ST38L_HUMAN
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 03-AUG-2022, entry version 188.
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},
GN NDR2 {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}.
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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. [Q9Y2H1-1]
DR RefSeq; XP_011518915.1; XM_011520613.2. [Q9Y2H1-2]
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; 57.
DR IntAct; Q9Y2H1; 106.
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 EPD; Q9Y2H1; -.
DR jPOST; Q9Y2H1; -.
DR MassIVE; Q9Y2H1; -.
DR MaxQB; Q9Y2H1; -.
DR PaxDb; Q9Y2H1; -.
DR PeptideAtlas; Q9Y2H1; -.
DR PRIDE; Q9Y2H1; -.
DR ProteomicsDB; 5904; -.
DR ProteomicsDB; 85780; -. [Q9Y2H1-1]
DR Antibodypedia; 24379; 259 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 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; PERYSEN; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; Q9Y2H1; -.
DR TreeFam; TF105337; -.
DR PathwayCommons; Q9Y2H1; -.
DR SignaLink; Q9Y2H1; -.
DR SIGNOR; Q9Y2H1; -.
DR BioGRID-ORCS; 23012; 11 hits in 1112 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 200 other tissues.
DR ExpressionAtlas; Q9Y2H1; baseline and differential.
DR Genevisible; Q9Y2H1; HS.
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: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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0051128; P:regulation of cellular component organization; ISS:UniProtKB.
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 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; SSF56112; 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.
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 aLL TEL/AML1+ sample; somatic
FT 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
