ID STK38_HUMAN Reviewed; 465 AA. AC Q15208; Q503A1; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 211. DE RecName: Full=Serine/threonine-protein kinase 38; DE EC=2.7.11.1; DE AltName: Full=NDR1 protein kinase; DE AltName: Full=Nuclear Dbf2-related kinase 1; GN Name=STK38 {ECO:0000312|EMBL:AAH12085.1}; GN Synonyms=NDR1 {ECO:0000303|PubMed:7761441}; 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] {ECO:0000305, ECO:0000312|EMBL:CAA84485.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR RP LOCATION, AND MUTAGENESIS OF LYS-118. RC TISSUE=Fetal brain {ECO:0000312|EMBL:CAA84485.1}; RX PubMed=7761441; DOI=10.1073/pnas.92.11.5022; RA Millward T.A., Cron P., Hemmings B.A.; RT "Molecular cloning and characterization of a conserved nuclear RT serine/threonine protein kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 92:5022-5026(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] {ECO:0000312|EMBL:AAH12085.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta, and Uterus {ECO:0000312|EMBL:AAH12085.1}; 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 [4] RP PROTEIN SEQUENCE OF 2-17; 25-44; 51-63; 72-78; 82-97; 110-118; 122-159; RP 182-239; 248-266; 277-301; 334-391; 394-402 AND 437-454, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V., Calvo F., Kolch W.; RL Submitted (MAR-2008) to UniProtKB. RN [5] {ECO:0000305} RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT THR-74; SER-281 AND RP THR-444, AND MUTAGENESIS OF THR-74; LYS-118; SER-281 AND THR-444. RX PubMed=12493777; DOI=10.1074/jbc.m210590200; RA Tamaskovic R., Bichsel S.J., Rogniaux H., Stegert M.R., Hemmings B.A.; RT "Mechanism of Ca2+-mediated regulation of NDR protein kinase through RT autophosphorylation and phosphorylation by an upstream kinase."; RL J. Biol. Chem. 278:6710-6718(2003). RN [6] {ECO:0000305} RP ACTIVITY REGULATION, AND INTERACTION WITH MOB1 AND MOB2. RX PubMed=15067004; DOI=10.1074/jbc.m401999200; RA Devroe E., Erdjument-Bromage H., Tempst P., Silver P.A.; RT "Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases."; RL J. Biol. Chem. 279:24444-24451(2004). RN [7] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ACTIVITY REGULATION, RP AND INTERACTION WITH MOB1 AND MOB2. RX PubMed=15197186; DOI=10.1074/jbc.m404542200; RA Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.; RT "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by RT the hMOB1 protein."; RL J. Biol. Chem. 279:35228-35235(2004). RN [8] RP ISGYLATION. RX PubMed=16884686; DOI=10.1016/j.bbrc.2006.07.076; RA Takeuchi T., Inoue S., Yokosawa H.; RT "Identification and Herc5-mediated ISGylation of novel target proteins."; RL Biochem. Biophys. Res. Commun. 348:473-477(2006). RN [9] RP INTERACTION WITH STK3/MST2 AND MOBKL1B, SUBCELLULAR LOCATION, AND RP PHOSPHORYLATION BY STK3/MST2. RX PubMed=18362890; DOI=10.1038/onc.2008.66; RA Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M., RA Kawata A., Ohno K., Hata Y.; RT "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to RT form the scaffold to activate nuclear Dbf2-related kinase 1."; RL Oncogene 27:4281-4292(2008). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAP3K1 AND MAP3K2. RX PubMed=17906693; DOI=10.1038/sj.onc.1210828; RA Enomoto A., Kido N., Ito M., Morita A., Matsumoto Y., Takamatsu N., RA Hosoi Y., Miyagawa K.; RT "Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 RT (STK38)."; RL Oncogene 27:1930-1938(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP RETRACTED PAPER. RX PubMed=19377461; DOI=10.1038/nature07954; RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., RA Kitagawa H., Kato S.; RT "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced RT granulopoiesis."; RL Nature 459:455-459(2009). RN [13] RP CAUTION, AND RETRACTION NOTICE OF PUBMED:19377461. RX PubMed=24336203; DOI=10.1038/nature12896; RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., RA Kitagawa H., Kato S.; RT "Retraction: GlcNAcylation of a histone methyltransferase in retinoic-acid- RT induced granulopoiesis."; RL Nature 505:574-574(2014). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION BY RP MASS 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 [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [18] {ECO:0000305} RP STRUCTURE BY NMR OF 62-84, ACTIVITY REGULATION, AND INTERACTION WITH S100B. RX PubMed=14661952; DOI=10.1021/bi035089a; RA Bhattacharya S., Large E., Heizmann C.W., Hemmings B.A., Chazin W.J.; RT "Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 RT target specificity and activation of the kinase."; RL Biochemistry 42:14416-14426(2003). RN [19] RP VARIANTS [LARGE SCALE ANALYSIS] LYS-18; ASN-145 AND ARG-267. 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: Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 CC from its phosphorylated form to its non-phosphorylated form and CC inhibits autophosphorylation of MAP3K2. {ECO:0000269|PubMed:12493777, CC ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:17906693, CC ECO:0000269|PubMed:7761441}. 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 -!- ACTIVITY REGULATION: Activated by binding of S100B which releases CC autoinhibitory N-lobe interactions, enabling ATP to bind and the CC autophosphorylation of Ser-281. Thr-444 then undergoes calcium- CC dependent phosphorylation by STK24/MST3. Interactions between CC phosphorylated Thr-444 and the N-lobe promote additional structural CC changes that complete the activation of the kinase. Autoinhibition is CC also released by the binding of MOB1/MOBKL1A and MOB2/HCCA2 to the N- CC terminal of STK38. {ECO:0000269|PubMed:12493777, CC ECO:0000269|PubMed:14661952, ECO:0000269|PubMed:15067004, CC ECO:0000269|PubMed:15197186}. CC -!- SUBUNIT: Homodimeric S100B binds two molecules of STK38 CC (PubMed:14661952). Interacts with MOB1 and MOB2 (PubMed:15067004, CC PubMed:15197186). Interacts with MAP3K1 and MAP3K2 (via the kinase CC catalytic domain) (PubMed:17906693). Forms a tripartite complex with CC MOBKL1B and STK3/MST2 (PubMed:18362890). Interacts with MICAL1; leading CC to inhibit the protein kinase activity by antagonizing activation by CC MST1/STK4 (By similarity). {ECO:0000250|UniProtKB:Q91VJ4, CC ECO:0000269|PubMed:14661952, ECO:0000269|PubMed:15067004, CC ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:17906693, CC ECO:0000269|PubMed:18362890}. CC -!- INTERACTION: CC Q15208; P49407: ARRB1; NbExp=3; IntAct=EBI-458376, EBI-743313; CC Q15208; P32121: ARRB2; NbExp=3; IntAct=EBI-458376, EBI-714559; CC Q15208; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-458376, EBI-11524452; CC Q15208; Q03135: CAV1; NbExp=3; IntAct=EBI-458376, EBI-603614; CC Q15208; P08238: HSP90AB1; NbExp=2; IntAct=EBI-458376, EBI-352572; CC Q15208; Q9H8S9: MOB1A; NbExp=3; IntAct=EBI-458376, EBI-748229; CC Q15208; P16333: NCK1; NbExp=3; IntAct=EBI-458376, EBI-389883; CC Q15208; P30086: PEBP1; NbExp=3; IntAct=EBI-458376, EBI-716384; CC Q15208; P02638: S100B; Xeno; NbExp=3; IntAct=EBI-458376, EBI-458452; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels observed CC in peripheral blood leukocytes. {ECO:0000269|PubMed:15197186, CC ECO:0000269|PubMed:7761441}. CC -!- PTM: ISGylated. {ECO:0000305|PubMed:16884686}. CC -!- PTM: Phosphorylated by STK3/MST2 and this is enhanced by MOBKL1B. CC {ECO:0000269|PubMed:12493777, ECO:0000269|PubMed:18362890}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- CAUTION: Was originally thought to be part of the MLL5-L complex, at CC least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and CC OGT (PubMed:19377461). However, the corresponding article has been CC retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461, CC ECO:0000269|PubMed:24336203}. 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; Z35102; CAA84485.1; -; mRNA. DR EMBL; Z85986; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC012085; AAH12085.1; -; mRNA. DR EMBL; BC095413; AAH95413.1; -; mRNA. DR CCDS; CCDS4822.1; -. DR PIR; I38133; I38133. DR RefSeq; NP_001292031.1; NM_001305102.1. DR RefSeq; NP_009202.1; NM_007271.3. DR RefSeq; XP_006715051.1; XM_006714988.3. DR RefSeq; XP_006715052.1; XM_006714989.3. DR PDB; 1PSB; NMR; -; C/D=62-87. DR PDB; 6BXI; X-ray; 2.20 A; A/B=82-414. DR PDBsum; 1PSB; -. DR PDBsum; 6BXI; -. DR AlphaFoldDB; Q15208; -. DR BMRB; Q15208; -. DR SMR; Q15208; -. DR BioGRID; 116457; 169. DR CORUM; Q15208; -. DR IntAct; Q15208; 61. DR MINT; Q15208; -. DR STRING; 9606.ENSP00000229812; -. DR BindingDB; Q15208; -. DR ChEMBL; CHEMBL1075155; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q15208; -. DR iPTMnet; Q15208; -. DR MetOSite; Q15208; -. DR PhosphoSitePlus; Q15208; -. DR BioMuta; STK38; -. DR DMDM; 56749457; -. DR CPTAC; CPTAC-2988; -. DR CPTAC; CPTAC-2989; -. DR EPD; Q15208; -. DR jPOST; Q15208; -. DR MassIVE; Q15208; -. DR MaxQB; Q15208; -. DR PaxDb; 9606-ENSP00000229812; -. DR PeptideAtlas; Q15208; -. DR ProteomicsDB; 60489; -. DR Pumba; Q15208; -. DR Antibodypedia; 29688; 471 antibodies from 33 providers. DR DNASU; 11329; -. DR Ensembl; ENST00000229812.8; ENSP00000229812.7; ENSG00000112079.9. DR GeneID; 11329; -. DR KEGG; hsa:11329; -. DR MANE-Select; ENST00000229812.8; ENSP00000229812.7; NM_007271.4; NP_009202.1. DR UCSC; uc003omh.3; human. DR AGR; HGNC:17847; -. DR CTD; 11329; -. DR DisGeNET; 11329; -. DR GeneCards; STK38; -. DR HGNC; HGNC:17847; STK38. DR HPA; ENSG00000112079; Low tissue specificity. DR MIM; 606964; gene. DR neXtProt; NX_Q15208; -. DR OpenTargets; ENSG00000112079; -. DR PharmGKB; PA38251; -. DR VEuPathDB; HostDB:ENSG00000112079; -. DR eggNOG; KOG0605; Eukaryota. DR GeneTree; ENSGT00940000153544; -. DR HOGENOM; CLU_000288_67_0_1; -. DR InParanoid; Q15208; -. DR OMA; EEIKCNS; -. DR OrthoDB; 988261at2759; -. DR PhylomeDB; Q15208; -. DR TreeFam; TF105337; -. DR BRENDA; 2.7.11.1; 2681. DR PathwayCommons; Q15208; -. DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle. DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle. DR SignaLink; Q15208; -. DR SIGNOR; Q15208; -. DR BioGRID-ORCS; 11329; 16 hits in 1115 CRISPR screens. DR ChiTaRS; STK38; human. DR EvolutionaryTrace; Q15208; -. DR GeneWiki; STK38; -. DR GenomeRNAi; 11329; -. DR Pharos; Q15208; Tchem. DR PRO; PR:Q15208; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q15208; Protein. DR Bgee; ENSG00000112079; Expressed in palpebral conjunctiva and 208 other cell types or tissues. DR ExpressionAtlas; Q15208; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:UniProtKB. 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:0035556; P:intracellular signal transduction; IDA:UniProtKB. DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB. DR GO; GO:0099173; P:postsynapse organization; IEA:Ensembl. DR GO; GO:0036211; P:protein modification process; IDA:ProtInc. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR CDD; cd21782; MobB_NDR1; 1. DR CDD; cd05628; STKc_NDR1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. DR IDEAL; IID00172; -. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24356:SF221; SERINE_THREONINE-PROTEIN KINASE 38; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q15208; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; KW Direct protein sequencing; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.4" FT CHAIN 2..465 FT /note="Serine/threonine-protein kinase 38" FT /id="PRO_0000086718" FT DOMAIN 89..382 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000312|EMBL:CAA84485.1" FT DOMAIN 383..455 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT REGION 62..87 FT /note="Interaction with S100B" FT /evidence="ECO:0000269|PubMed:14661952" FT ACT_SITE 212 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 95..103 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O95835, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:12493777, ECO:0000269|PubMed:7761441" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.4" FT MOD_RES 74 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:12493777" FT MOD_RES 264 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 281 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:12493777" FT MOD_RES 444 FT /note="Phosphothreonine; by STK24/MST3" FT /evidence="ECO:0000269|PubMed:12493777" FT VARIANT 18 FT /note="E -> K (in a metastatic melanoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041196" FT VARIANT 145 FT /note="D -> N (in dbSNP:rs56005153)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041197" FT VARIANT 267 FT /note="K -> R (in dbSNP:rs56105564)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041198" FT MUTAGEN 74 FT /note="T->A: Decreases autophosphorylation and kinase FT activity. Reduced binding of S100B." FT /evidence="ECO:0000269|PubMed:12493777" FT MUTAGEN 118 FT /note="K->A: Loss of autophosphorylation and kinase FT activity." FT /evidence="ECO:0000269|PubMed:12493777, FT ECO:0000269|PubMed:7761441" FT MUTAGEN 281 FT /note="S->A: Loss of autophosphorylation and kinase FT activity." FT /evidence="ECO:0000269|PubMed:12493777" FT MUTAGEN 444 FT /note="T->A: Decreases autophosphorylation and kinase FT activity." FT /evidence="ECO:0000269|PubMed:12493777" FT HELIX 74..85 FT /evidence="ECO:0007829|PDB:1PSB" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:6BXI" FT STRAND 89..98 FT /evidence="ECO:0007829|PDB:6BXI" FT STRAND 101..108 FT /evidence="ECO:0007829|PDB:6BXI" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:6BXI" FT STRAND 114..121 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 128..144 FT /evidence="ECO:0007829|PDB:6BXI" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:6BXI" FT STRAND 159..166 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 174..181 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 186..205 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 215..217 FT /evidence="ECO:0007829|PDB:6BXI" FT STRAND 218..220 FT /evidence="ECO:0007829|PDB:6BXI" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:6BXI" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 243..246 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 257..260 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 264..273 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 275..280 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 291..294 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 303..317 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 327..335 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 337..340 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 351..360 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 364..366 FT /evidence="ECO:0007829|PDB:6BXI" FT TURN 368..371 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 374..377 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 380..382 FT /evidence="ECO:0007829|PDB:6BXI" FT STRAND 387..389 FT /evidence="ECO:0007829|PDB:6BXI" FT HELIX 390..392 FT /evidence="ECO:0007829|PDB:6BXI" SQ SEQUENCE 465 AA; 54190 MW; 7262221DBFFAF83C CRC64; MAMTGSTPCS SMSNHTKERV TMTKVTLENF YSNLIAQHEE REMRQKKLEK VMEEEGLKDE EKRLRRSAHA RKETEFLRLK RTRLGLEDFE SLKVIGRGAF GEVRLVQKKD TGHVYAMKIL RKADMLEKEQ VGHIRAERDI LVEADSLWVV KMFYSFQDKL NLYLIMEFLP GGDMMTLLMK KDTLTEEETQ FYIAETVLAI DSIHQLGFIH RDIKPDNLLL DSKGHVKLSD FGLCTGLKKA HRTEFYRNLN HSLPSDFTFQ NMNSKRKAET WKRNRRQLAF STVGTPDYIA PEVFMQTGYN KLCDWWSLGV IMYEMLIGYP PFCSETPQET YKKVMNWKET LTFPPEVPIS EKAKDLILRF CCEWEHRIGA PGVEEIKSNS FFEGVDWEHI RERPAAISIE IKSIDDTSNF DEFPESDILK PTVATSNHPE TDYKNKDWVF INYTYKRFEG LTARGAIPSY MKAAK //