KCC2B_BOVIN
ID KCC2B_BOVIN Reviewed; 542 AA.
AC Q3MHJ9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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. Participates in the modulation of
CC skeletal muscle function in response to exercise. In slow-twitch
CC muscles, is involved in regulation of sarcoplasmic reticulum (SR)
CC Ca(2+) transport and in fast-twitch muscle participates in the control
CC of Ca(2+) release from the SR through phosphorylation of triadin, a
CC ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an
CC endogenous inhibitor of SERCA2A/ATP2A2. {ECO:0000250|UniProtKB:Q13554}.
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 (By similarity). {ECO:0000250}.
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. Interacts with FOXO3.
CC Interacts (when in a kinase inactive state not associated with
CC calmodulin) with ARC; leading to target ARC to inactive synapses.
CC Interacts with CAMK2N1; this interaction requires CAMK2B activation by
CC Ca(2+) (By similarity). {ECO:0000250|UniProtKB:P08413,
CC ECO:0000250|UniProtKB:Q13554}.
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 (By similarity). {ECO:0000250}.
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; BC105210; AAI05211.1; -; mRNA.
DR RefSeq; NP_001030434.1; NM_001035357.2.
DR AlphaFoldDB; Q3MHJ9; -.
DR SMR; Q3MHJ9; -.
DR STRING; 9913.ENSBTAP00000016813; -.
DR PaxDb; Q3MHJ9; -.
DR PeptideAtlas; Q3MHJ9; -.
DR PRIDE; Q3MHJ9; -.
DR Ensembl; ENSBTAT00000072316; ENSBTAP00000061316; ENSBTAG00000012653.
DR GeneID; 525416; -.
DR KEGG; bta:525416; -.
DR CTD; 816; -.
DR VEuPathDB; HostDB:ENSBTAG00000012653; -.
DR VGNC; VGNC:26722; CAMK2B.
DR eggNOG; KOG0033; Eukaryota.
DR GeneTree; ENSGT00940000158973; -.
DR HOGENOM; CLU_000288_71_0_1; -.
DR InParanoid; Q3MHJ9; -.
DR OMA; CIAYTRL; -.
DR OrthoDB; 330091at2759; -.
DR TreeFam; TF315229; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000012653; Expressed in Ammon's horn and 74 other tissues.
DR ExpressionAtlas; Q3MHJ9; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton; Differentiation;
KW Kinase; Membrane; Neurogenesis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum;
KW Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..542
FT /note="Calcium/calmodulin-dependent protein kinase type II
FT subunit beta"
FT /id="PRO_0000260268"
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..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..368
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:0000250|UniProtKB:P28652"
FT MOD_RES 287
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13554"
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 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28652"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08413"
FT MOD_RES 400
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28652"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13554"
SQ SEQUENCE 542 AA; 60482 MW; 29C877521DEC4FD1 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 IMAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL
KGAILTTMLA TRNFSVGRQT TAPATMSTAA SGATMGLVEQ AKSLLNKKAD GVKPQTNSTK
NSAAATSPKG TLPPAALEPQ TTVIHNPVDG IKESSDSTHT TIEDEDTKAR KQEIIKITEQ
LIEAVNNGDF EAYAKICDPG LTSFEPEALG NLVEGMDFHR FYFENLLAKN SKPIHTTILN
PHVHVIGEDA ACIAYIRLTQ YIDGQGRPRT SQSEETRVWH RRDGKWQNVH FHCSGAPVAP
LQ
