GenomeNet

Database: UniProt
Entry: Q9QX74
LinkDB: Q9QX74
Original site: Q9QX74 
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   27-MAR-2024, entry version 182.
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; Q99JE6: Plcb3; NbExp=4; IntAct=EBI-397902, EBI-36481538;
CC       Q9QX74; P26433: Slc9a3; NbExp=5; IntAct=EBI-397902, EBI-961694;
CC       Q9QX74; Q9ES28-2: Arhgef7; Xeno; NbExp=4; IntAct=EBI-397902, EBI-8620514;
CC       Q9QX74; P13569: CFTR; Xeno; NbExp=3; IntAct=EBI-397902, EBI-349854;
CC       Q9QX74-4; Q9ES28: Arhgef7; Xeno; NbExp=3; IntAct=EBI-36481413, EBI-642580;
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.
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; 20.
DR   MINT; Q9QX74; -.
DR   STRING; 10116.ENSRNOP00000065891; -.
DR   GlyCosmos; Q9QX74; 1 site, No reported glycans.
DR   GlyGen; Q9QX74; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9QX74; -.
DR   PhosphoSitePlus; Q9QX74; -.
DR   jPOST; Q9QX74; -.
DR   PaxDb; 10116-ENSRNOP00000067841; -.
DR   ABCD; Q9QX74; 2 sequenced antibodies.
DR   Ensembl; ENSRNOT00000075078.4; ENSRNOP00000065891.2; ENSRNOG00000050206.5. [Q9QX74-7]
DR   Ensembl; ENSRNOT00000092386.2; ENSRNOP00000075919.2; ENSRNOG00000050206.5. [Q9QX74-5]
DR   Ensembl; ENSRNOT00000092516.2; ENSRNOP00000075839.1; ENSRNOG00000050206.5. [Q9QX74-2]
DR   Ensembl; ENSRNOT00060050176; ENSRNOP00060041812; ENSRNOG00060028641. [Q9QX74-1]
DR   GeneID; 171093; -.
DR   KEGG; rno:171093; -.
DR   UCSC; RGD:628772; rat. [Q9QX74-1]
DR   AGR; RGD:628772; -.
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   OMA; GGDPACC; -.
DR   Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR   PRO; PR:Q9QX74; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000050206; Expressed in frontal cortex and 13 other cell types or tissues.
DR   ExpressionAtlas; Q9QX74; baseline and differential.
DR   Genevisible; Q9QX74; RN.
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: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: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; IC:SynGO.
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:0099175; P:regulation of postsynapse 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   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd09506; SAM_Shank1_2_3; 1.
DR   CDD; cd11983; SH3_Shank2; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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   PANTHER; PTHR24135; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR24135:SF17; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN 2; 1.
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; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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
//
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