ID MAST2_HUMAN Reviewed; 1798 AA. AC Q6P0Q8; O94899; Q5VT07; Q5VT08; Q7LGC4; Q8NDG1; Q96B94; Q9BYE8; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 27-MAR-2024, entry version 177. DE RecName: Full=Microtubule-associated serine/threonine-protein kinase 2; DE EC=2.7.11.1; GN Name=MAST2 {ECO:0000312|EMBL:CAH73245.1}; GN Synonyms=KIAA0807 {ECO:0000312|EMBL:BAA34527.2}, MAST205 GN {ECO:0000312|EMBL:BAB40778.1}; 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:BAB40778.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLU-388; MET-659 AND RP GLY-1551, SUBCELLULAR LOCATION, AND INTERACTION WITH CDHR2. RC TISSUE=Brain {ECO:0000312|EMBL:BAB40778.1}; RX PubMed=12117771; DOI=10.1093/carcin/23.7.1139; RA Okazaki N., Takahashi N., Kojima S., Masuho Y., Koga H.; RT "Protocadherin LKC, a new candidate for a tumor suppressor of colon and RT liver cancers, its association with contact inhibition of cell RT proliferation."; RL Carcinogenesis 23:1139-1148(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1). RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH65499.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 281-1798 (ISOFORM 2), AND VARIANT MET-659. RC TISSUE=Lymph {ECO:0000312|EMBL:AAH65499.1}, and Placenta RC {ECO:0000312|EMBL:AAH15816.2}; 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] {ECO:0000305, ECO:0000312|EMBL:BAA34527.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 470-1797 (ISOFORM 1), AND RP VARIANTS MET-659 AND GLY-1551. RC TISSUE=Brain {ECO:0000312|EMBL:BAA34527.2}; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [5] {ECO:0000305, ECO:0000312|EMBL:CAH73244.1} RP SEQUENCE REVISION TO C-TERMINUS. RA Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 833-1797 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] {ECO:0000305} RP TISSUE SPECIFICITY. RX PubMed=8902215; DOI=10.1095/biolreprod55.5.1039; RA Walden P.D., Millette C.F.; RT "Increased activity associated with the MAST205 protein kinase complex RT during mammalian spermiogenesis."; RL Biol. Reprod. 55:1039-1044(1996). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1508, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-900, AND 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-148, AND 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-209, AND 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-1032, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-74; SER-148; SER-209; RP SER-290; SER-876; SER-900; SER-1032; SER-1256; SER-1364 AND SER-1447, AND RP IDENTIFICATION BY 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-874, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1004, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [17] RP VARIANTS [LARGE SCALE ANALYSIS] PHE-69; GLU-275; GLU-388; ALA-655; MET-659; RP LEU-991; ARG-1197; GLU-1221; LEU-1246; MET-1304; THR-1463; ALA-1468; RP GLY-1551; ARG-1673 AND GLU-1703. 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: Appears to link the dystrophin/utrophin network with CC microtubule filaments via the syntrophins. Phosphorylation of DMD or CC UTRN may modulate their affinities for associated proteins. Functions CC in a multi-protein complex in spermatid maturation. Regulates CC lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a CC complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B CC activation (By similarity). {ECO:0000250}. 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 Evidence={ECO:0000250|UniProtKB:Q60592}; 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; Evidence={ECO:0000250|UniProtKB:Q60592}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q60592}; CC -!- SUBUNIT: Interacts with CDHR2. {ECO:0000269|PubMed:12117771}. CC -!- INTERACTION: CC Q6P0Q8; Q9BYE9: CDHR2; NbExp=4; IntAct=EBI-493777, EBI-493793; CC Q6P0Q8; P48764: SLC9A3; NbExp=2; IntAct=EBI-493777, EBI-7816923; CC Q6P0Q8; P62258: YWHAE; NbExp=3; IntAct=EBI-493777, EBI-356498; CC Q6P0Q8; Q28362: SLC9A3; Xeno; NbExp=2; IntAct=EBI-493777, EBI-7817027; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:12117771}. Cell membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. CC Note=Recruited to the sub-membranous area on interaction with CDHR2. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000269|PubMed:12117771}; CC IsoId=Q6P0Q8-1; Sequence=Displayed; CC Name=2 {ECO:0000305}; CC IsoId=Q6P0Q8-2; Sequence=VSP_051698, VSP_051699, VSP_051700; CC -!- TISSUE SPECIFICITY: Abundant in the testis. CC {ECO:0000269|PubMed:8902215}. CC -!- PTM: Phosphorylated and ubiquitinated. N-terminal ubiquitination leads CC to degradation of MAST2 by proteasome-mediated proteolysis. N-terminal CC phosphorylation appears to be a prerequisite for ubiquitination (By CC similarity). {ECO:0000250|UniProtKB:Q60592}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH15816.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH15816.2; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB40778.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAH73245.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAI16563.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAI21706.1; Type=Erroneous gene model prediction; Evidence={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; AB047005; BAB40778.1; ALT_FRAME; mRNA. DR EMBL; AL645480; CAH73244.1; -; Genomic_DNA. DR EMBL; AL358075; CAH73244.1; JOINED; Genomic_DNA. DR EMBL; AL603882; CAH73244.1; JOINED; Genomic_DNA. DR EMBL; AL603888; CAH73244.1; JOINED; Genomic_DNA. DR EMBL; AL645480; CAH73245.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL358075; CAH73245.1; JOINED; Genomic_DNA. DR EMBL; AL603888; CAH73245.1; JOINED; Genomic_DNA. DR EMBL; AL603882; CAI16217.1; -; Genomic_DNA. DR EMBL; AL358075; CAI16217.1; JOINED; Genomic_DNA. DR EMBL; AL603888; CAI16217.1; JOINED; Genomic_DNA. DR EMBL; AL645480; CAI16217.1; JOINED; Genomic_DNA. DR EMBL; AL603888; CAI16562.1; -; Genomic_DNA. DR EMBL; AL358075; CAI16562.1; JOINED; Genomic_DNA. DR EMBL; AL603882; CAI16562.1; JOINED; Genomic_DNA. DR EMBL; AL645480; CAI16562.1; JOINED; Genomic_DNA. DR EMBL; AL603888; CAI16563.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL358075; CAI16563.1; JOINED; Genomic_DNA. DR EMBL; AL645480; CAI16563.1; JOINED; Genomic_DNA. DR EMBL; AL358075; CAI21705.1; -; Genomic_DNA. DR EMBL; AL603882; CAI21705.1; JOINED; Genomic_DNA. DR EMBL; AL603888; CAI21705.1; JOINED; Genomic_DNA. DR EMBL; AL645480; CAI21705.1; JOINED; Genomic_DNA. DR EMBL; AL358075; CAI21706.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL603888; CAI21706.1; JOINED; Genomic_DNA. DR EMBL; AL645480; CAI21706.1; JOINED; Genomic_DNA. DR EMBL; BC015816; AAH15816.2; ALT_INIT; mRNA. DR EMBL; BC065499; AAH65499.1; -; mRNA. DR EMBL; AB018350; BAA34527.2; -; mRNA. DR EMBL; AL833919; CAD38775.1; -; mRNA. DR CCDS; CCDS41326.1; -. [Q6P0Q8-1] DR RefSeq; NP_001306174.1; NM_001319245.1. DR RefSeq; NP_055927.2; NM_015112.2. [Q6P0Q8-1] DR PDB; 2KQF; NMR; -; A=1099-1193. DR PDB; 2KYL; NMR; -; A=1099-1193. DR PDBsum; 2KQF; -. DR PDBsum; 2KYL; -. DR AlphaFoldDB; Q6P0Q8; -. DR BMRB; Q6P0Q8; -. DR SMR; Q6P0Q8; -. DR BioGRID; 116756; 54. DR ELM; Q6P0Q8; -. DR IntAct; Q6P0Q8; 27. DR MINT; Q6P0Q8; -. DR STRING; 9606.ENSP00000354671; -. DR ChEMBL; CHEMBL2417355; -. DR iPTMnet; Q6P0Q8; -. DR PhosphoSitePlus; Q6P0Q8; -. DR BioMuta; MAST2; -. DR DMDM; 62287152; -. DR CPTAC; non-CPTAC-5658; -. DR CPTAC; non-CPTAC-5659; -. DR EPD; Q6P0Q8; -. DR jPOST; Q6P0Q8; -. DR MassIVE; Q6P0Q8; -. DR MaxQB; Q6P0Q8; -. DR PaxDb; 9606-ENSP00000354671; -. DR PeptideAtlas; Q6P0Q8; -. DR ProteomicsDB; 66816; -. [Q6P0Q8-1] DR ProteomicsDB; 66817; -. [Q6P0Q8-2] DR Pumba; Q6P0Q8; -. DR Antibodypedia; 32722; 203 antibodies from 20 providers. DR DNASU; 23139; -. DR Ensembl; ENST00000361297.7; ENSP00000354671.2; ENSG00000086015.23. [Q6P0Q8-1] DR GeneID; 23139; -. DR KEGG; hsa:23139; -. DR MANE-Select; ENST00000361297.7; ENSP00000354671.2; NM_015112.3; NP_055927.2. DR UCSC; uc001cov.3; human. [Q6P0Q8-1] DR AGR; HGNC:19035; -. DR CTD; 23139; -. DR DisGeNET; 23139; -. DR GeneCards; MAST2; -. DR HGNC; HGNC:19035; MAST2. DR HPA; ENSG00000086015; Tissue enhanced (skeletal). DR MIM; 612257; gene. DR neXtProt; NX_Q6P0Q8; -. DR OpenTargets; ENSG00000086015; -. DR PharmGKB; PA134954073; -. DR VEuPathDB; HostDB:ENSG00000086015; -. DR eggNOG; KOG0606; Eukaryota. DR GeneTree; ENSGT00940000155705; -. DR HOGENOM; CLU_000288_9_2_1; -. DR InParanoid; Q6P0Q8; -. DR OMA; PHNIPPG; -. DR OrthoDB; 2915765at2759; -. DR PhylomeDB; Q6P0Q8; -. DR TreeFam; TF313149; -. DR PathwayCommons; Q6P0Q8; -. DR SignaLink; Q6P0Q8; -. DR SIGNOR; Q6P0Q8; -. DR BioGRID-ORCS; 23139; 29 hits in 1212 CRISPR screens. DR ChiTaRS; MAST2; human. DR GeneWiki; MAST2; -. DR GenomeRNAi; 23139; -. DR Pharos; Q6P0Q8; Tbio. DR PRO; PR:Q6P0Q8; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q6P0Q8; Protein. DR Bgee; ENSG00000086015; Expressed in gastrocnemius and 205 other cell types or tissues. DR ExpressionAtlas; Q6P0Q8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB. DR GO; GO:0032655; P:regulation of interleukin-12 production; ISS:UniProtKB. DR GO; GO:0048515; P:spermatid differentiation; ISS:UniProtKB. DR CDD; cd00992; PDZ_signaling; 1. DR CDD; cd05609; STKc_MAST; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR037711; MAST. DR InterPro; IPR015022; MAST_pre-PK_dom. DR InterPro; IPR023142; MAST_pre-PK_dom_sf. DR InterPro; IPR001478; PDZ. DR InterPro; IPR041489; PDZ_6. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24356:SF136; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 2; 1. DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF08926; DUF1908; 1. DR Pfam; PF17820; PDZ_6; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q6P0Q8; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; KW Cytoskeleton; Kinase; Magnesium; Membrane; Metal-binding; Methylation; KW Nucleotide-binding; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Ubl conjugation. FT CHAIN 1..1798 FT /note="Microtubule-associated serine/threonine-protein FT kinase 2" FT /id="PRO_0000086312" FT DOMAIN 512..785 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 786..854 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT DOMAIN 1104..1192 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT REGION 1..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 172..257 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 278..305 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 477..508 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 860..892 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 908..927 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 934..1013 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1067..1097 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1195..1725 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1738..1798 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7..24 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 39..54 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 172..188 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..211 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 230..257 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 278..292 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 860..889 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1068..1091 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1217..1231 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1234..1279 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1288..1314 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1346..1361 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1421..1445 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1481..1501 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1589..1604 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1624..1656 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1682..1705 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1774..1798 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 635 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9BXM7, FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027" FT BINDING 518..526 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q9BXM7, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 541 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q9BXM7, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 66 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 74 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 148 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 151 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q60592" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 290 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 874 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 876 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 895 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q60592" FT MOD_RES 900 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1004 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1032 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1256 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1337 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q60592" FT MOD_RES 1364 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1447 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1508 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983" FT VAR_SEQ 327..396 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_051698" FT VAR_SEQ 1091..1113 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_051699" FT VAR_SEQ 1290..1386 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_051700" FT VARIANT 69 FT /note="L -> F (in dbSNP:rs55914403)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040771" FT VARIANT 275 FT /note="K -> E (in an ovarian mucinous carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040772" FT VARIANT 388 FT /note="D -> E (in dbSNP:rs11211247)" FT /evidence="ECO:0000269|PubMed:12117771, FT ECO:0000269|PubMed:17344846" FT /id="VAR_040773" FT VARIANT 655 FT /note="G -> A (in a breast mucinous carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040774" FT VARIANT 659 FT /note="I -> M (in dbSNP:rs1707336)" FT /evidence="ECO:0000269|PubMed:12117771, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:9872452" FT /id="VAR_040775" FT VARIANT 991 FT /note="R -> L (in dbSNP:rs56114653)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040776" FT VARIANT 1197 FT /note="K -> R (in dbSNP:rs1052607)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040777" FT VARIANT 1221 FT /note="D -> E (in dbSNP:rs56060730)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040778" FT VARIANT 1246 FT /note="R -> L (in dbSNP:rs56309943)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040779" FT VARIANT 1304 FT /note="V -> M (in dbSNP:rs33931638)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040780" FT VARIANT 1463 FT /note="A -> T (in dbSNP:rs3737738)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040781" FT VARIANT 1468 FT /note="G -> A (in dbSNP:rs3737737)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040782" FT VARIANT 1551 FT /note="D -> G (in dbSNP:rs1052610)" FT /evidence="ECO:0000269|PubMed:12117771, FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:9872452" FT /id="VAR_040783" FT VARIANT 1608 FT /note="T -> I (in dbSNP:rs35474583)" FT /id="VAR_051645" FT VARIANT 1673 FT /note="K -> R (in dbSNP:rs34070850)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040784" FT VARIANT 1703 FT /note="G -> E" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040785" FT CONFLICT 1225 FT /note="Missing (in Ref. 3; AAH65499)" FT /evidence="ECO:0000305" FT STRAND 1104..1108 FT /evidence="ECO:0007829|PDB:2KQF" FT STRAND 1116..1124 FT /evidence="ECO:0007829|PDB:2KQF" FT STRAND 1126..1129 FT /evidence="ECO:0007829|PDB:2KQF" FT STRAND 1131..1140 FT /evidence="ECO:0007829|PDB:2KQF" FT STRAND 1142..1145 FT /evidence="ECO:0007829|PDB:2KQF" FT HELIX 1146..1149 FT /evidence="ECO:0007829|PDB:2KQF" FT STRAND 1156..1164 FT /evidence="ECO:0007829|PDB:2KQF" FT HELIX 1170..1180 FT /evidence="ECO:0007829|PDB:2KQF" FT STRAND 1182..1188 FT /evidence="ECO:0007829|PDB:2KQF" SQ SEQUENCE 1798 AA; 196436 MW; DF5C92078A3451AF CRC64; MKRSRCRDRP QPPPPDRRED GVQRAAELSQ SLPPRRRAPP GRQRLEERTG PAGPEGKEQD VVTGVSPLLF RKLSNPDIFS STGKVKLQRQ LSQDDCKLWR GNLASSLSGK QLLPLSSSVH SSVGQVTWQS SGEASNLVRM RNQSLGQSAP SLTAGLKELS LPRRGSFCRT SNRKSLIVTS STSPTLPRPH SPLHGHTGNS PLDSPRNFSP NAPAHFSFVP ARRTDGRRWS LASLPSSGYG TNTPSSTVSS SCSSQEKLHQ LPFQPTADEL HFLTKHFSTE SVPDEEGRQS PAMRPRSRSL SPGRSPVSFD SEIIMMNHVY KERFPKATAQ MEERLAEFIS SNTPDSVLPL ADGALSFIHH QVIEMARDCL DKSRSGLITS QYFYELQDNL EKLLQDAHER SESSEVAFVM QLVKKLMIII ARPARLLECL EFDPEEFYHL LEAAEGHAKE GQGIKCDIPR YIVSQLGLTR DPLEEMAQLS SCDSPDTPET DDSIEGHGAS LPSKKTPSEE DFETIKLISN GAYGAVFLVR HKSTRQRFAM KKINKQNLIL RNQIQQAFVE RDILTFAENP FVVSMFCSFD TKRHLCMVME YVEGGDCATL LKNIGALPVD MVRLYFAETV LALEYLHNYG IVHRDLKPDN LLITSMGHIK LTDFGLSKIG LMSLTTNLYE GHIEKDAREF LDKQVCGTPE YIAPEVILRQ GYGKPVDWWA MGIILYEFLV GCVPFFGDTP EELFGQVISD EIVWPEGDEA LPPDAQDLTS KLLHQNPLER LGTGSAYEVK QHPFFTGLDW TGLLRQKAEF IPQLESEDDT SYFDTRSERY HHMDSEDEEE VSEDGCLEIR QFSSCSPRFN KVYSSMERLS LLEERRTPPP TKRSLSEEKE DHSDGLAGLK GRDRSWVIGS PEILRKRLSV SESSHTESDS SPPMTVRRRC SGLLDAPRFP EGPEEASSTL RRQPQEGIWV LTPPSGEGVS GPVTEHSGEQ RPKLDEEAVG RSSGSSPAME TRGRGTSQLA EGATAKAISD LAVRRARHRL LSGDSTEKRT ARPVNKVIKS ASATALSLLI PSEHHTCSPL ASPMSPHSQS SNPSSRDSSP SRDFLPALGS MRPPIIIHRA GKKYGFTLRA IRVYMGDSDV YTVHHMVWHV EDGGPASEAG LRQGDLITHV NGEPVHGLVH TEVVELILKS GNKVAISTTP LENTSIKVGP ARKGSYKAKM ARRSKRSRGK DGQESRKRSS LFRKITKQAS LLHTSRSLSS LNRSLSSGES GPGSPTHSHS LSPRSPTQGY RVTPDAVHSV GGNSSQSSSP SSSVPSSPAG SGHTRPSSLH GLAPKLQRQY RSPRRKSAGS IPLSPLAHTP SPPPPTASPQ RSPSPLSGHV AQAFPTKLHL SPPLGRQLSR PKSAEPPRSP LLKRVQSAEK LAAALAASEK KLATSRKHSL DLPHSELKKE LPPREVSPLE VVGARSVLSG KGALPGKGVL QPAPSRALGT LRQDRAERRE SLQKQEAIRE VDSSEDDTEE GPENSQGAQE LSLAPHPEVS QSVAPKGAGE SGEEDPFPSR DPRSLGPMVP SLLTGITLGP PRMESPSGPH RRLGSPQAIE EAASSSSAGP NLGQSGATDP IPPEGCWKAQ HLHTQALTAL SPSTSGLTPT SSCSPPSSTS GKLSMWSWKS LIEGPDRASP SRKATMAGGL ANLQDLENTT PAQPKNLSPR EQGKTQPPSA PRLAHPSYED PSQGWLWESE CAQAVKEDPA LSITQVPDAS GDRRQDVPCR GCPLTQKSEP SLRRGQEPGG HQKHRDLALV PDELLKQT //