KCC2B_MOUSE
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 03-AUG-2022, entry version 208.
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;
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 {ECO:0000269|PubMed:21752990, 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}.
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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; 30.
DR DIP; DIP-31582N; -.
DR IntAct; P28652; 27.
DR MINT; P28652; -.
DR STRING; 10090.ENSMUSP00000105438; -.
DR iPTMnet; P28652; -.
DR PhosphoSitePlus; P28652; -.
DR SwissPalm; P28652; -.
DR EPD; P28652; -.
DR MaxQB; P28652; -.
DR PeptideAtlas; P28652; -.
DR PRIDE; P28652; -.
DR ProteomicsDB; 263487; -.
DR Antibodypedia; 3482; 557 antibodies from 38 providers.
DR DNASU; 12323; -.
DR Ensembl; ENSMUST00000109813; ENSMUSP00000105438; ENSMUSG00000057897.
DR Ensembl; ENSMUST00000109815; ENSMUSP00000105440; ENSMUSG00000057897.
DR GeneID; 12323; -.
DR KEGG; mmu:12323; -.
DR UCSC; uc007hxr.2; mouse.
DR CTD; 816; -.
DR MGI; MGI:88257; Camk2b.
DR VEuPathDB; HostDB:ENSMUSG00000057897; -.
DR eggNOG; KOG0033; Eukaryota.
DR GeneTree; ENSGT00940000158973; -.
DR InParanoid; P28652; -.
DR OrthoDB; 330091at2759; -.
DR TreeFam; TF315229; -.
DR BRENDA; 2.7.11.17; 3474.
DR Reactome; R-MMU-3371571; HSF1-dependent transactivation.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
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 75 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 197 other tissues.
DR ExpressionAtlas; P28652; baseline and differential.
DR Genevisible; P28652; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; ISO:MGI.
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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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: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:0002030; P:inhibitory G protein-coupled receptor phosphorylation; IDA: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:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
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:0032430; P:positive regulation of phospholipase A2 activity; ISO:MGI.
DR GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
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: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:0032222; P:regulation of synaptic transmission, cholinergic; IMP:MGI.
DR GO; GO:0046686; P:response to cadmium ion; IDA:MGI.
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; 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
