MAST2_HUMAN
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 03-AUG-2022, entry version 168.
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},
GN MAST205 {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
RC Placenta {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; 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};
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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; 44.
DR ELM; Q6P0Q8; -.
DR IntAct; Q6P0Q8; 22.
DR MINT; Q6P0Q8; -.
DR STRING; 9606.ENSP00000354671; -.
DR ChEMBL; CHEMBL2417355; -.
DR iPTMnet; Q6P0Q8; -.
DR PhosphoSitePlus; Q6P0Q8; -.
DR BioMuta; MAST2; -.
DR DMDM; 62287152; -.
DR EPD; Q6P0Q8; -.
DR jPOST; Q6P0Q8; -.
DR MassIVE; Q6P0Q8; -.
DR MaxQB; Q6P0Q8; -.
DR PaxDb; Q6P0Q8; -.
DR PeptideAtlas; Q6P0Q8; -.
DR PRIDE; Q6P0Q8; -.
DR ProteomicsDB; 66816; -. [Q6P0Q8-1]
DR ProteomicsDB; 66817; -. [Q6P0Q8-2]
DR Antibodypedia; 32722; 176 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 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; SVSEGFM; -.
DR OrthoDB; 323328at2759; -.
DR PhylomeDB; Q6P0Q8; -.
DR TreeFam; TF313149; -.
DR PathwayCommons; Q6P0Q8; -.
DR SignaLink; Q6P0Q8; -.
DR SIGNOR; Q6P0Q8; -.
DR BioGRID-ORCS; 23139; 25 hits in 1134 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 203 other tissues.
DR ExpressionAtlas; Q6P0Q8; baseline and differential.
DR Genevisible; Q6P0Q8; HS.
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:0018105; P:peptidyl-serine phosphorylation; 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; cd05609; STKc_MAST; 1.
DR Gene3D; 1.20.1480.20; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015022; MA_Ser/Thr_Kinase_dom.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR028779; MAST2.
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; PTHR24356:SF136; 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; SSF140482; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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
