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Protein

Calcium/calmodulin-dependent protein kinase type II subunit gamma

Gene

CAMK2G

Organism
Homo sapiens (Human)
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 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

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

BioCyciZFISH:HS07546-MONOMER.
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 uopn Ca2+ infux 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
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:1463. CAMK2G.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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 residuei381PhosphoserineBy similarity1
Modified residuei384PhosphoserineBy similarity1
Modified residuei387PhosphothreonineBy similarity1
Modified residuei388PhosphothreonineBy similarity1
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

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

HPAiHPA051783.
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

WithEntry#Exp.IntActNotes
CAMK2BQ13554-34EBI-12020154,EBI-11523526
CAMK2DQ13557-84EBI-12020154,EBI-11534483
HSP90AB1P082382EBI-1383465,EBI-352572

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi107268. 44 interactors.
DIPiDIP-51315N.
IntActiQ13555. 38 interactors.
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
Helixi390 – 397Combined sources8
Helixi427 – 443Combined sources17
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/F389-556[»]
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

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0033. Eukaryota.
ENOG410XNRX. LUCA.
GeneTreeiENSGT00760000118944.
HOVERGENiHBG108055.
InParanoidiQ13555.
KOiK04515.
PhylomeDBiQ13555.
TreeFamiTF315229.

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. 3 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 (10)i

Sequence statusi: Complete.

This entry describes 10 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 DEDLKARSPE
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):62,609
Last modified:April 12, 2005 - v3
Checksum:i38D4112C2FDBD44C
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):61,368
Checksum:i1A1B6D508CF3D210
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):58,963
Checksum:i75E1E7B03A01C061
GO
Isoform 4 (identifier: Q13555-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     396-425: ARSPEGRSSRDRTAPSAGMQPQPSLCSSAM → 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: ARSPEGRSSRDRTAPSAGMQPQPSLCSSAM → 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: RS → APLRTGNGSSV

Show »
Length:588
Mass (Da):65,242
Checksum:i2B608F45E8FD3F86
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: RS → APLRTGNGSSV

Show »
Length:533
Mass (Da):59,760
Checksum:i864E8CCF92872FB3
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: RS → APLRTGNGSSV

Show »
Length:556
Mass (Da):62,165
Checksum:iB0E88BF9F07715CB
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: RS → APLRTGNGSSV

Show »
Length:542
Mass (Da):60,743
Checksum:i99F906D2A0BBCA36
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: ARSPEGRSSRDRTAPSAGMQPQPSLCSSAM → V

Show »
Length:495
Mass (Da):55,961
Checksum:i168EA409723DF4C4
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 → P.2 PublicationsCorresponds to variant rs17853266dbSNPEnsembl.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_013350331 – 364Missing in isoform 3, isoform 7 and isoform 10. 2 PublicationsAdd BLAST34
Alternative sequenceiVSP_013349331 – 341Missing in isoform 2, isoform 8 and isoform 9. 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_004778396 – 425ARSPE…CSSAM → V in isoform 4, isoform 5 and isoform 10. 3 PublicationsAdd BLAST30
Alternative sequenceiVSP_035456397 – 398RS → APLRTGNGSSV in isoform 6, isoform 7, isoform 8 and isoform 9. 1 Publication2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL713896, AC022400, AL596247 Genomic DNA. Translation: CAI13789.1.
AL713896, AC022400, AL596247 Genomic DNA. Translation: CAI13790.1.
AL713896, AC022400, AL596247 Genomic DNA. Translation: CAI13791.1.
AL596247, AC022400, AL713896 Genomic DNA. Translation: CAI13965.1.
AL596247, AC022400, AL713896 Genomic DNA. Translation: CAI13966.1.
AL596247, AC022400, AL713896 Genomic DNA. Translation: CAI13968.1.
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.
CCDSiCCDS7336.1. [Q13555-10]
CCDS7337.1. [Q13555-5]
CCDS7338.1. [Q13555-8]
PIRiG01975.
G01978.
RefSeqiNP_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_005270258.1. XM_005270201.1. [Q13555-9]
XP_005270260.1. XM_005270203.1. [Q13555-4]
XP_006718056.1. XM_006717993.1. [Q13555-6]
UniGeneiHs.523045.
Hs.654811.

Genome annotation databases

EnsembliENST00000305762; ENSP00000307082; ENSG00000148660. [Q13555-4]
ENST00000322635; ENSP00000315599; ENSG00000148660. [Q13555-5]
ENST00000322680; ENSP00000319060; ENSG00000148660. [Q13555-8]
ENST00000351293; ENSP00000277853; ENSG00000148660. [Q13555-10]
GeneIDi818.
KEGGihsa:818.
UCSCiuc001jvm.2. human. [Q13555-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL713896, AC022400, AL596247 Genomic DNA. Translation: CAI13789.1.
AL713896, AC022400, AL596247 Genomic DNA. Translation: CAI13790.1.
AL713896, AC022400, AL596247 Genomic DNA. Translation: CAI13791.1.
AL596247, AC022400, AL713896 Genomic DNA. Translation: CAI13965.1.
AL596247, AC022400, AL713896 Genomic DNA. Translation: CAI13966.1.
AL596247, AC022400, AL713896 Genomic DNA. Translation: CAI13968.1.
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.
CCDSiCCDS7336.1. [Q13555-10]
CCDS7337.1. [Q13555-5]
CCDS7338.1. [Q13555-8]
PIRiG01975.
G01978.
RefSeqiNP_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_005270258.1. XM_005270201.1. [Q13555-9]
XP_005270260.1. XM_005270203.1. [Q13555-4]
XP_006718056.1. XM_006717993.1. [Q13555-6]
UniGeneiHs.523045.
Hs.654811.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UX0X-ray2.46A/B/C/D/E/F389-556[»]
2V7OX-ray2.25A5-315[»]
ProteinModelPortaliQ13555.
SMRiQ13555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107268. 44 interactors.
DIPiDIP-51315N.
IntActiQ13555. 38 interactors.
STRINGi9606.ENSP00000319060.

Chemistry databases

BindingDBiQ13555.
ChEMBLiCHEMBL3829.
DrugBankiDB06616. Bosutinib.
GuidetoPHARMACOLOGYi1557.

PTM databases

iPTMnetiQ13555.
PhosphoSitePlusiQ13555.

Polymorphism and mutation databases

BioMutaiCAMK2G.
DMDMi62512173.

Proteomic databases

EPDiQ13555.
MaxQBiQ13555.
PaxDbiQ13555.
PeptideAtlasiQ13555.
PRIDEiQ13555.

Protocols and materials databases

DNASUi818.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305762; ENSP00000307082; ENSG00000148660. [Q13555-4]
ENST00000322635; ENSP00000315599; ENSG00000148660. [Q13555-5]
ENST00000322680; ENSP00000319060; ENSG00000148660. [Q13555-8]
ENST00000351293; ENSP00000277853; ENSG00000148660. [Q13555-10]
GeneIDi818.
KEGGihsa:818.
UCSCiuc001jvm.2. human. [Q13555-1]

Organism-specific databases

CTDi818.
DisGeNETi818.
GeneCardsiCAMK2G.
HGNCiHGNC:1463. CAMK2G.
HPAiHPA051783.
HPA051785.
HPA053973.
MIMi602123. gene.
neXtProtiNX_Q13555.
OpenTargetsiENSG00000148660.
PharmGKBiPA93.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0033. Eukaryota.
ENOG410XNRX. LUCA.
GeneTreeiENSGT00760000118944.
HOVERGENiHBG108055.
InParanoidiQ13555.
KOiK04515.
PhylomeDBiQ13555.
TreeFamiTF315229.

Enzyme and pathway databases

BioCyciZFISH:HS07546-MONOMER.
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 uopn Ca2+ infux 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.

Miscellaneous databases

ChiTaRSiCAMK2G. human.
EvolutionaryTraceiQ13555.
GeneWikiiCAMK2G.
GenomeRNAii818.
PROiQ13555.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000148660.
ExpressionAtlasiQ13555. baseline and differential.
GenevisibleiQ13555. HS.

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. 3 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...

Entry informationi

Entry nameiKCC2G_HUMAN
AccessioniPrimary (citable) accession number: Q13555
Secondary accession number(s): O00561
, O15378, Q13279, Q13282, Q13556, Q5SQZ3, Q5SQZ4, Q5SWX4, Q7KYX5, Q8N4I3, Q8NIA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 12, 2005
Last modified: November 30, 2016
This is version 172 of the entry and version 3 of the sequence. [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

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.