; A=24-315. DR PDB; 4QMM; X-ray; 1.85 A; A=24-315. DR PDB; 4QMN; X-ray; 2.09 A; A=27-315. DR PDB; 4QMO; X-ray; 1.90 A; A=24-315. DR PDB; 4QMP; X-ray; 2.00 A; A=24-315. DR PDB; 4QMQ; X-ray; 1.77 A; A=24-315. DR PDB; 4QMS; X-ray; 1.88 A; A=24-315. DR PDB; 4QMT; X-ray; 1.50 A; A=24-315. DR PDB; 4QMU; X-ray; 1.55 A; A=24-315. DR PDB; 4QMV; X-ray; 2.40 A; A=24-315. DR PDB; 4QMW; X-ray; 1.60 A; A=24-315. DR PDB; 4QMX; X-ray; 1.88 A; A=24-315. DR PDB; 4QMY; X-ray; 1.88 A; A=24-315. DR PDB; 4QMZ; X-ray; 1.88 A; A=24-315. DR PDB; 4QNA; X-ray; 1.85 A; A=27-315. DR PDB; 4QO9; X-ray; 2.20 A; A/B=24-315. DR PDB; 4U8Z; X-ray; 1.63 A; A=24-310. DR PDB; 4W8D; X-ray; 1.77 A; A=24-310. DR PDB; 4W8E; X-ray; 1.79 A; A=24-311. DR PDB; 7B30; X-ray; 2.10 A; A=4-301. DR PDB; 7B31; X-ray; 1.80 A; A=4-301. DR PDB; 7B32; X-ray; 1.75 A; A=4-301. DR PDB; 7B33; X-ray; 1.90 A; A=4-301. DR PDB; 7B34; X-ray; 2.10 A; A=4-301. DR PDB; 7B35; X-ray; 2.40 A; A/B=4-301. DR PDB; 8BZI; X-ray; 1.72 A; A=4-301. DR PDB; 8BZJ; X-ray; 2.52 A; A/B=4-301. DR PDB; 8QLQ; X-ray; 1.64 A; A=4-301. DR PDB; 8QLR; X-ray; 1.85 A; A/B=4-301. DR PDB; 8QLS; X-ray; 1.61 A; A=4-301. DR PDB; 8QLT; X-ray; 1.47 A; A=4-301. DR PDBsum; 3A7F; -. DR PDBsum; 3A7G; -. DR PDBsum; 3A7H; -. DR PDBsum; 3A7I; -. DR PDBsum; 3A7J; -. DR PDBsum; 3CKW; -. DR PDBsum; 3CKX; -. DR PDBsum; 3ZHP; -. DR PDBsum; 4O27; -. DR PDBsum; 4QML; -. DR PDBsum; 4QMM; -. DR PDBsum; 4QMN; -. DR PDBsum; 4QMO; -. DR PDBsum; 4QMP; -. DR PDBsum; 4QMQ; -. DR PDBsum; 4QMS; -. DR PDBsum; 4QMT; -. DR PDBsum; 4QMU; -. DR PDBsum; 4QMV; -. DR PDBsum; 4QMW; -. DR PDBsum; 4QMX; -. DR PDBsum; 4QMY; -. DR PDBsum; 4QMZ; -. DR PDBsum; 4QNA; -. DR PDBsum; 4QO9; -. DR PDBsum; 4U8Z; -. DR PDBsum; 4W8D; -. DR PDBsum; 4W8E; -. DR PDBsum; 7B30; -. DR PDBsum; 7B31; -. DR PDBsum; 7B32; -. DR PDBsum; 7B33; -. DR PDBsum; 7B34; -. DR PDBsum; 7B35; -. DR PDBsum; 8BZI; -. DR PDBsum; 8BZJ; -. DR PDBsum; 8QLQ; -. DR PDBsum; 8QLR; -. DR PDBsum; 8QLS; -. DR PDBsum; 8QLT; -. DR AlphaFoldDB; Q9Y6E0; -. DR SMR; Q9Y6E0; -. DR BioGRID; 114011; 184. DR DIP; DIP-40608N; -. DR IntAct; Q9Y6E0; 62. DR MINT; Q9Y6E0; -. DR STRING; 9606.ENSP00000365730; -. DR BindingDB; Q9Y6E0; -. DR ChEMBL; CHEMBL5082; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q9Y6E0; -. DR GuidetoPHARMACOLOGY; 2217; -. DR GlyGen; Q9Y6E0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y6E0; -. DR MetOSite; Q9Y6E0; -. DR PhosphoSitePlus; Q9Y6E0; -. DR SwissPalm; Q9Y6E0; -. DR BioMuta; STK24; -. DR DMDM; 13626607; -. DR CPTAC; CPTAC-3208; -. DR CPTAC; CPTAC-3209; -. DR EPD; Q9Y6E0; -. DR jPOST; Q9Y6E0; -. DR MassIVE; Q9Y6E0; -. DR MaxQB; Q9Y6E0; -. DR PaxDb; 9606-ENSP00000365730; -. DR PeptideAtlas; Q9Y6E0; -. DR PRIDE; Q9Y6E0; -. DR ProteomicsDB; 86657; -. [Q9Y6E0-1] DR ProteomicsDB; 86658; -. [Q9Y6E0-2] DR Pumba; Q9Y6E0; -. DR Antibodypedia; 10785; 427 antibodies from 33 providers. DR DNASU; 8428; -. DR Ensembl; ENST00000376547.7; ENSP00000365730.3; ENSG00000102572.15. [Q9Y6E0-1] DR Ensembl; ENST00000539966.6; ENSP00000442539.2; ENSG00000102572.15. [Q9Y6E0-2] DR GeneID; 8428; -. DR KEGG; hsa:8428; -. DR MANE-Select; ENST00000539966.6; ENSP00000442539.2; NM_001032296.4; NP_001027467.2. [Q9Y6E0-2] DR UCSC; uc001vnm.3; human. [Q9Y6E0-1] DR AGR; HGNC:11403; -. DR CTD; 8428; -. DR DisGeNET; 8428; -. DR GeneCards; STK24; -. DR HGNC; HGNC:11403; STK24. DR HPA; ENSG00000102572; Low tissue specificity. DR MIM; 604984; gene. DR neXtProt; NX_Q9Y6E0; -. DR OpenTargets; ENSG00000102572; -. DR PharmGKB; PA36210; -. DR VEuPathDB; HostDB:ENSG00000102572; -. DR eggNOG; KOG0201; Eukaryota. DR GeneTree; ENSGT00940000153476; -. DR InParanoid; Q9Y6E0; -. DR OMA; ERSQACG; -. DR OrthoDB; 152877at2759; -. DR PhylomeDB; Q9Y6E0; -. DR TreeFam; TF354217; -. DR PathwayCommons; Q9Y6E0; -. DR Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins. DR Reactome; R-HSA-75153; Apoptotic execution phase. DR SABIO-RK; Q9Y6E0; -. DR SignaLink; Q9Y6E0; -. DR SIGNOR; Q9Y6E0; -. DR BioGRID-ORCS; 8428; 18 hits in 1189 CRISPR screens. DR ChiTaRS; STK24; human. DR EvolutionaryTrace; Q9Y6E0; -. DR GeneWiki; STK24; -. DR GenomeRNAi; 8428; -. DR Pharos; Q9Y6E0; Tchem. DR PRO; PR:Q9Y6E0; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q9Y6E0; Protein. DR Bgee; ENSG00000102572; Expressed in secondary oocyte and 210 other cell types or tissues. DR ExpressionAtlas; Q9Y6E0; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB. DR GO; GO:0097194; P:execution phase of apoptosis; IMP:UniProtKB. DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB. DR GO; GO:0048680; P:positive regulation of axon regeneration; IEA:Ensembl. DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0048679; P:regulation of axon regeneration; IMP:UniProtKB. DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd06609; STKc_MST3_like; 1. DR Gene3D; 1.10.12.70; -; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR046409; PDC10_dimerisation_sf. DR InterPro; IPR048288; PDCD10_N. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR PANTHER; PTHR48012:SF22; SERINE_THREONINE-PROTEIN KINASE 24; 1. DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1. DR Pfam; PF20929; PDCD10_N; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR Genevisible; Q9Y6E0; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; ATP-binding; KW Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..443 FT /note="Serine/threonine-protein kinase 24" FT /id="PRO_0000086711" FT CHAIN 1..325 FT /note="Serine/threonine-protein kinase 24 36 kDa subunit" FT /id="PRO_0000413618" FT CHAIN 326..443 FT /note="Serine/threonine-protein kinase 24 12 kDa subunit" FT /id="PRO_0000413619" FT DOMAIN 36..286 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 309..337 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 278..292 FT /note="Bipartite nuclear localization signal" FT MOTIF 335..386 FT /note="Nuclear export signal (NES)" FT ACT_SITE 156 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 42..50 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 65 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 112..114 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 161 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 174 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT SITE 325..326 FT /note="Cleavage; by caspase-3, caspase-7 and caspase-8" FT MOD_RES 18 FT /note="Phosphothreonine; by PKA" FT /evidence="ECO:0000269|PubMed:10644707" FT MOD_RES 190 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:17046825, FT ECO:0000269|PubMed:19604147, ECO:0000269|PubMed:20124694, FT ECO:0007744|PubMed:23186163" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT VAR_SEQ 1..26 FT /note="MDSRAQLWGLALNKRRATLPHPGGST -> MAHSPVQSGLPGMQ (in FT isoform A)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9353338" FT /id="VSP_004874" FT VARIANT 414 FT /note="A -> V (in dbSNP:rs55953606)" FT /evidence="ECO:0000269|PubMed:10644707, FT ECO:0000269|PubMed:17344846" FT /id="VAR_041148" FT VARIANT 426 FT /note="L -> I (in dbSNP:rs55897869)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041149" FT MUTAGEN 18 FT /note="T->A: Loss of phosphorylation by PKA." FT /evidence="ECO:0000269|PubMed:10644707" FT MUTAGEN 65 FT /note="K->A: Loss of activity and autophosphorylation." FT /evidence="ECO:0000269|PubMed:12107159" FT MUTAGEN 190 FT /note="T->A: Loss of activity and autophosphorylation." FT /evidence="ECO:0000269|PubMed:17046825" FT MUTAGEN 321 FT /note="D->N: Loss of proteolytic cleavage by caspases." FT /evidence="ECO:0000269|PubMed:12107159" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:8BZI" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 36..44 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 46..55 FT /evidence="ECO:0007829|PDB:3A7I" FT TURN 56..58 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 61..68 FT /evidence="ECO:0007829|PDB:3A7I" FT TURN 69..71 FT /evidence="ECO:0007829|PDB:3A7I" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:4QMT" FT HELIX 76..88 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 106..112 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:3A7J" FT HELIX 119..123 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:3A7H" FT HELIX 130..149 FT /evidence="ECO:0007829|PDB:3A7I" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:3ZHP" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:4QO9" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:4QMQ" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:3A7I" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:3A7I" FT HELIX 211..226 FT /evidence="ECO:0007829|PDB:3A7I" FT TURN 230..233 FT /evidence="ECO:0007829|PDB:3A7I" FT HELIX 236..245 FT /evidence="ECO:0007829|PDB:3A7I" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:4QML" FT HELIX 257..266 FT /evidence="ECO:0007829|PDB:3A7I" FT HELIX 271..273 FT /evidence="ECO:0007829|PDB:3A7I" FT HELIX 277..280 FT /evidence="ECO:0007829|PDB:3A7I" FT HELIX 284..289 FT /evidence="ECO:0007829|PDB:3A7I" FT HELIX 293..296 FT /evidence="ECO:0007829|PDB:3A7I" FT HELIX 297..309 FT /evidence="ECO:0007829|PDB:3A7I" FT INIT_MET Q9Y6E0-2:1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES Q9Y6E0-2:2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES Q9Y6E0-2:4 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" SQ SEQUENCE 443 AA; 49308 MW; 4A9FF1F6B6A88A97 CRC64; MDSRAQLWGL ALNKRRATLP HPGGSTNLKA DPEELFTKLE KIGKGSFGEV FKGIDNRTQK VVAIKIIDLE EAEDEIEDIQ QEITVLSQCD SPYVTKYYGS YLKDTKLWII MEYLGGGSAL DLLEPGPLDE TQIATILREI LKGLDYLHSE KKIHRDIKAA NVLLSEHGEV KLADFGVAGQ LTDTQIKRNT FVGTPFWMAP EVIKQSAYDS KADIWSLGIT AIELARGEPP HSELHPMKVL FLIPKNNPPT LEGNYSKPLK EFVEACLNKE PSFRPTAKEL LKHKFILRNA KKTSYLTELI DRYKRWKAEQ SHDDSSSEDS DAETDGQASG GSDSGDWIFT IREKDPKNLE NGALQPSDLD RNKMKDIPKR PFSQCLSTII SPLFAELKEK SQACGGNLGS IEELRGAIYL AEEACPGISD TMVAQLVQRL QRYSLSGGGT SSH //