SHAN2_MOUSE
ID SHAN2_MOUSE Reviewed; 1476 AA.
AC Q80Z38; E9QPH7; Q3UTK4; Q5DU07;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=SH3 and multiple ankyrin repeat domains protein 2;
DE Short=Shank2;
DE AltName: Full=Cortactin-binding protein 1;
DE Short=CortBP1;
GN Name=Shank2; Synonyms=Cortbp1, Kiaa1022;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH GRID2.
RX PubMed=15207857; DOI=10.1016/j.mcn.2004.02.007;
RA Uemura T., Mori H., Mishina M.;
RT "Direct interaction of GluRdelta2 with Shank scaffold proteins in
RT cerebellar Purkinje cells.";
RL Mol. Cell. Neurosci. 26:330-341(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-350 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-1476 (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=9742101; DOI=10.1128/mcb.18.10.5838;
RA Du Y., Weed S.A., Xiong W.-C., Marshall T.D., Parsons J.T.;
RT "Identification of a novel cortactin SH3 domain-binding protein and its
RT localization to growth cones of cultured neurons.";
RL Mol. Cell. Biol. 18:5838-5851(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586 AND THR-903, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-1292.
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [9]
RP INTERACTION WITH PDE4D, AND TISSUE SPECIFICITY.
RX PubMed=17244609; DOI=10.1074/jbc.m610857200;
RA Lee J.H., Richter W., Namkung W., Kim K.H., Kim E., Conti M., Lee M.G.;
RT "Dynamic regulation of cystic fibrosis transmembrane conductance regulator
RT by competitive interactions of molecular adaptors.";
RL J. Biol. Chem. 282:10414-10422(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; THR-485; SER-586;
RP SER-724; SER-1334 AND SER-1338, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-372 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162
RP (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=21423165; DOI=10.1038/nature09965;
RA Peca J., Feliciano C., Ting J.T., Wang W., Wells M.F., Venkatraman T.N.,
RA Lascola C.D., Fu Z., Feng G.;
RT "Shank3 mutant mice display autistic-like behaviours and striatal
RT dysfunction.";
RL Nature 472:437-442(2011).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=22699619; DOI=10.1038/nature11015;
RA Schmeisser M.J., Ey E., Wegener S., Bockmann J., Stempel A.V., Kuebler A.,
RA Janssen A.L., Udvardi P.T., Shiban E., Spilker C., Balschun D.,
RA Skryabin B.V., Dieck S.T., Smalla K.H., Montag D., Leblond C.S., Faure P.,
RA Torquet N., Le Sourd A.M., Toro R., Grabrucker A.M., Shoichet S.A.,
RA Schmitz D., Kreutz M.R., Bourgeron T., Gundelfinger E.D., Boeckers T.M.;
RT "Autistic-like behaviours and hyperactivity in mice lacking
RT ProSAP1/Shank2.";
RL Nature 486:256-260(2012).
CC -!- FUNCTION: Seems to be an adapter protein in the postsynaptic density
CC (PSD) of excitatory synapses that interconnects receptors of the
CC postsynaptic membrane including NMDA-type and metabotropic glutamate
CC receptors, and the actin-based cytoskeleton. May play a role in the
CC structural and functional organization of the dendritic spine and
CC synaptic junction (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP.
CC Interacts with CTTN/cortactin SH3 domain, DLGAP1/GKAP and alpha-
CC latrotoxin receptor 1. Interacts with DNM2, DBNL, GRID2, BAIAP2,
CC SLC9A3, PLCB3 and CFTR. Interacts (via proline-rich region) with PDE4D.
CC Interacts with ABI1 (via SH3 domain). {ECO:0000269|PubMed:15207857,
CC ECO:0000269|PubMed:17244609}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:15207857}. Synapse {ECO:0000269|PubMed:15207857}.
CC Postsynaptic density {ECO:0000269|PubMed:15207857}. Cell projection,
CC dendritic spine {ECO:0000269|PubMed:15207857}. Cell projection, growth
CC cone {ECO:0000250}. Note=Colocalizes with cortactin in growth cones in
CC differentiating hippocampal neurons. Colocalized with PDE4D to the
CC apical membrane of colonic crypt cells (By similarity). Present in the
CC dendritic spines of cerebellar Purkinje cells. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=E;
CC IsoId=Q80Z38-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80Z38-2; Sequence=VSP_020040;
CC Name=3;
CC IsoId=Q80Z38-3; Sequence=VSP_041614, VSP_041615, VSP_020040;
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level), where it is
CC highly expressed in Purkinje cells. {ECO:0000269|PubMed:17244609,
CC ECO:0000269|PubMed:21423165, ECO:0000269|PubMed:9742101}.
CC -!- DOMAIN: The PDZ domain is required for interaction with GRID2, PLCB3,
CC SLC9A3 and CFTR.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable, but with reduced body weight
CC and a lower survival rate compared to their wild-type littermates. They
CC are extremely hiperactive and display profound autistic-like behavioral
CC alterations including repetitive grooming as well as abnormalities in
CC vocal and social behaviors. Mutants exhibit fewer dendritic spines and
CC show reduced basal synaptic transmission, a reduced frequency of
CC miniature excitatory postsynaptic currents and enhanced NMDA receptor-
CC mediated excitatory currents at the physiological level. They also show
CC a brain-region-specific up-regulation of ionotropic glutamate receptors
CC and increased levels of SHANK3. {ECO:0000269|PubMed:22699619}.
CC -!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
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DR EMBL; AB099695; BAC58120.1; -; mRNA.
DR EMBL; AC124520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC152166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC167171; AAI67171.1; -; mRNA.
DR EMBL; AK139360; BAE23976.1; -; mRNA.
DR EMBL; AK220363; BAD90424.1; -; mRNA.
DR CCDS; CCDS40201.1; -. [Q80Z38-3]
DR CCDS; CCDS85484.1; -. [Q80Z38-2]
DR RefSeq; NP_001074839.2; NM_001081370.2. [Q80Z38-3]
DR RefSeq; NP_001106844.2; NM_001113373.2. [Q80Z38-2]
DR RefSeq; XP_006508596.1; XM_006508533.1. [Q80Z38-1]
DR AlphaFoldDB; Q80Z38; -.
DR SMR; Q80Z38; -.
DR BioGRID; 229144; 11.
DR CORUM; Q80Z38; -.
DR IntAct; Q80Z38; 11.
DR MINT; Q80Z38; -.
DR STRING; 10090.ENSMUSP00000101522; -.
DR GlyGen; Q80Z38; 1 site.
DR iPTMnet; Q80Z38; -.
DR PhosphoSitePlus; Q80Z38; -.
DR EPD; Q80Z38; -.
DR jPOST; Q80Z38; -.
DR MaxQB; Q80Z38; -.
DR PaxDb; Q80Z38; -.
DR PeptideAtlas; Q80Z38; -.
DR PRIDE; Q80Z38; -.
DR ProteomicsDB; 261212; -. [Q80Z38-1]
DR ProteomicsDB; 261213; -. [Q80Z38-2]
DR ProteomicsDB; 261214; -. [Q80Z38-3]
DR ABCD; Q80Z38; 1 sequenced antibody.
DR Antibodypedia; 2161; 312 antibodies from 28 providers.
DR DNASU; 210274; -.
DR Ensembl; ENSMUST00000105900; ENSMUSP00000101520; ENSMUSG00000037541. [Q80Z38-2]
DR Ensembl; ENSMUST00000146006; ENSMUSP00000146440; ENSMUSG00000037541. [Q80Z38-3]
DR GeneID; 210274; -.
DR KEGG; mmu:210274; -.
DR UCSC; uc009kqe.2; mouse. [Q80Z38-2]
DR UCSC; uc009kqf.1; mouse. [Q80Z38-3]
DR UCSC; uc009kqg.1; mouse. [Q80Z38-1]
DR CTD; 22941; -.
DR MGI; MGI:2671987; Shank2.
DR VEuPathDB; HostDB:ENSMUSG00000037541; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4375; Eukaryota.
DR GeneTree; ENSGT00940000153561; -.
DR HOGENOM; CLU_001824_0_0_1; -.
DR InParanoid; Q80Z38; -.
DR BioGRID-ORCS; 210274; 1 hit in 58 CRISPR screens.
DR ChiTaRS; Shank2; mouse.
DR PRO; PR:Q80Z38; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q80Z38; protein.
DR Bgee; ENSMUSG00000037541; Expressed in primary visual cortex and 108 other tissues.
DR ExpressionAtlas; Q80Z38; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISS:BHF-UCL.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; ISS:BHF-UCL.
DR GO; GO:0060170; C:ciliary membrane; ISS:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISS:BHF-UCL.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0005883; C:neurofilament; IDA:CACAO.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:BHF-UCL.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISS:BHF-UCL.
DR GO; GO:0048786; C:presynaptic active zone; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; ISO:MGI.
DR GO; GO:0030160; F:synaptic receptor adaptor activity; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; IMP:BHF-UCL.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:MGI.
DR GO; GO:0008306; P:associative learning; ISO:MGI.
DR GO; GO:0035640; P:exploration behavior; IMP:BHF-UCL.
DR GO; GO:0007612; P:learning; IMP:BHF-UCL.
DR GO; GO:0060292; P:long-term synaptic depression; IMP:BHF-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:BHF-UCL.
DR GO; GO:0099562; P:maintenance of postsynaptic density structure; IDA:SynGO.
DR GO; GO:0007613; P:memory; IMP:BHF-UCL.
DR GO; GO:0035331; P:negative regulation of hippo signaling; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:CACAO.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR GO; GO:0007416; P:synapse assembly; IMP:BHF-UCL.
DR GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; SH3 domain;
KW SH3-binding; Synapse.
FT CHAIN 1..1476
FT /note="SH3 and multiple ankyrin repeat domains protein 2"
FT /id="PRO_0000247760"
FT DOMAIN 147..206
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 247..341
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1413..1476
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 66..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1169..1175
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 66..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 485
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 903
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 1334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 1292
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT VAR_SEQ 1..210
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041614"
FT VAR_SEQ 211..238
FT /note="SQAETRADRSKKLFRHYTVGSYDSFDAA -> MMSVPGGGAATVMMTGYNNG
FT RYPRNSLY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041615"
FT VAR_SEQ 380..383
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_020040"
FT CONFLICT 1071
FT /note="S -> P (in Ref. 1; BAC58120 and 5; BAD90424)"
FT /evidence="ECO:0000305"
FT MOD_RES Q80Z38-2:372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q80Z38-3:162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1476 AA; 158969 MW; 0B5B0EBDFD6BAAA7 CRC64;
MKSLLNAFTK KEVPFREAPA YSNRRRRPPN TLAAPRVLLR SNSDNNLNAG APEWAVCSAA
TSHRSLSPQL LQQTPSKPDG ATKSLGSYTP GPRSRSPSLN RLGGTAEDGK RTQPHWHVGS
PFTPGANKDS LSTFEYPGPR RKLYSAVPGR LFVAVKPYQP QVDGEIPLHR GDRVKVLSIG
EGGFWEGSAR GHIGWFPAEC VEEVQCKPRD SQAETRADRS KKLFRHYTVG SYDSFDAASD
CIIEDKTVVL QKKDNEGFGF VLRGAKADTP IEEFTPTPAF PALQYLESVD EGGVAWQAGL
RTGDFLIEVN NENVVKVGHR QVVNMIRQGG NHLILKVVTV TRNLDPDDTA RKKAPPPPKR
APTTALTLRS KSMTAELEEL GLSLVDKASV RKKKDKPEEI VPASKPSRTA ENVAIESRVA
TIKQRPTSRC FPAASDVNSV YERQGIAVMT PTVPGSPKGP FLGLPRGTMR RQKSIDSRIF
LSGITEEERQ FLAPPMLKFT RSLSMPDTSE DIPPPPQSVP PSPPPPSPTT YNCPRSPTPR
VYGTIKPAFN QNPVVAKVPP ATRSDTVATM MREKGMFYRR ELDRFSLDSE DVYSRSPAPQ
AAFRTKRGQM PENPYSEVGK IASKAVYVPA KPARRKGVLV KQSNVEDSPE KTCSIPIPTI
IVKEPSTSSS GKSSQGSSME IDPQATEPGQ LRPDDSLTVS SPFAAAIAGA VRDREKRLEA
RRNSPAFLST DLGDEDVGLG PPAPRMQASK FPEEGGFGDE DETEQPLLPT PGAAPRELEN
HFLGGGEAGA QGEAGGPLSS TSKAKGPESG PAAPLKSSSP AGPENYVHPL TGRLLDPSSP
LALALSARDR AMQESQQGHK GEAPKADLNK PLYIDTKMRP SVESGFPPVT RQNTRGPLRR
QETENKYETD LGKDRRADDK KNMLINIVDT AQQKSAGLLM VHTVDVPMAG PPLEEEEDRE
DGDTKPDHSP STVPEGVPKT EGALQISAAP EPAVAPGRTI VAAGSVEEAV ILPFRIPPPP
LASVDLDEDF LFTEPLPPPL EFANSFDIPD DRAASVPALA DLVKQKKNDT SQPPTLNSSQ
PANSTDSKKP AGISNCLPSS FLPPPESFDA VTDSGIEEVD SRSSSDHHLE TTSTISTVSS
ISTLSSEGGE SMDTCTVYAD GQAFVVDKPP VPPKPKMKPI VHKSNALYQD TLPEEDTDGF
VIPPPAPPPP PGSAQAGVAK VIQPRTSKLW GDVPEVKSPI LSGPKANVIS ELNSILQQMN
RGKSVKPGEG LELPVGAKSA NLAPRSPEVM STVSGTRSTT VTFTVRPGTS QPITLQSRPP
DYESRTSGPR RAPSPVVSPT ELSKEILPTP PPPSATAASP SPTLSDVFSL PSQSPAGDLF
GLNPAGRSRS PSPSILQQPI SNKPFTTKPV HLWTKPDVAD WLESLNLGEH KETFMDNEID
GSHLPNLQKE DLIDLGVTRV GHRMNIERAL KQLLDR
