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Protein

Calcium/calmodulin-dependent protein kinase type II subunit gamma

Gene

Camk2g

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATPPROSITE-ProRule annotation
Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calmodulin-dependent protein kinase activity Source: RGD

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • nervous system development Source: UniProtKB-KW
  • protein autophosphorylation Source: RGD
  • regulation of long-term neuronal synaptic plasticity Source: RGD
  • response to hypoxia Source: RGD
  • response to oxidative stress Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17. 5301.
ReactomeiR-RNO-3371571. HSF1-dependent transactivation.
R-RNO-399719. Trafficking of AMPA receptors.
R-RNO-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-RNO-442729. CREB phosphorylation through the activation of CaMKII.
R-RNO-442742. CREB phosphorylation through the activation of Ras.
R-RNO-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-RNO-5576892. Phase 0 - rapid depolarisation.
R-RNO-5578775. Ion homeostasis.
R-RNO-5673001. RAF/MAP kinase cascade.
R-RNO-877300. Interferon gamma signaling.
R-RNO-936837. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type II subunit gamma (EC:2.7.11.17)
Short name:
CaM kinase II subunit gamma
Short name:
CaMK-II subunit gamma
Gene namesi
Name:Camk2g
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi621802. Camk2g.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2111382.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 527527Calcium/calmodulin-dependent protein kinase type II subunit gammaPRO_0000086103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei287 – 2871Phosphothreonine; by autocatalysisBy similarity
Modified residuei306 – 3061Phosphothreonine; by autocatalysisBy similarity
Modified residuei307 – 3071Phosphothreonine; by autocatalysisBy similarity
Modified residuei311 – 3111PhosphoserineCombined sources
Modified residuei321 – 3211PhosphoserineCombined sources
Modified residuei325 – 3251PhosphoserineCombined sources
Modified residuei329 – 3291PhosphoserineCombined sources
Modified residuei355 – 3551PhosphoserineCombined sources
Modified residuei453 – 4531PhosphoserineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP11730.
PRIDEiP11730.

PTM databases

iPTMnetiP11730.
PhosphoSiteiP11730.

Expressioni

Inductioni

By cocaine in cardiomyocytes.1 Publication

Gene expression databases

ExpressionAtlasiP11730. baseline and differential.
GenevisibleiP11730. RN.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi251145. 3 interactions.
IntActiP11730. 1 interaction.
STRINGi10116.ENSRNOP00000062321.

Structurei

3D structure databases

ProteinModelPortaliP11730.
SMRiP11730. Positions 3-302, 387-521.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 272259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni283 – 29210Autoinhibitory domainBy similarity
Regioni291 – 30111Calmodulin-bindingBy similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0033. Eukaryota.
ENOG410XNRX. LUCA.
GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiP11730.
KOiK04515.
PhylomeDBiP11730.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR032710. NTF2-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 2 hits.
PfamiPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform A (identifier: P11730-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MATTATCTRF TDDYQLFEEL GKGAFSVVRR CVKKTSTQEY AAKIINTKKL
60 70 80 90 100
SARDHQKLER EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE
110 120 130 140 150
DIVAREYYSE ADASHCIHQI LESVNHIHQH DIVHRDLKPE NLLLASKCKG
160 170 180 190 200
AAVKLADFGL AIEVQGEQQA WFGFAGTPGY LSPEVLRKDP YGKPVDIWAC
210 220 230 240 250
GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT VTPEAKNLIN
260 270 280 290 300
QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL
310 320 330 340 350
KGAILTTMLV SRNFSVGRQS SAPASPAASA AGLAGQAAKS LLNKKSDGGV
360 370 380 390 400
KKRKSSSSVH LMEPQTTVVH NATDGIKGST ESCNTTTEDE DLKVRKQEII
410 420 430 440 450
KITEQLIEAI NNGDFEAYTK ICDPGLTSFE PEALGNLVEG MDFHKFYFEN
460 470 480 490 500
LLSKNSKPIH TTILNPHVHV IGEDAACIAY IRLTQYIDGQ GRPRTSQSEE
510 520
TRVWHRRDGK WLNVHYHCSG APAAPLQ
Length:527
Mass (Da):59,038
Last modified:October 1, 1989 - v1
Checksum:i58DBF1B72F64FA31
GO
Isoform B (identifier: P11730-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     316-336: Missing.
     351-361: KKRKSSSSVHL → PEQQQKQSRKPSPRARDPLQTA

Show »
Length:517
Mass (Da):58,493
Checksum:i2F5FF73C9BDCBF0D
GO
Isoform C (identifier: P11730-3) [UniParc]FASTAAdd to basket

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

Show »
Length:495
Mass (Da):55,961
Checksum:i168EA409723DF4C4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → E in AAB30670 (PubMed:8172610).Curated
Sequence conflicti2 – 21A → E in AAB30671 (PubMed:8172610).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei316 – 33621Missing in isoform B and isoform C. 1 PublicationVSP_004781Add
BLAST
Alternative sequencei351 – 36111KKRKSSSSVHL → PEQQQKQSRKPSPRARDPLQ TA in isoform B. 1 PublicationVSP_004782Add
BLAST
Alternative sequencei352 – 36211Missing in isoform C. 1 PublicationVSP_004783Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04063 mRNA. Translation: AAA41857.1.
S71570 mRNA. Translation: AAB30670.1.
S71571 mRNA. Translation: AAB30671.1.
PIRiA31908.
S43845.
RefSeqiNP_598289.1. NM_133605.1. [P11730-1]
XP_008768721.1. XM_008770499.1. [P11730-3]
UniGeneiRn.10961.

Genome annotation databases

EnsembliENSRNOT00000066163; ENSRNOP00000062321; ENSRNOG00000009783. [P11730-1]
GeneIDi171140.
KEGGirno:171140.
UCSCiRGD:621802. rat. [P11730-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04063 mRNA. Translation: AAA41857.1.
S71570 mRNA. Translation: AAB30670.1.
S71571 mRNA. Translation: AAB30671.1.
PIRiA31908.
S43845.
RefSeqiNP_598289.1. NM_133605.1. [P11730-1]
XP_008768721.1. XM_008770499.1. [P11730-3]
UniGeneiRn.10961.

3D structure databases

ProteinModelPortaliP11730.
SMRiP11730. Positions 3-302, 387-521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251145. 3 interactions.
IntActiP11730. 1 interaction.
STRINGi10116.ENSRNOP00000062321.

Chemistry

ChEMBLiCHEMBL2111382.

PTM databases

iPTMnetiP11730.
PhosphoSiteiP11730.

Proteomic databases

PaxDbiP11730.
PRIDEiP11730.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000066163; ENSRNOP00000062321; ENSRNOG00000009783. [P11730-1]
GeneIDi171140.
KEGGirno:171140.
UCSCiRGD:621802. rat. [P11730-1]

Organism-specific databases

CTDi818.
RGDi621802. Camk2g.

Phylogenomic databases

eggNOGiKOG0033. Eukaryota.
ENOG410XNRX. LUCA.
GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiP11730.
KOiK04515.
PhylomeDBiP11730.

Enzyme and pathway databases

BRENDAi2.7.11.17. 5301.
ReactomeiR-RNO-3371571. HSF1-dependent transactivation.
R-RNO-399719. Trafficking of AMPA receptors.
R-RNO-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-RNO-442729. CREB phosphorylation through the activation of CaMKII.
R-RNO-442742. CREB phosphorylation through the activation of Ras.
R-RNO-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-RNO-5576892. Phase 0 - rapid depolarisation.
R-RNO-5578775. Ion homeostasis.
R-RNO-5673001. RAF/MAP kinase cascade.
R-RNO-877300. Interferon gamma signaling.
R-RNO-936837. Ion transport by P-type ATPases.

Miscellaneous databases

NextBioi621932.
PROiP11730.

Gene expression databases

ExpressionAtlasiP11730. baseline and differential.
GenevisibleiP11730. RN.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR032710. NTF2-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 2 hits.
PfamiPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-321; SER-325; SER-329; SER-355 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKCC2G_RAT
AccessioniPrimary (citable) accession number: P11730
Secondary accession number(s): Q64003, Q64004
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 11, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.