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UniProtKB/Swiss-Prot entry Q00168


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KCC2A_DROME
Primary accession number Q00168
Secondary accession numbers Q59DP1 Q59DP2 Q9V495
Integrated into Swiss-Prot on April 26, 2004
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 75)
Name and origin of the protein
Protein name Calcium/calmodulin-dependent protein kinase type II alpha chain
Synonyms CaM-kinase II alpha chain
EC 2.7.11.17
Gene name
Name: CaMKII
Synonyms: CaM
ORFNames: CG18069
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
PubMed=8380587 [NCBI, ExPASy, EBI, Israel, Japan]
Ohsako S., Nishida Y., Ryo H., Yamauchi T.;
"Molecular characterization and expression of the Drosophila Ca2+/calmodulin-dependent protein kinase II gene. Identification of four forms of the enzyme generated from a single gene by alternative splicing.";
J. Biol. Chem. 268:2052-2062(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
DOI=10.1016/0896-6273(91)90296-C; PubMed=1910789 [NCBI, ExPASy, EBI, Israel, Japan]
Cho K.O., Wall J.B., Pugh P.C., Ito M., Mueller S.A., Kennedy M.B.;
"The alpha subunit of type II Ca2+/calmodulin-dependent protein kinase is highly conserved in Drosophila.";
Neuron 7:439-450(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 347-388.
DOI=10.1111/j.1471-4159.1993.tb13650.x; PubMed=8397298 [NCBI, ExPASy, EBI, Israel, Japan]
Griffith L.C., Greenspan R.J.;
"The diversity of calcium/calmodulin-dependent protein kinase II isoforms in Drosophila is generated by alternative splicing of a single gene.";
J. Neurochem. 61:1534-1537(1993).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND MASS SPECTROMETRY.
TISSUE=Embryo;
DOI=10.1021/pr700696a; PubMed=18327897 [NCBI, ExPASy, EBI, Israel, Japan]
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D13330; BAA02593.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D13331; BAA02594.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D13332; BAA02595.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D13333; BAA02596.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M74583; AAA51459.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014135; AAF59388.3; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014135; AAF59390.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014135; AAN06568.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014135; AAX53595.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S65712; AAB28244.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S65716; AAB28245.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S65717; AAB28246.2; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S65719; AAB28247.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S65724; AAB28248.2; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B44412; B44412.
C44412; JU0270.
D44412; D44412.
RefSeq NP_001014696.1; -.
NP_726633.2; -.
NP_726634.1; -.
NP_726635.2; -.
UniGene Dm.1709
3D structure databases
HSSP P11798; 1HKX. [HSSP ENTRY / PDB]
SMR Q00168; 8-316, 389-515.
ModBase Q00168.
Protein-protein interaction databases
IntAct Q00168; 13.
Enzyme and pathway databases
BRENDA 2.7.11.17; 48.
Organism-specific databases
FlyBase FBgn0004624; CaMKII.
Gene expression databases
ArrayExpress Q00168; -.
GermOnline CG18069; Drosophila melanogaster.
Ontologies
GO
GO:0030424; Cellular component: axon (inferred from direct assay from FlyBase).
GO:0005954; Cellular component: calcium- and calmodulin-dependent protein kinase complex (traceable author statement from UniProtKB).
GO:0030425; Cellular component: dendrite (inferred from direct assay from FlyBase).
GO:0045211; Cellular component: postsynaptic membrane (inferred from direct assay from FlyBase).
GO:0048786; Cellular component: presynaptic active zone (inferred from direct assay from FlyBase).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005516; Molecular function: calmodulin binding (traceable author statement from FlyBase).
GO:0004683; Molecular function: calmodulin-dependent protein kinase activity (inferred from direct assay from FlyBase).
GO:0007616; Biological process: long-term memory (inferred from mutant phenotype from FlyBase).
GO:0008049; Biological process: male courtship behavior (inferred from mutant phenotype from FlyBase).
GO:0007528; Biological process: neuromuscular junction development (non-traceable author statement from FlyBase).
GO:0006468; Biological process: protein amino acid phosphorylation (traceable author statement from FlyBase).
GO:0051489; Biological process: regulation of filopodium assembly (inferred from mutant phenotype from FlyBase).
GO:0007268; Biological process: synaptic transmission (inferred from mutant phenotype from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR015742; Ca/calmodulin-dep_kinase.
IPR013543; Ca/calmodulin-dep_kinase-assoc.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
PANTHER PTHR22982:SF64; CaMKII; 1.
Pfam PF08332; CaMKII_AD; 1.
PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q00168; -.
Genome annotation databases
Ensembl FBgn0004624; Drosophila melanogaster. [Contig view]
GeneID 43828; -.
KEGG dme:Dmel_CG18069; -.
Phylogenomic databases
HOGENOM Q00168; -.
OMA Q00168; PIHTILL.
Other
NextBio 836100; -.
ProtoNet Q00168.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Calmodulin-binding; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   530  530     Calcium/calmodulin-dependent protein kinase type II alpha chain. PRO_0000086095
DOMAIN   12   272  261     Protein kinase. 
NP_BIND   20    28  9     ATP (By similarity). 
REGION   291   301  11     Calmodulin-binding. 
ACT_SITE   136   136        Proton acceptor (By similarity). 
BINDING   43    43        ATP (By similarity). 
MOD_RES   287   287        Phosphothreonine; by autocatalysis (By similarity). 
MOD_RES   327   327        Phosphoserine. 
VAR_SEQ   347   386        Missing (in isoform 4). VSP_050261
VAR_SEQ   366   387        DIRILCPAKTYQQNIGNSQCSS -> VNLFTNKA (in isoform 2). VSP_050262
VAR_SEQ   366   387        DIRILCPAKTYQQNIGNSQCSS -> A (in isoform 3). VSP_050263
VAR_SEQ   387   387        S -> A (in isoform 4). VSP_050264
Sequence information
Length: 530 AA [This is the length of the unprocessed precursor] Molecular weight: 59920 Da [This is the MW of the unprocessed precursor] CRC64: 4F3D83582ABDFCFD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAPAACTRF SDNYDIKEEL GKGAFSIVKR CVQKSTGFEF AAKIINTKKL TARDFQKLER 

        70         80         90        100        110        120 
EARICRKLHH PNIVRLHDSI QEENYHYLVF DLVTGGELFE DIVAREFYSE ADASHCIQQI 

       130        140        150        160        170        180 
LESVNHCHQN GVVHRDLKPE NLLLASKAKG AAVKLADFGL AIEVQGDHQA WFGFAGTPGY 

       190        200        210        220        230        240 
LSPEVLKKEP YGKSVDIWAC GVILYILLVG YPPFWDEDQH RLYSQIKAGA YDYPSPEWDT 

       250        260        270        280        290        300 
VTPEAKNLIN QMLTVNPNKR ITAAEALKHP WICQRERVAS VVHRQETVDC LKKFNARRKL 

       310        320        330        340        350        360 
KGAILTTMLA TRNFSSRSMI TKKGEGSQVK ESTDSSSTTL EDDDIKEDKK GTVDRSTTVV 

       370        380        390        400        410        420 
SKEPEDIRIL CPAKTYQQNI GNSQCSSARR QEIIKITEQL IEAINSGDFD GYTKICDPHL 

       430        440        450        460        470        480 
TAFEPEALGN LVEGIDFHKF YFENVLGKNC KAINTTILNP HVHLLGEEAA CIAYVRLTQY 

       490        500        510        520        530 
IDKQGHAHTH QSEETRVWHK RDNKWQNVHF HRSASAKISG ATTFDFIPQK 

Q00168 in FASTA format

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