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Database: UniProt
Entry: Q6P0Q8
LinkDB: Q6P0Q8
Original site: Q6P0Q8 
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   12-AUG-2020, entry version 159.
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};
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   SMR; Q6P0Q8; -.
DR   BioGRID; 116756; 26.
DR   ELM; Q6P0Q8; -.
DR   IntAct; Q6P0Q8; 20.
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; 156 antibodies.
DR   Ensembl; ENST00000361297; ENSP00000354671; ENSG00000086015. [Q6P0Q8-1]
DR   GeneID; 23139; -.
DR   KEGG; hsa:23139; -.
DR   UCSC; uc001cov.3; human. [Q6P0Q8-1]
DR   CTD; 23139; -.
DR   DisGeNET; 23139; -.
DR   EuPathDB; HostDB:ENSG00000086015.20; -.
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   eggNOG; KOG0606; Eukaryota.
DR   GeneTree; ENSGT00940000155705; -.
DR   HOGENOM; CLU_000288_9_2_1; -.
DR   InParanoid; Q6P0Q8; -.
DR   KO; K08789; -.
DR   OMA; EGFMPAI; -.
DR   OrthoDB; 323328at2759; -.
DR   PhylomeDB; Q6P0Q8; -.
DR   TreeFam; TF313149; -.
DR   PathwayCommons; Q6P0Q8; -.
DR   SignaLink; Q6P0Q8; -.
DR   SIGNOR; Q6P0Q8; -.
DR   BioGRID-ORCS; 23139; 12 hits in 911 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 247 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: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:0045075; P:regulation of interleukin-12 biosynthetic process; 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; Polymorphism; 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   DOMAIN          1104..1192
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   NP_BIND         518..526
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
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         541
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         74
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|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:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         874
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         876
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1004
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000244|PubMed:24129315"
FT   MOD_RES         1032
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|PubMed:23186163"
FT   MOD_RES         1447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         1508
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|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:0000244|PDB:2KQF"
FT   STRAND          1116..1124
FT                   /evidence="ECO:0000244|PDB:2KQF"
FT   STRAND          1126..1129
FT                   /evidence="ECO:0000244|PDB:2KQF"
FT   STRAND          1131..1140
FT                   /evidence="ECO:0000244|PDB:2KQF"
FT   STRAND          1142..1145
FT                   /evidence="ECO:0000244|PDB:2KQF"
FT   HELIX           1146..1149
FT                   /evidence="ECO:0000244|PDB:2KQF"
FT   STRAND          1156..1164
FT                   /evidence="ECO:0000244|PDB:2KQF"
FT   HELIX           1170..1180
FT                   /evidence="ECO:0000244|PDB:2KQF"
FT   STRAND          1182..1188
FT                   /evidence="ECO:0000244|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
//
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