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Q13554 (KCC2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium/calmodulin-dependent protein kinase type II subunit beta

Short name=CaM kinase II subunit beta
Short name=CaMK-II subunit beta
EC=2.7.11.17
Gene names
Name:CAMK2B
Synonyms:CAM2, CAMK2, CAMKB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length666 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca2+/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca2+ 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) Ca2+ transport and in fast-twitch muscle participates in the control of Ca2+ release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2. Ref.11

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by Ca2+/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 Ca2+-independent activity. Ref.9

Subunit structure

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. Interacts with SYNGAP1 and CAMK2N2 By similarity. Interacts with MPDZ. Ref.9 Ref.10

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note: In slow-twitch muscle, evenly distributed between longitudinal SR and junctional SR. Ref.13

Tissue specificity

Widely expressed. Expressed in adult and fetal brain. Expression is slightly lower in fetal brain. Expressed in skeletal muscle. Ref.11

Induction

Activity is induced in skeletal muscle during exercise. Ref.9 Ref.11

Domain

The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization.

Post-translational modification

Autophosphorylation of Thr-287 following activation by Ca2+/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAC99802.1 differs from that shown. Reason: Frameshift at positions 426, 433, 511 and 516.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Membrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

activation of meiosis involved in egg activation

Inferred from electronic annotation. Source: Ensembl

calcium ion transport

Inferred from electronic annotation. Source: Ensembl

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

inhibitory G-protein coupled receptor phosphorylation

Inferred from electronic annotation. Source: Ensembl

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synapse maturation

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.16. Source: UniProtKB

protein phosphorylation

Traceable author statement Ref.8. Source: ProtInc

regulation of calcium ion transport

Traceable author statement Ref.14. Source: UniProtKB

regulation of dendritic spine development

Traceable author statement Ref.16. Source: UniProtKB

regulation of long-term neuronal synaptic plasticity

Traceable author statement Ref.16. Source: UniProtKB

regulation of skeletal muscle adaptation

Traceable author statement Ref.14. Source: UniProtKB

regulation of synapse structural plasticity

Traceable author statement Ref.16. Source: UniProtKB

regulation of synaptic transmission, cholinergic

Inferred from electronic annotation. Source: Ensembl

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.8. Source: ProtInc

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

sarcoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle midzone

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calmodulin-dependent protein kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: 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.
Isoform 4 (identifier: Q13554-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: Q13554-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     410-533: Missing.
Isoform 2 (identifier: Q13554-3)

Also known as: Beta1; Beta'E;

The sequence of this isoform differs from the canonical sequence as follows:
     316-316: V → A
     317-340: Missing.
     379-393: Missing.
     410-533: Missing.
Isoform 3 (identifier: Q13554-4)

Also known as: Beta2;

The sequence of this isoform differs from the canonical sequence as follows:
     316-316: V → A
     317-340: Missing.
     354-392: Missing.
     410-533: Missing.
Isoform 5 (identifier: Q13554-5)

Also known as: Beta4; BetaE;

The sequence of this isoform differs from the canonical sequence as follows:
     316-316: V → A
     317-340: Missing.
     410-533: Missing.
Isoform 6 (identifier: Q13554-6)

Also known as: Beta6;

The sequence of this isoform differs from the canonical sequence as follows:
     354-377: Missing.
     410-533: Missing.
     559-584: Missing.
Isoform 7 (identifier: Q13554-7)

Also known as: Beta7;

The sequence of this isoform differs from the canonical sequence as follows:
     316-316: V → A
     317-533: Missing.
Isoform 8 (identifier: Q13554-8)

The sequence of this isoform differs from the canonical sequence as follows:
     316-340: Missing.
     410-533: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 666666Calcium/calmodulin-dependent protein kinase type II subunit beta
PRO_0000086096

Regions

Domain14 – 272259Protein kinase
Nucleotide binding20 – 289ATP By similarity
Region283 – 29210Autoinhibitory domain By similarity
Region291 – 30111Calmodulin-binding

Sites

Active site1361Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue171Phosphotyrosine By similarity
Modified residue2871Phosphothreonine; by autocatalysis Ref.11
Modified residue3061Phosphothreonine; by autocatalysis By similarity
Modified residue3071Phosphothreonine; by autocatalysis By similarity

Natural variations

Alternative sequence316 – 34025Missing in isoform 8.
VSP_041219
Alternative sequence3161V → A in isoform 2, isoform 3, isoform 5 and isoform 7.
VSP_004770
Alternative sequence317 – 533217Missing in isoform 7.
VSP_004772
Alternative sequence317 – 34024Missing in isoform 2, isoform 3 and isoform 5.
VSP_004771
Alternative sequence354 – 39239Missing in isoform 3.
VSP_004774
Alternative sequence354 – 37724Missing in isoform 6.
VSP_004773
Alternative sequence379 – 39315Missing in isoform 2.
VSP_004775
Alternative sequence410 – 533124Missing in isoform 1, isoform 2, isoform 3, isoform 5, isoform 6 and isoform 8.
VSP_004776
Alternative sequence559 – 58426Missing in isoform 6.
VSP_004777
Natural variant4891P → L in a colorectal adenocarcinoma sample; somatic mutation. Ref.19
VAR_045581
Natural variant5101E → K. Ref.19
Corresponds to variant rs35452727 [ dbSNP | Ensembl ].
VAR_045582

Experimental info

Sequence conflict681L → V in AAD03744. Ref.3
Sequence conflict681L → V in AAD03743. Ref.3
Sequence conflict5351K → N in AAB16863. Ref.8
Isoform 2:
Sequence conflict3161A → V in AAD42036. Ref.1

Secondary structure

............................................... 666
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 [UniParc].

Last modified May 31, 2011. Version 3.
Checksum: 8CACFC3E392C3857

FASTA66672,678
        10         20         30         40         50         60 
MATTVTCTRF TDEYQLYEDI GKGAFSVVRR CVKLCTGHEY AAKIINTKKL SARDHQKLER 

        70         80         90        100        110        120 
EARICRLLKH SNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI 

       130        140        150        160        170        180 
LEAVLHCHQM GVVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY 

       190        200        210        220        230        240 
LSPEVLRKEA YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT 

       250        260        270        280        290        300 
VTPEAKNLIN QMLTINPAKR ITAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL 

       310        320        330        340        350        360 
KGAILTTMLA TRNFSVGRQT TAPATMSTAA SGTTMGLVEQ AKSLLNKKAD GVKPQTNSTK 

       370        380        390        400        410        420 
NSAAATSPKG TLPPAALEPQ TTVIHNPVDG IKESSDSANT TIEDEDAKAP RVPDILSSVR 

       430        440        450        460        470        480 
RGSGAPEAEG PLPCPSPAPF SPLPAPSPRI SDILNSVRRG SGTPEAEGPL SAGPPPCLSP 

       490        500        510        520        530        540 
ALLGPLSSPS PRISDILNSV RRGSGTPEAE GPSPVGPPPC PSPTIPGPLP TPSRKQEIIK 

       550        560        570        580        590        600 
TTEQLIEAVN NGDFEAYAKI CDPGLTSFEP EALGNLVEGM DFHRFYFENL LAKNSKPIHT 

       610        620        630        640        650        660 
TILNPHVHVI GEDAACIAYI RLTQYIDGQG RPRTSQSEET RVWHRRDGKW QNVHFHCSGA 


PVAPLQ 

« Hide

Isoform 1 (Beta) [UniParc].

Checksum: 1F7AF874A78C9D26
Show »

FASTA54260,387
Isoform 2 (Beta1) (Beta'E) [UniParc].

Checksum: 4389A566D66A9FE1
Show »

FASTA50356,379
Isoform 3 (Beta2) [UniParc].

Checksum: E8A4B57BD6AA98AC
Show »

FASTA47954,074
Isoform 5 (Beta4) (BetaE) [UniParc].

Checksum: 5853A731579E86D8
Show »

FASTA51858,009
Isoform 6 (Beta6) [UniParc].

Checksum: 1102B7F9B979E307
Show »

FASTA49255,223
Isoform 7 (Beta7) [UniParc].

Checksum: 6EB6617646B54829
Show »

FASTA44950,955
Isoform 8 [UniParc].

Checksum: 1F4A8797FB7458A4
Show »

FASTA51757,938

References

« Hide 'large scale' references
[1]"Identification of alternative splicing variants of the beta subunit of human Ca(2+)/calmodulin-dependent protein kinase II with different activities."
Wang P., Wu Y., Zhou T.H., Sun Y., Pei G.
FEBS Lett. 475:107-110(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 5; 6 AND 7).
Tissue: Brain.
[2]Leddy J.J., Salih M., Tuana B.S.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Skeletal muscle.
[3]"Molecular cloning and sequencing of human calcium/calmodulin dependent protein kinase II beta subunit."
Li G.Y., Cooper N.G.F.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5).
Tissue: Brain.
[4]"Cloning and quantitative determination of the human Ca2+/calmodulin-dependent protein kinase II (CaMK II) isoforms in human beta cells."
Rochlitz H., Voigt A., Lankat-Buttgereit B., Goeke B., Heimberg H., Nauck M.A., Schiemann U., Schatz H., Pfeiffer A.F.
Diabetologia 43:465-473(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
Tissue: Insulinoma.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Testis and Thalamus.
[6]"Human chromosome 7: DNA sequence and biology."
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. expand/collapse author list , 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.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Lung.
[8]"Identification of novel human tumor cell-specific CaMK-II variants."
Tombes R.M., Krystal G.W.
Biochim. Biophys. Acta 1355:281-292(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-605 (ISOFORM 2).
[9]"Comparative analyses of the three-dimensional structures and enzymatic properties of alpha, beta, gamma and delta isoforms of Ca2+-calmodulin-dependent protein kinase II."
Gaertner T.R., Kolodziej S.J., Wang D., Kobayashi R., Koomen J.M., Stoops J.K., Waxham M.N.
J. Biol. Chem. 279:12484-12494(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, SUBUNIT, AUTOPHOSPHORYLATION.
[10]"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation."
Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.
Neuron 43:563-574(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPDZ.
[11]"Ca2+-calmodulin-dependent protein kinase expression and signalling in skeletal muscle during exercise."
Rose A.J., Kiens B., Richter E.A.
J. Physiol. (Lond.) 574:889-903(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SKELETAL MUSCLE, PHOSPHORYLATION AT THR-287, FUNCTION IN PHOSPHORYLATION OF PLN, TISSUE SPECIFICITY, INDUCTION.
[12]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Analysis of CaM-kinase signaling in cells."
Wayman G.A., Tokumitsu H., Davare M.A., Soderling T.R.
Cell Calcium 50:1-8(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"The role of calcium and calcium/calmodulin-dependent kinases in skeletal muscle plasticity and mitochondrial biogenesis."
Chin E.R.
Proc. Nutrit. Soc. 63:279-286(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN SKELETAL MUSCLE.
[15]"The Ca2+-calmodulin dependent protein kinase II system of skeletal muscle sarcoplasmic reticulum."
Sacchetto R., Bovo E., Damiani E.
Basic Appl. Myol. 15:5-17(2005)
Cited for: REVIEW ON FUNCTION IN SKELETAL MUSCLE.
[16]"Calmodulin-kinases: modulators of neuronal development and plasticity."
Wayman G.A., Lee Y.S., Tokumitsu H., Silva A.J., Silva A., Soderling T.R.
Neuron 59:914-931(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
[17]"The roles of CaMKII and F-actin in the structural plasticity of dendritic spines: a potential molecular identity of a synaptic tag?"
Okamoto K., Bosch M., Hayashi Y.
Physiology (Bethesda) 24:357-366(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
[18]"Crystal structure of human calcium/calmodulin-dependent protein kinase IIb isoform 1 (CAMK2B)."
Structural genomics consortium (SGC)
Submitted (DEC-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 11-303 IN COMPLEX WITH INHIBITOR.
[19]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-489 AND LYS-510.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF078803 mRNA. Translation: AAD42035.1.
AF081572 mRNA. Translation: AAD42036.1.
AF081924 mRNA. Translation: AAD42037.1.
AF083419 mRNA. Translation: AAD42038.1.
AF140350 mRNA. Translation: AAD42070.1.
U23460 mRNA. Translation: AAC99802.1. Frameshift.
AF112472 mRNA. Translation: AAD03744.1.
AF112471 mRNA. Translation: AAD03743.1.
AJ252236 mRNA. Translation: CAB65120.1.
AJ252237 mRNA. Translation: CAB65121.1.
AJ252238 mRNA. Translation: CAB65122.1.
AK290148 mRNA. Translation: BAF82837.1.
AK315663 mRNA. Translation: BAG38029.1.
CH236960 Genomic DNA. Translation: EAL23756.1.
CH236960 Genomic DNA. Translation: EAL23757.1.
CH236960 Genomic DNA. Translation: EAL23758.1.
CH236960 Genomic DNA. Translation: EAL23759.1.
CH236960 Genomic DNA. Translation: EAL23760.1.
CH236960 Genomic DNA. Translation: EAL23761.1.
CH236960 Genomic DNA. Translation: EAL23762.1.
BC019070 mRNA. Translation: AAH19070.1.
U50358 mRNA. Translation: AAB16863.1.
RefSeqNP_001211.3. NM_001220.4.
NP_742075.1. NM_172078.2.
NP_742076.1. NM_172079.2.
NP_742077.1. NM_172080.2.
NP_742078.1. NM_172081.2.
NP_742079.1. NM_172082.2.
NP_742080.1. NM_172083.2.
NP_742081.1. NM_172084.2.
XP_005249918.1. XM_005249861.1.
UniGeneHs.351887.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BHHX-ray2.40A/B/C/D11-303[»]
ProteinModelPortalQ13554.
SMRQ13554. Positions 8-662.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107266. 11 interactions.
DIPDIP-39770N.
IntActQ13554. 3 interactions.

Chemistry

BindingDBQ13554.
ChEMBLCHEMBL4121.
GuidetoPHARMACOLOGY1556.

PTM databases

PhosphoSiteQ13554.

Polymorphism databases

DMDM334302890.

Proteomic databases

PaxDbQ13554.
PRIDEQ13554.

Protocols and materials databases

DNASU816.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258682; ENSP00000258682; ENSG00000058404. [Q13554-8]
ENST00000346990; ENSP00000326518; ENSG00000058404. [Q13554-7]
ENST00000347193; ENSP00000326544; ENSG00000058404. [Q13554-6]
ENST00000350811; ENSP00000326375; ENSG00000058404. [Q13554-2]
ENST00000353625; ENSP00000326427; ENSG00000058404. [Q13554-4]
ENST00000358707; ENSP00000351542; ENSG00000058404. [Q13554-3]
ENST00000395747; ENSP00000379096; ENSG00000058404. [Q13554-5]
ENST00000395749; ENSP00000379098; ENSG00000058404. [Q13554-1]
ENST00000440254; ENSP00000397937; ENSG00000058404. [Q13554-2]
ENST00000457475; ENSP00000390292; ENSG00000058404. [Q13554-5]
GeneID816.
KEGGhsa:816.
UCSCuc003tkp.2. human. [Q13554-2]
uc003tkq.2. human. [Q13554-1]
uc003tkr.2. human. [Q13554-5]
uc003tks.2. human. [Q13554-8]
uc003tkt.2. human. [Q13554-6]
uc003tku.2. human. [Q13554-3]
uc003tkv.2. human. [Q13554-4]
uc003tkw.2. human. [Q13554-7]

Organism-specific databases

CTD816.
GeneCardsGC07M044225.
HGNCHGNC:1461. CAMK2B.
HPACAB006849.
HPA026307.
HPA051783.
HPA051785.
HPA053973.
MIM607707. gene.
neXtProtNX_Q13554.
PharmGKBPA91.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108055.
InParanoidQ13554.
KOK04515.
OMAQGPPPCL.
OrthoDBEOG7ZD1VM.
PhylomeDBQ13554.
TreeFamTF315229.

Enzyme and pathway databases

BRENDA2.7.11.17. 2681.
ReactomeREACT_13685. Neuronal System.
REACT_6900. Immune System.
SignaLinkQ13554.

Gene expression databases

ArrayExpressQ13554.
BgeeQ13554.
GenevestigatorQ13554.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13554.
GeneWikiCAMK2B.
GenomeRNAi816.
NextBio3310.
PROQ13554.
SOURCESearch...

Entry information

Entry nameKCC2B_HUMAN
AccessionPrimary (citable) accession number: Q13554
Secondary accession number(s): A4D2K0 expand/collapse secondary AC list , A4D2K1, A4D2K2, A4D2K3, A4D2K4, A4D2K5, A4D2K6, O95437, O95438, O95599, Q9UGH7, Q9UGH8, Q9UGH9, Q9UNX0, Q9UNX7, Q9UP00, Q9Y5N4, Q9Y6F4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 31, 2011
Last modified: April 16, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM