ID   MPP2_HUMAN              Reviewed;         576 AA.
AC   Q14168; B4DGE9; B4DRJ0; B7Z3G8; E7EV80; E7EV91; E7EX01; Q53ES9; Q5CZB9;
AC   Q9BQJ2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 3.
DT   27-MAR-2024, entry version 204.
DE   RecName: Full=MAGUK p55 subfamily member 2;
DE   AltName: Full=Discs large homolog 2;
DE   AltName: Full=Protein MPP2;
GN   Name=MPP2 {ECO:0000312|HGNC:HGNC:7220}; Synonyms=DLG2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=7590743; DOI=10.1006/geno.1995.1101;
RA   Mazoyer S., Gayther S.A., Nagai M.A., Smith S.A., Dunning A.,
RA   van Rensburg E.J., Albertsen H., White R., Ponder B.A.J.;
RT   "A gene (DLG2) located at 17q12-q21 encodes a new homologue of the
RT   Drosophila tumor suppressor dlg-A.";
RL   Genomics 28:25-31(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Amygdala;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC   TISSUE=Amygdala, and Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Salivary gland;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   FUNCTION, INTERACTION WITH SRC, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP   TYR-363, AND PHOSPHORYLATION.
RX   PubMed=19665017; DOI=10.1016/j.yexcr.2009.07.028;
RA   Baumgartner M., Weiss A., Fritzius T., Heinrich J., Moelling K.;
RT   "The PDZ protein MPP2 interacts with c-Src in epithelial cells.";
RL   Exp. Cell Res. 315:2888-2898(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   STRUCTURE BY NMR OF 163-240.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PDZ domain from human maguk p55 subfamily member
RT   2.";
RL   Submitted (JAN-2008) to the PDB data bank.
CC   -!- FUNCTION: Postsynaptic MAGUK scaffold protein that links CADM1 cell
CC       adhesion molecules to core components of the postsynaptic density (By
CC       similarity). In CA1 pyramidal neurons, required for synaptic KCNN2-
CC       containing channel function and long-term potentiation expression (By
CC       similarity). Seems to negatively regulate SRC function in epithelial
CC       cells (PubMed:19665017). {ECO:0000250|UniProtKB:D3ZAA9,
CC       ECO:0000250|UniProtKB:Q9WV34, ECO:0000269|PubMed:19665017}.
CC   -!- SUBUNIT: Can homomultimerise. Interacts with CACNG2. Interacts (via the
CC       SH3-Guanylate kinase-like sub-module) with DLG4/PSD95 and DLGAP1/GKAP.
CC       Interacts (via the PDZ domain) with CADM1 (via C-terminus) (By
CC       similarity). Interacts with KCNN2/SK2 (via N-terminal domain) (By
CC       similarity). Interacts with SRC (PubMed:19665017).
CC       {ECO:0000250|UniProtKB:D3ZAA9, ECO:0000250|UniProtKB:Q9WV34,
CC       ECO:0000269|PubMed:19665017}.
CC   -!- INTERACTION:
CC       Q14168-2; O14910: LIN7A; NbExp=4; IntAct=EBI-10181752, EBI-2513988;
CC       Q14168-4; O14910: LIN7A; NbExp=7; IntAct=EBI-14385193, EBI-2513988;
CC       Q14168-4; Q9HAP6: LIN7B; NbExp=3; IntAct=EBI-14385193, EBI-821335;
CC       Q14168-4; Q9NUP9: LIN7C; NbExp=7; IntAct=EBI-14385193, EBI-1171517;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:19665017}. Membrane {ECO:0000269|PubMed:19665017}.
CC       Cell projection, dendrite {ECO:0000250|UniProtKB:Q9WV34}. Postsynaptic
CC       density {ECO:0000250|UniProtKB:Q9WV34}. Note=Prominently expressed in
CC       the postsynaptic densities of dendritic spines, is also detected in
CC       dendritic shafts. {ECO:0000250|UniProtKB:Q9WV34}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q14168-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14168-2; Sequence=VSP_003156;
CC       Name=3;
CC         IsoId=Q14168-3; Sequence=VSP_022951, VSP_003156;
CC       Name=4;
CC         IsoId=Q14168-4; Sequence=VSP_055138, VSP_003156;
CC       Name=5;
CC         IsoId=Q14168-5; Sequence=VSP_055136;
CC       Name=6;
CC         IsoId=Q14168-6; Sequence=VSP_055137, VSP_003156;
CC   -!- PTM: Phosphorylated by SRC. {ECO:0000269|PubMed:19665017}.
CC   -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR   EMBL; X82895; CAA58067.1; -; mRNA.
DR   EMBL; AL136554; CAB66489.1; -; mRNA.
DR   EMBL; AK294564; BAG57760.1; -; mRNA.
DR   EMBL; AK295858; BAH12204.1; -; mRNA.
DR   EMBL; AK299286; BAG61302.1; -; mRNA.
DR   EMBL; CR936598; CAI56746.1; -; mRNA.
DR   EMBL; AK223560; BAD97280.1; -; mRNA.
DR   EMBL; AC007993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC030287; AAH30287.1; -; mRNA.
DR   CCDS; CCDS11471.1; -. [Q14168-2]
DR   CCDS; CCDS62206.1; -. [Q14168-5]
DR   CCDS; CCDS62207.1; -. [Q14168-6]
DR   CCDS; CCDS62208.1; -. [Q14168-3]
DR   CCDS; CCDS62209.1; -. [Q14168-1]
DR   CCDS; CCDS62210.1; -. [Q14168-4]
DR   PIR; A57653; A57653.
DR   RefSeq; NP_001265299.1; NM_001278370.1.
DR   RefSeq; NP_001265300.1; NM_001278371.1.
DR   RefSeq; NP_001265301.1; NM_001278372.1.
DR   RefSeq; NP_001265302.1; NM_001278373.1.
DR   RefSeq; NP_001265303.1; NM_001278374.1. [Q14168-5]
DR   RefSeq; NP_001265304.1; NM_001278375.1.
DR   RefSeq; NP_001265305.2; NM_001278376.2.
DR   RefSeq; NP_001265310.1; NM_001278381.1.
DR   RefSeq; NP_005365.4; NM_005374.4.
DR   PDB; 2E7K; NMR; -; A=163-240.
DR   PDBsum; 2E7K; -.
DR   AlphaFoldDB; Q14168; -.
DR   BMRB; Q14168; -.
DR   SMR; Q14168; -.
DR   BioGRID; 110495; 42.
DR   IntAct; Q14168; 19.
DR   MINT; Q14168; -.
DR   STRING; 9606.ENSP00000428182; -.
DR   iPTMnet; Q14168; -.
DR   PhosphoSitePlus; Q14168; -.
DR   SwissPalm; Q14168; -.
DR   BioMuta; MPP2; -.
DR   DMDM; 290457681; -.
DR   EPD; Q14168; -.
DR   jPOST; Q14168; -.
DR   MassIVE; Q14168; -.
DR   MaxQB; Q14168; -.
DR   PaxDb; 9606-ENSP00000428182; -.
DR   PeptideAtlas; Q14168; -.
DR   ProteomicsDB; 18580; -.
DR   ProteomicsDB; 18587; -.
DR   ProteomicsDB; 18952; -.
DR   ProteomicsDB; 59895; -. [Q14168-1]
DR   ProteomicsDB; 59896; -. [Q14168-2]
DR   ProteomicsDB; 59897; -. [Q14168-3]
DR   Pumba; Q14168; -.
DR   TopDownProteomics; Q14168-2; -. [Q14168-2]
DR   Antibodypedia; 17305; 243 antibodies from 26 providers.
DR   DNASU; 4355; -.
DR   Ensembl; ENST00000520305.5; ENSP00000428136.1; ENSG00000108852.16. [Q14168-5]
DR   GeneID; 4355; -.
DR   KEGG; hsa:4355; -.
DR   UCSC; uc010win.3; human. [Q14168-1]
DR   AGR; HGNC:7220; -.
DR   CTD; 4355; -.
DR   DisGeNET; 4355; -.
DR   GeneCards; MPP2; -.
DR   HGNC; HGNC:7220; MPP2.
DR   HPA; ENSG00000108852; Tissue enhanced (brain).
DR   MIM; 600723; gene.
DR   neXtProt; NX_Q14168; -.
DR   OpenTargets; ENSG00000108852; -.
DR   PharmGKB; PA30925; -.
DR   VEuPathDB; HostDB:ENSG00000108852; -.
DR   eggNOG; KOG0609; Eukaryota.
DR   GeneTree; ENSGT00940000155348; -.
DR   HOGENOM; CLU_001715_5_1_1; -.
DR   InParanoid; Q14168; -.
DR   OrthoDB; 2873706at2759; -.
DR   PhylomeDB; Q14168; -.
DR   TreeFam; TF314263; -.
DR   PathwayCommons; Q14168; -.
DR   SignaLink; Q14168; -.
DR   BioGRID-ORCS; 4355; 22 hits in 1149 CRISPR screens.
DR   ChiTaRS; MPP2; human.
DR   EvolutionaryTrace; Q14168; -.
DR   GeneWiki; MPP2; -.
DR   GenomeRNAi; 4355; -.
DR   Pharos; Q14168; Tbio.
DR   PRO; PR:Q14168; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q14168; Protein.
DR   Bgee; ENSG00000108852; Expressed in C1 segment of cervical spinal cord and 149 other cell types or tissues.
DR   ExpressionAtlas; Q14168; baseline and differential.
DR   GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0032590; C:dendrite membrane; ISS:UniProtKB.
DR   GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; ISS:UniProtKB.
DR   GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   CDD; cd00071; GMPK; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd12037; SH3_MPP2; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.10.287.650; L27 domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR004172; L27_dom.
DR   InterPro; IPR036892; L27_dom_sf.
DR   InterPro; IPR035602; MPP2_SH3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23122:SF35; MAGUK P55 SUBFAMILY MEMBER 2; 1.
DR   PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF101288; L27 domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW   Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   SH3 domain; Synapse.
FT   CHAIN           1..576
FT                   /note="MAGUK p55 subfamily member 2"
FT                   /id="PRO_0000094573"
FT   DOMAIN          8..60
FT                   /note="L27 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT   DOMAIN          84..142
FT                   /note="L27 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT   DOMAIN          185..240
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          249..317
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          374..561
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D3ZAA9"
FT   MOD_RES         141
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         145
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WV34"
FT   VAR_SEQ         1..163
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055136"
FT   VAR_SEQ         1..11
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055137"
FT   VAR_SEQ         1..10
FT                   /note="MPVAATNSET -> MAGSPGSGVSLEGISLESSEEAELQRE (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_022951"
FT   VAR_SEQ         1
FT                   /note="M -> MSWAPPPQVGQNLRSQTVLRILNGMEDLMWVAMEERRFRALASFTM
FT                   (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055138"
FT   VAR_SEQ         51..74
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT                   isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:11230166,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|Ref.5"
FT                   /id="VSP_003156"
FT   MUTAGEN         363
FT                   /note="Y->A: Enhances association with the cytoskeleton.
FT                   Diminishes the inhibitory effect on SRC."
FT                   /evidence="ECO:0000269|PubMed:19665017"
FT   MUTAGEN         363
FT                   /note="Y->D: Enhances association with the cytoskeleton."
FT                   /evidence="ECO:0000269|PubMed:19665017"
FT   CONFLICT        80
FT                   /note="E -> G (in Ref. 4; CAI56746)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104..105
FT                   /note="HV -> QL (in Ref. 1; CAA58067, 2; BAD97280, 5;
FT                   CAB66489, 4; CAI56746, 7; AAH30287 and 3;
FT                   BAG61302/BAH12204)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="S -> N (in Ref. 1; CAA58067)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        531
FT                   /note="R -> C (in Ref. 3; BAG57760)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554
FT                   /note="R -> C (in Ref. 3; BAG61302)"
FT                   /evidence="ECO:0000305"
FT   STRAND          177..191
FT                   /evidence="ECO:0007829|PDB:2E7K"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:2E7K"
FT   HELIX           196..200
FT                   /evidence="ECO:0007829|PDB:2E7K"
FT   STRAND          208..212
FT                   /evidence="ECO:0007829|PDB:2E7K"
FT   HELIX           221..229
FT                   /evidence="ECO:0007829|PDB:2E7K"
FT   STRAND          233..235
FT                   /evidence="ECO:0007829|PDB:2E7K"
FT   STRAND          237..240
FT                   /evidence="ECO:0007829|PDB:2E7K"
SQ   SEQUENCE   576 AA;  64581 MW;  A08E858EA646A305 CRC64;
     MPVAATNSET AMQQVLDNLG SLPSATGAAE LDLIFLRGIM ESPIVRSLAK VIMVLWFMQQ
     NVFVPMKYML KYFGAHERLE ETKLEAVRDN NLELVQEILR DLAHVAEQSS TAAELAHILQ
     EPHFQSLLET HDSVASKTYE TPPPSPGLDP TFSNQPVPPD AVRMVGIRKT AGEHLGVTFR
     VEGGELVIAR ILHGGMVAQQ GLLHVGDIIK EVNGQPVGSD PRALQELLRN ASGSVILKIL
     PSYQEPHLPR QVFVKCHFDY DPARDSLIPC KEAGLRFNAG DLLQIVNQDD ANWWQACHVE
     GGSAGLIPSQ LLEEKRKAFV KRDLELTPNS GTLCGSLSGK KKKRMMYLTT KNAEFDRHEL
     LIYEEVARMP PFRRKTLVLI GAQGVGRRSL KNKLIMWDPD RYGTTVPYTS RRPKDSEREG
     QGYSFVSRGE MEADVRAGRY LEHGEYEGNL YGTRIDSIRG VVAAGKVCVL DVNPQAVKVL
     RTAEFVPYVV FIEAPDFETL RAMNRAALES GISTKQLTEA DLRRTVEESS RIQRGYGHYF
     DLCLVNSNLE RTFRELQTAM EKLRTEPQWV PVSWVY
//