ID   Q5SVI9_MOUSE            Unreviewed;       479 AA.
AC   Q5SVI9;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   19-JAN-2022, entry version 140.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase {ECO:0000256|ARBA:ARBA00012434};
DE            EC=2.7.11.17 {ECO:0000256|ARBA:ARBA00012434};
GN   Name=Camk2b {ECO:0000313|Ensembl:ENSMUSP00000065101,
GN   ECO:0000313|MGI:MGI:88257};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000065101, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:16452087}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [2] {ECO:0007829|PubMed:17114649}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3] {ECO:0007829|PubMed:18034455}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000065101, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000065101,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6] {ECO:0000313|Ensembl:ENSMUSP00000065101}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000065101};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
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=2.7.11.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000902};
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=2.7.11.17; Evidence={ECO:0000256|ARBA:ARBA00000517};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. CaMK subfamily. {ECO:0000256|ARBA:ARBA00005354}.
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DR   SMR; Q5SVI9; -.
DR   SwissPalm; Q5SVI9; -.
DR   jPOST; Q5SVI9; -.
DR   MaxQB; Q5SVI9; -.
DR   PeptideAtlas; Q5SVI9; -.
DR   ProteomicsDB; 321006; -.
DR   Antibodypedia; 3482; 545 antibodies from 38 providers.
DR   Ensembl; ENSMUST00000066431; ENSMUSP00000065101; ENSMUSG00000057897.
DR   MGI; MGI:88257; Camk2b.
DR   VEuPathDB; HostDB:ENSMUSG00000057897; -.
DR   GeneTree; ENSGT00940000158973; -.
DR   HOGENOM; CLU_000288_71_3_1; -.
DR   ChiTaRS; Camk2b; mouse.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000057897; Expressed in dentate gyrus of hippocampal formation and 236 other tissues.
DR   ExpressionAtlas; Q5SVI9; baseline and differential.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:RHEA.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54427; SSF54427; 1.
DR   SUPFAM; SSF56112; SSF56112; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Kinase {ECO:0000256|RuleBase:RU000304};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Proteomics identification {ECO:0007829|MaxQB:Q5SVI9,
KW   ECO:0007829|PeptideAtlas:Q5SVI9};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|RuleBase:RU000304}.
FT   DOMAIN          14..272
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         43
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   479 AA;  54104 MW;  12F45B7A66AA83AD CRC64;
     MATTVTCTRF TDEYQLYEDI GKGAFSVVRR CVKLCTGHEY AAKIINTKKL SARDHQKLER
     EARICRLLKH SNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI
     LEAVLHCHQM GVVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY
     LSPEVLRKEA YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT
     VTPEAKNLIN QMLTINPAKR ITAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL
     KGAILTTMLA TRNFSAAKSL LNKKADGVKE SSDSTNTTIE DEDAKARKQE IIKTTEQLIE
     AVNNGDFEAY AKICDPGLTS FEPEALGNLV EGMDFHRFYF ENLLAKNSKP IHTTILNPHV
     HVIGEDAACI AYIRLTQYID GQGRPRTSQS EETRVWHRRD GKWQNVHFHC SGAPVAPLQ
//