Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q13555 (KCC2G_HUMAN)

Last modified February 9, 2010. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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: CAMKG
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

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

Hide | Top

General annotation (Comments)

Function

CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Autophosphorylation of CAMK2 plays an important role in the regulation of the kinase activity.

Subunit structure

CAMK2 is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits.

Sequence similarities

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

Contains 1 protein kinase domain.

Hide | Top

Alternative products

This entry describes 9 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.
Isoform 3 (identifier: Q13555-3)

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

Hide | Top

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
Region291 – 30111Calmodulin-binding By similarity

Sites

Active site1361Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue2351Phosphoserine By similarity
Modified residue2871Phosphothreonine Ref.8 Ref.11
Modified residue3071Phosphothreonine
Modified residue3111Phosphoserine
Modified residue3151Phosphoserine Ref.9
Modified residue3191Phosphoserine Ref.9
Modified residue3251Phosphoserine Ref.10
Modified residue3491Phosphoserine Ref.10
Modified residue3521Phosphoserine
Modified residue3751Phosphothreonine
Modified residue3811Phosphoserine
Modified residue3821Phosphothreonine
Modified residue3841Phosphoserine
Modified residue3871Phosphothreonine
Modified residue3881Phosphothreonine
Modified residue4191Phosphoserine

Natural variations

Alternative sequence3151S → SVGRQSSAPASPAASAAGLA GQ in isoform 5 and isoform 6.
VSP_032699
Alternative sequence331 – 36434Missing in isoform 3 and isoform 7.
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 and isoform 5.
VSP_004778
Alternative sequence397 – 3982RS → APLRTGNGSSV in isoform 6, isoform 7, isoform 8 and isoform 9.
VSP_035456
Natural variant361S → P: dbSNP rs17853266. Ref.2 Ref.3
VAR_042430

Secondary structure

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

Details...

Hide | Top

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.

Checksum: 1A1B6D508CF3D210
Show »

FASTA54761,368
Isoform 3.

Checksum: 75E1E7B03A01C061
Show »

FASTA52458,963
Isoform 4.

Checksum: EE1D127BBA178544
Show »

FASTA52959,607
Isoform 5.

Checksum: 58DBF1B72F64FA31
Show »

FASTA52759,038
Isoform 6.

Checksum: 2B608F45E8FD3F86
Show »

FASTA58865,242
Isoform 7 (gamma F).

Checksum: 864E8CCF92872FB3
Show »

FASTA53359,760
Isoform 8 (gamma E).

Checksum: B0E88BF9F07715CB
Show »

FASTA55662,165
Isoform 9 (gamma D).

Checksum: 99F906D2A0BBCA36
Show »

FASTA54260,743

Hide | Top

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: 15164054] [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: 15489334] [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: 9240463] [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: 12032636] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-558, ALTERNATIVE SPLICING (ISOFORM 6).
[6]"Identification of novel human tumor cell-specific CaMK-II variants."
Tombes R.M., Krystal G.W.
Biochim. Biophys. Acta 1355:281-292(1997) [PubMed: 9060999] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-497 (ISOFORMS 2 AND 4).
[7]"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: 7557101] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 326-432 (ISOFORMS 7; 8 AND 9).
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-319, MASS SPECTROMETRY.
[10]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 AND SER-349, MASS SPECTROMETRY.
[11]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, MASS SPECTROMETRY.
[12]"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: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287; THR-307; SER-311; SER-315; SER-319; SER-325; SER-349; SER-352; THR-375; SER-381; THR-382; SER-384; THR-387; THR-388 AND SER-419, MASS SPECTROMETRY.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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: CAI13968.1.
CH471083 Genomic DNA. Translation: EAW54532.1.
BC034044 mRNA. Translation: AAH34044.1.
U66064 mRNA. Translation: AAB80848.1.
AF415197 expand/collapse EMBL AC list , AF415177, AF415178, AF415179, AF415180, AF415181, AF415182, AF415183, AF415184, AF415185, AF415186, AF415187, AF415188, AF415189, AF415190, AF415191, AF415192, AF415193, AF415194, AF415195, AF415196 Genomic DNA. Translation: AAM33514.1.
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.
IPI00556423.
IPI00908444.
IPI00915309.
IPI00915327.
IPI00915383.
IPI00915393.
PIRG01975.
G01978.
RefSeqNP_001213.2.
NP_751909.1.
NP_751911.1.
NP_751913.1.
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[»]
SMRQ13555. Positions 3-302.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ13555.

PTM databases

PhosphoSiteQ13555.

Proteomic databases

PRIDEQ13555.

Genome annotation databases

EnsemblENST00000394763; ENSP00000378244; ENSG00000148660; Homo sapiens. [Genome view]
GeneID818.
KEGGhsa:818.
UCSCuc001jvo.1. human.
uc001jvs.1. human.
uc001jvv.1. human.

Organism-specific databases

CTD818.
GeneCardsGC10M075242.
HGNCHGNC:1463. CAMK2G.
MIM602123. gene.
PharmGKBPA93.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ13555.
InParanoidQ13555.
OMAXPQSNNK.
OrthoDBEOG9T1M5P.
PhylomeDBQ13555.

Enzyme and pathway databases

BRENDA2.7.11.17. 247.
Pathway_Interaction_DBbcr_5pathway. BCR signaling pathway.
ifngpathway. IFN-gamma pathway.
ReactomeREACT_13685. Synaptic Transmission.

Gene expression databases

ArrayExpressQ13555.
BgeeQ13555.
GenevestigatorQ13555.
GermOnlineENSG00000148660. Homo sapiens.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_prot_kinase-like.
IPR015742. Ca/CaM-dep_prot_kinase_2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PANTHERPTHR22982. Ca/CaM-dep_prot_kinase-like. 1 hit.
PTHR22982:SF64. CaMKII. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio3340.
SOURCESearch...

Hide | Top

Entry information

Entry nameKCC2G_HUMAN
AccessionPrimary (citable) accession number: Q13555
Secondary accession number(s): O15378 expand/collapse secondary AC list , Q13279, Q13282, Q13556, Q5SQZ3, Q5SQZ4, Q7KYX5, Q8N4I3, Q8NIA4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 12, 2005
Last modified: February 9, 2010
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Hide | Top

Relevant documents

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents