ID MAGI2_RAT Reviewed; 1277 AA. AC O88382; Q9R271; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 176. DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2; DE AltName: Full=Atrophin-1-interacting protein 1; DE Short=AIP-1; DE AltName: Full=Membrane-associated guanylate kinase inverted 2; DE Short=MAGI-2; DE AltName: Full=Synaptic-scaffolding molecule; DE Short=S-SCAM; GN Name=Magi2; Synonyms=Acvrinp1, Aip1, Sscam; 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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND INTERACTION WITH DLGAP1; NLGN1 AND GRIN2A. RX PubMed=9694864; DOI=10.1074/jbc.273.33.21105; RA Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M., RA Toyoda A., Suedhof T.C., Takai Y.; RT "A novel multiple PDZ domain-containing molecule interacting with N-methyl- RT d-aspartate receptors and neuronal cell adhesion proteins."; RL J. Biol. Chem. 273:21105-21110(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING (ISOFORM RP 3). RX PubMed=10644767; DOI=10.1074/jbc.275.4.2966; RA Hirao K., Hata Y., Yao I., Deguchi M., Kawabe H., Mizoguchi A., Takai Y.; RT "Three isoforms of synaptic scaffolding molecule and their RT characterization: multimerization between the isoforms and their RT interaction with N-methyl-D-aspartate receptors and SAP90/PSD-95-associated RT protein."; RL J. Biol. Chem. 275:2966-2972(2000). RN [3] RP INTERACTION WITH CTNND2. RX PubMed=10080919; DOI=10.1006/bbrc.1999.0364; RA Ide N., Hata Y., Deguchi M., Hirao K., Yao I., Takai Y.; RT "Interaction of S-SCAM with neural plakophilin-related Armadillo-repeat RT protein/delta-catenin."; RL Biochem. Biophys. Res. Commun. 256:456-461(1999). RN [4] RP INTERACTION WITH RAPGEF2. RX PubMed=10548487; DOI=10.1006/bbrc.1999.1619; RA Ohtsuka T., Hata Y., Ide N., Yasuda T., Inoue E., Inoue T., Mizoguchi A., RA Takai Y.; RT "nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G protein RT that interacts with synaptic scaffolding molecule (S-SCAM)."; RL Biochem. Biophys. Res. Commun. 265:38-44(1999). RN [5] RP INTERACTION WITH MAGUIN-1. RX PubMed=10207009; DOI=10.1074/jbc.274.17.11889; RA Yao I., Hata Y., Ide N., Hirao K., Deguchi M., Nishioka H., Mizoguchi A., RA Takai Y.; RT "MAGUIN, a novel neuronal membrane-associated guanylate kinase-interacting RT protein."; RL J. Biol. Chem. 274:11889-11896(1999). RN [6] RP INTERACTION WITH GRID2. RX PubMed=12589829; DOI=10.1016/s0006-291x(03)00070-6; RA Yap C.C., Muto Y., Kishida H., Hashikawa T., Yano R.; RT "PKC regulates the delta2 glutamate receptor interaction with S-SCAM/MAGI-2 RT protein."; RL Biochem. Biophys. Res. Commun. 301:1122-1128(2003). RN [7] RP INTERACTION WITH PTEN. RX PubMed=15951562; DOI=10.1074/jbc.m504761200; RA Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C., RA Antonarakis S.E., Pulido R.; RT "Binding of PTEN to specific PDZ domains contributes to PTEN protein RT stability and phosphorylation by microtubule-associated serine/threonine RT kinases."; RL J. Biol. Chem. 280:28936-28943(2005). RN [8] RP IDENTIFICATION IN A COMPLEX WITH ACTN4; CASK; IQGAP1; NPHS1; SPTAN1 AND RP SPTBN1, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=Sprague-Dawley; TISSUE=Renal glomerulus; RX PubMed=15994232; DOI=10.1073/pnas.0504166102; RA Lehtonen S., Ryan J.J., Kudlicka K., Iino N., Zhou H., Farquhar M.G.; RT "Cell junction-associated proteins IQGAP1, MAGI-2, CASK, spectrins, and RT alpha-actinin are components of the nephrin multiprotein complex."; RL Proc. Natl. Acad. Sci. U.S.A. 102:9814-9819(2005). RN [9] RP INTERACTION WITH DDN. RX PubMed=16751601; DOI=10.1093/jb/mvj105; RA Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K., RA Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y.; RT "CIN85 is localized at synapses and forms a complex with S-SCAM via RT dendrin."; RL J. Biochem. 139:931-939(2006). RN [10] RP INTERACTION WITH DDN. RX PubMed=16464232; DOI=10.1111/j.1471-4159.2006.03679.x; RA Kremerskothen J., Kindler S., Finger I., Veltel S., Barnekow A.; RT "Postsynaptic recruitment of Dendrin depends on both dendritic mRNA RT transport and synaptic anchoring."; RL J. Neurochem. 96:1659-1666(2006). RN [11] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH KIDINS220; RAPGEF2 AND NTRK1, RP INTERACTION WITH RAPGEF2 AND KIDINS220, AND SUBCELLULAR LOCATION. RX PubMed=17724123; DOI=10.1083/jcb.200610073; RA Hisata S., Sakisaka T., Baba T., Yamada T., Aoki K., Matsuda M., Takai Y.; RT "Rap1-PDZ-GEF1 interacts with a neurotrophin receptor at late endosomes, RT leading to sustained activation of Rap1 and ERK and neurite outgrowth."; RL J. Cell Biol. 178:843-860(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686; SER-884 AND SER-885, 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 IDENTIFICATION IN A COMPLEX WITH IGSF9B AND NLGN2. RX PubMed=23751499; DOI=10.1083/jcb.201209132; RA Woo J., Kwon S.K., Nam J., Choi S., Takahashi H., Krueger D., Park J., RA Lee Y., Bae J.Y., Lee D., Ko J., Kim H., Kim M.H., Bae Y.C., Chang S., RA Craig A.M., Kim E.; RT "The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to RT promote inhibitory synapse development."; RL J. Cell Biol. 201:929-944(2013). CC -!- FUNCTION: Seems to act as scaffold molecule at synaptic junctions by CC assembling neurotransmitter receptors and cell adhesion proteins CC (PubMed:9694864). Plays a role in nerve growth factor (NGF)-induced CC recruitment of RAPGEF2 to late endosomes and neurite outgrowth CC (PubMed:17724123). May play a role in regulating activin-mediated CC signaling in neuronal cells (By similarity). Enhances the ability of CC PTEN to suppress AKT1 activation (By similarity). Plays a role in CC receptor-mediated clathrin-dependent endocytosis which is required for CC ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q86UL8, CC ECO:0000250|UniProtKB:Q9WVQ1, ECO:0000269|PubMed:17724123, CC ECO:0000269|PubMed:9694864}. CC -!- SUBUNIT: Interacts (via its WW domains) with DRPLA (By similarity). CC Interacts with CTNNB1, ACVR2A, SMAD2 and SMAD3 (By similarity). Part of CC a complex consisting of MAGI2/ARIP1, ACVR2A, ACVR1B and SMAD3 (By CC similarity). May interact with HTR2A and IGSF9 (By similarity). CC Interacts with HTR4 (By similarity). Interacts (via guanylate kinase CC domain) with DLGAP1 (PubMed:9694864). Interacts (via PDZ domains) with CC GRIN2A, GRID2 and NLGN1 (PubMed:9694864, PubMed:12589829). Interacts CC with CTNND2 (PubMed:10080919). Interacts with MAGUIN-1 CC (PubMed:10207009). Interacts (via its second PDZ domain) with PTEN (via CC unphosphorylated C-terminus); this interaction diminishes the CC degradation rate of PTEN (PubMed:15951562). Found in a complex, at CC least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is CC mainly formed at late endosomes in a NGF-dependent manner CC (PubMed:17724123). Interacts with RAPGEF2; the interaction occurs CC before or after nerve growth factor (NGF) stimulation CC (PubMed:10548487). Isoform 1 interacts (via PDZ domain) with KIDINS220 CC isoform 2 (via C-terminal domain) (PubMed:17724123). Interacts with DDN CC (PubMed:16751601, PubMed:16464232). Identified in a complex with ACTN4, CC CASK, IQGAP1, NPHS1, SPTAN1 and SPTBN1 (PubMed:15994232). Interacts CC with DLL1 (By similarity). Found in a complex with IGSF9B and NLGN2; CC the interaction with IGSF9B is mediated via the PDZ 5 and PDZ 6 CC domains, while the interaction with NLGN2 is mediated via the WW1, WW2 CC and PDZ2 domains (PubMed:23751499). Interacts (via PDZ 6 domain) with CC USH1G (via SAM domain); the interaction is triggered by phosphorylation CC of USH1G by CK2 and negatively regulates MAGI2-mediated endocytosis (By CC similarity). {ECO:0000250|UniProtKB:Q9WVQ1, CC ECO:0000269|PubMed:10080919, ECO:0000269|PubMed:10207009, CC ECO:0000269|PubMed:10548487, ECO:0000269|PubMed:12589829, CC ECO:0000269|PubMed:15951562, ECO:0000269|PubMed:15994232, CC ECO:0000269|PubMed:16464232, ECO:0000269|PubMed:16751601, CC ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:23751499, CC ECO:0000269|PubMed:9694864}. CC -!- INTERACTION: CC O88382; P97836: Dlgap1; NbExp=3; IntAct=EBI-696179, EBI-80901; CC O88382; Q8R4T5: Tamalin; NbExp=5; IntAct=EBI-696179, EBI-7361884; CC O88382; P34998: CRHR1; Xeno; NbExp=2; IntAct=EBI-696179, EBI-3870393; CC O88382; O94850: DDN; Xeno; NbExp=3; IntAct=EBI-696179, EBI-5240523; CC O88382; P60484: PTEN; Xeno; NbExp=3; IntAct=EBI-696179, EBI-696162; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Late endosome. Synapse, synaptosome. CC Cell membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome CC {ECO:0000250|UniProtKB:Q9WVQ1}. Cell projection, cilium CC {ECO:0000250|UniProtKB:Q9WVQ1}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome, centriole CC {ECO:0000250|UniProtKB:Q9WVQ1}. Photoreceptor inner segment CC {ECO:0000250|UniProtKB:Q9WVQ1}. Cell projection, cilium, photoreceptor CC outer segment {ECO:0000250|UniProtKB:Q9WVQ1}. Note=Membrane-associated CC in synaptosomes. Localized diffusely in the cytoplasm before nerve CC growth factor (NGF) stimulation. Recruited to late endosomes after NGF CC stimulation. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=alpha; CC IsoId=O88382-1; Sequence=Displayed; CC Name=2; Synonyms=beta; CC IsoId=O88382-2; Sequence=VSP_008438; CC Name=3; Synonyms=gamma; CC IsoId=O88382-3; Sequence=VSP_008439; CC -!- TISSUE SPECIFICITY: Expressed in the foot process layer of podocytes of CC the kidney glomeruli but not in tubules (at protein level). Expressed CC in the brain. {ECO:0000269|PubMed:15994232, CC ECO:0000269|PubMed:9694864}. CC -!- DEVELOPMENTAL STAGE: Expressed during the late capillary loop stage of CC glomerulogenesis. First detected in junctional complexes in podocytes CC after their migration to the base of cells. Up-regulated upon foot CC process differentiation. {ECO:0000269|PubMed:15994232}. CC -!- SIMILARITY: Belongs to the MAGUK family. {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; AF034863; AAC31124.1; -; mRNA. DR EMBL; AF130819; AAD31015.1; -; mRNA. DR PIR; T14152; T14152. DR RefSeq; NP_446073.1; NM_053621.1. DR AlphaFoldDB; O88382; -. DR SMR; O88382; -. DR BioGRID; 250241; 7. DR CORUM; O88382; -. DR IntAct; O88382; 28. DR MINT; O88382; -. DR STRING; 10116.ENSRNOP00000059912; -. DR iPTMnet; O88382; -. DR PhosphoSitePlus; O88382; -. DR PaxDb; 10116-ENSRNOP00000059912; -. DR GeneID; 113970; -. DR KEGG; rno:113970; -. DR AGR; RGD:621855; -. DR CTD; 9863; -. DR RGD; 621855; Magi2. DR eggNOG; KOG3209; Eukaryota. DR InParanoid; O88382; -. DR OrthoDB; 2902917at2759; -. DR PhylomeDB; O88382; -. DR PRO; PR:O88382; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central. DR GO; GO:0005814; C:centriole; ISS:UniProtKB. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0097546; C:ciliary base; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0030425; C:dendrite; IDA:UniProtKB. DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IDA:SynGO. DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005770; C:late endosome; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB. DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0036057; C:slit diaphragm; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IDA:UniProtKB. DR GO; GO:0070697; F:activin receptor binding; ISO:RGD. DR GO; GO:0031697; F:beta-1 adrenergic receptor binding; ISS:UniProtKB. DR GO; GO:0019894; F:kinesin binding; IPI:RGD. DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD. DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISS:UniProtKB. DR GO; GO:0046332; F:SMAD binding; ISS:UniProtKB. DR GO; GO:0098919; F:structural constituent of postsynaptic density; IDA:SynGO. DR GO; GO:0098879; F:structural constituent of postsynaptic specialization; IDA:SynGO. DR GO; GO:0070699; F:type II activin receptor binding; ISS:UniProtKB. DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB. DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB. DR GO; GO:0003094; P:glomerular filtration; IC:UniProtKB. DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB. DR GO; GO:0038180; P:nerve growth factor signaling pathway; IDA:UniProtKB. DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; ISO:RGD. DR GO; GO:0072015; P:podocyte development; IEP:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB. DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:UniProtKB. DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB. DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; ISO:RGD. DR GO; GO:0043113; P:receptor clustering; IDA:RGD. DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO. DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; IDA:SynGO. DR GO; GO:0007165; P:signal transduction; ISO:RGD. DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB. DR CDD; cd00992; PDZ_signaling; 6. DR CDD; cd00201; WW; 2. DR Gene3D; 2.20.70.10; -; 2. DR Gene3D; 2.30.42.10; -; 6. DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR10316; MEMBRANE ASSOCIATED GUANYLATE KINASE-RELATED; 1. DR PANTHER; PTHR10316:SF27; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 2; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF16663; MAGI_u1; 1. DR Pfam; PF00595; PDZ; 6. DR Pfam; PF00397; WW; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00228; PDZ; 6. DR SMART; SM00456; WW; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 6. DR SUPFAM; SSF51045; WW domain; 2. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 6. DR PROSITE; PS01159; WW_DOMAIN_1; 2. DR PROSITE; PS50020; WW_DOMAIN_2; 2. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm; KW Cytoskeleton; Endocytosis; Endosome; Membrane; Neurogenesis; KW Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome. FT CHAIN 1..1277 FT /note="Membrane-associated guanylate kinase, WW and PDZ FT domain-containing protein 2" FT /id="PRO_0000094588" FT DOMAIN 17..101 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 109..283 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT DOMAIN 302..335 FT /note="WW 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 348..381 FT /note="WW 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 426..510 FT /note="PDZ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 605..683 FT /note="PDZ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 778..860 FT /note="PDZ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 920..1010 FT /note="PDZ 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 1141..1223 FT /note="PDZ 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT REGION 205..308 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 302..381 FT /note="Interaction with DDN" FT /evidence="ECO:0000250" FT REGION 556..575 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 869..913 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1011..1130 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 282..301 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 874..913 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1011..1044 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1045..1059 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1071..1087 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1113..1130 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 362 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9WVQ1" FT MOD_RES 686 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 827 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9WVQ1" FT MOD_RES 884 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 885 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT VAR_SEQ 1..223 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_008439" FT VAR_SEQ 1..163 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10644767" FT /id="VSP_008438" FT CONFLICT 645 FT /note="L -> F (in Ref. 2; AAD31015)" FT /evidence="ECO:0000305" SQ SEQUENCE 1277 AA; 141072 MW; E1A435FF35549DF9 CRC64; MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EDFMELEKSG ALLESGTYED NYYGTPKPPA EPAPLLLNVT DQILPGATPS AEGKRKRNKS VTNMEKASIE PPEEEEEERP VVNGNGVVIT PESSEHEDKS AGASGETPSQ PYPAPVYSQP EELKDQMDDT KSTKPEENED SDPLPDNWEM AYTEKGEVYF IDHNTKTTSW LDPRLAKKAK PAEECKENEL PYGWEKIDDP IYGTYYVDHI NRRTQFENPV LEAKRKLQQH NMPHTELGTK PLQAPGFREK PLFTRDASQL KGTFLSTTLK KSNMGFGFTI IGGDEPDEFL QVKSVIPDGP AAQDGKMETG DVIVYINEVC VLGHTHADVV KLFQSVPIGQ SVNLVLCRGY PLPFDPEDPA NSMVPPLAIM ERPPPVMVNG RHNYETYLEY ISRTSQSVPD ITDRPPHSLH SMPADGQLDG TYPPPVHDDN VSVASSGATQ AELMTLTIVK GAKGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN QQNVQNLSHT EVVDILKDCP VGSETSLIIH RGGFFSPWKT PKPMVDRWEN QGSPQTSLSA PAVPQSLPFP PALHRSSFPD STEAFDPRKP DPYELYEKSR AIYESRQQVP PRTSFRMDSS GPDYKELDVH LRRMESGFGF RILGGDEPGQ PILIGAVIAM GSADRDGRLH PGDELVYVDG IPVAGKTHRY VIDLMHHAAR NGQVNLTVRR KVLCGGEPCP ENGRSPGSVS THHSSPRSDY ATYANSNHAA PSNNASPPEG FASHSLQTSD VIIHRKENEG FGFVIISSLN RPESGATITV PHKIGRIIDG SPADRCAKLK VGDRILAVNG QSIINMPHAD IVKLIKDAGL SVTLRIIPQE ELNNPTSAPS SEKQSPMAQQ HSPLAQQHSP LAQPSPATPN SPVAQPAPPQ PLQLQGHENS YRSEVKARQD VKPDIRQPPF TDYRQPPLDY RQPPGGDYSQ PSPLDYRQHS PDTRQYPLSD YRQPQDFDYF TVDMEKGAKG FGFSIRGGRE YKMDLYVLRL AEDGPAIRNG RMRVGDQIIE INGESTRDMT HARAIELIKS GGRRVRLLLK RGTGQVPEYG MVPSSLSMCM KSDKHGSPYF YLLGHPKDTT NPTPGALPLP PPQACRK //