ID KCC2B_MOUSE Reviewed; 542 AA. AC P28652; Q5SVH9; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 27-MAR-2024, entry version 217. DE RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit beta; DE Short=CaM kinase II subunit beta; DE Short=CaMK-II subunit beta; DE EC=2.7.11.17 {ECO:0000250|UniProtKB:Q13554}; GN Name=Camk2b; Synonyms=Camk2d; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=1321343; DOI=10.1128/mcb.12.8.3644-3652.1992; RA Karls U., Mueller U., Gilbert D.J., Copeland N.G., Jenkins N.A., RA Harbers K.; RT "Structure, expression, and chromosome location of the gene for the beta RT subunit of brain-specific Ca2+/calmodulin-dependent protein kinase II RT identified by transgene integration in an embryonic lethal mouse mutant."; RL Mol. Cell. Biol. 12:3644-3652(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; 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 [4] RP PROTEIN SEQUENCE OF 136-147, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371; SER-394; THR-400 AND RP THR-401, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; 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 [9] RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ALA-303. RX PubMed=21752990; DOI=10.1523/jneurosci.5105-10.2011; RA Borgesius N.Z., van Woerden G.M., Buitendijk G.H., Keijzer N., Jaarsma D., RA Hoogenraad C.C., Elgersma Y.; RT "{beta}CaMKII plays a nonenzymatic role in hippocampal synaptic plasticity RT and learning by targeting {alpha}CaMKII to synapses."; RL J. Neurosci. 31:10141-10148(2011). RN [10] RP INTERACTION WITH FOXO3. RX PubMed=23805378; DOI=10.7554/elife.00518; RA Tao L., Xie Q., Ding Y.H., Li S.T., Peng S., Zhang Y.P., Tan D., Yuan Z., RA Dong M.Q.; RT "CAMKII and Calcineurin regulate the lifespan of Caenorhabditis elegans RT through the FOXO transcription factor DAF-16."; RL Elife 2:E00518-E00518(2013). RN [11] RP FUNCTION. RX PubMed=29100089; DOI=10.1016/j.ajhg.2017.10.003; RG Undiagnosed Diseases Network; RG GEM HUGO; RG Deciphering Developmental Disorders Study; RA Kuery S., van Woerden G.M., Besnard T., Proietti Onori M., Latypova X., RA Towne M.C., Cho M.T., Prescott T.E., Ploeg M.A., Sanders S., RA Stessman H.A.F., Pujol A., Distel B., Robak L.A., Bernstein J.A., RA Denomme-Pichon A.S., Lesca G., Sellars E.A., Berg J., Carre W., Busk O.L., RA van Bon B.W.M., Waugh J.L., Deardorff M., Hoganson G.E., Bosanko K.B., RA Johnson D.S., Dabir T., Holla O.L., Sarkar A., Tveten K., de Bellescize J., RA Braathen G.J., Terhal P.A., Grange D.K., van Haeringen A., Lam C., RA Mirzaa G., Burton J., Bhoj E.J., Douglas J., Santani A.B., Nesbitt A.I., RA Helbig K.L., Andrews M.V., Begtrup A., Tang S., van Gassen K.L.I., RA Juusola J., Foss K., Enns G.M., Moog U., Hinderhofer K., Paramasivam N., RA Lincoln S., Kusako B.H., Lindenbaum P., Charpentier E., Nowak C.B., RA Cherot E., Simonet T., Ruivenkamp C.A.L., Hahn S., Brownstein C.A., Xia F., RA Schmitt S., Deb W., Bonneau D., Nizon M., Quinquis D., Chelly J., RA Rudolf G., Sanlaville D., Parent P., Gilbert-Dussardier B., Toutain A., RA Sutton V.R., Thies J., Peart-Vissers L.E.L.M., Boisseau P., Vincent M., RA Grabrucker A.M., Dubourg C., Tan W.H., Verbeek N.E., Granzow M., RA Santen G.W.E., Shendure J., Isidor B., Pasquier L., Redon R., Yang Y., RA State M.W., Kleefstra T., Cogne B., Petrovski S., Retterer K., RA Eichler E.E., Rosenfeld J.A., Agrawal P.B., Bezieau S., Odent S., RA Elgersma Y., Mercier S.; RT "De Novo Mutations in Protein Kinase Genes CAMK2A and CAMK2B Cause RT Intellectual Disability."; RL Am. J. Hum. Genet. 101:768-788(2017). CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that functions CC autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, CC and is involved in dendritic spine and synapse formation, neuronal CC plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in CC skeletal muscle. In neurons, plays an essential structural role in the CC reorganization of the actin cytoskeleton during plasticity by binding CC and bundling actin filaments in a kinase-independent manner. This CC structural function is required for correct targeting of CaMK2A, which CC acts downstream of NMDAR to promote dendritic spine and synapse CC formation and maintain synaptic plasticity which enables long-term CC potentiation (LTP) and hippocampus-dependent learning. In developing CC hippocampal neurons, promotes arborization of the dendritic tree and in CC mature neurons, promotes dendritic remodeling. Also regulates the CC migration of developing neurons (PubMed:29100089). Participates in the CC modulation of skeletal muscle function in response to exercise. In CC slow-twitch muscles, is involved in regulation of sarcoplasmic CC reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates CC in the control of Ca(2+) release from the SR through phosphorylation of CC triadin, a ryanodine receptor-coupling factor, and phospholamban CC (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2 (PubMed:21752990). CC In response to interferon-gamma (IFN-gamma) stimulation, catalyzes CC phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway CC (By similarity). Phosphorylates reticulophagy regulator RETREG1 at CC 'Thr-134' under endoplasmic reticulum stress conditions which enhances CC RETREG1 oligomerization and its membrane scission and reticulophagy CC activity (By similarity). {ECO:0000250|UniProtKB:P08413, CC ECO:0000250|UniProtKB:Q13554, ECO:0000269|PubMed:21752990, CC ECO:0000269|PubMed:29100089}. 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 -!- 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; CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of CC calmodulin results in conformational change that relieves intrasteric CC autoinhibition and allows autophosphorylation of Thr-287 which turns CC the kinase in a constitutively active form and confers to the kinase a CC Ca(2+)-independent activity. CC -!- SUBUNIT: CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta CC (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms CC assemble into homo- or heteromultimeric holoenzymes composed of 12 CC subunits with two hexameric rings stacked one on top of the other. CC Interacts with SYNGAP1, CAMK2N2 and MPDZ (By similarity). Interacts CC with FOXO3 (PubMed:23805378). Interacts (when in a kinase inactive CC state not associated with calmodulin) with ARC; leading to target ARC CC to inactive synapses (By similarity). Interacts with CAMK2N1; this CC interaction requires CAMK2B activation by Ca(2+) (By similarity). CC {ECO:0000250|UniProtKB:P08413, ECO:0000250|UniProtKB:Q13554, CC ECO:0000269|PubMed:23805378}. CC -!- INTERACTION: CC P28652; Q9WV31: Arc; NbExp=2; IntAct=EBI-397029, EBI-397779; CC P28652; P11716: RYR1; Xeno; NbExp=4; IntAct=EBI-397029, EBI-6477441; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome. Sarcoplasmic reticulum CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; CC Cytoplasmic side {ECO:0000250}. Synapse {ECO:0000250|UniProtKB:P08413}. CC -!- DOMAIN: The CAMK2 protein kinases contain a unique C-terminal subunit CC association domain responsible for oligomerization. CC -!- PTM: Autophosphorylation of Thr-287 following activation by CC Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an CC activated state. CC -!- DISRUPTION PHENOTYPE: Impaired long-term potentiation (LTP) and CC hippocampus-dependent learning. {ECO:0000269|PubMed:21752990}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. CaMK subfamily. {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; X63615; CAA45160.1; -; mRNA. DR EMBL; AK163698; BAE37464.1; -; mRNA. DR EMBL; AL611926; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL645469; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS24411.1; -. DR PIR; A45025; A45025. DR RefSeq; NP_031621.3; NM_007595.5. DR AlphaFoldDB; P28652; -. DR SMR; P28652; -. DR BioGRID; 198462; 32. DR DIP; DIP-31582N; -. DR IntAct; P28652; 27. DR MINT; P28652; -. DR STRING; 10090.ENSMUSP00000087925; -. DR GlyGen; P28652; 10 sites, 1 O-linked glycan (10 sites). DR iPTMnet; P28652; -. DR PhosphoSitePlus; P28652; -. DR SwissPalm; P28652; -. DR EPD; P28652; -. DR MaxQB; P28652; -. DR PaxDb; 10090-ENSMUSP00000105438; -. DR PeptideAtlas; P28652; -. DR ProteomicsDB; 263487; -. DR Antibodypedia; 3482; 622 antibodies from 38 providers. DR DNASU; 12323; -. DR Ensembl; ENSMUST00000109813.9; ENSMUSP00000105438.3; ENSMUSG00000057897.15. DR Ensembl; ENSMUST00000109815.9; ENSMUSP00000105440.3; ENSMUSG00000057897.15. DR GeneID; 12323; -. DR KEGG; mmu:12323; -. DR UCSC; uc007hxr.2; mouse. DR AGR; MGI:88257; -. DR CTD; 816; -. DR MGI; MGI:88257; Camk2b. DR VEuPathDB; HostDB:ENSMUSG00000057897; -. DR eggNOG; KOG0033; Eukaryota. DR GeneTree; ENSGT00940000158973; -. DR InParanoid; P28652; -. DR OrthoDB; 1121238at2759; -. DR TreeFam; TF315229; -. DR BRENDA; 2.7.11.17; 3474. DR Reactome; R-MMU-3371571; HSF1-dependent transactivation. DR Reactome; R-MMU-399719; Trafficking of AMPA receptors. DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation. DR Reactome; R-MMU-5578775; Ion homeostasis. DR Reactome; R-MMU-5673000; RAF activation. DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade. DR Reactome; R-MMU-877300; Interferon gamma signaling. DR Reactome; R-MMU-936837; Ion transport by P-type ATPases. DR BioGRID-ORCS; 12323; 1 hit in 80 CRISPR screens. DR ChiTaRS; Camk2b; mouse. DR PRO; PR:P28652; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P28652; Protein. DR Bgee; ENSMUSG00000057897; Expressed in dentate gyrus of hippocampal formation granule cell and 198 other cell types or tissues. DR ExpressionAtlas; P28652; baseline and differential. DR GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; ISO:MGI. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0043204; C:perikaryon; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; IDA:MGI. DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051233; C:spindle midzone; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central. DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0043274; F:phospholipase binding; ISO:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI. DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; ISO:MGI. DR GO; GO:0060466; P:activation of meiosis involved in egg activation; IMP:MGI. DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI. DR GO; GO:0006816; P:calcium ion transport; IMP:MGI. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0048858; P:cell projection morphogenesis; ISO:MGI. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI. DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:MGI. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI. DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB. DR GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI. DR GO; GO:2001222; P:regulation of neuron migration; IMP:UniProtKB. DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI. DR GO; GO:0090128; P:regulation of synapse maturation; ISO: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 CDD; cd14086; STKc_CaMKII; 1. DR Gene3D; 3.10.450.50; -; 1. DR Gene3D; 6.10.140.620; -; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24347:SF403; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT BETA; 1. DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF08332; CaMKII_AD; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF54427; NTF2-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P28652; MM. PE 1: Evidence at protein level; KW ATP-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton; Differentiation; KW Direct protein sequencing; Kinase; Membrane; Neurogenesis; KW Nucleotide-binding; Phosphoprotein; Reference proteome; KW Sarcoplasmic reticulum; Serine/threonine-protein kinase; Synapse; KW Transferase. FT CHAIN 1..542 FT /note="Calcium/calmodulin-dependent protein kinase type II FT subunit beta" FT /id="PRO_0000086097" FT DOMAIN 14..272 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 283..292 FT /note="Autoinhibitory domain" FT /evidence="ECO:0000250" FT REGION 291..301 FT /note="Calmodulin-binding" FT REGION 349..376 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 350..369 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 136 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 20..28 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 17 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455" FT MOD_RES 287 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0007744|PubMed:16452087" FT MOD_RES 306 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 307 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 367 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08413" FT MOD_RES 371 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 394 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 397 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08413" FT MOD_RES 400 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 401 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MUTAGEN 303 FT /note="A->R: Blocks calcium/calmodulin binding." FT /evidence="ECO:0000269|PubMed:21752990" FT CONFLICT 19 FT /note="D -> E (in Ref. 1; CAA45160)" FT /evidence="ECO:0000305" SQ SEQUENCE 542 AA; 60461 MW; 8A7962A6495FD0D0 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 TRNFSVGRQT TAPATMSTAA SGTTMGLVEQ AKSLLNKKAD GVKPQTNSTK NSSAITSPKG SLPPAALEPQ TTVIHNPVDG IKESSDSTNT TIEDEDAKAR KQEIIKTTEQ LIEAVNNGDF EAYAKICDPG LTSFEPEALG NLVEGMDFHR FYFENLLAKN SKPIHTTILN PHVHVIGEDA ACIAYIRLTQ YIDGQGRPRT SQSEETRVWH RRDGKWQNVH FHCSGAPVAP LQ //