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Protein

Calcium/calmodulin-dependent protein kinase type II subunit gamma

Gene

CAMK2G

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca2+/calmodulin-binding and autophosphorylation, and is involved in sarcoplsamic 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.1 Publication

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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43ATPPROSITE-ProRule annotation1
Active sitei136Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 28ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionCalmodulin-binding, Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase
Biological processDifferentiation, Neurogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17 2681
ReactomeiR-HSA-3371571 HSF1-dependent transactivation
R-HSA-399719 Trafficking of AMPA receptors
R-HSA-438066 Unblocking of NMDA receptor, glutamate binding and activation
R-HSA-442729 CREB phosphorylation through the activation of CaMKII
R-HSA-442742 CREB phosphorylation through the activation of Ras
R-HSA-442982 Ras activation upon Ca2+ influx through NMDA receptor
R-HSA-5576892 Phase 0 - rapid depolarisation
R-HSA-5578775 Ion homeostasis
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-877300 Interferon gamma signaling
R-HSA-936837 Ion transport by P-type ATPases
SignaLinkiQ13555
SIGNORiQ13555

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
Synonyms:CAMK, CAMK-II, CAMKG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi

Organism-specific databases

EuPathDBiHostDB:ENSG00000148660.20
HGNCiHGNC:1463 CAMK2G
MIMi602123 gene
neXtProtiNX_Q13555

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

DisGeNETi818
OpenTargetsiENSG00000148660
PharmGKBiPA93

Chemistry databases

ChEMBLiCHEMBL3829
DrugBankiDB06616 Bosutinib
GuidetoPHARMACOLOGYi1557

Polymorphism and mutation databases

BioMutaiCAMK2G
DMDMi62512173

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000861011 – 558Calcium/calmodulin-dependent protein kinase type II subunit gammaAdd BLAST558

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei287Phosphothreonine; by autocatalysisCombined sources1 Publication1
Modified residuei306Phosphothreonine; by autocatalysisBy similarity1
Modified residuei307Phosphothreonine; by autocatalysisCurated1
Modified residuei311PhosphoserineCombined sources1
Modified residuei334PhosphoserineBy similarity1
Modified residuei349PhosphoserineCombined sources1
Modified residuei352PhosphoserineCombined sources1
Modified residuei419PhosphoserineCombined sources1
Modified residuei484PhosphoserineBy similarity1
Isoform 2 (identifier: Q13555-2)
Modified residuei325PhosphoserineCombined sources1
Isoform 3 (identifier: Q13555-3)
Modified residuei325PhosphoserineCombined sources1
Isoform 5 (identifier: Q13555-5)
Modified residuei325PhosphoserineCombined sources1
Isoform 6 (identifier: Q13555-6)
Modified residuei325PhosphoserineCombined sources1
Isoform 7 (identifier: Q13555-7)
Modified residuei325PhosphoserineCombined sources1
Isoform 8 (identifier: Q13555-8)
Modified residuei325PhosphoserineCombined sources1
Isoform 9 (identifier: Q13555-9)
Modified residuei325PhosphoserineCombined sources1
Modified residuei338PhosphoserineCombined sources1
Isoform 10 (identifier: Q13555-10)
Modified residuei325PhosphoserineCombined sources1
Isoform 11 (identifier: Q13555-11)
Modified residuei325PhosphoserineCombined sources1

Post-translational modificationi

Autophosphorylation of Thr-287 following activation by Ca2+/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ13555
MaxQBiQ13555
PaxDbiQ13555
PeptideAtlasiQ13555
PRIDEiQ13555

PTM databases

iPTMnetiQ13555
PhosphoSitePlusiQ13555

Expressioni

Tissue specificityi

Expressed in skeletal muscle.1 Publication

Inductioni

Activity is induced in skeletal muscle during exercise.1 Publication

Gene expression databases

BgeeiENSG00000148660
ExpressionAtlasiQ13555 baseline and differential
GenevisibleiQ13555 HS

Organism-specific databases

HPAiHPA040656
HPA051783
HPA051785
HPA053973

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.2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • calmodulin binding Source: GO_Central
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome

Protein-protein interaction databases

BioGridi107268, 50 interactors
DIPiDIP-51315N
IntActiQ13555, 40 interactors
MINTiQ13555
STRINGi9606.ENSP00000319060

Chemistry databases

BindingDBiQ13555

Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 13Combined sources5
Beta strandi14 – 22Combined sources9
Beta strandi26 – 33Combined sources8
Turni34 – 37Combined sources4
Beta strandi38 – 46Combined sources9
Helixi52 – 67Combined sources16
Beta strandi76 – 81Combined sources6
Beta strandi83 – 91Combined sources9
Helixi98 – 103Combined sources6
Helixi110 – 129Combined sources20
Helixi139 – 141Combined sources3
Beta strandi142 – 145Combined sources4
Beta strandi153 – 155Combined sources3
Helixi178 – 180Combined sources3
Helixi183 – 187Combined sources5
Helixi194 – 209Combined sources16
Helixi219 – 227Combined sources9
Helixi237 – 240Combined sources4
Helixi243 – 252Combined sources10
Turni257 – 259Combined sources3
Helixi263 – 266Combined sources4
Helixi270 – 273Combined sources4
Helixi275 – 278Combined sources4
Helixi285 – 301Combined sources17
Helixi425 – 443Combined sources19
Helixi446 – 452Combined sources7
Beta strandi453 – 460Combined sources8
Helixi462 – 464Combined sources3
Beta strandi468 – 470Combined sources3
Helixi471 – 481Combined sources11
Turni482 – 485Combined sources4
Beta strandi490 – 501Combined sources12
Beta strandi506 – 518Combined sources13
Beta strandi524 – 538Combined sources15
Beta strandi541 – 550Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UX0X-ray2.46A/B/C/D/E/F426-558[»]
2V7OX-ray2.25A5-315[»]
ProteinModelPortaliQ13555
SMRiQ13555
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13555

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 272Protein kinasePROSITE-ProRule annotationAdd BLAST259

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni283 – 292Autoinhibitory domain10
Regioni291 – 301Calmodulin-bindingBy similarityAdd BLAST11
Regioni294 – 316Calmodulin-bindingAdd BLAST23

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0033 Eukaryota
ENOG410XNRX LUCA
GeneTreeiENSGT00760000118944
HOVERGENiHBG108055
InParanoidiQ13555
KOiK04515
OMAiSTESCNN
OrthoDBiEOG091G0SCS
PhylomeDBiQ13555
TreeFamiTF315229

Family and domain databases

InterProiView protein in InterPro
IPR013543 Ca/CaM-dep_prot_kinase-assoc
IPR011009 Kinase-like_dom_sf
IPR032710 NTF2-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF08332 CaMKII_AD, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF54427 SSF54427, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (11)i

Sequence statusi: Complete.

This entry describes 11 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13555-1) [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 DEDLKGRVPE
410 420 430 440 450
GRSSRDRTAP SAGMQPQPSL CSSAMRKQEI IKITEQLIEA INNGDFEAYT
460 470 480 490 500
KICDPGLTSF EPEALGNLVE GMDFHKFYFE NLLSKNSKPI HTTILNPHVH
510 520 530 540 550
VIGEDAACIA YIRLTQYIDG QGRPRTSQSE ETRVWHRRDG KWLNVHYHCS

GAPAAPLQ
Length:558
Mass (Da):62,607
Last modified:March 28, 2018 - v4
Checksum:i7D61AB799B8F8CEB
GO
Isoform 2 (identifier: Q13555-2) [UniParc]FASTAAdd to basket

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

Show »
Length:547
Mass (Da):61,366
Checksum:i5FAED70538A78AB7
GO
Isoform 3 (identifier: Q13555-3) [UniParc]FASTAAdd to basket

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

Show »
Length:524
Mass (Da):58,961
Checksum:i30545DE58E5598C6
GO
Isoform 4 (identifier: Q13555-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     396-425: GRVPEGRSSRDRTAPSAGMQPQPSLCSSAM → V

Show »
Length:529
Mass (Da):59,607
Checksum:iEE1D127BBA178544
GO
Isoform 5 (identifier: Q13555-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     315-315: S → SVGRQSSAPASPAASAAGLAGQ
     341-363: Missing.
     396-425: GRVPEGRSSRDRTAPSAGMQPQPSLCSSAM → V

Show »
Length:527
Mass (Da):59,038
Checksum:i58DBF1B72F64FA31
GO
Isoform 6 (identifier: Q13555-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     315-315: S → SVGRQSSAPASPAASAAGLAGQ
     397-398: RV → APLRTGNGSSV

Show »
Length:588
Mass (Da):65,228
Checksum:i6244199DF09FCF38
GO
Isoform 7 (identifier: Q13555-7) [UniParc]FASTAAdd to basket
Also known as: gamma F

The sequence of this isoform differs from the canonical sequence as follows:
     331-364: Missing.
     397-398: RV → APLRTGNGSSV

Show »
Length:533
Mass (Da):59,746
Checksum:iCF6A1A178AE5DF0D
GO
Isoform 8 (identifier: Q13555-8) [UniParc]FASTAAdd to basket
Also known as: gamma E

The sequence of this isoform differs from the canonical sequence as follows:
     331-341: Missing.
     397-398: RV → APLRTGNGSSV

Show »
Length:556
Mass (Da):62,151
Checksum:iF9CC1D21E815E575
GO
Isoform 9 (identifier: Q13555-9) [UniParc]FASTAAdd to basket
Also known as: gamma D

The sequence of this isoform differs from the canonical sequence as follows:
     331-341: Missing.
     351-364: Missing.
     397-398: RV → APLRTGNGSSV

Show »
Length:542
Mass (Da):60,729
Checksum:iD0DD900AB8D93A88
GO
Isoform 10 (identifier: Q13555-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     331-364: Missing.
     396-425: GRVPEGRSSRDRTAPSAGMQPQPSLCSSAM → V

Show »
Length:495
Mass (Da):55,961
Checksum:i168EA409723DF4C4
GO
Isoform 11 (identifier: Q13555-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     316-316: A → VGRQSSAPASPAASAAGLAGQA
     331-341: Missing.
     396-426: GRVPEGRSSRDRTAPSAGMQPQPSLCSSAMR → VR

Show »
Length:539
Mass (Da):60,201
Checksum:i24989285F7564529
GO

Sequence cautioni

The sequence AAB61379 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti230A → T in AAB61379 (PubMed:8449910).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04243036S → P2 PublicationsCorresponds to variant dbSNP:rs17853266Ensembl.1
Natural variantiVAR_069390292R → P Found in a patient with severe mental retardation, myopia, strabismus; unknown pathological significance. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_032699315S → SVGRQSSAPASPAASAAGLA GQ in isoform 5 and isoform 6. 1 Publication1
Alternative sequenceiVSP_059393316A → VGRQSSAPASPAASAAGLAG QA in isoform 11. 1
Alternative sequenceiVSP_013350331 – 364Missing in isoform 3, isoform 7 and isoform 10. 2 PublicationsAdd BLAST34
Alternative sequenceiVSP_013349331 – 341Missing in isoform 2, isoform 8, isoform 9 and isoform 11. 2 PublicationsAdd BLAST11
Alternative sequenceiVSP_032700341 – 363Missing in isoform 5. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_036027351 – 364Missing in isoform 9. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_059394396 – 426GRVPE…SSAMR → VR in isoform 11. Add BLAST31
Alternative sequenceiVSP_004778396 – 425GRVPE…CSSAM → V in isoform 4, isoform 5 and isoform 10. 3 PublicationsAdd BLAST30
Alternative sequenceiVSP_035456397 – 398RV → APLRTGNGSSV in isoform 6, isoform 7, isoform 8 and isoform 9. 1 Publication2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC022400 Genomic DNA No translation available.
AL596247 Genomic DNA No translation available.
AL713896 Genomic DNA No translation available.
KF455257 Genomic DNA No translation available.
CH471083 Genomic DNA Translation: EAW54527.1
CH471083 Genomic DNA Translation: EAW54532.1
CH471083 Genomic DNA Translation: EAW54536.1
BC034044 mRNA Translation: AAH34044.1
U66064 mRNA Translation: AAB80848.1
AH011636 Genomic DNA Translation: AAM33514.1
L07043 mRNA Translation: AAB61379.1 Different initiation.
U50359 mRNA Translation: AAB16864.1
U50360 mRNA Translation: AAB16865.1
U32472 mRNA Translation: AAA75201.1
U32473 mRNA Translation: AAA75202.1
U32509 mRNA Translation: AAA75203.1
CCDSiCCDS73153.1 [Q13555-11]
CCDS7336.1 [Q13555-10]
CCDS7337.1 [Q13555-5]
CCDS7338.1 [Q13555-8]
PIRiG01975
G01978
RefSeqiNP_001191421.1, NM_001204492.1 [Q13555-11]
NP_001213.2, NM_001222.3 [Q13555-10]
NP_001307827.1, NM_001320898.1
NP_751909.1, NM_172169.2 [Q13555-5]
NP_751913.1, NM_172173.2
XP_005270260.1, XM_005270203.1 [Q13555-4]
UniGeneiHs.523045
Hs.654811

Genome annotation databases

EnsembliENST00000305762; ENSP00000307082; ENSG00000148660 [Q13555-4]
ENST00000322635; ENSP00000315599; ENSG00000148660 [Q13555-5]
ENST00000351293; ENSP00000277853; ENSG00000148660 [Q13555-10]
ENST00000394762; ENSP00000378243; ENSG00000148660 [Q13555-11]
ENST00000423381; ENSP00000410298; ENSG00000148660 [Q13555-1]
GeneIDi818
KEGGihsa:818
UCSCiuc001jvm.2 human [Q13555-1]
uc001jvs.2 human

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiKCC2G_HUMAN
AccessioniPrimary (citable) accession number: Q13555
Secondary accession number(s): A0A0A0MS52
, A0A0A0MT11, O00561, O15378, Q13279, Q13282, Q13556, Q5SQZ3, Q5SQZ4, Q5SWX4, Q7KYX5, Q8N4I3, Q8NIA4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 28, 2018
Last modified: May 23, 2018
This is version 185 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

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