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Calcium/calmodulin-dependent protein kinase type II subunit beta (CaM kinase II subunit beta) (CaMK-II subunit beta) (EC 2.7.11.17)

 KCC2B_HUMAN             Reviewed;         666 AA.
Q13554; A4D2K0; A4D2K1; A4D2K2; A4D2K3; A4D2K4; A4D2K5; A4D2K6;
O95437; O95438; O95599; Q9UGH7; Q9UGH8; Q9UGH9; Q9UNX0; Q9UNX7;
Q9UP00; Q9Y5N4; Q9Y6F4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
31-MAY-2011, sequence version 3.
30-AUG-2017, entry version 181.
RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit beta;
Short=CaM kinase II subunit beta;
Short=CaMK-II subunit beta;
EC=2.7.11.17;
Name=CAMK2B; Synonyms=CAM2, CAMK2, CAMKB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 5; 6 AND 7).
TISSUE=Brain;
PubMed=10858498; DOI=10.1016/S0014-5793(00)01634-3;
Wang P., Wu Y., Zhou T.H., Sun Y., Pei G.;
"Identification of alternative splicing variants of the beta subunit
of human Ca(2+)/calmodulin-dependent protein kinase II with different
activities.";
FEBS Lett. 475:107-110(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Skeletal muscle;
Leddy J.J., Salih M., Tuana B.S.;
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5).
TISSUE=Brain;
Li G.Y., Cooper N.G.F.;
"Molecular cloning and sequencing of human calcium/calmodulin
dependent protein kinase II beta subunit.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
TISSUE=Insulinoma;
PubMed=10819240; DOI=10.1007/s001250051330;
Rochlitz H., Voigt A., Lankat-Buttgereit B., Goeke B., Heimberg H.,
Nauck M.A., Schiemann U., Schatz H., Pfeiffer A.F.;
"Cloning and quantitative determination of the human Ca2+/calmodulin-
dependent protein kinase II (CaMK II) isoforms in human beta cells.";
Diabetologia 43:465-473(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 302-605 (ISOFORM 2).
PubMed=9060999; DOI=10.1016/S0167-4889(96)00141-3;
Tombes R.M., Krystal G.W.;
"Identification of novel human tumor cell-specific CaMK-II variants.";
Biochim. Biophys. Acta 1355:281-292(1997).
[9]
ENZYME REGULATION, SUBUNIT, AND AUTOPHOSPHORYLATION.
PubMed=14722083; DOI=10.1074/jbc.M313597200;
Gaertner T.R., Kolodziej S.J., Wang D., Kobayashi R., Koomen J.M.,
Stoops J.K., Waxham M.N.;
"Comparative analyses of the three-dimensional structures and
enzymatic properties of alpha, beta, gamma and delta isoforms of Ca2+-
calmodulin-dependent protein kinase II.";
J. Biol. Chem. 279:12484-12494(2004).
[10]
INTERACTION WITH MPDZ.
PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase
activity and NMDA receptor-dependent synaptic AMPA receptor
potentiation.";
Neuron 43:563-574(2004).
[11]
FUNCTION IN SKELETAL MUSCLE, PHOSPHORYLATION AT THR-287, FUNCTION IN
PHOSPHORYLATION OF PLN, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16690701; DOI=10.1113/jphysiol.2006.111757;
Rose A.J., Kiens B., Richter E.A.;
"Ca2+-calmodulin-dependent protein kinase expression and signalling in
skeletal muscle during exercise.";
J. Physiol. (Lond.) 574:889-903(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[13]
SUBCELLULAR LOCATION.
PubMed=21529938; DOI=10.1016/j.ceca.2011.02.007;
Wayman G.A., Tokumitsu H., Davare M.A., Soderling T.R.;
"Analysis of CaM-kinase signaling in cells.";
Cell Calcium 50:1-8(2011).
[14]
REVIEW ON FUNCTION IN SKELETAL MUSCLE.
PubMed=15294044; DOI=10.1079/PNS2004335;
Chin E.R.;
"The role of calcium and calcium/calmodulin-dependent kinases in
skeletal muscle plasticity and mitochondrial biogenesis.";
Proc. Nutrit. Soc. 63:279-286(2004).
[15]
REVIEW ON FUNCTION IN SKELETAL MUSCLE.
Sacchetto R., Bovo E., Damiani E.;
"The Ca2+-calmodulin dependent protein kinase II system of skeletal
muscle sarcoplasmic reticulum.";
Basic Appl. Myol. 15:5-17(2005).
[16]
REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
PubMed=18817731; DOI=10.1016/j.neuron.2008.08.021;
Wayman G.A., Lee Y.S., Tokumitsu H., Silva A.J., Silva A.,
Soderling T.R.;
"Calmodulin-kinases: modulators of neuronal development and
plasticity.";
Neuron 59:914-931(2008).
[17]
REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
PubMed=19996366; DOI=10.1152/physiol.00029.2009;
Okamoto K., Bosch M., Hayashi Y.;
"The roles of CaMKII and F-actin in the structural plasticity of
dendritic spines: a potential molecular identity of a synaptic tag?";
Physiology (Bethesda) 24:357-366(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 11-303 IN COMPLEX WITH
INHIBITOR.
Structural genomics consortium (SGC);
"Crystal structure of human calcium/calmodulin-dependent protein
kinase IIb isoform 1 (CAMK2B).";
Submitted (DEC-2007) to the PDB data bank.
[20]
VARIANTS [LARGE SCALE ANALYSIS] LEU-489 AND LYS-510.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Calcium/calmodulin-dependent protein kinase that
functions autonomously after Ca(2+)/calmodulin-binding and
autophosphorylation, and is involved in dendritic spine and
synapse formation, neuronal plasticity and regulation of
sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In
neurons, plays an essential structural role in the reorganization
of the actin cytoskeleton during plasticity by binding and
bundling actin filaments in a kinase-independent manner. This
structural function is required for correct targeting of CaMK2A,
which acts downstream of NMDAR to promote dendritic spine and
synapse formation and maintain synaptic plasticity which enables
long-term potentiation (LTP) and hippocampus-dependent learning.
In developing hippocampal neurons, promotes arborization of the
dendritic tree and in mature neurons, promotes dendritic
remodeling. Participates in the modulation of skeletal muscle
function in response to exercise. In slow-twitch muscles, is
involved in regulation of sarcoplasmic reticulum (SR) Ca(2+)
transport and in fast-twitch muscle participates in the control of
Ca(2+) release from the SR through phosphorylation of triadin, a
ryanodine receptor-coupling factor, and phospholamban (PLN/PLB),
an endogenous inhibitor of SERCA2A/ATP2A2.
{ECO:0000269|PubMed:16690701}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of
calmodulin results in conformational change that relieves
intrasteric autoinhibition and allows autophosphorylation of Thr-
287 which turns the kinase in a constitutively active form and
confers to the kinase a Ca(2+)-independent activity.
{ECO:0000269|PubMed:14722083}.
-!- SUBUNIT: CAMK2 is composed of 4 different chains: alpha (CAMK2A),
beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different
isoforms assemble into homo- or heteromultimeric holoenzymes
composed of 12 subunits with two hexameric rings stacked one on
top of the other (PubMed:14722083, Ref.19). Interacts with SYNGAP1
and CAMK2N2 (By similarity). Interacts with MPDZ
(PubMed:15312654). Interacts with FOXO3 (By similarity).
{ECO:0000250|UniProtKB:P08413, ECO:0000250|UniProtKB:Q13554,
ECO:0000269|PubMed:14722083, ECO:0000269|PubMed:15312654,
ECO:0000269|Ref.19}.
-!- INTERACTION:
B3KWQ7:-; NbExp=3; IntAct=EBI-1058722, EBI-10175974;
O00154:ACOT7; NbExp=3; IntAct=EBI-1058722, EBI-948905;
Q2VPB7:AP5B1; NbExp=3; IntAct=EBI-1058722, EBI-5917279;
Q13555-5:CAMK2G; NbExp=4; IntAct=EBI-11523526, EBI-12020154;
Q16543:CDC37; NbExp=4; IntAct=EBI-11523526, EBI-295634;
Q8N0U1:FAM171A2; NbExp=3; IntAct=EBI-1058722, EBI-10264767;
P60412:KRTAP10-11; NbExp=3; IntAct=EBI-1058722, EBI-10217483;
Q3LI72:KRTAP19-5; NbExp=3; IntAct=EBI-1058722, EBI-1048945;
Q3SYF9:KRTAP19-7; NbExp=3; IntAct=EBI-1058722, EBI-10241353;
Q9UI95:MAD2L2; NbExp=3; IntAct=EBI-1058722, EBI-77889;
Q9BUE0:MED18; NbExp=3; IntAct=EBI-1058722, EBI-394640;
Q9UBU8:MORF4L1; NbExp=3; IntAct=EBI-1058722, EBI-399246;
Q9UBU8-2:MORF4L1; NbExp=3; IntAct=EBI-1058722, EBI-10288852;
Q9Y3B7:MRPL11; NbExp=3; IntAct=EBI-1058722, EBI-5453723;
Q93100:PHKB; NbExp=3; IntAct=EBI-1058722, EBI-740559;
Q969H6:POP5; NbExp=3; IntAct=EBI-1058722, EBI-366525;
P61225:RAP2B; NbExp=3; IntAct=EBI-1058722, EBI-750871;
O43251:RBFOX2; NbExp=3; IntAct=EBI-1058722, EBI-746056;
Q93062:RBPMS; NbExp=3; IntAct=EBI-1058722, EBI-740322;
P62913:RPL11; NbExp=3; IntAct=EBI-1058722, EBI-354380;
Q9NTN9-3:SEMA4G; NbExp=3; IntAct=EBI-1058722, EBI-9089805;
Q5W111:SPRYD7; NbExp=3; IntAct=EBI-1058722, EBI-10248098;
Q8N0Z6:TTC5; NbExp=3; IntAct=EBI-1058722, EBI-9526213;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:21529938}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome {ECO:0000250}.
Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:21529938};
Peripheral membrane protein {ECO:0000269|PubMed:21529938};
Cytoplasmic side {ECO:0000269|PubMed:21529938}. Note=In slow-
twitch muscle, evenly distributed between longitudinal SR and
junctional SR.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=The variable region of the CAMK2B protein is encoded by
at least 7 exons (V1 to V7). Alternative splicing within this
region gives rise to CAMK2B isoforms.;
Name=4;
IsoId=Q13554-1; Sequence=Displayed;
Name=1; Synonyms=Beta;
IsoId=Q13554-2; Sequence=VSP_004776;
Name=2; Synonyms=Beta1, Beta'E;
IsoId=Q13554-3; Sequence=VSP_004770, VSP_004771, VSP_004775,
VSP_004776;
Note=Ref.1 (AAD42036) sequence is in conflict in position:
316:A->V. {ECO:0000305};
Name=3; Synonyms=Beta2;
IsoId=Q13554-4; Sequence=VSP_004770, VSP_004771, VSP_004774,
VSP_004776;
Name=5; Synonyms=Beta4, BetaE;
IsoId=Q13554-5; Sequence=VSP_004770, VSP_004771, VSP_004776;
Name=6; Synonyms=Beta6;
IsoId=Q13554-6; Sequence=VSP_004773, VSP_004776, VSP_004777;
Name=7; Synonyms=Beta7;
IsoId=Q13554-7; Sequence=VSP_004770, VSP_004772;
Name=8;
IsoId=Q13554-8; Sequence=VSP_041219, VSP_004776;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in adult and fetal
brain. Expression is slightly lower in fetal brain. Expressed in
skeletal muscle. {ECO:0000269|PubMed:16690701}.
-!- INDUCTION: Activity is induced in skeletal muscle during exercise.
{ECO:0000269|PubMed:16690701}.
-!- DOMAIN: The CAMK2 protein kinases contain a unique C-terminal
subunit association domain responsible for oligomerization.
-!- PTM: Autophosphorylation of Thr-287 following activation by
Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase
into an activated state. {ECO:0000269|PubMed:16690701}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. CaMK subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC99802.1; Type=Frameshift; Positions=426, 433, 511, 516; Evidence={ECO:0000305};
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EMBL; AF078803; AAD42035.1; -; mRNA.
EMBL; AF081572; AAD42036.1; -; mRNA.
EMBL; AF081924; AAD42037.1; -; mRNA.
EMBL; AF083419; AAD42038.1; -; mRNA.
EMBL; AF140350; AAD42070.1; -; mRNA.
EMBL; U23460; AAC99802.1; ALT_FRAME; mRNA.
EMBL; AF112472; AAD03744.1; -; mRNA.
EMBL; AF112471; AAD03743.1; -; mRNA.
EMBL; AJ252236; CAB65120.1; -; mRNA.
EMBL; AJ252237; CAB65121.1; -; mRNA.
EMBL; AJ252238; CAB65122.1; -; mRNA.
EMBL; AK290148; BAF82837.1; -; mRNA.
EMBL; AK315663; BAG38029.1; -; mRNA.
EMBL; CH236960; EAL23756.1; -; Genomic_DNA.
EMBL; CH236960; EAL23757.1; -; Genomic_DNA.
EMBL; CH236960; EAL23758.1; -; Genomic_DNA.
EMBL; CH236960; EAL23759.1; -; Genomic_DNA.
EMBL; CH236960; EAL23760.1; -; Genomic_DNA.
EMBL; CH236960; EAL23761.1; -; Genomic_DNA.
EMBL; CH236960; EAL23762.1; -; Genomic_DNA.
EMBL; BC019070; AAH19070.1; -; mRNA.
EMBL; U50358; AAB16863.1; -; mRNA.
CCDS; CCDS43573.1; -. [Q13554-8]
CCDS; CCDS5483.1; -. [Q13554-1]
CCDS; CCDS5484.1; -. [Q13554-2]
CCDS; CCDS5485.1; -. [Q13554-5]
CCDS; CCDS5486.1; -. [Q13554-3]
CCDS; CCDS5487.1; -. [Q13554-6]
CCDS; CCDS5488.1; -. [Q13554-4]
CCDS; CCDS5489.1; -. [Q13554-7]
RefSeq; NP_001211.3; NM_001220.4. [Q13554-1]
RefSeq; NP_001280099.1; NM_001293170.1. [Q13554-2]
RefSeq; NP_742075.1; NM_172078.2. [Q13554-2]
RefSeq; NP_742076.1; NM_172079.2. [Q13554-5]
RefSeq; NP_742077.1; NM_172080.2. [Q13554-8]
RefSeq; NP_742078.1; NM_172081.2. [Q13554-3]
RefSeq; NP_742079.1; NM_172082.2. [Q13554-6]
RefSeq; NP_742080.1; NM_172083.2. [Q13554-4]
RefSeq; NP_742081.1; NM_172084.2. [Q13554-7]
UniGene; Hs.351887; -.
PDB; 3BHH; X-ray; 2.40 A; A/B/C/D=11-303.
PDBsum; 3BHH; -.
ProteinModelPortal; Q13554; -.
SMR; Q13554; -.
BioGrid; 107266; 49.
DIP; DIP-39770N; -.
IntAct; Q13554; 45.
STRING; 9606.ENSP00000379098; -.
BindingDB; Q13554; -.
ChEMBL; CHEMBL4121; -.
DrugBank; DB07168; [4-({4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]-6-(methylamino)pyrimidin-2-yl}amino)phenyl]acetonitrile.
GuidetoPHARMACOLOGY; 1556; -.
iPTMnet; Q13554; -.
PhosphoSitePlus; Q13554; -.
BioMuta; CAMK2B; -.
DMDM; 334302890; -.
MaxQB; Q13554; -.
PaxDb; Q13554; -.
PeptideAtlas; Q13554; -.
PRIDE; Q13554; -.
DNASU; 816; -.
Ensembl; ENST00000258682; ENSP00000258682; ENSG00000058404. [Q13554-8]
Ensembl; ENST00000346990; ENSP00000326518; ENSG00000058404. [Q13554-7]
Ensembl; ENST00000347193; ENSP00000326544; ENSG00000058404. [Q13554-6]
Ensembl; ENST00000350811; ENSP00000326375; ENSG00000058404. [Q13554-2]
Ensembl; ENST00000353625; ENSP00000326427; ENSG00000058404. [Q13554-4]
Ensembl; ENST00000358707; ENSP00000351542; ENSG00000058404. [Q13554-3]
Ensembl; ENST00000395747; ENSP00000379096; ENSG00000058404. [Q13554-5]
Ensembl; ENST00000395749; ENSP00000379098; ENSG00000058404. [Q13554-1]
Ensembl; ENST00000440254; ENSP00000397937; ENSG00000058404. [Q13554-2]
Ensembl; ENST00000457475; ENSP00000390292; ENSG00000058404. [Q13554-5]
GeneID; 816; -.
KEGG; hsa:816; -.
UCSC; uc003tkp.3; human. [Q13554-1]
CTD; 816; -.
DisGeNET; 816; -.
GeneCards; CAMK2B; -.
HGNC; HGNC:1461; CAMK2B.
HPA; CAB006849; -.
HPA; HPA026307; -.
HPA; HPA051783; -.
HPA; HPA051785; -.
HPA; HPA053973; -.
MIM; 607707; gene.
neXtProt; NX_Q13554; -.
OpenTargets; ENSG00000058404; -.
PharmGKB; PA91; -.
eggNOG; KOG0033; Eukaryota.
eggNOG; ENOG410XNRX; LUCA.
GeneTree; ENSGT00760000118944; -.
HOVERGEN; HBG108055; -.
InParanoid; Q13554; -.
KO; K04515; -.
OMA; NVHFHGS; -.
OrthoDB; EOG091G0SCS; -.
PhylomeDB; Q13554; -.
TreeFam; TF315229; -.
BRENDA; 2.7.11.17; 2681.
Reactome; R-HSA-3371571; HSF1-dependent transactivation.
Reactome; R-HSA-399719; Trafficking of AMPA receptors.
Reactome; R-HSA-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-HSA-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-HSA-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-HSA-442982; Ras activation uopn Ca2+ infux through NMDA receptor.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
SignaLink; Q13554; -.
SIGNOR; Q13554; -.
EvolutionaryTrace; Q13554; -.
GeneWiki; CAMK2B; -.
GenomeRNAi; 816; -.
PRO; PR:Q13554; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000058404; -.
ExpressionAtlas; Q13554; baseline and differential.
Genevisible; Q13554; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0051924; P:regulation of calcium ion transport; TAS:UniProtKB.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0060998; P:regulation of dendritic spine development; TAS:UniProtKB.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; TAS:UniProtKB.
GO; GO:0014733; P:regulation of skeletal muscle adaptation; TAS:UniProtKB.
GO; GO:0051823; P:regulation of synapse structural plasticity; TAS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase.
InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032710; NTF2-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24347; PTHR24347; 1.
Pfam; PF08332; CaMKII_AD; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF54427; SSF54427; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; ATP-binding;
Calmodulin-binding; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Kinase; Membrane;
Neurogenesis; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Sarcoplasmic reticulum;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 666 Calcium/calmodulin-dependent protein
kinase type II subunit beta.
/FTId=PRO_0000086096.
DOMAIN 14 272 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 20 28 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 283 292 Autoinhibitory domain. {ECO:0000250}.
REGION 291 301 Calmodulin-binding.
ACT_SITE 136 136 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 43 43 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 17 17 Phosphotyrosine.
{ECO:0000250|UniProtKB:P28652}.
MOD_RES 287 287 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:16690701}.
MOD_RES 306 306 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 307 307 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000250|UniProtKB:P08413}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:P28652}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000250|UniProtKB:P08413}.
MOD_RES 400 400 Phosphothreonine.
{ECO:0000250|UniProtKB:P28652}.
MOD_RES 401 401 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 316 340 Missing (in isoform 8). {ECO:0000305}.
/FTId=VSP_041219.
VAR_SEQ 316 316 V -> A (in isoform 2, isoform 3, isoform
5 and isoform 7).
{ECO:0000303|PubMed:10819240,
ECO:0000303|PubMed:10858498,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9060999,
ECO:0000303|Ref.3}.
/FTId=VSP_004770.
VAR_SEQ 317 533 Missing (in isoform 7).
{ECO:0000303|PubMed:10858498}.
/FTId=VSP_004772.
VAR_SEQ 317 340 Missing (in isoform 2, isoform 3 and
isoform 5). {ECO:0000303|PubMed:10819240,
ECO:0000303|PubMed:10858498,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9060999,
ECO:0000303|Ref.3}.
/FTId=VSP_004771.
VAR_SEQ 354 392 Missing (in isoform 3).
{ECO:0000303|PubMed:10819240}.
/FTId=VSP_004774.
VAR_SEQ 354 377 Missing (in isoform 6).
{ECO:0000303|PubMed:10858498}.
/FTId=VSP_004773.
VAR_SEQ 379 393 Missing (in isoform 2).
{ECO:0000303|PubMed:10819240,
ECO:0000303|PubMed:10858498,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9060999}.
/FTId=VSP_004775.
VAR_SEQ 410 533 Missing (in isoform 1, isoform 2, isoform
3, isoform 5, isoform 6 and isoform 8).
{ECO:0000303|PubMed:10819240,
ECO:0000303|PubMed:10858498,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9060999,
ECO:0000303|Ref.3}.
/FTId=VSP_004776.
VAR_SEQ 559 584 Missing (in isoform 6).
{ECO:0000303|PubMed:10858498}.
/FTId=VSP_004777.
VARIANT 489 489 P -> L (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs555460132).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_045581.
VARIANT 510 510 E -> K (in dbSNP:rs35452727).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_045582.
CONFLICT 68 68 L -> V (in Ref. 3; AAD03744/AAD03743).
{ECO:0000305}.
CONFLICT 535 535 K -> N (in Ref. 8; AAB16863).
{ECO:0000305}.
STRAND 14 19 {ECO:0000244|PDB:3BHH}.
STRAND 27 33 {ECO:0000244|PDB:3BHH}.
TURN 34 36 {ECO:0000244|PDB:3BHH}.
STRAND 39 46 {ECO:0000244|PDB:3BHH}.
HELIX 52 67 {ECO:0000244|PDB:3BHH}.
STRAND 76 81 {ECO:0000244|PDB:3BHH}.
STRAND 83 91 {ECO:0000244|PDB:3BHH}.
STRAND 95 97 {ECO:0000244|PDB:3BHH}.
HELIX 98 102 {ECO:0000244|PDB:3BHH}.
HELIX 110 129 {ECO:0000244|PDB:3BHH}.
HELIX 139 141 {ECO:0000244|PDB:3BHH}.
STRAND 142 145 {ECO:0000244|PDB:3BHH}.
STRAND 153 155 {ECO:0000244|PDB:3BHH}.
HELIX 178 180 {ECO:0000244|PDB:3BHH}.
HELIX 183 186 {ECO:0000244|PDB:3BHH}.
HELIX 194 209 {ECO:0000244|PDB:3BHH}.
HELIX 219 228 {ECO:0000244|PDB:3BHH}.
TURN 235 238 {ECO:0000244|PDB:3BHH}.
STRAND 239 241 {ECO:0000244|PDB:3BHH}.
HELIX 243 252 {ECO:0000244|PDB:3BHH}.
TURN 257 259 {ECO:0000244|PDB:3BHH}.
HELIX 263 266 {ECO:0000244|PDB:3BHH}.
HELIX 270 273 {ECO:0000244|PDB:3BHH}.
HELIX 275 278 {ECO:0000244|PDB:3BHH}.
HELIX 285 298 {ECO:0000244|PDB:3BHH}.
SEQUENCE 666 AA; 72678 MW; 8CACFC3E392C3857 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
NSAAATSPKG TLPPAALEPQ TTVIHNPVDG IKESSDSANT TIEDEDAKAP RVPDILSSVR
RGSGAPEAEG PLPCPSPAPF SPLPAPSPRI SDILNSVRRG SGTPEAEGPL SAGPPPCLSP
ALLGPLSSPS PRISDILNSV RRGSGTPEAE GPSPVGPPPC PSPTIPGPLP TPSRKQEIIK
TTEQLIEAVN NGDFEAYAKI CDPGLTSFEP EALGNLVEGM DFHRFYFENL LAKNSKPIHT
TILNPHVHVI GEDAACIAYI RLTQYIDGQG RPRTSQSEET RVWHRRDGKW QNVHFHCSGA
PVAPLQ


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