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Protein

Calcium/calmodulin-dependent protein kinase type II subunit gamma

Gene

Camk2g

Organism
Mus musculus (Mouse)
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

GO - Biological processi

  • calcium ion transport Source: MGI
  • cell differentiation Source: UniProtKB-KW
  • G1/S transition of mitotic cell cycle Source: MGI
  • nervous system development Source: UniProtKB-KW
  • protein autophosphorylation Source: MGI
  • protein oligomerization Source: MGI
  • regulation of relaxation of cardiac muscle Source: BHF-UCL
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. 3474.
ReactomeiREACT_288168. HSF1-dependent transactivation.
REACT_309838. CREB phosphorylation through the activation of CaMKII.
REACT_327612. CREB phosphorylation through the activation of Ras.
REACT_331187. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_331823. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_349056. Interferon gamma signaling.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:88259. Camk2g.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: MGI
  • neuronal postsynaptic density Source: MGI
  • sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Calcium/calmodulin-dependent protein kinase type II subunit gammaPRO_0000086102Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphotyrosineBy similarity
Modified residuei287 – 2871Phosphothreonine; by autocatalysis1 Publication
Modified residuei306 – 3061Phosphothreonine; by autocatalysisBy similarity
Modified residuei307 – 3071Phosphothreonine; by autocatalysisBy similarity
Modified residuei311 – 3111PhosphoserineBy similarity
Modified residuei349 – 3491PhosphoserineBy similarity
Modified residuei352 – 3521PhosphoserineBy similarity

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

MaxQBiQ923T9.
PRIDEiQ923T9.

PTM databases

PhosphoSiteiQ923T9.

Expressioni

Gene expression databases

BgeeiQ923T9.
ExpressionAtlasiQ923T9. baseline and differential.
GenevisibleiQ923T9. MM.

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

BioGridi198463. 1 interaction.
IntActiQ923T9. 4 interactions.
MINTiMINT-4099582.
STRINGi10090.ENSMUSP00000071720.

Structurei

3D structure databases

ProteinModelPortaliQ923T9.
SMRiQ923T9. Positions 3-302, 317-525.
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

GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiQ923T9.
KOiK04515.
OMAiDCIPSVG.
OrthoDBiEOG7ZD1VM.
PhylomeDBiQ923T9.
TreeFamiTF315229.

Family and domain databases

InterProiIPR020636. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. 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 1 (identifier: Q923T9-1) [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 SRNFSAAKSL LNKKSDGGVK KRKSSSSVHL MPQSNNKNSL
360 370 380 390 400
VSPAQEPAPL QTAMEPQTTV VHNATDGIKG STESCNTTTE DEDLKVRKQE
410 420 430 440 450
IIKITEQLIE AINNGDFEAY TKICDPGLTS FEPEALGNLV EGMDFHKFYF
460 470 480 490 500
ENLLSKNSKP IHTTILNPHV HVIGEDAACI AYIRLTQYID GQGRPRTSQS
510 520
EETRVWHRRD GKWLNVHYHC SGAPAAPLQ
Length:529
Mass (Da):59,607
Last modified:December 1, 2001 - v1
Checksum:iEE1D127BBA178544
GO
Isoform 2 (identifier: Q923T9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     331-341: Missing.

Show »
Length:518
Mass (Da):58,365
Checksum:i127250AF541196BF
GO
Isoform 3 (identifier: Q923T9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     331-364: Missing.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei331 – 36434Missing in isoform 3. 1 PublicationVSP_004780Add
BLAST
Alternative sequencei331 – 34111Missing in isoform 2. 2 PublicationsVSP_004779Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF395884 mRNA. Translation: AAK84142.1.
AK154764 mRNA. Translation: BAE32813.1.
BC019162 mRNA. Translation: AAH19162.1.
BC025597 mRNA. Translation: AAH25597.1.
CCDSiCCDS26855.1. [Q923T9-2]
CCDS26856.1. [Q923T9-3]
CCDS26857.1. [Q923T9-1]
RefSeqiNP_001034227.1. NM_001039138.2. [Q923T9-2]
NP_001034228.1. NM_001039139.2. [Q923T9-3]
NP_848712.2. NM_178597.5. [Q923T9-1]
UniGeneiMm.235182.

Genome annotation databases

EnsembliENSMUST00000071816; ENSMUSP00000071720; ENSMUSG00000021820. [Q923T9-1]
ENSMUST00000080440; ENSMUSP00000079298; ENSMUSG00000021820. [Q923T9-2]
GeneIDi12325.
KEGGimmu:12325.
UCSCiuc007skt.2. mouse. [Q923T9-1]
uc007sku.2. mouse. [Q923T9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF395884 mRNA. Translation: AAK84142.1.
AK154764 mRNA. Translation: BAE32813.1.
BC019162 mRNA. Translation: AAH19162.1.
BC025597 mRNA. Translation: AAH25597.1.
CCDSiCCDS26855.1. [Q923T9-2]
CCDS26856.1. [Q923T9-3]
CCDS26857.1. [Q923T9-1]
RefSeqiNP_001034227.1. NM_001039138.2. [Q923T9-2]
NP_001034228.1. NM_001039139.2. [Q923T9-3]
NP_848712.2. NM_178597.5. [Q923T9-1]
UniGeneiMm.235182.

3D structure databases

ProteinModelPortaliQ923T9.
SMRiQ923T9. Positions 3-302, 317-525.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198463. 1 interaction.
IntActiQ923T9. 4 interactions.
MINTiMINT-4099582.
STRINGi10090.ENSMUSP00000071720.

PTM databases

PhosphoSiteiQ923T9.

Proteomic databases

MaxQBiQ923T9.
PRIDEiQ923T9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000071816; ENSMUSP00000071720; ENSMUSG00000021820. [Q923T9-1]
ENSMUST00000080440; ENSMUSP00000079298; ENSMUSG00000021820. [Q923T9-2]
GeneIDi12325.
KEGGimmu:12325.
UCSCiuc007skt.2. mouse. [Q923T9-1]
uc007sku.2. mouse. [Q923T9-2]

Organism-specific databases

CTDi818.
MGIiMGI:88259. Camk2g.

Phylogenomic databases

GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiQ923T9.
KOiK04515.
OMAiDCIPSVG.
OrthoDBiEOG7ZD1VM.
PhylomeDBiQ923T9.
TreeFamiTF315229.

Enzyme and pathway databases

BRENDAi2.7.11.17. 3474.
ReactomeiREACT_288168. HSF1-dependent transactivation.
REACT_309838. CREB phosphorylation through the activation of CaMKII.
REACT_327612. CREB phosphorylation through the activation of Ras.
REACT_331187. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_331823. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_349056. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiCamk2g. mouse.
NextBioi280908.
PROiQ923T9.
SOURCEiSearch...

Gene expression databases

BgeeiQ923T9.
ExpressionAtlasiQ923T9. baseline and differential.
GenevisibleiQ923T9. MM.

Family and domain databases

InterProiIPR020636. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. 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. "Identification of a mouse Ca2+/calmodulin-dependent protein kinase II."
    Szendro P.I., Cadenas C., Eichele G.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: NOD.
    Tissue: Dendritic cell.
  3. "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] (ISOFORMS 2 AND 3).
  4. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.

Entry informationi

Entry nameiKCC2G_MOUSE
AccessioniPrimary (citable) accession number: Q923T9
Secondary accession number(s): Q3U3H3, Q8VED3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 141 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.