ID KCC2A_RAT Reviewed; 478 AA. AC P11275; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 02-SEP-2026, entry version 213. DE RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit alpha; DE Short=CaM kinase II subunit alpha; DE Short=CaMK-II subunit alpha; DE EC=2.7.11.17 {ECO:0000269|PubMed:11972023}; GN Name=Camk2a; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3475713; DOI=10.1073/pnas.84.16.5962; RA Lin C.R., Kapiloff M.S., Durgerian S., Tatemoto K., Russo A.F., Hanson P., RA Schulman H., Rosenfeld M.G.; RT "Molecular cloning of a brain-specific calcium/calmodulin-dependent protein RT kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 84:5962-5966(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2856087; DOI=10.1016/0896-6273(88)90210-3; RA Bulleit R.F., Bennett M.K., Molloy S.S., Hurley J.B., Kennedy M.B.; RT "Conserved and variable regions in the subunits of brain type II RT Ca2+/calmodulin-dependent protein kinase."; RL Neuron 1:63-72(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 132-327. RX PubMed=3037704; DOI=10.1126/science.3037704; RA Hanley R.M., Means A.R., Ono T., Kemp B.E., Burgin K.E., Waxham N., RA Kelly P.T.; RT "Functional analysis of a complementary DNA for the 50-kilodalton subunit RT of calmodulin kinase II."; RL Science 237:293-297(1987). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6. RX PubMed=2153289; DOI=10.1073/pnas.87.1.278; RA Sunyer T., Sahyoun N.; RT "Sequence analysis and DNA-protein interactions within the 5' flanking RT region of the Ca2+/calmodulin-dependent protein kinase II alpha-subunit RT gene."; RL Proc. Natl. Acad. Sci. U.S.A. 87:278-282(1990). RN [5] RP PROTEIN SEQUENCE OF 231-236; 238-246 AND 461-476, AND INTERACTION WITH RP SYN1. RX PubMed=1328883; DOI=10.1038/359417a0; RA Benfenati F., Valtorta F., Rubenstein J.L., Gorelick F.S., Greengard P., RA Czernik A.J.; RT "Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is RT a binding protein for synapsin I."; RL Nature 359:417-420(1992). RN [6] RP PROTEIN SEQUENCE OF 282-299, ACTIVITY REGULATION, AND PHOSPHORYLATION AT RP THR-286. RX PubMed=2842767; DOI=10.1073/pnas.85.17.6337; RA Thiel G., Czernik A.J., Gorelick F., Nairn A.C., Greengard P.; RT "Ca2+/calmodulin-dependent protein kinase II: identification of threonine- RT 286 as the autophosphorylation site in the alpha subunit associated with RT the generation of Ca2+-independent activity."; RL Proc. Natl. Acad. Sci. U.S.A. 85:6337-6341(1988). RN [7] RP INTERACTION WITH CAMK2N2. RX PubMed=9724800; DOI=10.1073/pnas.95.18.10890; RA Chang B.H., Mukherji S., Soderling T.R.; RT "Characterization of a calmodulin kinase II inhibitor protein in brain."; RL Proc. Natl. Acad. Sci. U.S.A. 95:10890-10895(1998). RN [8] RP INTERACTION WITH CAMK2N1. RX PubMed=11182241; DOI=10.1016/s0306-4522(00)00520-0; RA Chang B.H., Mukherji S., Soderling T.R.; RT "Calcium/calmodulin-dependent protein kinase II inhibitor protein: RT localization of isoforms in rat brain."; RL Neuroscience 102:767-777(2001). RN [9] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=11972023; DOI=10.1073/pnas.052159099; RA Nair J.S., DaFonseca C.J., Tjernberg A., Sun W., Darnell J.E. Jr., RA Chait B.T., Zhang J.J.; RT "Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in RT response to IFN-gamma."; RL Proc. Natl. Acad. Sci. U.S.A. 99:5971-5976(2002). RN [10] RP INTERACTION WITH SYNGAP1 AND MPDZ, MUTAGENESIS OF 432-ILE--THR-435, AND RP FUNCTION. RX PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003; RA Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.; RT "SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity RT and NMDA receptor-dependent synaptic AMPA receptor potentiation."; RL Neuron 43:563-574(2004). RN [11] RP INTERACTION WITH BAALC, AND SUBCELLULAR LOCATION. RX PubMed=15659234; DOI=10.1111/j.1471-4159.2004.02902.x; RA Wang X., Tian Q.-B., Okano A., Sakagami H., Moon I.S., Kondo H., Endo S., RA Suzuki T.; RT "BAALC 1-6-8 protein is targeted to postsynaptic lipid rafts by its N- RT terminal myristoylation and palmitoylation, and interacts with a, but not RT b, subunit of Ca2+/calmodulin-dependent protein kinase II."; RL J. Neurochem. 92:647-659(2005). RN [12] RP INTERACTION WITH SYNPO2. RX PubMed=17923693; DOI=10.1128/mcb.00950-07; RA Faul C., Dhume A., Schecter A.D., Mundel P.; RT "Protein kinase A, Ca2+/calmodulin-dependent kinase II, and calcineurin RT regulate the intracellular trafficking of myopodin between the Z-disc and RT the nucleus of cardiac myocytes."; RL Mol. Cell. Biol. 27:8215-8227(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND SER-404, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [14] RP PALMITOYLATION. RX PubMed=23687301; DOI=10.1074/jbc.m112.431676; RA Oku S., Takahashi N., Fukata Y., Fukata M.; RT "In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10 RT (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to RT Rab5-positive endosomes."; RL J. Biol. Chem. 288:19816-19829(2013). CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that functions CC autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, CC and is involved in various processes, such as synaptic plasticity, CC neurotransmitter release and long-term potentiation. Member of the CC NMDAR signaling complex in excitatory synapses, it regulates NMDAR- CC dependent potentiation of the AMPAR and therefore excitatory synaptic CC transmission (PubMed:15312654). Regulates dendritic spine development. CC Also regulates the migration of developing neurons. Phosphorylates the CC transcription factor FOXO3 to activate its transcriptional activity (By CC similarity). Phosphorylates the transcription factor ETS1 in response CC to calcium signaling, thereby decreasing ETS1 affinity for DNA (By CC similarity). In response to interferon-gamma (IFN-gamma) stimulation, CC catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling CC pathway (PubMed:11972023). In response to interferon-beta (IFN-beta) CC stimulation, stimulates the JAK-STAT signaling pathway (By similarity). CC In response to interferon-gamma (IFN-gamma) stimulation, catalyzes CC phosphorylation of PSAT1, inhibiting ferroptosis by promoting GPX4 CC hydroxylation and stability (By similarity). Acts as a negative CC regulator of 2-arachidonoylglycerol (2-AG)-mediated synaptic signaling CC via modulation of DAGLA activity (By similarity). CC {ECO:0000250|UniProtKB:P11798, ECO:0000250|UniProtKB:Q9UQM7, CC ECO:0000269|PubMed:11972023, ECO:0000269|PubMed:15312654}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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 Evidence={ECO:0000269|PubMed:11972023}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.17; CC Evidence={ECO:0000250|UniProtKB:Q9UQM7}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q9UQM7}; CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of CC calmodulin results in conformational change that relieves intrasteric CC autoinhibition and allows autophosphorylation of Thr-286 which turns CC the kinase in a constitutively active form and confers to the kinase a CC Ca(2+)-independent activity. {ECO:0000269|PubMed:2842767}. CC -!- SUBUNIT: There are 4 genes encoding calcium/calmodulin-dependent CC protein kinase type II chains: CAMK2A, CAMK2B, CAMK2G and CAMK2D. The CC corresponding proteins assemble into homo- or heteromultimeric CC holoenzymes composed of 12 subunits with two hexameric rings stacked CC one on top of the other (By similarity). Interacts with BAALC CC (PubMed:15659234). Interacts with MPDZ (PubMed:15312654). Interacts CC with SYN1 (PubMed:1328883). Interacts with CAMK2N2 (PubMed:9724800). CC Interacts with SYNGAP1 (PubMed:15312654). Interacts with SYNPO2 CC (PubMed:17923693). Interacts with SHANK3. Interacts with GRIN2B. CC Interacts with CACNB2. Interacts with LRRC7. Interacts with GRM5 (By CC similarity). Interacts with DAGLA (via C-terminal); this interaction is CC enhanced by autophosphorylation of CAMK2A at Thr-286 (By similarity). CC Interacts with CAMK2N1; this interaction requires CAMK2A activation by CC Ca(2+) (PubMed:11182241). Interaction with LRRC7 (By similarity). CC {ECO:0000250|UniProtKB:P11798, ECO:0000250|UniProtKB:Q9UQM7, CC ECO:0000269|PubMed:11182241, ECO:0000269|PubMed:1328883, CC ECO:0000269|PubMed:15312654, ECO:0000269|PubMed:15659234, CC ECO:0000269|PubMed:17923693, ECO:0000269|PubMed:9724800}. CC -!- INTERACTION: CC P11275; P54282: Cacna1a; NbExp=3; IntAct=EBI-2640645, EBI-3507416; CC P11275; P08483: Chrm3; NbExp=2; IntAct=EBI-2640645, EBI-7946407; CC P11275; P08485: Chrm4; NbExp=10; IntAct=EBI-2640645, EBI-7946147; CC P11275; P19490: Gria1; NbExp=3; IntAct=EBI-2640645, EBI-371642; CC P11275; Q00960: Grin2b; NbExp=2; IntAct=EBI-2640645, EBI-396905; CC P11275; P70587: Lrrc7; NbExp=2; IntAct=EBI-2640645, EBI-7798464; CC P11275; P62195: PSMC5; Xeno; NbExp=4; IntAct=EBI-2640645, EBI-357745; CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:15659234}. CC Postsynaptic density {ECO:0000269|PubMed:15659234}. Cell projection, CC dendritic spine {ECO:0000250|UniProtKB:Q9UQM7}. Cell projection, CC dendrite {ECO:0000250|UniProtKB:Q9UQM7}. Note=Postsynaptic lipid rafts. CC {ECO:0000269|PubMed:15659234}. CC -!- PTM: Autophosphorylation of Thr-286 following activation by CC Ca(2+)/calmodulin. Phosphorylation of Thr-286 locks the kinase into an CC activated state. {ECO:0000250|UniProtKB:Q9UQM7}. CC -!- PTM: Palmitoylated (PubMed:23687301). Probably palmitoylated by ZDHHC3 CC and ZDHHC7 (PubMed:23687301). {ECO:0000269|PubMed:23687301}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. CaMK subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J02942; AAA41870.1; -; mRNA. DR EMBL; M16960; AAA41855.1; -; mRNA. DR EMBL; M29699; AAA40841.1; -; Genomic_DNA. DR PIR; A30355; A30355. DR RefSeq; NP_037052.1; NM_012920.1. DR PDB; 1CDM; X-ray; 2.00 A; B=290-314. DR PDB; 1CM1; X-ray; 2.00 A; B=290-314. DR PDB; 1CM4; X-ray; 2.00 A; B=290-314. DR PDB; 5U6Y; EM; 20.00 A; A/B/C/D/E/F/G/H/I/J/K/L=13-472. DR PDB; 8SYG; EM; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=345-478. DR PDB; 8T15; EM; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=345-478. DR AlphaFoldDB; P11275; -. DR EMDB; EMD-40873; -. DR EMDB; EMD-40955; -. DR EMDB; EMD-8514; -. DR SMR; P11275; -. DR BioGRID; 247435; 124. DR CORUM; P11275; -. DR DIP; DIP-29639N; -. DR FunCoup; P11275; 2230. DR IntAct; P11275; 21. DR MINT; P11275; -. DR STRING; 10116.ENSRNOP00000041940; -. DR BindingDB; P11275; -. DR ChEMBL; CHEMBL2359; -. DR GuidetoPHARMACOLOGY; 1555; -. DR CarbonylDB; P11275; -. DR GlyGen; P11275; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P11275; -. DR PhosphoSitePlus; P11275; -. DR SwissPalm; P11275; -. DR jPOST; P11275; -. DR PaxDb; 10116-ENSRNOP00000041940; -. DR GeneID; 25400; -. DR KEGG; rno:25400; -. DR UCSC; RGD:2261; rat. DR AGR; RGD:2261; -. DR CTD; 815; -. DR RGD; 2261; Camk2a. DR eggNOG; KOG0033; Eukaryota. DR InParanoid; P11275; -. DR PhylomeDB; P11275; -. DR BRENDA; 2.7.11.17; 5301. DR Reactome; R-RNO-3371571; HSF1-dependent transactivation. DR Reactome; R-RNO-399719; Trafficking of AMPA receptors. DR Reactome; R-RNO-4086398; Ca2+ pathway. DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation. DR Reactome; R-RNO-5578775; Ion homeostasis. DR Reactome; R-RNO-5673000; RAF activation. DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade. DR Reactome; R-RNO-877300; Interferon gamma signaling. DR Reactome; R-RNO-936837; Ion transport by P-type ATPases. DR CD-CODE; A7E9CBB4; Postsynaptic density. DR EvolutionaryTrace; P11275; -. DR PRO; PR:P11275; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0030424; C:axon; IDA:RGD. DR GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030425; C:dendrite; IDA:UniProtKB. DR GO; GO:0032839; C:dendrite cytoplasm; IDA:BHF-UCL. DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005739; C:mitochondrion; ISS:ParkinsonsUK-UCL. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO. DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO. DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD. DR GO; GO:0045202; C:synapse; EXP:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004683; F:calcium/calmodulin-dependent protein kinase activity; IDA:UniProtKB. DR GO; GO:0005516; F:calmodulin binding; ISO:RGD. DR GO; GO:0035254; F:glutamate receptor binding; ISS:ParkinsonsUK-UCL. DR GO; GO:0032794; F:GTPase activating protein binding; IPI:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD. DR GO; GO:0106310; F:protein serine kinase activity; EXP:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:ParkinsonsUK-UCL. DR GO; GO:0038166; P:angiotensin-activated signaling pathway; ISO:RGD. DR GO; GO:0006816; P:calcium ion transport; ISS:ParkinsonsUK-UCL. DR GO; GO:0035458; P:cellular response to interferon-beta; ISS:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; ISO:RGD. DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD. DR GO; GO:0060996; P:dendritic spine development; ISS:UniProtKB. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:ParkinsonsUK-UCL. DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0110076; P:negative regulation of ferroptosis; ISS:UniProtKB. DR GO; GO:0098877; P:neurotransmitter receptor transport to plasma membrane; IMP:RGD. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:RGD. DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:ParkinsonsUK-UCL. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:RGD. DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISS:ParkinsonsUK-UCL. DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISS:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD. DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD. DR GO; GO:2000124; P:regulation of endocannabinoid signaling pathway; ISS:UniProtKB. DR GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; ISS:ParkinsonsUK-UCL. DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB. DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISS:ParkinsonsUK-UCL. DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO. DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS:ParkinsonsUK-UCL. DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IGI:ARUK-UCL. DR GO; GO:0099148; P:regulation of synaptic vesicle docking; ISO:RGD. DR GO; GO:0002931; P:response to ischemia; ISS:ParkinsonsUK-UCL. DR CDD; cd14086; STKc_CaMKII; 1. DR FunFam; 1.10.510.10:FF:000001; Calcium/calmodulin-dependent protein kinase type II subunit delta; 1. DR FunFam; 3.30.200.20:FF:000002; Calcium/calmodulin-dependent protein kinase type II subunit delta isoform 2; 1. DR FunFam; 3.10.450.50:FF:000001; calcium/calmodulin-dependent protein kinase type II subunit gamma isoform X1; 1. DR Gene3D; 3.10.450.50; -; 1. DR Gene3D; 6.10.140.620; -; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF08332; CaMKII_AD; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF54427; NTF2-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PDBsum; 1CDM; -. DR PDBsum; 1CM1; -. DR PDBsum; 1CM4; -. DR PDBsum; 5U6Y; -. DR PDBsum; 8SYG; -. DR PDBsum; 8T15; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Calmodulin-binding; Cell projection; KW Direct protein sequencing; Kinase; Lipoprotein; Magnesium; Metal-binding; KW Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Synapse; Transferase. FT CHAIN 1..478 FT /note="Calcium/calmodulin-dependent protein kinase type II FT subunit alpha" FT /id="PRO_0000086094" FT DOMAIN 13..271 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 290..300 FT /note="Calmodulin-binding" FT REGION 310..320 FT /note="Interaction with BAALC" FT /evidence="ECO:0000269|PubMed:15659234" FT REGION 314..341 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 322..331 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 135 FT /note="Proton acceptor" FT BINDING 19..27 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 42 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 13 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P11798" FT MOD_RES 257 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 286 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:2842767" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11798" FT MOD_RES 331 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11798" FT MOD_RES 333 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11798" FT MOD_RES 336 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P11798" FT MOD_RES 337 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P11798" FT MOD_RES 404 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MUTAGEN 432..435 FT /note="IRIT->MGTA: Loss of interaction with MPDZ." FT /evidence="ECO:0000269|PubMed:15312654" FT CONFLICT 301 FT /note="G -> A (in Ref. 3; AAA41855)" FT /evidence="ECO:0000305" FT HELIX 295..309 FT /evidence="ECO:0007829|PDB:1CDM" FT HELIX 346..363 FT /evidence="ECO:0007829|PDB:8SYG" FT HELIX 366..372 FT /evidence="ECO:0007829|PDB:8SYG" FT STRAND 373..380 FT /evidence="ECO:0007829|PDB:8SYG" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:8SYG" FT STRAND 389..392 FT /evidence="ECO:0007829|PDB:8SYG" FT HELIX 393..398 FT /evidence="ECO:0007829|PDB:8SYG" FT HELIX 399..403 FT /evidence="ECO:0007829|PDB:8SYG" FT STRAND 410..421 FT /evidence="ECO:0007829|PDB:8SYG" FT STRAND 423..438 FT /evidence="ECO:0007829|PDB:8SYG" FT STRAND 444..458 FT /evidence="ECO:0007829|PDB:8SYG" FT STRAND 461..472 FT /evidence="ECO:0007829|PDB:8SYG" SQ SEQUENCE 478 AA; 54115 MW; 306F416CCE9B5F62 CRC64; MATITCTRFT EEYQLFEELG KGAFSVVRRC VKVLAGQEYA AKIINTKKLS ARDHQKLERE ARICRLLKHP NIVRLHDSIS EEGHHYLIFD LVTGGELFED IVAREYYSEA DASHCIQQIL EAVLHCHQMG VVHRDLKPEN LLLASKLKGA AVKLADFGLA IEVEGEQQAW FGFAGTPGYL SPEVLRKDPY GKPVDLWACG VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV TPEAKDLINK MLTINPSKRI TAAEALKHPW ISHRSTVASC MHRQETVDCL KKFNARRKLK GAILTTMLAT RNFSGGKSGG NKKNDGVKES SESTNTTIED EDTKVRKQEI IKVTEQLIEA ISNGDFESYT KMCDPGMTAF EPEALGNLVE GLDFHRFYFE NLWSRNSKPV HTTILNPHIH LMGDESACIA YIRITQYLDA GGIPRTAQSE ETRVWHRRDG KWQIVHFHRS GAPSVLPH //