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P11730 (KCC2G_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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 gamma
Short name=CaM kinase II subunit gamma
Short name=CaMK-II subunit gamma
EC=2.7.11.17
Gene names
Name:Camk2g
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca2+/calmodulin-binding and autophosphorylation, and is involved in sarcoplasmic reticulum Ca2+ transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity. 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 the ryanodine receptor-coupling factor triadin. In neurons, may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning By similarity.

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.

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 By similarity.

Subcellular location

Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Probable.

Induction

By cocaine in cardiomyocytes. Ref.3

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 By similarity.

Sequence similarities

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

Contains 1 protein kinase domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform A (identifier: P11730-1)

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 B (identifier: P11730-2)

The sequence of this isoform differs from the canonical sequence as follows:
     316-336: Missing.
     351-361: KKRKSSSSVHL → PEQQQKQSRKPSPRARDPLQTA
Isoform C (identifier: P11730-3)

The sequence of this isoform differs from the canonical sequence as follows:
     316-336: Missing.
     352-362: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527Calcium/calmodulin-dependent protein kinase type II subunit gamma
PRO_0000086103

Regions

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

Sites

Active site1361Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue2351Phosphoserine By similarity
Modified residue2871Phosphothreonine; by autocatalysis By similarity
Modified residue3061Phosphothreonine; by autocatalysis By similarity
Modified residue3071Phosphothreonine; by autocatalysis By similarity
Modified residue3111Phosphoserine By similarity

Natural variations

Alternative sequence316 – 33621Missing in isoform B and isoform C.
VSP_004781
Alternative sequence351 – 36111KKRKSSSSVHL → PEQQQKQSRKPSPRARDPLQ TA in isoform B.
VSP_004782
Alternative sequence352 – 36211Missing in isoform C.
VSP_004783

Experimental info

Sequence conflict21A → E in AAB30670. Ref.2
Sequence conflict21A → E in AAB30671. Ref.2

Sequences

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

Last modified October 1, 1989. Version 1.
Checksum: 58DBF1B72F64FA31

FASTA52759,038
        10         20         30         40         50         60 
MATTATCTRF TDDYQLFEEL GKGAFSVVRR CVKKTSTQEY AAKIINTKKL SARDHQKLER 

        70         80         90        100        110        120 
EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIHQI 

       130        140        150        160        170        180 
LESVNHIHQH DIVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGEQQA WFGFAGTPGY 

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

       250        260        270        280        290        300 
VTPEAKNLIN QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL 

       310        320        330        340        350        360 
KGAILTTMLV SRNFSVGRQS SAPASPAASA AGLAGQAAKS LLNKKSDGGV KKRKSSSSVH 

       370        380        390        400        410        420 
LMEPQTTVVH NATDGIKGST ESCNTTTEDE DLKVRKQEII KITEQLIEAI NNGDFEAYTK 

       430        440        450        460        470        480 
ICDPGLTSFE PEALGNLVEG MDFHKFYFEN LLSKNSKPIH TTILNPHVHV IGEDAACIAY 

       490        500        510        520 
IRLTQYIDGQ GRPRTSQSEE TRVWHRRDGK WLNVHYHCSG APAAPLQ

« Hide

Isoform B [UniParc].

Checksum: 2F5FF73C9BDCBF0D
Show »

FASTA51758,493
Isoform C [UniParc].

Checksum: 168EA409723DF4C4
Show »

FASTA49555,961

References

[1]"Molecular cloning of the cDNA encoding the third polypeptide (gamma) of brain calmodulin-dependent protein kinase II."
Tobimatsu T., Kameshita I., Fujisawa H.
J. Biol. Chem. 263:16082-16086(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Brain.
[2]"New isoforms of Ca2+/calmodulin-dependent protein kinase II in smooth muscle."
Zhou Z.L., Ikebe M.
Biochem. J. 299:489-495(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C).
Tissue: Aortic smooth muscle.
[3]"Cocaine activates calcium/calmodulin kinase II and causes cardiomyocyte hypertrophy."
Henning R.J., Cuevas J.
J. Cardiovasc. Pharmacol. 48:802-813(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY COCAINE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04063 mRNA. Translation: AAA41857.1.
S71570 mRNA. Translation: AAB30670.1.
S71571 mRNA. Translation: AAB30671.1.
IPIIPI00196730.
IPI00231086.
IPI00231087.
PIRA31908.
S43845.
RefSeqNP_598289.1. NM_133605.1.
UniGeneRn.10961.

3D structure databases

ProteinModelPortalP11730.
SMRP11730. Positions 3-302, 387-521.
ModBaseSearch...

Protein-protein interaction databases

IntActP11730. 1 interaction.

PTM databases

PhosphoSiteP11730.

Proteomic databases

PaxDbP11730.
PRIDEP11730.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID171140.
KEGGrno:171140.
UCSCRGD:621802. rat.

Organism-specific databases

CTD818.
RGD621802. Camk2g.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233016.
HOVERGENHBG108055.
KOK04515.
OrthoDBEOG42JNR7.

Enzyme and pathway databases

BRENDA2.7.11.17. 5301.

Gene expression databases

ArrayExpressP11730.
GenevestigatorP11730.

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_cat_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. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP11730.
ChEMBLCHEMBL5109.
NextBio621932.

Entry information

Entry nameKCC2G_RAT
AccessionPrimary (citable) accession number: P11730
Secondary accession number(s): Q64003, Q64004
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 3, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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