Reviewed, UniProtKB/Swiss-Prot P28652 (KCC2B_MOUSE)

Names and origin

Protein names

Recommended name:
    Calcium/calmodulin-dependent protein kinase type II beta chain
      Short name=CaM-kinase II beta chain
      Short name=CaM kinase II subunit beta
      Short name=CaMK-II subunit beta
    EC=2.7.11.17

Gene names

Name:	Camk2b
Synonyms:	Camk2d

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Autophosphorylation of CAMK2 plays an important role in the regulation of the kinase activity.
Subunit structure	CAMK2 is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Interacts with SYNGAP1, CAMK2N2 and MPDZ By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	G1/S transition of mitotic cell cycle Inferred from mutant phenotype. Source: MGI calcium ion transport Inferred from mutant phenotype. Source: MGI protein amino acid autophosphorylation Inferred from mutant phenotype. Source: MGI
Cellular component	calcium- and calmodulin-dependent protein kinase complex Traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Camk2a	P11798-2	2	EBI-397029,EBI-400402

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 542	542	Calcium/calmodulin-dependent protein kinase type II beta chain		PRO_0000086097
Regions
	Domain	14 – 272	259	Protein kinase
	Nucleotide binding	20 – 28	9	ATP 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 Ref.7
	Modified residue	287	1	Phosphothreonine Ref.6 Ref.8
	Modified residue	315	1	Phosphoserine Ref.5
	Modified residue	367	1	Phosphoserine Ref.8
	Modified residue	397	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	19	1	D → E in CAA45160. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P28652-1 [UniParc]. Last modified May 2, 2006. Version 2. Checksum: 8A7962A6495FD0D0	FASTA	542	60,461
	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 NSSAITSPKG SLPPAALEPQ TTVIHNPVDG IKESSDSTNT 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure, expression, and chromosome location of the gene for the beta subunit of brain-specific Ca2+/calmodulin-dependent protein kinase II identified by transgene integration in an embryonic lethal mouse mutant." Karls U., Mueller U., Gilbert D.J., Copeland N.G., Jenkins N.A., Harbers K. Mol. Cell. Biol. 12:3644-3652(1992) [PubMed: 1321343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 136-147, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[5]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed: 15572359] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17, MASS SPECTROMETRY. Tissue: Brain.
[8]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-287 AND SER-397, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X63615 mRNA. Translation: CAA45160.1. AK163698 mRNA. Translation: BAE37464.1. AL611926, AL645469 Genomic DNA. Translation: CAI24948.1. AL645469, AL611926 Genomic DNA. Translation: CAI25258.1.
IPI	IPI00474502.
PIR	A45025.
RefSeq	NP_031621.3.
UniGene	Mm.439733
3D structure databases
HSSP	HSSP built from PDB template 1HKX based on UniProtKB P11798.
SMR	P28652. Positions 8-315, 403-536.
ModBase	Search...
Protein-protein interaction databases
IntAct	P28652. 5 interactions.
STRING	P28652.
PTM databases
PhosphoSite	P28652.
Proteomic databases
PRIDE	P28652.
Genome annotation databases
Ensembl	ENSMUST00000019133; ENSMUSP00000019133; ENSMUSG00000057897; Mus musculus. [Genome view] ENSMUST00000109813; ENSMUSP00000105438; ENSMUSG00000057897; Mus musculus. [Genome view] ENSMUST00000109815; ENSMUSP00000105440; ENSMUSG00000057897; Mus musculus. [Genome view]
GeneID	12323.
KEGG	mmu:12323.
UCSC	uc007hxr.1. mouse.
Organism-specific databases
CTD	12323.
MGI	MGI:88257. Camk2b.
Phylogenomic databases
HOVERGEN	P28652.
Enzyme and pathway databases
BRENDA	2.7.11.17. 244.
Gene expression databases
ArrayExpress	P28652.
Bgee	P28652.
Genevestigator	P28652.
GermOnline	ENSMUSG00000057897. Mus musculus.
Family and domain databases
InterPro	IPR015742. Ca/calmodulin-dep_kinase. IPR013543. Ca/calmodulin-dep_kinase-assoc. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
PANTHER	PTHR22982:SF64. CaMKII. 1 hit.
Pfam	PF08332. CaMKII_AD. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

KCC2B_MOUSE

Accession

Primary (citable) accession number: P28652
Secondary accession number(s): Q5SVH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	May 2, 2006
Last modified:	October 13, 2009
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)