ID Q5SVI9_MOUSE Unreviewed; 479 AA. AC Q5SVI9; DT 21-DEC-2004, integrated into UniProtKB/TrEMBL. DT 21-DEC-2004, sequence version 1. DT 09-DEC-2015, entry version 108. DE SubName: Full=Calcium/calmodulin-dependent protein kinase type II subunit beta {ECO:0000313|Ensembl:ENSMUSP00000065101}; GN Name=Camk2b {ECO:0000313|Ensembl:ENSMUSP00000065101, GN ECO:0000313|MGI:MGI:88257}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000065101, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000213|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., RA 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:0000213|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., RA Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in RT naive and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [3] {ECO:0000213|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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] {ECO:0000213|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 RT 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 -!- SIMILARITY: Contains protein kinase domain. CC {ECO:0000256|SAAS:SAAS00348683}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMUSP00000065101}. 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; AL611926; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL645469; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; Q5SVI9; -. DR SMR; Q5SVI9; 8-474. DR PRIDE; Q5SVI9; -. DR Ensembl; ENSMUST00000066431; ENSMUSP00000065101; ENSMUSG00000057897. DR MGI; MGI:88257; Camk2b. DR GeneTree; ENSGT00760000118944; -. DR HOGENOM; HOG000233016; -. DR HOVERGEN; HBG108055; -. DR ChiTaRS; Camk2b; mouse. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; Q5SVI9; -. DR ExpressionAtlas; Q5SVI9; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0097481; C:neuronal postsynaptic density; IDA:MGI. DR GO; GO:0051233; C:spindle midzone; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI. DR GO; GO:0060466; P:activation of meiosis involved in egg activation; IMP:MGI. DR GO; GO:0006816; P:calcium ion transport; IMP:MGI. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI. DR GO; GO:0002030; P:inhibitory G-protein coupled receptor phosphorylation; IDA:MGI. DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:MGI. DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI. DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI. DR GO; GO:0046777; P:protein autophosphorylation; IMP:MGI. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI. DR GO; GO:0032222; P:regulation of synaptic transmission, cholinergic; IMP:MGI. DR GO; GO:0046686; P:response to cadmium ion; IDA:MGI. DR InterPro; IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase. DR InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24347; PTHR24347; 1. DR Pfam; PF08332; CaMKII_AD; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 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|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00315823}; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Kinase {ECO:0000256|SAAS:SAAS00315850}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00315860}; KW Proteomics identification {ECO:0000213|MaxQB:Q5SVI9, KW ECO:0000213|PeptideAtlas:Q5SVI9}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00315853}; KW Transferase {ECO:0000256|SAAS:SAAS00315858}. FT DOMAIN 14 272 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. 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 //