SHAN2_RAT
ID SHAN2_RAT Reviewed; 1474 AA.
AC Q9QX74; O70470; Q6WB19; Q9QX93; Q9QZZ9; Q9WUV9; Q9WUW0; Q9WV46;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=SH3 and multiple ankyrin repeat domains protein 2;
DE Short=Shank2;
DE AltName: Full=Cortactin-binding protein 1;
DE Short=CortBP1;
DE AltName: Full=GKAP/SAPAP-interacting protein;
DE AltName: Full=Proline-rich synapse-associated protein 1;
DE Short=ProSAP1;
DE AltName: Full=SPANK-3;
GN Name=Shank2; Synonyms=Cortbp1;
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 5), AND INTERACTION WITH CTTN.
RC TISSUE=Hippocampus;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 5 AND 6), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain, and Hippocampus;
RX PubMed=10414979; DOI=10.1523/jneurosci.19-15-06506.1999;
RA Boeckers T.M., Kreutz M.R., Winter C., Zuschratter W., Smalla K.-H.,
RA Sanmarti-Vila L., Wex H., Langnaese K., Bockmann J., Garner C.C.,
RA Gundelfinger E.D.;
RT "Proline-rich synapse-associated protein-1/cortactin binding protein 1
RT (ProSAP1/CortBP1) is a PDZ-domain protein highly enriched in the
RT postsynaptic density.";
RL J. Neurosci. 19:6506-6518(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND TISSUE SPECIFICITY.
RC TISSUE=Hepatocyte;
RX PubMed=14977424; DOI=10.1042/bj20031577;
RA McWilliams R.R., Gidey E., Fouassier L., Weed S.A., Doctor R.B.;
RT "Characterization of an ankyrin repeat-containing Shank2 isoform (Shank2E)
RT in liver epithelial cells.";
RL Biochem. J. 380:181-191(2004).
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4/5/6), TISSUE
RP SPECIFICITY, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=10506216; DOI=10.1074/jbc.274.41.29510;
RA Lim S., Naisbitt S., Yoon J., Hwang J.-I., Suh P.-G., Sheng M., Kim E.;
RT "Characterization of the shank family of synaptic proteins. Multiple genes,
RT alternative splicing, and differential expression in brain and
RT development.";
RL J. Biol. Chem. 274:29510-29518(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-656 (ISOFORM 3).
RX PubMed=10958799; DOI=10.1074/jbc.m006448200;
RA Tobaben S., Suedhof T.C., Stahl B.;
RT "The G protein-coupled receptor CL1 interacts directly with proteins of the
RT Shank family.";
RL J. Biol. Chem. 275:36204-36210(2000).
RN [6]
RP INTERACTION WITH DLGAP1 AND DLG4.
RX PubMed=10527873; DOI=10.1006/bbrc.1999.1489;
RA Boeckers T.M., Winter C., Smalla K.-H., Kreutz M.R., Bockmann J.,
RA Seidenbecher C., Garner C.C., Gundelfinger E.D.;
RT "Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with
RT synaptic proteins of the SAPAP/GKAP family.";
RL Biochem. Biophys. Res. Commun. 264:247-252(1999).
RN [7]
RP INTERACTION WITH ALPHA-LATROTOXIN RECEPTOR 1.
RX PubMed=10964907; DOI=10.1074/jbc.c000490200;
RA Kreienkamp H.-J., Zitzer H., Gundelfinger E.D., Richter D., Bockers T.M.;
RT "The calcium-independent receptor for alpha-latrotoxin from human and
RT rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of
RT multidomain proteins.";
RL J. Biol. Chem. 275:32387-32390(2000).
RN [8]
RP REVIEW.
RX PubMed=10806096; DOI=10.1242/jcs.113.11.1851;
RA Sheng M., Kim E.;
RT "The Shank family of scaffold proteins.";
RL J. Cell Sci. 113:1851-1856(2000).
RN [9]
RP TISSUE SPECIFICITY, AND INTERACTION WITH CFTR.
RX PubMed=14679199; DOI=10.1074/jbc.m312871200;
RA Kim J.Y., Han W., Namkung W., Lee J.H., Kim K.H., Shin H., Kim E.,
RA Lee M.G.;
RT "Inhibitory regulation of cystic fibrosis transmembrane conductance
RT regulator anion-transporting activities by Shank2.";
RL J. Biol. Chem. 279:10389-10396(2004).
RN [10]
RP INTERACTION WITH DBNL.
RX PubMed=15014124; DOI=10.1523/jneurosci.5479-03.2004;
RA Qualmann B., Boeckers T.M., Jeromin M., Gundelfinger E.D., Kessels M.M.;
RT "Linkage of the actin cytoskeleton to the postsynaptic density via direct
RT interactions of Abp1 with the ProSAP/Shank family.";
RL J. Neurosci. 24:2481-2495(2004).
RN [11]
RP INTERACTION WITH PLCB3.
RX PubMed=15632121; DOI=10.1074/jbc.m410740200;
RA Hwang J.-I., Kim H.S., Lee J.R., Kim E., Ryu S.H., Suh P.-G.;
RT "The interaction of phospholipase C-beta3 with Shank2 regulates mGluR-
RT mediated calcium signal.";
RL J. Biol. Chem. 280:12467-12473(2005).
RN [12]
RP INTERACTION WITH SLC9A3.
RX PubMed=16293618; DOI=10.1074/jbc.m509786200;
RA Han W., Kim K.H., Jo M.J., Lee J.H., Yang J., Doctor R.B., Moe O.W.,
RA Lee J., Kim E., Lee M.G.;
RT "Shank2 associates with and regulates Na+/H+ exchanger 3.";
RL J. Biol. Chem. 281:1461-1469(2006).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=16758162; DOI=10.1007/s00418-006-0199-9;
RA Redecker P., Bockmann J., Boeckers T.M.;
RT "Expression of postsynaptic density proteins of the ProSAP/Shank family in
RT the thymus.";
RL Histochem. Cell Biol. 126:679-685(2006).
RN [14]
RP INTERACTION WITH ABI1.
RX PubMed=17304222; DOI=10.1038/sj.emboj.7601569;
RA Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J.,
RA Kreutz M.R., Gundelfinger E.D., Boeckers T.M.;
RT "Abelson interacting protein 1 (Abi-1) is essential for dendrite
RT morphogenesis and synapse formation.";
RL EMBO J. 26:1397-1409(2007).
RN [15]
RP INTERACTION WITH PDE4D, SUBCELLULAR LOCATION, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373 (ISOFORMS 2 AND 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 (ISOFORMS 4; 5 AND 6),
RP AND 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).
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. {ECO:0000269|PubMed:10506216}.
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 with ABI1 (via SH3 domain). Interacts
CC (via proline-rich region) with PDE4D isoform 5 (via N-terminal region).
CC Interacts with PDE4D isoform 33, isoform 4, isoform 7, isoform 8 and
CC isoform 9 but not isoform 32 and isoform 6. Interacts weakly with PDE4D
CC isoform 31. Interacts with ABI1. {ECO:0000269|PubMed:10527873,
CC ECO:0000269|PubMed:10964907, ECO:0000269|PubMed:14679199,
CC ECO:0000269|PubMed:15014124, ECO:0000269|PubMed:15632121,
CC ECO:0000269|PubMed:16293618, ECO:0000269|PubMed:17244609,
CC ECO:0000269|PubMed:17304222, ECO:0000269|PubMed:9742101}.
CC -!- INTERACTION:
CC Q9QX74; P14270-8: Pde4d; NbExp=4; IntAct=EBI-397902, EBI-9032440;
CC Q9QX74; P26433: Slc9a3; NbExp=2; IntAct=EBI-397902, EBI-961694;
CC Q9QX74; Q9ES28-2: Arhgef7; Xeno; NbExp=4; IntAct=EBI-397902, EBI-8620514;
CC Q9QX74; P13569: CFTR; Xeno; NbExp=2; IntAct=EBI-397902, EBI-349854;
CC Q9QX74-7; P27732: Cacna1d; NbExp=2; IntAct=EBI-20939146, EBI-8072674;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:17244609}. Cytoplasm {ECO:0000269|PubMed:17244609}.
CC Synapse {ECO:0000269|PubMed:17244609}. Postsynaptic density
CC {ECO:0000269|PubMed:17244609}. Cell projection, growth cone
CC {ECO:0000269|PubMed:17244609}. Cell projection, dendritic spine
CC {ECO:0000250}. Note=Colocalizes with cortactin in growth cones in
CC differentiating hippocampal neurons. Present in the dendritic spines of
CC cerebellar Purkinje cells (By similarity). Colocalizes with cortactin
CC in growth cones in differentiating hippocampal neurons. Colocalized
CC with PDE4D to the apical membrane of colonic crypt cells.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=So far detected are complete isoforms 2 to 5. Experimental
CC confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9QX74-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QX74-2; Sequence=VSP_006083;
CC Name=3;
CC IsoId=Q9QX74-3; Sequence=VSP_006083, VSP_006084, VSP_006086;
CC Name=4;
CC IsoId=Q9QX74-4; Sequence=VSP_006081, VSP_006082, VSP_006083;
CC Name=5;
CC IsoId=Q9QX74-5; Sequence=VSP_006081, VSP_006082, VSP_006083,
CC VSP_006084;
CC Name=6;
CC IsoId=Q9QX74-6; Sequence=VSP_006081, VSP_006082, VSP_006083,
CC VSP_006085;
CC Name=7; Synonyms=E;
CC IsoId=Q9QX74-7; Sequence=VSP_020049, VSP_020050;
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells (at protein level).
CC All isoforms except isoform 7 are expressed predominantly in brain,
CC with highest levels in olfactory bulb, cerebral cortex, cerebellum,
CC central gray matter and hippocampus. Moderate levels of expression are
CC seen in the caudate putamen, thalamic nuclei and brain stem. In
CC cerebellum primarily expressed in Purkinje cells. Isoform 7 is not
CC expressed in brain but expressed in liver, cholangiocytes and thymus.
CC Isoform 7 is present in pancreas, colonic mucosa and thymocytes (at
CC protein level). {ECO:0000269|PubMed:10414979,
CC ECO:0000269|PubMed:10506216, ECO:0000269|PubMed:14679199,
CC ECO:0000269|PubMed:14977424, ECO:0000269|PubMed:16758162,
CC ECO:0000269|PubMed:17244609}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early postnatal brain
CC development, especially in the caudate putamen and thalamic nuclei.
CC Expression in the cerebral cortex, the hippocampus and the cerebellum
CC is moderate to high at P5 and shows a stable expression throughout
CC development. Isoforms 1, 2, 4 and 6 are predominantly expressed in
CC cerebellum up to the age of approximately 3 weeks. Isoform 1 expression
CC decreases during development of cortex but slightly increases in
CC cerebellum. {ECO:0000269|PubMed:10414979}.
CC -!- DOMAIN: The PDZ domain is required for interaction with GRID2, PLCB3,
CC SLC9A3 and CFTR.
CC -!- MISCELLANEOUS: [Isoform 7]: Contains 6 ANK repeats at positions 196-
CC 226, 230-259, 263-293, 297-326, 330-359, 363-393. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD42977.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF060116; AAC62226.1; -; mRNA.
DR EMBL; AJ249562; CAB56522.1; -; mRNA.
DR EMBL; AJ131899; CAB44314.1; -; mRNA.
DR EMBL; AJ131899; CAB44312.1; -; mRNA.
DR EMBL; AJ131899; CAB44313.1; -; mRNA.
DR EMBL; AY298755; AAP85236.1; -; mRNA.
DR EMBL; AF141903; AAF02497.1; -; mRNA.
DR EMBL; AF159048; AAD42977.1; ALT_FRAME; mRNA.
DR PIR; T14272; T14272.
DR RefSeq; NP_001004133.1; NM_001004133.1.
DR RefSeq; NP_597684.1; NM_133440.1. [Q9QX74-4]
DR RefSeq; NP_597685.1; NM_133441.1. [Q9QX74-2]
DR RefSeq; NP_958738.1; NM_201350.1. [Q9QX74-7]
DR RefSeq; XP_017444213.1; XM_017588724.1. [Q9QX74-7]
DR PDB; 6CPJ; NMR; -; A=148-206.
DR PDBsum; 6CPJ; -.
DR AlphaFoldDB; Q9QX74; -.
DR SMR; Q9QX74; -.
DR BioGRID; 251104; 4.
DR CORUM; Q9QX74; -.
DR IntAct; Q9QX74; 13.
DR MINT; Q9QX74; -.
DR STRING; 10116.ENSRNOP00000067841; -.
DR GlyGen; Q9QX74; 1 site.
DR iPTMnet; Q9QX74; -.
DR PhosphoSitePlus; Q9QX74; -.
DR jPOST; Q9QX74; -.
DR PaxDb; Q9QX74; -.
DR PRIDE; Q9QX74; -.
DR ABCD; Q9QX74; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000075078; ENSRNOP00000065891; ENSRNOG00000050206. [Q9QX74-7]
DR Ensembl; ENSRNOT00000092386; ENSRNOP00000075919; ENSRNOG00000050206. [Q9QX74-5]
DR Ensembl; ENSRNOT00000092516; ENSRNOP00000075839; ENSRNOG00000050206. [Q9QX74-2]
DR GeneID; 171093; -.
DR KEGG; rno:171093; -.
DR UCSC; RGD:628772; rat. [Q9QX74-1]
DR CTD; 22941; -.
DR RGD; 628772; Shank2.
DR VEuPathDB; HostDB:ENSRNOG00000050206; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4375; Eukaryota.
DR GeneTree; ENSGT00940000153561; -.
DR InParanoid; Q9QX74; -.
DR PRO; PR:Q9QX74; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000050206; Expressed in frontal cortex and 13 other tissues.
DR ExpressionAtlas; Q9QX74; baseline and differential.
DR Genevisible; Q9QX74; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0032279; C:asymmetric synapse; IDA:SynGO.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0060170; C:ciliary membrane; IDA:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0005883; C:neurofilament; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISS:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:BHF-UCL.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISS:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; IDA:SynGO.
DR GO; GO:0030160; F:synaptic receptor adaptor activity; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; ISS:BHF-UCL.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:RGD.
DR GO; GO:0008306; P:associative learning; IMP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0035640; P:exploration behavior; ISS:BHF-UCL.
DR GO; GO:0007612; P:learning; ISS:BHF-UCL.
DR GO; GO:0060292; P:long-term synaptic depression; ISS:BHF-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:BHF-UCL.
DR GO; GO:0099562; P:maintenance of postsynaptic density structure; ISO:RGD.
DR GO; GO:0007613; P:memory; ISS:BHF-UCL.
DR GO; GO:0035331; P:negative regulation of hippo signaling; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:RGD.
DR GO; GO:0035176; P:social behavior; IMP:RGD.
DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
DR GO; GO:0071625; P:vocalization behavior; ISS: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 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW SH3 domain; SH3-binding; Synapse.
FT CHAIN 1..1474
FT /note="SH3 and multiple ankyrin repeat domains protein 2"
FT /id="PRO_0000174674"
FT DOMAIN 148..207
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 248..342
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1411..1474
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 66..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..995
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..1401
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..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..534
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..920
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..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 1356..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z38"
FT MOD_RES 486
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z38"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z38"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z38"
FT MOD_RES 903
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z38"
FT MOD_RES 1334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z38"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z38"
FT CARBOHYD 1292
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..211
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10414979,
FT ECO:0000303|PubMed:9742101"
FT /id="VSP_006081"
FT VAR_SEQ 1..12
FT /note="MKSLLNAFTKKE -> MPRSPTSSEDEMAQSFSDYSVGSESDSSKEETIYDT
FT IRATTEKPGGVKMEDLQGNTLVIRVVIQDLQQTKCIRFNPDATVWVAKQRILCTLNQGL
FT KDVLNYGLFQPASNGRDGKFLDEERLLREYPQPMGQGVPSLEFRYKKRVYKQSNLDEKQ
FT LARLHTKTNLKKFMDHTQHRSVEKLVKLLDRGLDPNFHDLETGETPLTLAAQLDGSMEV
FT IKALRNGGAHLDFRSRDGMTALHKAARMRNQVALKTLLELGASPDYKDSYGLTPLYHTA
FT IVGGDPYCCELLLHEHASVCCKDENGWHEIHQACRYGHVQHLEHLLFYGADMSAQNASG
FT NTALHICALYNQDSCARVLLFRGGDKELKNYNSQTPFQVAIIAGNFELAEYIKNHKETD
FT I (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14977424"
FT /id="VSP_020049"
FT VAR_SEQ 212..239
FT /note="SQAETRADRSKKLFRHYTVGSYDSFDAA -> MMSVPGGGAATVMMTGYNNG
FT RYPRNSLY (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10414979,
FT ECO:0000303|PubMed:9742101"
FT /id="VSP_006082"
FT VAR_SEQ 382..395
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14977424"
FT /id="VSP_020050"
FT VAR_SEQ 382..385
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10414979,
FT ECO:0000303|PubMed:10958799, ECO:0000303|PubMed:9742101"
FT /id="VSP_006083"
FT VAR_SEQ 388..394
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10414979,
FT ECO:0000303|PubMed:10958799, ECO:0000303|PubMed:9742101"
FT /id="VSP_006084"
FT VAR_SEQ 468..483
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10958799"
FT /id="VSP_006086"
FT VAR_SEQ 468..476
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:10414979"
FT /id="VSP_006085"
FT CONFLICT 35..41
FT /note="PRVLLRS -> QKNLGAA (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="L -> F (in Ref. 3; AAF02497)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="L -> V (in Ref. 1; AAC62226)"
FT /evidence="ECO:0000305"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:6CPJ"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:6CPJ"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:6CPJ"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:6CPJ"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6CPJ"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6CPJ"
FT MOD_RES Q9QX74-2:373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9QX74-3:373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9QX74-4:162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9QX74-5:162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9QX74-6:162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1474 AA; 158684 MW; F503D44D0D9AB7C1 CRC64;
MKSLLNAFTK KEVPFREAPA YSNRRRRPPN TLAAPRVLLR SNSDNNLNAG APEWAVCSAA
TSHRSLSPQL LQQTPSKPDG ATKSLGSYAP GPRSRSPSLN RLGGAGEDGK RPQPPHWHVG
SPFTPGANKD SLSTFEYPGP RRKLYSAVPG RLFVAIKPYQ PQVDGEIPLH RGDRVKVLSI
GEGGFWEGSA RGHIGWFPAE CVEEVQCKPR DSQAETRADR SKKLFRHYTV GSYDSFDAAS
DCIIEDKTVV LQKKDNEGFG FVLRGAKADT PIEEFTPTPA FPALQYLESV DEGGVAWQAG
LRTGDFLIEV NNENVVKVGH RQVVNMIRQG GNHLVLKVVT VTRNLDPDDT ARKKAPPPPK
RAPTTALTLR SKSMTAELEE LGLSLVDKAS VRKKKDKPEE IVPASKPSRT AENVAIESRV
ATIKQRPTSR CFPAASDVNS VYERQGIAVM TPTVPGSPKG PFLGLPRGTM RRQKSIDSRI
FLSGITEEER QFLAPPMLKF TRSLSMPDTS EDIPPPPQSV PPSPPPPSPT TYNCPRSPTP
RVYGTIKPAF NQNPVAKVPP ATRSDTVATM MREKGMFYRR ELDRFSLDSE DVYSRSPAPQ
AAFRTKRGQM PENPYSEVGK IASKAVYVPA KPARRKGMLV KQSNVEDSPE KTCSIPIPTI
IVKEPSTSSS GKSSQGSSME IDPQATEPGQ LRPDDSLTVS SPFAAAIAGA VRDREKRLEA
RRNSPAFLST DLGDEDVGLG PPAPRMQPSK FPEEGGFGDE DETEQPLLPT PGAAPRELEN
HFLGGGEAGA QGEAGGPLSS TSKAKGPESG PAAALKSSSP ASPENYVHPL TGRLLDPSSP
LALALSARDR AMQESQQGHK GEAPKADLNK PLYIDTKMRP SVESGFPPVT RQNTRGPLRR
QETENKYETD LSKDRRADDK KNMLINIVDT AQQKSAGLLM VHTVDIPVAG PPLEEEEDRE
DGDTKPDHSP STVPEGVPKT EGALQISAAP EPAAAPGRTI VAAGSVEEAV ILPFRIPPPP
LASVDLDEDF LFTEPLPPPL EFANSFDIPD DRAASVPALA DLVKQKKSDT PQPPSLNSSQ
PANSTDSKKP AGISNCLPSS FLPPPESFDA VTDSGIEEVD SRSSSDHHLE TTSTISTVSS
ISTLSSEGGE SMDTCTVYAD GQAFVVDKPP VPPKPKMKPI VHKSNALYQD TLPEEDTDGF
VIPPPAPPPP PGSAQAGVAK VIQPRTSKLW GDVTEVKSPI LSGPKANVIS ELNSILQQMN
RGKSVKPGEG LELPVGAKSA NLAPRSPEVM STVSGTRSTT VTFTVRPGTS QPITLQSRPP
DYESRTSGPR RAPSPVVSPT ELSKEILPTP PSAAAASPSP TLSDVFSLPS QSPAGDLFGL
NPAGRSRSPS PSILQQPISN KPFTTKPVHL WTKPDVADWL ESLNLGEHKE TFMDNEIDGS
HLPNLQKEDL IDLGVTRVGH RMNIERALKQ LLDR
