Calcium/calmodulin-dependent protein kinase type II subunit beta

Preferred order of sections

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	666 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome 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 process	Differentiation Neurogenesis
Cellular component	Cytoplasm Cytoskeleton Membrane Sarcoplasmic reticulum
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara activation of meiosis involved in egg activation Inferred from electronic annotation. Source: Compara calcium ion transport Inferred from electronic annotation. Source: Compara inhibitory G-protein coupled receptor phosphorylation Inferred from electronic annotation. Source: Compara interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome neuromuscular process controlling balance Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of apoptotic signaling pathway Inferred from electronic annotation. Source: Compara 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 regulation of calcium ion transport Traceable author statement Ref.14. 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: Compara response to cadmium ion Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol 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: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Inferred from electronic annotation. Source: 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 666

666

Calcium/calmodulin-dependent protein kinase type II subunit beta

PRO_0000086096

Regions

Domain

14 – 272

259

Protein kinase

Nucleotide binding

20 – 28

9

ATP By similarity

Region

283 – 292

10

Autoinhibitory domain By similarity

Region

291 – 301

11

Calmodulin-binding

Sites

Active site

136

1

Proton acceptor By similarity

Binding site

43

1

ATP By similarity

Amino acid modifications

Modified residue

17

1

Phosphotyrosine By similarity

Modified residue

287

1

Phosphothreonine; by autocatalysis Ref.11

Modified residue

306

1

Phosphothreonine; by autocatalysis By similarity

Modified residue

307

1

Phosphothreonine; by autocatalysis By similarity

Modified residue

315

1

Phosphoserine By similarity

Modified residue

367

1

Phosphoserine By similarity

Modified residue

397

1

Phosphoserine By similarity

Natural variations

Alternative sequence

316 – 340

25

Missing in isoform 8.

VSP_041219

Alternative sequence

316

1

V → A in isoform 2, isoform 3, isoform 5 and isoform 7.

VSP_004770

Alternative sequence

317 – 533

217

Missing in isoform 7.

VSP_004772

Alternative sequence

317 – 340

24

Missing in isoform 2, isoform 3 and isoform 5.

VSP_004771

Alternative sequence

354 – 392

39

Missing in isoform 3.

VSP_004774

Alternative sequence

354 – 377

24

Missing in isoform 6.

VSP_004773

Alternative sequence

379 – 393

15

Missing in isoform 2.

VSP_004775

Alternative sequence

410 – 533

124

Missing in isoform 1, isoform 2, isoform 3, isoform 5, isoform 6 and isoform 8.

VSP_004776

Alternative sequence

559 – 584

26

Missing in isoform 6.

VSP_004777

Natural variant

489

1

P → L in a colorectal adenocarcinoma sample; somatic mutation. Ref.19

VAR_045581

Natural variant

510

1

E → K. Ref.19

VAR_045582

Experimental info

Sequence conflict

68

1

L → V in AAD03744. Ref.3

Sequence conflict

68

1

L → V in AAD03743. Ref.3

Sequence conflict

535

1

K → N in AAB16863. Ref.8

Isoform 2:

Sequence conflict

316

1

A → V in AAD42036. Ref.1

Secondary structure

1

.

666

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform 4 [UniParc]. Last modified May 31, 2011. Version 3. Checksum: 8CACFC3E392C3857 Show »	FASTA	666	72,678
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 »	FASTA	542	60,387
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 TIEDEDAKAR KQEIIKTTEQ 430 440 450 460 470 480 LIEAVNNGDF EAYAKICDPG LTSFEPEALG NLVEGMDFHR FYFENLLAKN SKPIHTTILN 490 500 510 520 530 540 PHVHVIGEDA ACIAYIRLTQ YIDGQGRPRT SQSEETRVWH RRDGKWQNVH FHCSGAPVAP LQ « Hide
Isoform 2 (Beta1) (Beta'E) [UniParc]. Checksum: 4389A566D66A9FE1 Show »	FASTA	503	56,379
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 TRNFSAAKSL LNKKADGVKP QTNSTKNSAA ATSPKGTLPP AALESSDSAN 370 380 390 400 410 420 TTIEDEDAKA RKQEIIKTTE QLIEAVNNGD FEAYAKICDP GLTSFEPEAL GNLVEGMDFH 430 440 450 460 470 480 RFYFENLLAK NSKPIHTTIL NPHVHVIGED AACIAYIRLT QYIDGQGRPR TSQSEETRVW 490 500 HRRDGKWQNV HFHCSGAPVA PLQ « Hide
Isoform 3 (Beta2) [UniParc]. Checksum: E8A4B57BD6AA98AC Show »	FASTA	479	54,074
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 TRNFSAAKSL LNKKADGVKE SSDSANTTIE DEDAKARKQE IIKTTEQLIE 370 380 390 400 410 420 AVNNGDFEAY AKICDPGLTS FEPEALGNLV EGMDFHRFYF ENLLAKNSKP IHTTILNPHV 430 440 450 460 470 HVIGEDAACI AYIRLTQYID GQGRPRTSQS EETRVWHRRD GKWQNVHFHC SGAPVAPLQ « Hide
Isoform 5 (Beta4) (BetaE) [UniParc]. Checksum: 5853A731579E86D8 Show »	FASTA	518	58,009
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 TRNFSAAKSL LNKKADGVKP QTNSTKNSAA ATSPKGTLPP AALEPQTTVI 370 380 390 400 410 420 HNPVDGIKES SDSANTTIED EDAKARKQEI IKTTEQLIEA VNNGDFEAYA KICDPGLTSF 430 440 450 460 470 480 EPEALGNLVE GMDFHRFYFE NLLAKNSKPI HTTILNPHVH VIGEDAACIA YIRLTQYIDG 490 500 510 QGRPRTSQSE ETRVWHRRDG KWQNVHFHCS GAPVAPLQ « Hide
Isoform 6 (Beta6) [UniParc]. Checksum: 1102B7F9B979E307 Show »	FASTA	492	55,223
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 GVKEPQTTVI 370 380 390 400 410 420 HNPVDGIKES SDSANTTIED EDAKARKQEI IKTTEQLIEA VNNGDFEAYA FYFENLLAKN 430 440 450 460 470 480 SKPIHTTILN PHVHVIGEDA ACIAYIRLTQ YIDGQGRPRT SQSEETRVWH RRDGKWQNVH 490 FHCSGAPVAP LQ « Hide
Isoform 7 (Beta7) [UniParc]. Checksum: 6EB6617646B54829 Show »	FASTA	449	50,955
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 TRNFSARKQE IIKTTEQLIE AVNNGDFEAY AKICDPGLTS FEPEALGNLV 370 380 390 400 410 420 EGMDFHRFYF ENLLAKNSKP IHTTILNPHV HVIGEDAACI AYIRLTQYID GQGRPRTSQS 430 440 EETRVWHRRD GKWQNVHFHC SGAPVAPLQ « Hide
Isoform 8 [UniParc]. Checksum: 1F4A8797FB7458A4 Show »	FASTA	517	57,938
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 TRNFSAKSLL NKKADGVKPQ TNSTKNSAAA TSPKGTLPPA ALEPQTTVIH 370 380 390 400 410 420 NPVDGIKESS DSANTTIEDE DAKARKQEII KTTEQLIEAV NNGDFEAYAK ICDPGLTSFE 430 440 450 460 470 480 PEALGNLVEG MDFHRFYFEN LLAKNSKPIH TTILNPHVHV IGEDAACIAY IRLTQYIDGQ 490 500 510 GRPRTSQSEE TRVWHRRDGK WQNVHFHCSG APVAPLQ « Hide

References

	« Hide 'large scale' referencesShow '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. 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. 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. 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.

IPI

IPI00182944.
IPI00183066.
IPI00219165.
IPI00219166.
IPI00221305.
IPI00298090.
IPI00334271.
IPI00377174.

RefSeq

NP_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.

UniGene

Hs.351887.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BHH	X-ray	2.40	A/B/C/D	11-303	[»]

ProteinModelPortal

Q13554.

SMR

Q13554. Positions 8-662.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39770N.

IntAct

Q13554. 3 interactions.

PTM databases

PhosphoSite

Q13554.

Polymorphism databases

DMDM

12643413.

Proteomic databases

PaxDb

Q13554.

PRIDE

Q13554.

Protocols and materials databases

DNASU

816.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

GeneID

816.

KEGG

hsa:816.

UCSC

uc003tkp.2. human.
uc003tkq.2. human.
uc003tkr.2. human.
uc003tkt.2. human.
uc003tku.2. human.
uc003tkv.2. human.
uc003tkw.2. human.

Organism-specific databases

CTD

816.

GeneCards

GC07M044225.

HGNC

HGNC:1461. CAMK2B.

HPA

CAB006849.
HPA026307.

MIM

607707. gene.

neXtProt

NX_Q13554.

PharmGKB

PA91.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG108055.

InParanoid

Q13554.

KO

K04515.

OMA

VGPPPCL.

PhylomeDB

Q13554.

Enzyme and pathway databases

BRENDA

2.7.11.17. 2681.

Pathway_Interaction_DB

ifngpathway. IFN-gamma pathway.
p38_mkk3_6pathway. p38 MAPK signaling pathway.

Reactome

REACT_13685. Neuronal System.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q13554.

Bgee

Q13554.

Genevestigator

Q13554.

GermOnline

ENSG00000058404. Homo sapiens.

Family and domain databases

InterPro

IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

PANTHER

PTHR24347. PTHR24347. 1 hit.

Pfam

PF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q13554.

ChEMBL

CHEMBL4121.

EvolutionaryTrace

Q13554.

GenomeRNAi

816.

NextBio

3310.

SOURCE

Search...

Entry information

Entry name

KCC2B_HUMAN

Accession

Primary (citable) accession number: Q13554
Secondary accession number(s): A4D2K0

Q9Y6F4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 31, 2011
Last modified:	April 3, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.