ID ST38L_HUMAN Reviewed; 464 AA. AC Q9Y2H1; A8K4U0; B4E3J8; Q8TBX7; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 3. DT 27-MAR-2024, entry version 197. DE RecName: Full=Serine/threonine-protein kinase 38-like; DE EC=2.7.11.1; DE AltName: Full=NDR2 protein kinase; DE AltName: Full=Nuclear Dbf2-related kinase 2; GN Name=STK38L {ECO:0000312|EMBL:AAH28603.1}; GN Synonyms=KIAA0965 {ECO:0000312|EMBL:BAA76809.2}, NDR2 GN {ECO:0000303|PubMed:15037617}; 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} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, RP ACTIVITY REGULATION, INTERACTION WITH S100, PHOSPHORYLATION AT THR-75; RP SER-282 AND THR-442, AND MUTAGENESIS OF THR-75; LYS-119; SER-282 AND RP THR-442. RC TISSUE=Brain {ECO:0000269|PubMed:15037617}; RX PubMed=15037617; DOI=10.1074/jbc.m402472200; RA Stegert M.R., Tamaskovic R., Bichsel S.J., Hergovich A., Hemmings B.A.; RT "Regulation of NDR2 protein kinase by multi-site phosphorylation and the RT S100B calcium-binding protein."; RL J. Biol. Chem. 279:23806-23812(2004). RN [2] {ECO:0000312|EMBL:BAA76809.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain {ECO:0000312|EMBL:BAA76809.2}; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [3] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] 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 [7] {ECO:0000312|EMBL:AAH28603.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis {ECO:0000312|EMBL:AAH28603.1}; 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 [8] RP PROTEIN SEQUENCE OF 2-18; 26-42; 48-64; 73-79; 83-98; 123-161; 213-224; RP 229-240; 249-266; 340-392 AND 433-460, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma, and Lung carcinoma; RA Bienvenut W.V., Vousden K.H., Lukashchuk N., Calvo F., Kolch W.; RL Submitted (MAR-2008) to UniProtKB. RN [9] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ACTIVITY REGULATION, RP 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 [10] RP PHOSPHORYLATION AT THR-442, ACTIVITY REGULATION, 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 [11] RP IDENTIFICATION BY 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 [12] 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 [13] RP IDENTIFICATION BY 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 [14] RP VARIANT [LARGE SCALE ANALYSIS] ALA-99. 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: Involved in the regulation of structural processes in CC differentiating and mature neuronal cells. {ECO:0000250, CC ECO:0000269|PubMed:15037617, ECO:0000269|PubMed:15067004}. 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-282. Thr-442 then undergoes calcium- CC dependent phosphorylation by STK24/MST3. Interactions between CC phosphorylated Thr-442 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 STK38L. {ECO:0000269|PubMed:15037617, CC ECO:0000269|PubMed:15067004, ECO:0000269|PubMed:16314523}. CC -!- SUBUNIT: Homodimeric S100B binds two molecules of STK38L. Interacts CC with MICAL1; leading to inhibit the protein kinase activity by CC antagonizing activation by MST1/STK4 (By similarity). Interacts with CC MOB1 and MOB2. {ECO:0000250, ECO:0000269|PubMed:15037617, CC ECO:0000269|PubMed:15067004}. CC -!- INTERACTION: CC Q9Y2H1; Q16543: CDC37; NbExp=6; IntAct=EBI-991501, EBI-295634; CC Q9Y2H1; Q9H8S9: MOB1A; NbExp=5; IntAct=EBI-991501, EBI-748229; CC Q9Y2H1; Q70IA6: MOB2; NbExp=10; IntAct=EBI-991501, EBI-2558739; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Membrane. CC Note=Associated with the actin cytoskeleton. Co-localizes with CC STK24/MST3 in the membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y2H1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y2H1-2; Sequence=VSP_056233, VSP_056234; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels observed CC in the thymus. {ECO:0000269|PubMed:15067004}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. {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; AB023182; BAA76809.2; -; mRNA. DR EMBL; AK291055; BAF83744.1; -; mRNA. DR EMBL; AK304755; BAG65510.1; -; mRNA. DR EMBL; AC092827; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471094; EAW96549.1; -; Genomic_DNA. DR EMBL; BC028603; AAH28603.1; -; mRNA. DR CCDS; CCDS31761.1; -. [Q9Y2H1-1] DR RefSeq; NP_055815.1; NM_015000.3. [Q9Y2H1-1] DR RefSeq; XP_006719121.1; XM_006719058.3. DR RefSeq; XP_011518915.1; XM_011520613.2. DR RefSeq; XP_016874525.1; XM_017019036.1. DR PDB; 5XQZ; X-ray; 2.10 A; C/D=25-87. DR PDBsum; 5XQZ; -. DR AlphaFoldDB; Q9Y2H1; -. DR SMR; Q9Y2H1; -. DR BioGRID; 116654; 70. DR IntAct; Q9Y2H1; 107. DR MINT; Q9Y2H1; -. DR STRING; 9606.ENSP00000373684; -. DR BindingDB; Q9Y2H1; -. DR ChEMBL; CHEMBL4851; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q9Y2H1; -. DR iPTMnet; Q9Y2H1; -. DR PhosphoSitePlus; Q9Y2H1; -. DR BioMuta; STK38L; -. DR DMDM; 56749668; -. DR CPTAC; non-CPTAC-6002; -. DR CPTAC; non-CPTAC-6003; -. DR EPD; Q9Y2H1; -. DR jPOST; Q9Y2H1; -. DR MassIVE; Q9Y2H1; -. DR MaxQB; Q9Y2H1; -. DR PaxDb; 9606-ENSP00000373684; -. DR PeptideAtlas; Q9Y2H1; -. DR ProteomicsDB; 5904; -. DR ProteomicsDB; 85780; -. [Q9Y2H1-1] DR Pumba; Q9Y2H1; -. DR Antibodypedia; 24379; 280 antibodies from 28 providers. DR DNASU; 23012; -. DR Ensembl; ENST00000389032.8; ENSP00000373684.3; ENSG00000211455.8. [Q9Y2H1-1] DR GeneID; 23012; -. DR KEGG; hsa:23012; -. DR MANE-Select; ENST00000389032.8; ENSP00000373684.3; NM_015000.4; NP_055815.1. DR UCSC; uc001rhr.4; human. [Q9Y2H1-1] DR AGR; HGNC:17848; -. DR CTD; 23012; -. DR DisGeNET; 23012; -. DR GeneCards; STK38L; -. DR HGNC; HGNC:17848; STK38L. DR HPA; ENSG00000211455; Low tissue specificity. DR MIM; 615836; gene. DR neXtProt; NX_Q9Y2H1; -. DR OpenTargets; ENSG00000211455; -. DR PharmGKB; PA38252; -. DR VEuPathDB; HostDB:ENSG00000211455; -. DR eggNOG; KOG0605; Eukaryota. DR GeneTree; ENSGT00940000153544; -. DR HOGENOM; CLU_000288_67_2_1; -. DR InParanoid; Q9Y2H1; -. DR OMA; HDNAYYQ; -. DR OrthoDB; 988261at2759; -. DR PhylomeDB; Q9Y2H1; -. DR TreeFam; TF105337; -. DR PathwayCommons; Q9Y2H1; -. DR SignaLink; Q9Y2H1; -. DR SIGNOR; Q9Y2H1; -. DR BioGRID-ORCS; 23012; 16 hits in 1195 CRISPR screens. DR ChiTaRS; STK38L; human. DR GeneWiki; STK38L; -. DR GenomeRNAi; 23012; -. DR Pharos; Q9Y2H1; Tchem. DR PRO; PR:Q9Y2H1; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9Y2H1; Protein. DR Bgee; ENSG00000211455; Expressed in ascending aorta and 201 other cell types or tissues. DR ExpressionAtlas; Q9Y2H1; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB. 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:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA: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:0010507; P:negative regulation of autophagy; IDA:UniProt. DR GO; GO:0099173; P:postsynapse organization; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0051128; P:regulation of cellular component organization; ISS:UniProtKB. DR CDD; cd05627; STKc_NDR2; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. 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:SF160; SERINE_THREONINE-PROTEIN KINASE 38-LIKE; 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; Q9Y2H1; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; KW ATP-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing; Kinase; KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8" FT CHAIN 2..464 FT /note="Serine/threonine-protein kinase 38-like" FT /id="PRO_0000086720" FT DOMAIN 90..383 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 384..453 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT REGION 63..88 FT /note="S100B binding" FT /evidence="ECO:0000250" FT ACT_SITE 213 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 96..104 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O95835, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:15037617" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.8" FT MOD_RES 75 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:15037617" FT MOD_RES 282 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:15037617" FT MOD_RES 442 FT /note="Phosphothreonine; by STK24/MST3" FT /evidence="ECO:0000269|PubMed:15037617, FT ECO:0000269|PubMed:16314523" FT VAR_SEQ 1..52 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056233" FT VAR_SEQ 62..102 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056234" FT VARIANT 99 FT /note="G -> A (in a aLLTEL/AML1+ sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041199" FT MUTAGEN 75 FT /note="T->A: Decreased kinase activity. Reduced binding of FT S100B." FT /evidence="ECO:0000269|PubMed:15037617" FT MUTAGEN 119 FT /note="K->A: Loss of autophosphorylation and kinase FT activity." FT /evidence="ECO:0000269|PubMed:15037617" FT MUTAGEN 282 FT /note="S->A: Loss of autophosphorylation and kinase FT activity." FT /evidence="ECO:0000269|PubMed:15037617" FT MUTAGEN 442 FT /note="T->A: Decreased kinase activity." FT /evidence="ECO:0000269|PubMed:15037617" FT HELIX 25..56 FT /evidence="ECO:0007829|PDB:5XQZ" FT HELIX 60..83 FT /evidence="ECO:0007829|PDB:5XQZ" SQ SEQUENCE 464 AA; 54003 MW; 71347E80BC3ADCB3 CRC64; MAMTAGTTTT FPMSNHTRER VTVAKLTLEN FYSNLILQHE ERETRQKKLE VAMEEEGLAD EEKKLRRSQH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA FGEVRLVQKK DTGHIYAMKI LRKSDMLEKE QVAHIRAERD ILVEADGAWV VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM KKDTLTEEET QFYISETVLA IDAIHQLGFI HRDIKPDNLL LDAKGHVKLS DFGLCTGLKK AHRTEFYRNL THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY NKLCDWWSLG VIMYEMLIGY PPFCSETPQE TYRKVMNWKE TLVFPPEVPI SEKAKDLILR FCIDSENRIG NSGVEEIKGH PFFEGVDWEH IRERPAAIPI EIKSIDDTSN FDDFPESDIL QPVPNTTEPD YKSKDWVFLN YTYKRFEGLT QRGSIPTYMK AGKL //