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Q13555 (KCC2G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium/calmodulin-dependent protein kinase type II subunit gamma
Short name=CaM kinase II subunit gamma
Short name=CaMK-II subunit gamma
EC=2.7.11.17
Gene names
Name:CAMK2G
Synonyms:CAMK, CAMK-II, CAMKG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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. Ref.9

Subunit structure

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. Ref.9

Subcellular location

Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Probable.

Tissue specificity

Expressed in skeletal muscle. Ref.10

Induction

Activity is induced in skeletal muscle during exercise. Ref.9 Ref.10

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentMembrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Compara

calcium ion transport

Inferred from electronic annotation. Source: Compara

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

insulin secretion

Non-traceable author statement Ref.4. Source: UniProtKB

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

protein autophosphorylation

Inferred from electronic annotation. Source: Compara

protein phosphorylation

Non-traceable author statement. Source: UniProtKB

regulation of calcium ion transport

Traceable author statement Ref.11. Source: UniProtKB

regulation of skeletal muscle adaptation

Traceable author statement Ref.11. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcalcium- and calmodulin-dependent protein kinase complex

Traceable author statement PubMed 11264466. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

sarcoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Non-traceable author statement. Source: UniProtKB

calcium-dependent protein serine/threonine phosphatase activity

Non-traceable author statement Ref.7. Source: UniProtKB

calmodulin binding

Non-traceable author statement Ref.7. Source: UniProtKB

calmodulin-dependent protein kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSP90AB1P082382EBI-1383465,EBI-352572

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13555-1)

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.
Isoform 2 (identifier: Q13555-2)

The sequence of this isoform differs from the canonical sequence as follows:
     331-341: Missing.
Note: Contains a phosphoserine at position 325.
Isoform 3 (identifier: Q13555-3)

The sequence of this isoform differs from the canonical sequence as follows:
     331-364: Missing.
Note: Contains a phosphoserine at position 325.
Isoform 4 (identifier: Q13555-4)

The sequence of this isoform differs from the canonical sequence as follows:
     396-425: ARSPEGRSSRDRTAPSAGMQPQPSLCSSAM → V
Isoform 5 (identifier: Q13555-5)

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.
Isoform 6 (identifier: Q13555-6)

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.
Isoform 7 (identifier: Q13555-7)

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.
Isoform 8 (identifier: Q13555-8)

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.
Isoform 9 (identifier: Q13555-9)

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.
Isoform 10 (identifier: Q13555-10)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 558558Calcium/calmodulin-dependent protein kinase type II subunit gamma
PRO_0000086101

Regions

Domain14 – 272259Protein kinase
Nucleotide binding20 – 289ATP By similarity
Region283 – 29210Autoinhibitory domain
Region291 – 30111Calmodulin-binding By similarity
Region294 – 31623Calmodulin-binding

Sites

Active site1361Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue2351Phosphoserine By similarity
Modified residue2871Phosphothreonine; by autocatalysis Ref.10 Ref.14
Modified residue3061Phosphothreonine; by autocatalysis By similarity
Modified residue3071Phosphothreonine; by autocatalysis Probable
Modified residue3111Phosphoserine Ref.12 Ref.14 Ref.15
Modified residue3491Phosphoserine Ref.12
Modified residue3521Phosphoserine Ref.12 Ref.14
Modified residue4191Phosphoserine Ref.12 Ref.14

Natural variations

Alternative sequence3151S → SVGRQSSAPASPAASAAGLA GQ in isoform 5 and isoform 6.
VSP_032699
Alternative sequence331 – 36434Missing in isoform 3, isoform 7 and isoform 10.
VSP_013350
Alternative sequence331 – 34111Missing in isoform 2, isoform 8 and isoform 9.
VSP_013349
Alternative sequence341 – 36323Missing in isoform 5.
VSP_032700
Alternative sequence351 – 36414Missing in isoform 9.
VSP_036027
Alternative sequence396 – 42530ARSPE…CSSAM → V in isoform 4, isoform 5 and isoform 10.
VSP_004778
Alternative sequence397 – 3982RS → APLRTGNGSSV in isoform 6, isoform 7, isoform 8 and isoform 9.
VSP_035456
Natural variant361S → P. Ref.2 Ref.3
Corresponds to variant rs17853266 [ dbSNP | Ensembl ].
VAR_042430

Experimental info

Sequence conflict2301A → T in AAB61379. Ref.6

Secondary structure

1 ................................................................ 558
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 12, 2005. Version 3.
Checksum: 38D4112C2FDBD44C

FASTA55862,609
        10         20         30         40         50         60 
MATTATCTRF TDDYQLFEEL GKGAFSVVRR CVKKTSTQEY AAKIINTKKL SARDHQKLER 

        70         80         90        100        110        120 
EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIHQI 

       130        140        150        160        170        180 
LESVNHIHQH DIVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGEQQA WFGFAGTPGY 

       190        200        210        220        230        240 
LSPEVLRKDP YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT 

       250        260        270        280        290        300 
VTPEAKNLIN QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL 

       310        320        330        340        350        360 
KGAILTTMLV SRNFSAAKSL LNKKSDGGVK KRKSSSSVHL MPQSNNKNSL VSPAQEPAPL 

       370        380        390        400        410        420 
QTAMEPQTTV VHNATDGIKG STESCNTTTE DEDLKARSPE GRSSRDRTAP SAGMQPQPSL 

       430        440        450        460        470        480 
CSSAMRKQEI IKITEQLIEA INNGDFEAYT KICDPGLTSF EPEALGNLVE GMDFHKFYFE 

       490        500        510        520        530        540 
NLLSKNSKPI HTTILNPHVH VIGEDAACIA YIRLTQYIDG QGRPRTSQSE ETRVWHRRDG 

       550 
KWLNVHYHCS GAPAAPLQ

« Hide

Isoform 2 [UniParc].

Checksum: 1A1B6D508CF3D210
Show »

FASTA54761,368
Isoform 3 [UniParc].

Checksum: 75E1E7B03A01C061
Show »

FASTA52458,963
Isoform 4 [UniParc].

Checksum: EE1D127BBA178544
Show »

FASTA52959,607
Isoform 5 [UniParc].

Checksum: 58DBF1B72F64FA31
Show »

FASTA52759,038
Isoform 6 [UniParc].

Checksum: 2B608F45E8FD3F86
Show »

FASTA58865,242
Isoform 7 (gamma F) [UniParc].

Checksum: 864E8CCF92872FB3
Show »

FASTA53359,760
Isoform 8 (gamma E) [UniParc].

Checksum: B0E88BF9F07715CB
Show »

FASTA55662,165
Isoform 9 (gamma D) [UniParc].

Checksum: 99F906D2A0BBCA36
Show »

FASTA54260,743
Isoform 10 [UniParc].

Checksum: 168EA409723DF4C4
Show »

FASTA49555,961

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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), MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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), MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00172450.
IPI00296678.
IPI00334344.
IPI00336118.
IPI00556423.
IPI00908444.
IPI00915309.
IPI00915327.
IPI00915383.
IPI00915393.
PIRG01975.
G01978.
RefSeqNP_001213.2. NM_001222.3.
NP_751909.1. NM_172169.2.
NP_751913.1. NM_172173.2.
UniGeneHs.523045.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2UX0X-ray2.46A/B/C/D/E/F426-556[»]
2V7OX-ray2.25A5-315[»]
ProteinModelPortalQ13555.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-51315N.
IntActQ13555. 2 interactions.

PTM databases

PhosphoSiteQ13555.

Polymorphism databases

DMDM62512173.

Proteomic databases

PaxDbQ13555.
PRIDEQ13555.

Protocols and materials databases

DNASU818.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305762; ENSP00000307082; ENSG00000148660.
ENST00000322635; ENSP00000315599; ENSG00000148660.
ENST00000322680; ENSP00000319060; ENSG00000148660.
ENST00000351293; ENSP00000277853; ENSG00000148660.
ENST00000394762; ENSP00000378243; ENSG00000148660.
ENST00000423381; ENSP00000410298; ENSG00000148660.
GeneID818.
KEGGhsa:818.
UCSCuc001jvm.2. human.
uc001jvo.2. human.
uc001jvq.2. human.

Organism-specific databases

CTD818.
GeneCardsGC10M075572.
HGNCHGNC:1463. CAMK2G.
MIM602123. gene.
neXtProtNX_Q13555.
PharmGKBPA93.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108055.
InParanoidQ13555.
KOK04515.
OMACIPSVGR.

Enzyme and pathway databases

Pathway_Interaction_DBbcr_5pathway. BCR signaling pathway.
ifngpathway. IFN-gamma pathway.
ReactomeREACT_13685. Neuronal System.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ13555.
BgeeQ13555.
GenevestigatorQ13555.
GermOnlineENSG00000148660. Homo sapiens.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ13555.
ChEMBLCHEMBL3829.
ChiTaRSCAMK2G. human.
EvolutionaryTraceQ13555.
GenomeRNAi818.
NextBio3340.
SOURCESearch...

Entry information

Entry nameKCC2G_HUMAN
AccessionPrimary (citable) accession number: Q13555
Secondary accession number(s): O00561 expand/collapse secondary AC list , O15378, Q13279, Q13282, Q13556, Q5SQZ3, Q5SQZ4, Q5SWX4, Q7KYX5, Q8N4I3, Q8NIA4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 12, 2005
Last modified: May 1, 2013
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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