KCC2A_DROME
ID KCC2A_DROME Reviewed; 530 AA.
AC Q00168; Q59DP1; Q59DP2; Q9V495;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type II alpha chain;
DE Short=CaM-kinase II alpha chain;
DE EC=2.7.11.17;
GN Name=CaMKII; Synonyms=CaM; ORFNames=CG18069;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Head;
RX PubMed=8380587; DOI=10.1016/s0021-9258(18)53961-2;
RA Ohsako S., Nishida Y., Ryo H., Yamauchi T.;
RT "Molecular characterization and expression of the Drosophila
RT Ca2+/calmodulin-dependent protein kinase II gene. Identification of four
RT forms of the enzyme generated from a single gene by alternative splicing.";
RL J. Biol. Chem. 268:2052-2062(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
RC TISSUE=Head;
RX PubMed=1910789; DOI=10.1016/0896-6273(91)90296-c;
RA Cho K.O., Wall J.B., Pugh P.C., Ito M., Mueller S.A., Kennedy M.B.;
RT "The alpha subunit of type II Ca2+/calmodulin-dependent protein kinase is
RT highly conserved in Drosophila.";
RL Neuron 7:439-450(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 347-388.
RX PubMed=8397298; DOI=10.1111/j.1471-4159.1993.tb13650.x;
RA Griffith L.C., Greenspan R.J.;
RT "The diversity of calcium/calmodulin-dependent protein kinase II isoforms
RT in Drosophila is generated by alternative splicing of a single gene.";
RL J. Neurochem. 61:1534-1537(1993).
RN [6]
RP FUNCTION.
RX PubMed=11980904; DOI=10.1074/jbc.m201949200;
RA Wang Z., Wilson G.F., Griffith L.C.;
RT "Calcium/calmodulin-dependent protein kinase II phosphorylates and
RT regulates the Drosophila eag potassium channel.";
RL J. Biol. Chem. 277:24022-24029(2002).
RN [7]
RP FUNCTION, INTERACTION WITH CASK, PHOSPHORYLATION AT THR-287; THR-306 AND
RP THR-307, AND MUTAGENESIS OF THR-306 AND THR-307.
RX PubMed=14687552; DOI=10.1016/s0896-6273(03)00786-4;
RA Lu C.S., Hodge J.J., Mehren J., Sun X.X., Griffith L.C.;
RT "Regulation of the Ca2+/CaM-responsive pool of CaMKII by scaffold-dependent
RT autophosphorylation.";
RL Neuron 40:1185-1197(2003).
RN [8]
RP PHOSPHORYLATION AT THR-287, AND ACTIVITY REGULATION.
RX PubMed=16880127; DOI=10.1016/j.neuron.2006.06.020;
RA Hodge J.J., Mullasseril P., Griffith L.C.;
RT "Activity-dependent gating of CaMKII autonomous activity by Drosophila
RT CASK.";
RL Neuron 51:327-337(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: A key regulator of plasticity in synaptic physiology and
CC behavior, alterations in its activity produce pleiotrophic effects that
CC involve synaptic transmission and development as well as various
CC aspects of behavior. Directly modulates eag potassium channels.
CC {ECO:0000269|PubMed:11980904, ECO:0000269|PubMed:14687552}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.17;
CC -!- ACTIVITY REGULATION: CASK plays a role in regulation of CaMKII
CC autophosphorylation. When complexed with CASK and in the presence
CC Ca[2+]/CaM, autophosphorylation of Thr-287 causes constitutive
CC activation of the kinase. In the absence of Ca[2+]/CaM,
CC autophosphorylation of Thr-306 causes inactivation of the kinase.
CC {ECO:0000269|PubMed:16880127}.
CC -!- SUBUNIT: Interacts with CASK. {ECO:0000269|PubMed:14687552}.
CC -!- INTERACTION:
CC Q00168; Q24210: CASK; NbExp=5; IntAct=EBI-124595, EBI-214423;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=530aa, D;
CC IsoId=Q00168-1; Sequence=Displayed;
CC Name=2; Synonyms=516aa, G;
CC IsoId=Q00168-2; Sequence=VSP_050262;
CC Name=3; Synonyms=509aa, B, E;
CC IsoId=Q00168-3; Sequence=VSP_050263;
CC Name=4; Synonyms=490aa, A, C;
CC IsoId=Q00168-4; Sequence=VSP_050261, VSP_050264;
CC -!- TISSUE SPECIFICITY: Expressed at a high level in the central nervous
CC system during the late embryonic stage. In adults, expression is more
CC abundant in the head than in the body. {ECO:0000269|PubMed:1910789,
CC ECO:0000269|PubMed:8380587}.
CC -!- PTM: Autophosphorylation at Thr-287 is independent of
CC autophosphorylation at Thr-306 and Thr-307.
CC {ECO:0000269|PubMed:14687552, ECO:0000269|PubMed:16880127,
CC ECO:0000269|PubMed:18327897}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Calmodulin-dependent kinase entry;
CC URL="https://en.wikipedia.org/wiki/Calmodulin_dependent_kinase";
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DR EMBL; D13330; BAA02593.1; -; mRNA.
DR EMBL; D13331; BAA02594.1; -; mRNA.
DR EMBL; D13332; BAA02595.1; -; mRNA.
DR EMBL; D13333; BAA02596.1; -; mRNA.
DR EMBL; M74583; AAA51459.1; -; mRNA.
DR EMBL; AE014135; AAF59388.3; -; Genomic_DNA.
DR EMBL; AE014135; AAF59390.2; -; Genomic_DNA.
DR EMBL; AE014135; AAN06568.2; -; Genomic_DNA.
DR EMBL; AE014135; AAX53595.1; -; Genomic_DNA.
DR EMBL; S65712; AAB28244.1; -; mRNA.
DR EMBL; S65716; AAB28245.1; -; mRNA.
DR EMBL; S65717; AAB28246.2; -; mRNA.
DR EMBL; S65719; AAB28247.1; -; mRNA.
DR EMBL; S65724; AAB28248.2; -; mRNA.
DR PIR; B44412; B44412.
DR PIR; C44412; JU0270.
DR PIR; D44412; D44412.
DR RefSeq; NP_001014696.1; NM_001014696.2. [Q00168-2]
DR RefSeq; NP_001162831.1; NM_001169360.2. [Q00168-4]
DR RefSeq; NP_001162832.1; NM_001169361.2. [Q00168-1]
DR RefSeq; NP_524635.3; NM_079896.4. [Q00168-4]
DR RefSeq; NP_726633.2; NM_166810.5. [Q00168-4]
DR RefSeq; NP_726634.1; NM_166811.2. [Q00168-3]
DR RefSeq; NP_726635.2; NM_166812.3. [Q00168-1]
DR RefSeq; NP_726636.2; NM_166813.3. [Q00168-3]
DR PDB; 5FG8; X-ray; 1.96 A; A=1-283.
DR PDB; 5H9B; X-ray; 2.25 A; A=1-283.
DR PDB; 5HU3; X-ray; 1.89 A; A=1-283.
DR PDBsum; 5FG8; -.
DR PDBsum; 5H9B; -.
DR PDBsum; 5HU3; -.
DR AlphaFoldDB; Q00168; -.
DR SMR; Q00168; -.
DR BioGRID; 68654; 31.
DR IntAct; Q00168; 5.
DR MINT; Q00168; -.
DR STRING; 7227.FBpp0289608; -.
DR iPTMnet; Q00168; -.
DR PaxDb; Q00168; -.
DR PRIDE; Q00168; -.
DR DNASU; 43828; -.
DR EnsemblMetazoa; FBtr0089217; FBpp0088281; FBgn0264607. [Q00168-4]
DR EnsemblMetazoa; FBtr0089218; FBpp0088282; FBgn0264607. [Q00168-4]
DR EnsemblMetazoa; FBtr0089219; FBpp0088283; FBgn0264607. [Q00168-3]
DR EnsemblMetazoa; FBtr0100146; FBpp0099496; FBgn0264607. [Q00168-1]
DR EnsemblMetazoa; FBtr0100147; FBpp0099497; FBgn0264607. [Q00168-3]
DR EnsemblMetazoa; FBtr0100148; FBpp0099498; FBgn0264607. [Q00168-2]
DR EnsemblMetazoa; FBtr0300377; FBpp0289606; FBgn0264607. [Q00168-4]
DR EnsemblMetazoa; FBtr0300378; FBpp0289607; FBgn0264607. [Q00168-1]
DR GeneID; 43828; -.
DR KEGG; dme:Dmel_CG18069; -.
DR CTD; 43828; -.
DR FlyBase; FBgn0264607; CaMKII.
DR VEuPathDB; VectorBase:FBgn0264607; -.
DR eggNOG; KOG0033; Eukaryota.
DR GeneTree; ENSGT00940000159769; -.
DR InParanoid; Q00168; -.
DR PhylomeDB; Q00168; -.
DR BRENDA; 2.7.11.17; 1994.
DR Reactome; R-DME-3371571; HSF1-dependent transactivation.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR Reactome; R-DME-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-DME-5578775; Ion homeostasis.
DR Reactome; R-DME-5673000; RAF activation.
DR Reactome; R-DME-936837; Ion transport by P-type ATPases.
DR SignaLink; Q00168; -.
DR BioGRID-ORCS; 43828; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43828; -.
DR PRO; PR:Q00168; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0264607; Expressed in brain and 52 other tissues.
DR ExpressionAtlas; Q00168; baseline and differential.
DR Genevisible; Q00168; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:FlyBase.
DR GO; GO:0048786; C:presynaptic active zone; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0007619; P:courtship behavior; TAS:FlyBase.
DR GO; GO:0007611; P:learning or memory; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:FlyBase.
DR GO; GO:0010888; P:negative regulation of lipid storage; IMP:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; NAS:FlyBase.
DR GO; GO:1990443; P:peptidyl-threonine autophosphorylation; IDA:FlyBase.
DR GO; GO:0032226; P:positive regulation of synaptic transmission, dopaminergic; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; TAS:FlyBase.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0060278; P:regulation of ovulation; IGI:FlyBase.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF08332; CaMKII_AD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..530
FT /note="Calcium/calmodulin-dependent protein kinase type II
FT alpha chain"
FT /id="PRO_0000086095"
FT DOMAIN 12..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 291..301
FT /note="Calmodulin-binding"
FT REGION 320..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 287
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:14687552,
FT ECO:0000269|PubMed:16880127"
FT MOD_RES 306
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:14687552"
FT MOD_RES 307
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:14687552"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 347..386
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1910789,
FT ECO:0000303|PubMed:8380587"
FT /id="VSP_050261"
FT VAR_SEQ 366..387
FT /note="DIRILCPAKTYQQNIGNSQCSS -> VNLFTNKA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8380587"
FT /id="VSP_050262"
FT VAR_SEQ 366..387
FT /note="DIRILCPAKTYQQNIGNSQCSS -> A (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8380587"
FT /id="VSP_050263"
FT VAR_SEQ 387
FT /note="S -> A (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1910789,
FT ECO:0000303|PubMed:8380587"
FT /id="VSP_050264"
FT MUTAGEN 306
FT /note="T->A: Fails to interact with CASK, catalytically
FT active but fails to autophosphorylate, when associated with
FT A-307."
FT /evidence="ECO:0000269|PubMed:14687552"
FT MUTAGEN 306
FT /note="T->D: Fails to interact with CASK, kinase inactive,
FT when associated with D-307."
FT /evidence="ECO:0000269|PubMed:14687552"
FT MUTAGEN 306
FT /note="T->S: Fails to interact with CASK, catalytically
FT active and can autophosphorylate, when associated with S-
FT 307."
FT /evidence="ECO:0000269|PubMed:14687552"
FT MUTAGEN 307
FT /note="T->A: Fails to interact with CASK, catalytically
FT active but fails to autophosphorylate, when associated with
FT A-306."
FT /evidence="ECO:0000269|PubMed:14687552"
FT MUTAGEN 307
FT /note="T->D: Fails to interact with CASK, kinase inactive,
FT when associated with D-306."
FT /evidence="ECO:0000269|PubMed:14687552"
FT MUTAGEN 307
FT /note="T->S: Fails to interact with CASK, catalytically
FT active and can autophosphorylate, when associated with S-
FT 306."
FT /evidence="ECO:0000269|PubMed:14687552"
FT CONFLICT 388
FT /note="A -> S (in Ref. 2; AAB28246/AAB28248)"
FT /evidence="ECO:0000305"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:5HU3"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:5HU3"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:5HU3"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5HU3"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:5HU3"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:5HU3"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:5HU3"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:5HU3"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:5HU3"
FT HELIX 110..128
FT /evidence="ECO:0007829|PDB:5HU3"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:5HU3"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5HU3"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5HU3"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5HU3"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5HU3"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5HU3"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:5HU3"
FT HELIX 194..209
FT /evidence="ECO:0007829|PDB:5HU3"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:5HU3"
FT TURN 235..240
FT /evidence="ECO:0007829|PDB:5HU3"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:5HU3"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:5FG8"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:5HU3"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:5FG8"
SQ SEQUENCE 530 AA; 59920 MW; 4F3D83582ABDFCFD CRC64;
MAAPAACTRF SDNYDIKEEL GKGAFSIVKR CVQKSTGFEF AAKIINTKKL TARDFQKLER
EARICRKLHH PNIVRLHDSI QEENYHYLVF DLVTGGELFE DIVAREFYSE ADASHCIQQI
LESVNHCHQN GVVHRDLKPE NLLLASKAKG AAVKLADFGL AIEVQGDHQA WFGFAGTPGY
LSPEVLKKEP YGKSVDIWAC GVILYILLVG YPPFWDEDQH RLYSQIKAGA YDYPSPEWDT
VTPEAKNLIN QMLTVNPNKR ITAAEALKHP WICQRERVAS VVHRQETVDC LKKFNARRKL
KGAILTTMLA TRNFSSRSMI TKKGEGSQVK ESTDSSSTTL EDDDIKEDKK GTVDRSTTVV
SKEPEDIRIL CPAKTYQQNI GNSQCSSARR QEIIKITEQL IEAINSGDFD GYTKICDPHL
TAFEPEALGN LVEGIDFHKF YFENVLGKNC KAINTTILNP HVHLLGEEAA CIAYVRLTQY
IDKQGHAHTH QSEETRVWHK RDNKWQNVHF HRSASAKISG ATTFDFIPQK
