KCC2A_RAT
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 03-AUG-2022, entry version 195.
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:0000250|UniProtKB:Q9UQM7};
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 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 [10]
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 [11]
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 [12]
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 [13]
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 synaptic plasticity, neurotransmitter release and
CC long-term potentiation. Member of the NMDAR signaling complex in
CC excitatory synapses, it regulates NMDAR-dependent potentiation of the
CC AMPAR and therefore excitatory synaptic transmission (PubMed:15312654).
CC Regulates dendritic spine development. Also regulates the migration of
CC developing neurons. Phosphorylates the transcription factor FOXO3 to
CC activate its transcriptional activity (By similarity). Acts as a
CC negative regulator of 2-arachidonoylglycerol (2-AG)-mediated synaptic
CC signaling via modulation of DAGLA activity (By similarity).
CC {ECO:0000250|UniProtKB:P11798, ECO:0000250|UniProtKB:Q9UQM7,
CC ECO:0000269|PubMed:15312654}.
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 Evidence={ECO:0000250|UniProtKB:Q9UQM7};
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; 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). {ECO:0000250|UniProtKB:P11798,
CC ECO:0000250|UniProtKB:Q9UQM7, ECO:0000269|PubMed:11182241,
CC ECO:0000269|PubMed:1328883, ECO:0000269|PubMed:15312654,
CC ECO:0000269|PubMed:15659234, ECO:0000269|PubMed:17923693,
CC 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}.
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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 PDBsum; 1CDM; -.
DR PDBsum; 1CM1; -.
DR PDBsum; 1CM4; -.
DR PDBsum; 5U6Y; -.
DR AlphaFoldDB; P11275; -.
DR SMR; P11275; -.
DR BioGRID; 247435; 124.
DR CORUM; P11275; -.
DR DIP; DIP-29639N; -.
DR IntAct; P11275; 21.
DR MINT; P11275; -.
DR STRING; 10116.ENSRNOP00000041940; -.
DR BindingDB; P11275; -.
DR ChEMBL; CHEMBL2359; -.
DR GuidetoPHARMACOLOGY; 1555; -.
DR CarbonylDB; P11275; -.
DR iPTMnet; P11275; -.
DR PhosphoSitePlus; P11275; -.
DR SwissPalm; P11275; -.
DR jPOST; P11275; -.
DR PRIDE; P11275; -.
DR GeneID; 25400; -.
DR KEGG; rno:25400; -.
DR UCSC; RGD:2261; rat.
DR CTD; 815; -.
DR RGD; 2261; Camk2a.
DR eggNOG; KOG0033; Eukaryota.
DR InParanoid; P11275; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; P11275; -.
DR BRENDA; 2.7.11.17; 5301.
DR Reactome; R-RNO-3371571; HSF1-dependent transactivation.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
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 EvolutionaryTrace; P11275; -.
DR PRO; PR:P11275; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; IDA:RGD.
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:0099573; C:glutamatergic postsynaptic density; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
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:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:GOC.
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; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:BHF-UCL.
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:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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:0099004; P:calmodulin dependent kinase signaling pathway; IMP:SynGO.
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:0051346; P:negative regulation of hydrolase activity; ISS:UniProtKB.
DR GO; GO:0098989; P:NMDA selective glutamate receptor signaling pathway; IMP:SynGO.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:RGD.
DR GO; GO:1990443; P:peptidyl-threonine autophosphorylation; ISS:UniProtKB.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISS:ParkinsonsUK-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0098970; P:postsynaptic neurotransmitter receptor diffusion trapping; IMP:SynGO.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
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 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; 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..341
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"
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
