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Q13555

- KCC2G_HUMAN

UniProt

Q13555 - KCC2G_HUMAN

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Protein
Calcium/calmodulin-dependent protein kinase type II subunit gamma
Gene
CAMK2G, CAMK, CAMK-II, CAMKG
Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATP By similarity
Active sitei136 – 1361Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium-dependent protein serine/threonine phosphatase activity Source: UniProtKB
  3. calmodulin binding Source: UniProtKB
  4. calmodulin-dependent protein kinase activity Source: UniProtKB-EC
  5. protein binding Source: IntAct

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: Ensembl
  2. calcium ion transport Source: Ensembl
  3. cell differentiation Source: UniProtKB-KW
  4. cytokine-mediated signaling pathway Source: Reactome
  5. dephosphorylation Source: GOC
  6. insulin secretion Source: UniProtKB
  7. interferon-gamma-mediated signaling pathway Source: Reactome
  8. nervous system development Source: UniProtKB-KW
  9. protein autophosphorylation Source: Ensembl
  10. regulation of calcium ion transport Source: UniProtKB
  11. regulation of relaxation of cardiac muscle Source: Ensembl
  12. regulation of skeletal muscle adaptation Source: UniProtKB
  13. synaptic transmission Source: Reactome
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

ReactomeiREACT_18307. Trafficking of AMPA receptors.
REACT_200775. HSF1-dependent transactivation.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
REACT_25078. Interferon gamma signaling.
SignaLinkiQ13555.

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
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:1463. CAMK2G.

Subcellular locationi

GO - Cellular componenti

  1. calcium- and calmodulin-dependent protein kinase complex Source: UniProtKB
  2. cytosol Source: Reactome
  3. endocytic vesicle membrane Source: Reactome
  4. nucleoplasm Source: Reactome
  5. plasma membrane Source: Reactome
  6. sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA93.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Calcium/calmodulin-dependent protein kinase type II subunit gamma
PRO_0000086101Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei287 – 2871Phosphothreonine; by autocatalysis2 Publications
Modified residuei306 – 3061Phosphothreonine; by autocatalysis By similarity
Modified residuei307 – 3071Phosphothreonine; by autocatalysis Inferred
Modified residuei311 – 3111Phosphoserine3 Publications
Modified residuei349 – 3491Phosphoserine1 Publication
Modified residuei352 – 3521Phosphoserine2 Publications
Modified residuei419 – 4191Phosphoserine2 Publications

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13555.
PaxDbiQ13555.
PRIDEiQ13555.

PTM databases

PhosphoSiteiQ13555.

Expressioni

Tissue specificityi

Expressed in skeletal muscle.1 Publication

Inductioni

Activity is induced in skeletal muscle during exercise.2 Publications

Gene expression databases

ArrayExpressiQ13555.
BgeeiQ13555.
GenevestigatoriQ13555.

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-1383465,EBI-352572

Protein-protein interaction databases

BioGridi107268. 20 interactions.
DIPiDIP-51315N.
IntActiQ13555. 5 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 135
Beta strandi14 – 229
Beta strandi26 – 338
Turni34 – 374
Beta strandi38 – 469
Helixi52 – 6716
Beta strandi76 – 816
Beta strandi83 – 919
Helixi98 – 1036
Helixi110 – 12920
Helixi139 – 1413
Beta strandi142 – 1454
Beta strandi153 – 1553
Helixi178 – 1803
Helixi183 – 1875
Helixi194 – 20916
Helixi219 – 2279
Helixi237 – 2404
Helixi243 – 25210
Turni257 – 2593
Helixi263 – 2664
Helixi270 – 2734
Helixi275 – 2784
Helixi285 – 30117
Helixi390 – 3978
Helixi427 – 44317
Helixi446 – 4527
Beta strandi453 – 4608
Helixi462 – 4643
Beta strandi468 – 4703
Helixi471 – 48111
Turni482 – 4854
Beta strandi490 – 50112
Beta strandi506 – 51813
Beta strandi524 – 53815
Beta strandi541 – 55010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UX0X-ray2.46A/B/C/D/E/F389-556[»]
2V7OX-ray2.25A5-315[»]
ProteinModelPortaliQ13555.
SMRiQ13555. Positions 3-302, 387-552.

Miscellaneous databases

EvolutionaryTraceiQ13555.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 272259Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni283 – 29210Autoinhibitory domain
Regioni291 – 30111Calmodulin-binding By similarity
Add
BLAST
Regioni294 – 31623Calmodulin-binding
Add
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG108055.
InParanoidiQ13555.
KOiK04515.
OMAiERIRESC.
OrthoDBiEOG7ZD1VM.
PhylomeDBiQ13555.
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_dom.
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 (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. Align

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

MATTATCTRF TDDYQLFEEL GKGAFSVVRR CVKKTSTQEY AAKIINTKKL    50
SARDHQKLER EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE 100
DIVAREYYSE ADASHCIHQI LESVNHIHQH DIVHRDLKPE NLLLASKCKG 150
AAVKLADFGL AIEVQGEQQA WFGFAGTPGY LSPEVLRKDP YGKPVDIWAC 200
GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT VTPEAKNLIN 250
QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL 300
KGAILTTMLV SRNFSAAKSL LNKKSDGGVK KRKSSSSVHL MPQSNNKNSL 350
VSPAQEPAPL QTAMEPQTTV VHNATDGIKG STESCNTTTE DEDLKARSPE 400
GRSSRDRTAP SAGMQPQPSL CSSAMRKQEI IKITEQLIEA INNGDFEAYT 450
KICDPGLTSF EPEALGNLVE GMDFHKFYFE NLLSKNSKPI HTTILNPHVH 500
VIGEDAACIA YIRLTQYIDG QGRPRTSQSE ETRVWHRRDG KWLNVHYHCS 550
GAPAAPLQ 558
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.

Note: Contains a phosphoserine at position 325.

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.

Note: Contains a phosphoserine at position 325.

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

Note: Contains a phosphoserine at position 325.

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

Note: Contains a phosphoserine at position 325.

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

Note: Contains a phosphoserine at position 325.

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

Note: Contains a phosphoserine at position 325.

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

Note: Contains a phosphoserine at position 325. Contains a phosphoserine at position 338.

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

Note: Contains a phosphoserine at position 325.

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

Sequence cautioni

The sequence AAB61379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361S → P.2 Publications
Corresponds to variant rs17853266 [ dbSNP | Ensembl ].
VAR_042430
Natural varianti292 – 2921R → P Found in a patient with severe mental retardation, myopia, strabismus, low ATP production and decreased oxidation velocities. 1 Publication
VAR_069390

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei315 – 3151S → SVGRQSSAPASPAASAAGLA GQ in isoform 5 and isoform 6.
VSP_032699
Alternative sequencei331 – 36434Missing in isoform 3, isoform 7 and isoform 10.
VSP_013350Add
BLAST
Alternative sequencei331 – 34111Missing in isoform 2, isoform 8 and isoform 9.
VSP_013349Add
BLAST
Alternative sequencei341 – 36323Missing in isoform 5.
VSP_032700Add
BLAST
Alternative sequencei351 – 36414Missing in isoform 9.
VSP_036027Add
BLAST
Alternative sequencei396 – 42530ARSPE…CSSAM → V in isoform 4, isoform 5 and isoform 10.
VSP_004778Add
BLAST
Alternative sequencei397 – 3982RS → APLRTGNGSSV in isoform 6, isoform 7, isoform 8 and isoform 9.
VSP_035456

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2301A → T in AAB61379. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_751909.1. NM_172169.2. [Q13555-5]
NP_751913.1. NM_172173.2.
XP_005270258.1. XM_005270201.1. [Q13555-9]
XP_005270259.1. XM_005270202.1. [Q13555-7]
XP_005270260.1. XM_005270203.1. [Q13555-4]
XP_006718056.1. XM_006717993.1. [Q13555-6]
UniGeneiHs.523045.

Genome annotation databases

EnsembliENST00000305762; ENSP00000307082; ENSG00000148660. [Q13555-4]
ENST00000322635; ENSP00000315599; ENSG00000148660. [Q13555-5]
ENST00000322680; ENSP00000319060; ENSG00000148660. [Q13555-8]
ENST00000351293; ENSP00000277853; ENSG00000148660. [Q13555-10]
ENST00000394762; ENSP00000378243; ENSG00000148660. [Q13555-7]
ENST00000423381; ENSP00000410298; ENSG00000148660. [Q13555-6]
GeneIDi818.
KEGGihsa:818.
UCSCiuc001jvm.2. human. [Q13555-8]
uc001jvo.2. human. [Q13555-5]
uc001jvq.2. human. [Q13555-10]

Polymorphism databases

DMDMi62512173.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7336.1. [Q13555-10 ]
CCDS7337.1. [Q13555-5 ]
CCDS7338.1. [Q13555-8 ]
PIRi G01975.
G01978.
RefSeqi NP_001213.2. NM_001222.3. [Q13555-10 ]
NP_751909.1. NM_172169.2. [Q13555-5 ]
NP_751913.1. NM_172173.2.
XP_005270258.1. XM_005270201.1. [Q13555-9 ]
XP_005270259.1. XM_005270202.1. [Q13555-7 ]
XP_005270260.1. XM_005270203.1. [Q13555-4 ]
XP_006718056.1. XM_006717993.1. [Q13555-6 ]
UniGenei Hs.523045.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2UX0 X-ray 2.46 A/B/C/D/E/F 389-556 [» ]
2V7O X-ray 2.25 A 5-315 [» ]
ProteinModelPortali Q13555.
SMRi Q13555. Positions 3-302, 387-552.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107268. 20 interactions.
DIPi DIP-51315N.
IntActi Q13555. 5 interactions.

Chemistry

BindingDBi Q13555.
ChEMBLi CHEMBL2097164.
GuidetoPHARMACOLOGYi 1557.

PTM databases

PhosphoSitei Q13555.

Polymorphism databases

DMDMi 62512173.

Proteomic databases

MaxQBi Q13555.
PaxDbi Q13555.
PRIDEi Q13555.

Protocols and materials databases

DNASUi 818.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305762 ; ENSP00000307082 ; ENSG00000148660 . [Q13555-4 ]
ENST00000322635 ; ENSP00000315599 ; ENSG00000148660 . [Q13555-5 ]
ENST00000322680 ; ENSP00000319060 ; ENSG00000148660 . [Q13555-8 ]
ENST00000351293 ; ENSP00000277853 ; ENSG00000148660 . [Q13555-10 ]
ENST00000394762 ; ENSP00000378243 ; ENSG00000148660 . [Q13555-7 ]
ENST00000423381 ; ENSP00000410298 ; ENSG00000148660 . [Q13555-6 ]
GeneIDi 818.
KEGGi hsa:818.
UCSCi uc001jvm.2. human. [Q13555-8 ]
uc001jvo.2. human. [Q13555-5 ]
uc001jvq.2. human. [Q13555-10 ]

Organism-specific databases

CTDi 818.
GeneCardsi GC10M075572.
HGNCi HGNC:1463. CAMK2G.
MIMi 602123. gene.
neXtProti NX_Q13555.
PharmGKBi PA93.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG108055.
InParanoidi Q13555.
KOi K04515.
OMAi ERIRESC.
OrthoDBi EOG7ZD1VM.
PhylomeDBi Q13555.
TreeFami TF315229.

Enzyme and pathway databases

Reactomei REACT_18307. Trafficking of AMPA receptors.
REACT_200775. HSF1-dependent transactivation.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
REACT_25078. Interferon gamma signaling.
SignaLinki Q13555.

Miscellaneous databases

ChiTaRSi CAMK2G. human.
EvolutionaryTracei Q13555.
GeneWikii CAMK2G.
GenomeRNAii 818.
NextBioi 3340.
PROi Q13555.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13555.
Bgeei Q13555.
Genevestigatori Q13555.

Family and domain databases

InterProi IPR020636. 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_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24347. PTHR24347. 1 hit.
Pfami PF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-36.
  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] (ISOFORM 5), VARIANT PRO-36.
    Tissue: Brain.
  4. "Human islets of Langerhans express multiple isoforms of calcium/calmodulin-dependent protein kinase II."
    Breen M.A., Ashcroft S.J.
    Biochem. Biophys. Res. Commun. 236:473-478(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-315.
  5. "Human calcium/calmodulin-dependent protein kinase II gamma: cloning, genomic structure and detection of variants in subjects with type II diabetes."
    Gloyn A.L., Desai M., Clark A., Levy J.C., Holman R.R., Frayling T.M., Hattersley A.T., Ashcroft S.J.
    Diabetologia 45:580-583(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-558, ALTERNATIVE SPLICING (ISOFORM 6).
  6. "Cloning and analysis of two new isoforms of multifunctional Ca2+/calmodulin-dependent protein kinase. Expression in multiple human tissues."
    Nghiem P., Saati S.M., Martens C.L., Gardner P., Schulman H.
    J. Biol. Chem. 268:5471-5479(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-436 (ISOFORM 10).
  7. "Identification of novel human tumor cell-specific CaMK-II variants."
    Tombes R.M., Krystal G.W.
    Biochim. Biophys. Acta 1355:281-292(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-497 (ISOFORMS 2 AND 4).
  8. "Human biliary epithelial cell line Mz-ChA-1 expresses new isoforms of calmodulin-dependent protein kinase II."
    Kwiatkowski A.P., McGill J.M.
    Gastroenterology 109:1316-1323(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 326-432 (ISOFORMS 7; 8 AND 9).
  9. "Comparative analyses of the three-dimensional structures and enzymatic properties of alpha, beta, gamma and delta isoforms of Ca2+-calmodulin-dependent protein kinase II."
    Gaertner T.R., Kolodziej S.J., Wang D., Kobayashi R., Koomen J.M., Stoops J.K., Waxham M.N.
    J. Biol. Chem. 279:12484-12494(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBUNIT, AUTOPHOSPHORYLATION.
  10. "Ca2+-calmodulin-dependent protein kinase expression and signalling in skeletal muscle during exercise."
    Rose A.J., Kiens B., Richter E.A.
    J. Physiol. (Lond.) 574:889-903(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SKELETAL MUSCLE, PHOSPHORYLATION AT THR-287, FUNCTION IN PHOSPHORYLATION OF PLN, TISSUE SPECIFICITY, INDUCTION.
  11. "The role of calcium and calcium/calmodulin-dependent kinases in skeletal muscle plasticity and mitochondrial biogenesis."
    Chin E.R.
    Proc. Nutrit. Soc. 63:279-286(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN SKELETAL MUSCLE.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-349; SER-352 AND SER-419, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 (ISOFORMS 10; 2; 3; 5; 6; 7; 8 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 (ISOFORM 9), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287; SER-311; SER-352 AND SER-419, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 (ISOFORMS 10; 2; 3; 7; 8 AND 9), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation."
    Rellos P., Pike A.C., Niesen F.H., Salah E., Lee W.H., von Delft F., Knapp S.
    PLoS Biol. 8:E1000426-E1000426(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 5-315 AND 426-556 IN COMPLEX WITH INHIBITOR.
  18. Cited for: VARIANT PRO-292.

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: September 3, 2014
This is version 147 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

External Data

Dasty 3

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