Full text data of STK24
STK24
(MST3, STK3)
[Confidence: low (only semi-automatic identification from reviews)]
Serine/threonine-protein kinase 24; 2.7.11.1 (Mammalian STE20-like protein kinase 3; MST-3; STE20-like kinase MST3; Serine/threonine-protein kinase 24 36 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)
Serine/threonine-protein kinase 24; 2.7.11.1 (Mammalian STE20-like protein kinase 3; MST-3; STE20-like kinase MST3; Serine/threonine-protein kinase 24 36 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)
UniProt
Q9Y6E0
ID STK24_HUMAN Reviewed; 443 AA.
AC Q9Y6E0; O14840; Q5JV92;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 136.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT with 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.,
RA Pei G.;
RT "Identification of a human brain-specific isoform of mammalian STE20-
RT like 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.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA 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.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA 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.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-65 AND 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.,
RA Huang C.L., Leu T.H., Shih H.M., Fang H.I., Robinson D.R., Kung H.J.,
RA 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.,
RA Lu T.L., Jeng W.Y., Lai M.D.;
RT "Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has
RT a 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.,
RA 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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.,
RA Chang W.T., Leu T.H., Chang W.C., Chuang W.J., Tang M.J., Chen T.Y.,
RA Lu T.L., Lai M.D.;
RT "Inhibition of cell migration by autophosphorylated mammalian sterile
RT 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine
RT phosphatase-PEST.";
RL J. Biol. Chem. 281:38405-38417(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), AND MASS
RP SPECTROMETRY.
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
RT the 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
RT novel striatin-interacting phosphatase and kinase complex linked to
RT the cerebral 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),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), MASS
RP SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
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
RT CNS and 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),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 27-315 IN COMPLEX WITH
RP ADENINE; ADP AND MANGANESE IONS, SUBUNIT, AND PHOSPHORYLATION AT
RP 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
RT Mn2+.";
RL Acta Crystallogr. D 66:145-154(2010).
RN [22]
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.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., 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
CC and threonine residues and promotes apoptosis in response to
CC stress stimuli and caspase activation. Mediates oxidative-stress-
CC induced cell death by modulating phosphorylation of JNK1-JNK2
CC (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during
CC oxidative stress. Plays a role in a staurosporine-induced caspase-
CC independent apoptotic pathway by regulating the nuclear
CC translocation of AIFM1 and ENDOG and the DNase activity associated
CC with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its
CC kinase activity. Regulates cellular migration with alteration of
CC PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and
CC inhibits its activity and may regulate PXN phosphorylation through
CC PTPN12. May act as a key regulator of axon regeneration in the
CC optic nerve and radial nerve.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Mg(2+) or Mn(2+) or Co(2+) or Zn(2+).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.8 uM for manganese ions;
CC KM=34.9 uM for cobalt ions;
CC KM=22.7 uM for magnesium ions;
CC KM=4.1 uM for zinc ions;
CC Vmax=2623.1 pmol/min/mg enzyme for manganese ions;
CC Vmax=1746.1 pmol/min/mg enzyme for cobalt ions;
CC Vmax=129.1 pmol/min/mg enzyme for magnesium ions;
CC Vmax=22.3 pmol/min/mg enzyme for zinc ions;
CC -!- SUBUNIT: Monomer. Interacts with CTTNBP2NL.
CC -!- INTERACTION:
CC Q9P2B4:CTTNBP2NL; NbExp=4; IntAct=EBI-740175, EBI-1774273;
CC Q9BUL8:PDCD10; NbExp=7; IntAct=EBI-740175, EBI-740195;
CC O43815:STRN; NbExp=3; IntAct=EBI-740175, EBI-1046642;
CC Q9Y228:TRAF3IP3; NbExp=2; IntAct=EBI-740175, EBI-765817;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane. Note=The
CC truncated form (MST3/N) translocates to the nucleus. Colocalizes
CC with STK38L in 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 Note=Initiator Met-1 is removed. Contains a phosphoserine at
CC position 4. Contains a N-acetylalanine at position 2;
CC -!- TISSUE SPECIFICITY: Isoform A is ubiquitous. Isoform B is
CC expressed in brain with high expression in hippocampus and
CC 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.
CC -!- PTM: Isoform B is activated by phosphorylation by PKA. Oxidative
CC stress induces phosphorylation. Activated by autophosphorylation
CC at Thr-190 and phosphorylation at this site is essential for its
CC function. Manganese, magnesium and cobalt-dependent
CC autophosphorylation is mainly on threonine residues while zinc-
CC dependent autophosphorylation is on both serine and threonine
CC residues.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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DR EMBL; AF024636; AAB82560.1; -; mRNA.
DR EMBL; AF083420; AAD42039.1; -; mRNA.
DR EMBL; AL356423; CAI13114.1; -; Genomic_DNA.
DR EMBL; AL137249; CAI13114.1; JOINED; Genomic_DNA.
DR EMBL; AL137249; CAI39453.1; -; Genomic_DNA.
DR EMBL; AL356423; CAI39453.1; JOINED; Genomic_DNA.
DR EMBL; CH471085; EAX08986.1; -; Genomic_DNA.
DR EMBL; BC035578; AAH35578.1; -; mRNA.
DR RefSeq; NP_001027467.2; NM_001032296.3.
DR RefSeq; NP_003567.2; NM_003576.4.
DR UniGene; Hs.508514; -.
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 PDBsum; 3A7F; -.
DR PDBsum; 3A7G; -.
DR PDBsum; 3A7H; -.
DR PDBsum; 3A7I; -.
DR PDBsum; 3A7J; -.
DR PDBsum; 3CKW; -.
DR PDBsum; 3CKX; -.
DR PDBsum; 3ZHP; -.
DR ProteinModelPortal; Q9Y6E0; -.
DR SMR; Q9Y6E0; 27-350, 375-434.
DR DIP; DIP-40608N; -.
DR IntAct; Q9Y6E0; 33.
DR MINT; MINT-3088034; -.
DR STRING; 9606.ENSP00000365730; -.
DR BindingDB; Q9Y6E0; -.
DR ChEMBL; CHEMBL5082; -.
DR GuidetoPHARMACOLOGY; 2217; -.
DR PhosphoSite; Q9Y6E0; -.
DR DMDM; 13626607; -.
DR PaxDb; Q9Y6E0; -.
DR PRIDE; Q9Y6E0; -.
DR DNASU; 8428; -.
DR Ensembl; ENST00000376547; ENSP00000365730; ENSG00000102572.
DR Ensembl; ENST00000397517; ENSP00000380651; ENSG00000102572.
DR GeneID; 8428; -.
DR KEGG; hsa:8428; -.
DR UCSC; uc001vnm.1; human.
DR CTD; 8428; -.
DR GeneCards; GC13M099103; -.
DR HGNC; HGNC:11403; STK24.
DR HPA; HPA026435; -.
DR HPA; HPA026502; -.
DR MIM; 604984; gene.
DR neXtProt; NX_Q9Y6E0; -.
DR PharmGKB; PA36210; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000234203; -.
DR HOVERGEN; HBG108518; -.
DR KO; K08838; -.
DR OMA; GSDDWIF; -.
DR PhylomeDB; Q9Y6E0; -.
DR Reactome; REACT_578; Apoptosis.
DR SignaLink; Q9Y6E0; -.
DR ChiTaRS; STK24; human.
DR EvolutionaryTrace; Q9Y6E0; -.
DR GeneWiki; STK24; -.
DR GenomeRNAi; 8428; -.
DR NextBio; 31540; -.
DR PRO; PR:Q9Y6E0; -.
DR ArrayExpress; Q9Y6E0; -.
DR Bgee; Q9Y6E0; -.
DR CleanEx; HS_STK24; -.
DR CleanEx; HS_STK3; -.
DR Genevestigator; Q9Y6E0; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
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:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0048679; P:regulation of axon regeneration; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1 443 Serine/threonine-protein kinase 24.
FT /FTId=PRO_0000086711.
FT CHAIN 1 325 Serine/threonine-protein kinase 24 36 kDa
FT subunit.
FT /FTId=PRO_0000413618.
FT CHAIN 326 443 Serine/threonine-protein kinase 24 12 kDa
FT subunit.
FT /FTId=PRO_0000413619.
FT DOMAIN 36 286 Protein kinase.
FT NP_BIND 42 50 ATP.
FT NP_BIND 112 114 ATP.
FT REGION 335 386 Nuclear export signal (NES).
FT MOTIF 278 292 Bipartite nuclear localization signal.
FT ACT_SITE 156 156 Proton acceptor (By similarity).
FT METAL 161 161 Magnesium.
FT METAL 174 174 Magnesium.
FT BINDING 65 65 ATP.
FT SITE 325 326 Cleavage; by caspase-3, caspase-7 and
FT caspase-8.
FT MOD_RES 18 18 Phosphothreonine; by PKA.
FT MOD_RES 190 190 Phosphothreonine; by autocatalysis.
FT MOD_RES 320 320 Phosphoserine.
FT VAR_SEQ 1 26 MDSRAQLWGLALNKRRATLPHPGGST -> MAHSPVQSGLP
FT GMQ (in isoform A).
FT /FTId=VSP_004874.
FT VARIANT 414 414 A -> V (in dbSNP:rs55953606).
FT /FTId=VAR_041148.
FT VARIANT 426 426 L -> I (in dbSNP:rs55897869).
FT /FTId=VAR_041149.
FT MUTAGEN 18 18 T->A: Loss of phosphorylation by PKA.
FT MUTAGEN 65 65 K->A: Loss of activity and
FT autophosphorylation.
FT MUTAGEN 190 190 T->A: Loss of activity and
FT autophosphorylation.
FT MUTAGEN 321 321 D->N: Loss of proteolytic cleavage by
FT caspases.
FT HELIX 32 34
FT STRAND 36 44
FT STRAND 46 55
FT TURN 56 58
FT STRAND 61 68
FT TURN 69 71
FT HELIX 76 88
FT STRAND 97 103
FT STRAND 106 112
FT STRAND 116 118
FT HELIX 119 123
FT STRAND 124 126
FT HELIX 130 149
FT HELIX 159 161
FT STRAND 162 164
FT STRAND 166 168
FT STRAND 170 172
FT HELIX 180 183
FT STRAND 186 188
FT HELIX 195 197
FT HELIX 200 203
FT HELIX 211 226
FT TURN 230 233
FT HELIX 236 245
FT HELIX 257 266
FT HELIX 271 273
FT HELIX 277 280
FT HELIX 284 289
FT HELIX 293 296
FT HELIX 297 309
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
//
ID STK24_HUMAN Reviewed; 443 AA.
AC Q9Y6E0; O14840; Q5JV92;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 136.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT with 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.,
RA Pei G.;
RT "Identification of a human brain-specific isoform of mammalian STE20-
RT like 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.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA 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.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA 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.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-65 AND 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.,
RA Huang C.L., Leu T.H., Shih H.M., Fang H.I., Robinson D.R., Kung H.J.,
RA 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.,
RA Lu T.L., Jeng W.Y., Lai M.D.;
RT "Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has
RT a 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.,
RA 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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.,
RA Chang W.T., Leu T.H., Chang W.C., Chuang W.J., Tang M.J., Chen T.Y.,
RA Lu T.L., Lai M.D.;
RT "Inhibition of cell migration by autophosphorylated mammalian sterile
RT 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine
RT phosphatase-PEST.";
RL J. Biol. Chem. 281:38405-38417(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), AND MASS
RP SPECTROMETRY.
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
RT the 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
RT novel striatin-interacting phosphatase and kinase complex linked to
RT the cerebral 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),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), MASS
RP SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
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
RT CNS and 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),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 27-315 IN COMPLEX WITH
RP ADENINE; ADP AND MANGANESE IONS, SUBUNIT, AND PHOSPHORYLATION AT
RP 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
RT Mn2+.";
RL Acta Crystallogr. D 66:145-154(2010).
RN [22]
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.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., 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
CC and threonine residues and promotes apoptosis in response to
CC stress stimuli and caspase activation. Mediates oxidative-stress-
CC induced cell death by modulating phosphorylation of JNK1-JNK2
CC (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during
CC oxidative stress. Plays a role in a staurosporine-induced caspase-
CC independent apoptotic pathway by regulating the nuclear
CC translocation of AIFM1 and ENDOG and the DNase activity associated
CC with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its
CC kinase activity. Regulates cellular migration with alteration of
CC PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and
CC inhibits its activity and may regulate PXN phosphorylation through
CC PTPN12. May act as a key regulator of axon regeneration in the
CC optic nerve and radial nerve.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Mg(2+) or Mn(2+) or Co(2+) or Zn(2+).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.8 uM for manganese ions;
CC KM=34.9 uM for cobalt ions;
CC KM=22.7 uM for magnesium ions;
CC KM=4.1 uM for zinc ions;
CC Vmax=2623.1 pmol/min/mg enzyme for manganese ions;
CC Vmax=1746.1 pmol/min/mg enzyme for cobalt ions;
CC Vmax=129.1 pmol/min/mg enzyme for magnesium ions;
CC Vmax=22.3 pmol/min/mg enzyme for zinc ions;
CC -!- SUBUNIT: Monomer. Interacts with CTTNBP2NL.
CC -!- INTERACTION:
CC Q9P2B4:CTTNBP2NL; NbExp=4; IntAct=EBI-740175, EBI-1774273;
CC Q9BUL8:PDCD10; NbExp=7; IntAct=EBI-740175, EBI-740195;
CC O43815:STRN; NbExp=3; IntAct=EBI-740175, EBI-1046642;
CC Q9Y228:TRAF3IP3; NbExp=2; IntAct=EBI-740175, EBI-765817;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane. Note=The
CC truncated form (MST3/N) translocates to the nucleus. Colocalizes
CC with STK38L in 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 Note=Initiator Met-1 is removed. Contains a phosphoserine at
CC position 4. Contains a N-acetylalanine at position 2;
CC -!- TISSUE SPECIFICITY: Isoform A is ubiquitous. Isoform B is
CC expressed in brain with high expression in hippocampus and
CC 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.
CC -!- PTM: Isoform B is activated by phosphorylation by PKA. Oxidative
CC stress induces phosphorylation. Activated by autophosphorylation
CC at Thr-190 and phosphorylation at this site is essential for its
CC function. Manganese, magnesium and cobalt-dependent
CC autophosphorylation is mainly on threonine residues while zinc-
CC dependent autophosphorylation is on both serine and threonine
CC residues.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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DR EMBL; AF024636; AAB82560.1; -; mRNA.
DR EMBL; AF083420; AAD42039.1; -; mRNA.
DR EMBL; AL356423; CAI13114.1; -; Genomic_DNA.
DR EMBL; AL137249; CAI13114.1; JOINED; Genomic_DNA.
DR EMBL; AL137249; CAI39453.1; -; Genomic_DNA.
DR EMBL; AL356423; CAI39453.1; JOINED; Genomic_DNA.
DR EMBL; CH471085; EAX08986.1; -; Genomic_DNA.
DR EMBL; BC035578; AAH35578.1; -; mRNA.
DR RefSeq; NP_001027467.2; NM_001032296.3.
DR RefSeq; NP_003567.2; NM_003576.4.
DR UniGene; Hs.508514; -.
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 PDBsum; 3A7F; -.
DR PDBsum; 3A7G; -.
DR PDBsum; 3A7H; -.
DR PDBsum; 3A7I; -.
DR PDBsum; 3A7J; -.
DR PDBsum; 3CKW; -.
DR PDBsum; 3CKX; -.
DR PDBsum; 3ZHP; -.
DR ProteinModelPortal; Q9Y6E0; -.
DR SMR; Q9Y6E0; 27-350, 375-434.
DR DIP; DIP-40608N; -.
DR IntAct; Q9Y6E0; 33.
DR MINT; MINT-3088034; -.
DR STRING; 9606.ENSP00000365730; -.
DR BindingDB; Q9Y6E0; -.
DR ChEMBL; CHEMBL5082; -.
DR GuidetoPHARMACOLOGY; 2217; -.
DR PhosphoSite; Q9Y6E0; -.
DR DMDM; 13626607; -.
DR PaxDb; Q9Y6E0; -.
DR PRIDE; Q9Y6E0; -.
DR DNASU; 8428; -.
DR Ensembl; ENST00000376547; ENSP00000365730; ENSG00000102572.
DR Ensembl; ENST00000397517; ENSP00000380651; ENSG00000102572.
DR GeneID; 8428; -.
DR KEGG; hsa:8428; -.
DR UCSC; uc001vnm.1; human.
DR CTD; 8428; -.
DR GeneCards; GC13M099103; -.
DR HGNC; HGNC:11403; STK24.
DR HPA; HPA026435; -.
DR HPA; HPA026502; -.
DR MIM; 604984; gene.
DR neXtProt; NX_Q9Y6E0; -.
DR PharmGKB; PA36210; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000234203; -.
DR HOVERGEN; HBG108518; -.
DR KO; K08838; -.
DR OMA; GSDDWIF; -.
DR PhylomeDB; Q9Y6E0; -.
DR Reactome; REACT_578; Apoptosis.
DR SignaLink; Q9Y6E0; -.
DR ChiTaRS; STK24; human.
DR EvolutionaryTrace; Q9Y6E0; -.
DR GeneWiki; STK24; -.
DR GenomeRNAi; 8428; -.
DR NextBio; 31540; -.
DR PRO; PR:Q9Y6E0; -.
DR ArrayExpress; Q9Y6E0; -.
DR Bgee; Q9Y6E0; -.
DR CleanEx; HS_STK24; -.
DR CleanEx; HS_STK3; -.
DR Genevestigator; Q9Y6E0; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
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:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0048679; P:regulation of axon regeneration; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1 443 Serine/threonine-protein kinase 24.
FT /FTId=PRO_0000086711.
FT CHAIN 1 325 Serine/threonine-protein kinase 24 36 kDa
FT subunit.
FT /FTId=PRO_0000413618.
FT CHAIN 326 443 Serine/threonine-protein kinase 24 12 kDa
FT subunit.
FT /FTId=PRO_0000413619.
FT DOMAIN 36 286 Protein kinase.
FT NP_BIND 42 50 ATP.
FT NP_BIND 112 114 ATP.
FT REGION 335 386 Nuclear export signal (NES).
FT MOTIF 278 292 Bipartite nuclear localization signal.
FT ACT_SITE 156 156 Proton acceptor (By similarity).
FT METAL 161 161 Magnesium.
FT METAL 174 174 Magnesium.
FT BINDING 65 65 ATP.
FT SITE 325 326 Cleavage; by caspase-3, caspase-7 and
FT caspase-8.
FT MOD_RES 18 18 Phosphothreonine; by PKA.
FT MOD_RES 190 190 Phosphothreonine; by autocatalysis.
FT MOD_RES 320 320 Phosphoserine.
FT VAR_SEQ 1 26 MDSRAQLWGLALNKRRATLPHPGGST -> MAHSPVQSGLP
FT GMQ (in isoform A).
FT /FTId=VSP_004874.
FT VARIANT 414 414 A -> V (in dbSNP:rs55953606).
FT /FTId=VAR_041148.
FT VARIANT 426 426 L -> I (in dbSNP:rs55897869).
FT /FTId=VAR_041149.
FT MUTAGEN 18 18 T->A: Loss of phosphorylation by PKA.
FT MUTAGEN 65 65 K->A: Loss of activity and
FT autophosphorylation.
FT MUTAGEN 190 190 T->A: Loss of activity and
FT autophosphorylation.
FT MUTAGEN 321 321 D->N: Loss of proteolytic cleavage by
FT caspases.
FT HELIX 32 34
FT STRAND 36 44
FT STRAND 46 55
FT TURN 56 58
FT STRAND 61 68
FT TURN 69 71
FT HELIX 76 88
FT STRAND 97 103
FT STRAND 106 112
FT STRAND 116 118
FT HELIX 119 123
FT STRAND 124 126
FT HELIX 130 149
FT HELIX 159 161
FT STRAND 162 164
FT STRAND 166 168
FT STRAND 170 172
FT HELIX 180 183
FT STRAND 186 188
FT HELIX 195 197
FT HELIX 200 203
FT HELIX 211 226
FT TURN 230 233
FT HELIX 236 245
FT HELIX 257 266
FT HELIX 271 273
FT HELIX 277 280
FT HELIX 284 289
FT HELIX 293 296
FT HELIX 297 309
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
//
MIM
604984
*RECORD*
*FIELD* NO
604984
*FIELD* TI
*604984 SERINE/THREONINE PROTEIN KINASE 24; STK24
;;MAMMALIAN STERILE 20-LIKE 3; MST3
read moreMAMMALIAN STERILE 20-LIKE 3, ISOFORM B, INCLUDED; MST3B, INCLUDED
*FIELD* TX
DESCRIPTION
The yeast 'Sterile 20' gene (STE20) functions upstream of the
mitogen-activated protein kinase (MAPK) cascade. In mammals, protein
kinases related to STE20 can be divided into 2 subfamilies based on
their structure and regulation. Members of the PAK subfamily (see PAK3;
300142) contain a C-terminal catalytic domain and an N-terminal
regulatory domain that has a CDC42 (116952)-binding domain. In contrast,
members of the GCK subfamily (see MAP4K2; 603166), also called the Sps1
subfamily, have an N-terminal catalytic domain and a C-terminal
regulatory domain without a CDC42-binding domain. STK24 belongs to the
GCK subfamily of STE20-like kinases (Zhou et al., 2000).
CLONING
Using PCR with degenerate primers based on conserved regions of the
kinase domains of STE20 and p65 PAK (PAK2; 605022), Schinkmann and
Blenis (1997) obtained a fragment from a HeLa cell cDNA library. By
screening T cell and HeLa cell cDNA libraries using the fragment as the
probe, they isolated a cDNA encoding STK24, which they termed MST3.
Sequence analysis showed that the predicted 431-amino acid STK24 protein
contains an N-terminal kinase domain and a C-terminal regulatory domain.
STK24 shares 69% amino acid identity with STK25 (602255) and is a member
of the GCK subfamily of STE20-like proteins. Northern blot analysis
revealed ubiquitous expression of a 2.0-kb STK24 transcript, with
highest levels detected in heart, skeletal muscle, and pancreas. Western
blot analysis detected a 52-kD STK24 protein in all cell lines tested.
By searching an EST database using the conserved catalytic domain of
STE20 as the probe, Zhou et al. (2000) identified an STK24 isoform that
they called MST3B. The sequence of MST3B is identical after nucleotide
223 to the MST3 sequence reported by Schinkmann and Blenis (1997). MST3B
encodes a predicted 443-amino acid protein. RT-PCR and Northern blot
analyses revealed that expression of the 2.5-kb MST3B transcript is
restricted to brain; Western blot analysis confirmed the brain-specific
expression. In situ hybridization analysis showed that MST3B is widely
expressed in different brain regions, with high levels in hippocampus,
cerebral cortex, and hypothalamus, and moderate levels in geniculate
nucleus and thalamic nucleus. Reduced MST3B expression was observed in
cerebellum.
By analyzing the subcellular localization of truncated MST3 proteins in
transfected HeLa cells, Lee et al. (2004) identified a nuclear
localization signal at the C terminus of the kinase domain and a nuclear
export signal in the C-terminal regulatory domain.
GENE FUNCTION
By in vitro kinase assays, Schinkmann and Blenis (1997) demonstrated
that STK24 readily phosphorylates MBP (159430), histone H3, and itself
but not histones H1, H2, and H4 (see 142711), casein (see 115450), or
phosvitin (CSNK2B; 115441); phosphorylation occurs with manganese as the
cofactor. Immunofluorescence microscopy showed that STK24 is expressed
in the cytoplasm.
By functional analyses, Zhou et al. (2000) demonstrated that MST3 but
not MST3B phosphorylates and activates p42 MAPK (MAPK1; 176948)/p44 MAPK
(MAPK3; 601795) but not MAPK14 (602896) or JNK (see MAPK8; 601158).
Mutational analysis indicated that protein kinase A (see 176911)
phosphorylation of thr18 at the N terminus of MST3B negatively regulates
its ability to phosphorylate and activate MAPK3.
The purine nucleoside inosine stimulates axon outgrowth in certain types
of neurons in culture and in vivo after central nervous system injury.
Inosine activates Mst3b kinase activity. The purine analog 6-thioguanine
blocks outgrowth induced by neurotrophic factors, and this effect is
paralleled by the inhibition of a previously unidentified 45- to 50-kD
serine-threonine protein kinase. Irwin et al. (2006) identified Mst3b as
this protein kinase. Mst3b was a key regulator of axon outgrowth in a
rat pheochromocytoma cell line and in forebrain neurons.
MAPPING
Zhou et al. (2000) identified an STS (GenBank GENBANK G13373) within the
STK24 gene that maps to chromosome 13, between markers D13S159 and
D13S280; electronic PCR analysis confirmed these results.
*FIELD* RF
1. Irwin, N.; Li, Y.-M.; O'Toole, J. E.; Benowitz, L. I.: Mst3b,
a purine-sensitive Ste20-like protein kinase, regulates axon outgrowth. Proc.
Nat. Acad. Sci. 103: 18320-18325, 2006.
2. Lee, W.-S.; Hsu, C.-Y.; Wang, P.-L.; Huang, C.-Y. F.; Chang, C.-H.;
Yuan, C.-J.: Identification and characterization of the nuclear import
and export signals of the mammalian Ste20-like protein kinase 3. FEBS
Lett. 572: 41-45, 2004.
3. Schinkmann, K.; Blenis, J.: Cloning and characterization of a
human STE20-like protein kinase with unusual cofactor requirements. J.
Biol. Chem. 272: 28695-28703, 1997.
4. Zhou, T.-H.; Ling, K.; Guo, J.; Zhou, H.; Wu, Y.-L.; Jing, Q.;
Ma, L.; Pei, G.: Identification of a human brain-specific isoform
of mammalian STE20-like kinase 3 that is regulated by cAMP-dependent
protein kinase. J. Biol. Chem. 275: 2513-2519, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 02/08/2007
Patricia A. Hartz - updated: 6/23/2005
*FIELD* CD
Paul J. Converse: 5/22/2000
*FIELD* ED
alopez: 02/08/2007
wwang: 8/4/2005
wwang: 7/20/2005
terry: 6/23/2005
mgross: 5/22/2000
*RECORD*
*FIELD* NO
604984
*FIELD* TI
*604984 SERINE/THREONINE PROTEIN KINASE 24; STK24
;;MAMMALIAN STERILE 20-LIKE 3; MST3
read moreMAMMALIAN STERILE 20-LIKE 3, ISOFORM B, INCLUDED; MST3B, INCLUDED
*FIELD* TX
DESCRIPTION
The yeast 'Sterile 20' gene (STE20) functions upstream of the
mitogen-activated protein kinase (MAPK) cascade. In mammals, protein
kinases related to STE20 can be divided into 2 subfamilies based on
their structure and regulation. Members of the PAK subfamily (see PAK3;
300142) contain a C-terminal catalytic domain and an N-terminal
regulatory domain that has a CDC42 (116952)-binding domain. In contrast,
members of the GCK subfamily (see MAP4K2; 603166), also called the Sps1
subfamily, have an N-terminal catalytic domain and a C-terminal
regulatory domain without a CDC42-binding domain. STK24 belongs to the
GCK subfamily of STE20-like kinases (Zhou et al., 2000).
CLONING
Using PCR with degenerate primers based on conserved regions of the
kinase domains of STE20 and p65 PAK (PAK2; 605022), Schinkmann and
Blenis (1997) obtained a fragment from a HeLa cell cDNA library. By
screening T cell and HeLa cell cDNA libraries using the fragment as the
probe, they isolated a cDNA encoding STK24, which they termed MST3.
Sequence analysis showed that the predicted 431-amino acid STK24 protein
contains an N-terminal kinase domain and a C-terminal regulatory domain.
STK24 shares 69% amino acid identity with STK25 (602255) and is a member
of the GCK subfamily of STE20-like proteins. Northern blot analysis
revealed ubiquitous expression of a 2.0-kb STK24 transcript, with
highest levels detected in heart, skeletal muscle, and pancreas. Western
blot analysis detected a 52-kD STK24 protein in all cell lines tested.
By searching an EST database using the conserved catalytic domain of
STE20 as the probe, Zhou et al. (2000) identified an STK24 isoform that
they called MST3B. The sequence of MST3B is identical after nucleotide
223 to the MST3 sequence reported by Schinkmann and Blenis (1997). MST3B
encodes a predicted 443-amino acid protein. RT-PCR and Northern blot
analyses revealed that expression of the 2.5-kb MST3B transcript is
restricted to brain; Western blot analysis confirmed the brain-specific
expression. In situ hybridization analysis showed that MST3B is widely
expressed in different brain regions, with high levels in hippocampus,
cerebral cortex, and hypothalamus, and moderate levels in geniculate
nucleus and thalamic nucleus. Reduced MST3B expression was observed in
cerebellum.
By analyzing the subcellular localization of truncated MST3 proteins in
transfected HeLa cells, Lee et al. (2004) identified a nuclear
localization signal at the C terminus of the kinase domain and a nuclear
export signal in the C-terminal regulatory domain.
GENE FUNCTION
By in vitro kinase assays, Schinkmann and Blenis (1997) demonstrated
that STK24 readily phosphorylates MBP (159430), histone H3, and itself
but not histones H1, H2, and H4 (see 142711), casein (see 115450), or
phosvitin (CSNK2B; 115441); phosphorylation occurs with manganese as the
cofactor. Immunofluorescence microscopy showed that STK24 is expressed
in the cytoplasm.
By functional analyses, Zhou et al. (2000) demonstrated that MST3 but
not MST3B phosphorylates and activates p42 MAPK (MAPK1; 176948)/p44 MAPK
(MAPK3; 601795) but not MAPK14 (602896) or JNK (see MAPK8; 601158).
Mutational analysis indicated that protein kinase A (see 176911)
phosphorylation of thr18 at the N terminus of MST3B negatively regulates
its ability to phosphorylate and activate MAPK3.
The purine nucleoside inosine stimulates axon outgrowth in certain types
of neurons in culture and in vivo after central nervous system injury.
Inosine activates Mst3b kinase activity. The purine analog 6-thioguanine
blocks outgrowth induced by neurotrophic factors, and this effect is
paralleled by the inhibition of a previously unidentified 45- to 50-kD
serine-threonine protein kinase. Irwin et al. (2006) identified Mst3b as
this protein kinase. Mst3b was a key regulator of axon outgrowth in a
rat pheochromocytoma cell line and in forebrain neurons.
MAPPING
Zhou et al. (2000) identified an STS (GenBank GENBANK G13373) within the
STK24 gene that maps to chromosome 13, between markers D13S159 and
D13S280; electronic PCR analysis confirmed these results.
*FIELD* RF
1. Irwin, N.; Li, Y.-M.; O'Toole, J. E.; Benowitz, L. I.: Mst3b,
a purine-sensitive Ste20-like protein kinase, regulates axon outgrowth. Proc.
Nat. Acad. Sci. 103: 18320-18325, 2006.
2. Lee, W.-S.; Hsu, C.-Y.; Wang, P.-L.; Huang, C.-Y. F.; Chang, C.-H.;
Yuan, C.-J.: Identification and characterization of the nuclear import
and export signals of the mammalian Ste20-like protein kinase 3. FEBS
Lett. 572: 41-45, 2004.
3. Schinkmann, K.; Blenis, J.: Cloning and characterization of a
human STE20-like protein kinase with unusual cofactor requirements. J.
Biol. Chem. 272: 28695-28703, 1997.
4. Zhou, T.-H.; Ling, K.; Guo, J.; Zhou, H.; Wu, Y.-L.; Jing, Q.;
Ma, L.; Pei, G.: Identification of a human brain-specific isoform
of mammalian STE20-like kinase 3 that is regulated by cAMP-dependent
protein kinase. J. Biol. Chem. 275: 2513-2519, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 02/08/2007
Patricia A. Hartz - updated: 6/23/2005
*FIELD* CD
Paul J. Converse: 5/22/2000
*FIELD* ED
alopez: 02/08/2007
wwang: 8/4/2005
wwang: 7/20/2005
terry: 6/23/2005
mgross: 5/22/2000