Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

SH3 and multiple ankyrin repeat domains protein 3 (Shank3) (Proline-rich synapse-associated protein 2) (ProSAP2) (SPANK-2)

 SHAN3_RAT               Reviewed;        1740 AA.
Q9JLU4; Q9WUY7; Q9WV47;
26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
19-FEB-2014, sequence version 3.
25-OCT-2017, entry version 160.
RecName: Full=SH3 and multiple ankyrin repeat domains protein 3;
Short=Shank3;
AltName: Full=Proline-rich synapse-associated protein 2;
Short=ProSAP2;
AltName: Full=SPANK-2;
Name=Shank3; Synonyms=Prosap2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DLGAP1 AND
DLG4, AND TISSUE SPECIFICITY.
PubMed=10527873; DOI=10.1006/bbrc.1999.1489;
Boeckers T.M., Winter C., Smalla K.-H., Kreutz M.R., Bockmann J.,
Seidenbecher C., Garner C.C., Gundelfinger E.D.;
"Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact
with synaptic proteins of the SAPAP/GKAP family.";
Biochem. Biophys. Res. Commun. 264:247-252(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DLGAP1 AND
CTTN, AND OLIGOMERIZATION.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
PubMed=10433268; DOI=10.1016/S0896-6273(00)80809-0;
Naisbitt S., Kim E., Tu J.C., Xiao B., Sala C., Valtschanoff J.,
Weinberg R.J., Worley P.F., Sheng M.;
"Shank, a novel family of postsynaptic density proteins that binds to
the NMDA receptor/PSD-95/GKAP complex and cortactin.";
Neuron 23:569-582(1999).
[3]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=10958799; DOI=10.1074/jbc.M006448200;
Tobaben S., Suedhof T.C., Stahl B.;
"The G protein-coupled receptor CL1 interacts directly with proteins
of the Shank family.";
J. Biol. Chem. 275:36204-36210(2000).
[4]
INTERACTION WITH HOMER1; HOMER2; HOMER3; DLGAP1; MGLUR1A AND MGLUR5,
AND MUTAGENESIS OF PRO-1311 AND PHE-1314.
PubMed=10433269; DOI=10.1016/S0896-6273(00)80810-7;
Tu J.C., Xiao B., Naisbitt S., Yuan J.P., Petralia R.S., Brakeman P.,
Doan A., Aakalu V.K., Lanahan A.A., Sheng M., Worley P.F.;
"Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of
postsynaptic density proteins.";
Neuron 23:583-592(1999).
[5]
REVIEW.
PubMed=10806096;
Sheng M., Kim E.;
"The Shank family of scaffold proteins.";
J. Cell Sci. 113:1851-1856(2000).
[6]
INTERACTION WITH DBNL, AND TISSUE SPECIFICITY.
PubMed=15014124; DOI=10.1523/JNEUROSCI.5479-03.2004;
Qualmann B., Boeckers T.M., Jeromin M., Gundelfinger E.D.,
Kessels M.M.;
"Linkage of the actin cytoskeleton to the postsynaptic density via
direct interactions of Abp1 with the ProSAP/Shank family.";
J. Neurosci. 24:2481-2495(2004).
[7]
INTERACTION WITH LZTS3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16522626; DOI=10.1074/jbc.M601101200;
Wendholt D., Spilker C., Schmitt A., Dolnik A., Smalla K.H.,
Proepper C., Bockmann J., Sobue K., Gundelfinger E.D., Kreutz M.R.,
Boeckers T.M.;
"ProSAP-interacting protein 1 (ProSAPiP1), a novel protein of the
postsynaptic density that links the spine-associated Rap-Gap (SPAR) to
the scaffolding protein ProSAP2/Shank3.";
J. Biol. Chem. 281:13805-13816(2006).
[8]
INTERACTION WITH ABI1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF PRO-677; PRO-678; PRO-679; PRO-680 AND PRO-684.
PubMed=17304222; DOI=10.1038/sj.emboj.7601569;
Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J.,
Kreutz M.R., Gundelfinger E.D., Boeckers T.M.;
"Abelson interacting protein 1 (Abi-1) is essential for dendrite
morphogenesis and synapse formation.";
EMBO J. 26:1397-1409(2007).
[9]
FUNCTION IN MGLUR5 SIGNALING REGULATION, AND TISSUE SPECIFICITY.
PubMed=21795692; DOI=10.1074/jbc.M111.258384;
Verpelli C., Dvoretskova E., Vicidomini C., Rossi F., Chiappalone M.,
Schoen M., Di Stefano B., Mantegazza R., Broccoli V., Boeckers T.M.,
Dityatev A., Sala C.;
"Importance of Shank3 protein in regulating metabotropic glutamate
receptor 5 (mGluR5) expression and signaling at synapses.";
J. Biol. Chem. 286:34839-34850(2011).
[10]
FUNCTION, AND MUTAGENESIS OF ARG-12; ARG-300 AND GLN-321.
PubMed=23100419; DOI=10.1523/JNEUROSCI.2215-12.2012;
Arons M.H., Thynne C.J., Grabrucker A.M., Li D., Schoen M.,
Cheyne J.E., Boeckers T.M., Montgomery J.M., Garner C.C.;
"Autism-associated mutations in ProSAP2/Shank3 impair synaptic
transmission and neurexin-neuroligin-mediated transsynaptic
signaling.";
J. Neurosci. 32:14966-14978(2012).
[11]
FUNCTION, ACTIN-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ARG-12; ARG-300 AND GLN-321.
PubMed=21606927; DOI=10.1038/mp.2011.57;
Durand C.M., Perroy J., Loll F., Perrais D., Fagni L., Bourgeron T.,
Montcouquiol M., Sans N.;
"SHANK3 mutations identified in autism lead to modification of
dendritic spine morphology via an actin-dependent mechanism.";
Mol. Psychiatry 17:71-84(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-387; SER-394;
TYR-931; THR-1131; SER-1135; SER-1160; SER-1167; THR-1235; SER-1254;
SER-1421; SER-1511 AND SER-1644, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[13]
FUNCTION, DOMAIN, INTERACTION WITH SHARPIN AND SPTAN1, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LEU-68; ARG-300 AND GLN-321.
PubMed=23897824; DOI=10.1074/jbc.M112.424747;
Mameza M.G., Dvoretskova E., Bamann M., Hoenck H.H., Gueler T.,
Boeckers T.M., Schoen M., Verpelli C., Sala C., Barsukov I.,
Dityatev A., Kreienkamp H.J.;
"SHANK3 gene mutations associated with autism facilitate ligand
binding to the Shank3 ankyrin repeat region.";
J. Biol. Chem. 288:26697-26708(2013).
[14]
FUNCTION IN NMDA RECEPTOR SIGNALING REGULATION.
PubMed=24089484; DOI=10.1523/JNEUROSCI.1175-13.2013;
Duffney L.J., Wei J., Cheng J., Liu W., Smith K.R., Kittler J.T.,
Yan Z.;
"Shank3 deficiency induces NMDA receptor hypofunction via an actin-
dependent mechanism.";
J. Neurosci. 33:15767-15778(2013).
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1674-1740.
PubMed=16439662; DOI=10.1126/science.1118995;
Baron M.K., Boeckers T.M., Vaida B., Faham S., Gingery M.,
Sawaya M.R., Salyer D., Gundelfinger E.D., Bowie J.U.;
"An architectural framework that may lie at the core of the
postsynaptic density.";
Science 311:531-535(2006).
-!- FUNCTION: Major scaffold postsynaptic density protein which
interacts with multiple proteins and complexes to orchestrate the
dendritic spine and synapse formation, maturation and maintenance.
Interconnects receptors of the postsynaptic membrane including
NMDA-type and metabotropic glutamate receptors via complexes with
GKAP/PSD-95 and HOMER, respectively, and the actin-based
cytoskeleton. Plays a role in the structural and functional
organization of the dendritic spine and synaptic junction through
the interaction with Arp2/3 and WAVE1 complex as well as the
promotion of the F-actin clusters. By way of this control of actin
dynamics, participates in the regulation of developing neurons
growth cone motility and the NMDA receptor-signaling. Also
modulates GRIA1 exocytosis and GRM5/MGLUR5 expression and
signaling to control the AMPA and metabotropic glutamate receptor-
mediated synaptic transmission and plasticity. May be required at
an early stage of synapse formation and be inhibited by IGF1 to
promote synapse maturation. {ECO:0000269|PubMed:21606927,
ECO:0000269|PubMed:21795692, ECO:0000269|PubMed:23100419,
ECO:0000269|PubMed:23897824, ECO:0000269|PubMed:24089484}.
-!- SUBUNIT: May homomultimerize via its SAM domain. Interacts with
BAIAP2, DBNL and SLC17A7/VGLUT1. Interacts with DLGAP1/GKAP,
GRM1/MGLUR1, GRM5/MGLUR5 and LZTS3 C-termini via its PDZ domain.
Interacts with ABI1, HOMER1, HOMER2, HOMER3 and CTTN/cortactin SH3
domain. Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP.
Interacts (via PDZ domain) with the GRIA1 subunit of the AMPA
receptor (via PDZ-binding motif). Interacts with WASF1 and CYFIP2;
the interactions mediate the association of SHANK3 with the WAVE1
complex. Interacts with ARPC2; the interaction probably mediates
the association of SHANK3 with the Arp2/3 complex. Interacts (via
ANK repeats) with SHARPIN and SPTAN1. Interacts (via PDZ domain)
with ARHGAP44 (probably via PDZ-binding motif); the interaction
takes place in dendritic spines and promotes GRIA1 exocytosis.
{ECO:0000269|PubMed:10433268, ECO:0000269|PubMed:10433269,
ECO:0000269|PubMed:10527873, ECO:0000269|PubMed:15014124,
ECO:0000269|PubMed:16522626, ECO:0000269|PubMed:17304222,
ECO:0000269|PubMed:23897824}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-6271152, EBI-6271152;
Q9QZM5:Abi1; NbExp=7; IntAct=EBI-6271152, EBI-920097;
Q9ES28-2:Arhgef7 (xeno); NbExp=2; IntAct=EBI-6271152, EBI-8620514;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density. Cell projection,
dendritic spine. Note=In neuronal cells, extends into the region
subjacent to the PSD.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist. These isoforms may be
the product of multiple intragenic promoter and/or alternative
splicing.;
Name=2;
IsoId=Q9JLU4-1; Sequence=Displayed;
Name=1; Synonyms=A;
IsoId=Q9JLU4-2; Sequence=VSP_006089;
Name=3;
IsoId=Q9JLU4-3; Sequence=VSP_006087, VSP_006088;
-!- TISSUE SPECIFICITY: Widely expressed in brain (at protein level).
{ECO:0000269|PubMed:10527873, ECO:0000269|PubMed:15014124,
ECO:0000269|PubMed:16522626, ECO:0000269|PubMed:17304222,
ECO:0000269|PubMed:21795692}.
-!- DOMAIN: In isoform 1, the N-terminal region preceding the ANK
repeats interacts with the 6 ANK repeats in an intramolecular
manner, thereby restricting access to ligands, such as SHARPIN and
SPTAN1. {ECO:0000269|PubMed:23897824}.
-!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD42976.1; Type=Frameshift; Positions=898, 925; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF133301; AAF61375.1; -; mRNA.
EMBL; AJ133120; CAB45688.1; -; mRNA.
EMBL; AF159047; AAD42976.1; ALT_FRAME; mRNA.
RefSeq; NP_067708.1; NM_021676.1.
UniGene; Rn.42876; -.
PDB; 2F3N; X-ray; 2.10 A; A/B/C=1674-1740.
PDB; 2F44; X-ray; 2.40 A; A/B/C=1674-1740.
PDB; 5G4X; X-ray; 2.17 A; A=1-348.
PDB; 5O99; X-ray; 0.87 A; A/B=470-528.
PDBsum; 2F3N; -.
PDBsum; 2F44; -.
PDBsum; 5G4X; -.
PDBsum; 5O99; -.
SMR; Q9JLU4; -.
BioGrid; 248756; 9.
IntAct; Q9JLU4; 8.
MINT; MINT-1486849; -.
STRING; 10116.ENSRNOP00000041083; -.
iPTMnet; Q9JLU4; -.
PhosphoSitePlus; Q9JLU4; -.
PaxDb; Q9JLU4; -.
PRIDE; Q9JLU4; -.
GeneID; 59312; -.
KEGG; rno:59312; -.
CTD; 85358; -.
RGD; 69264; Shank3.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4375; Eukaryota.
eggNOG; COG0666; LUCA.
HOGENOM; HOG000293276; -.
HOVERGEN; HBG054027; -.
InParanoid; Q9JLU4; -.
KO; K15009; -.
Reactome; R-RNO-6794361; Neurexins and neuroligins.
EvolutionaryTrace; Q9JLU4; -.
PRO; PR:Q9JLU4; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0060170; C:ciliary membrane; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; ISS:BHF-UCL.
GO; GO:0044309; C:neuron spine; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0030160; F:GKAP/Homer scaffold activity; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0035255; F:ionotropic glutamate receptor binding; ISS:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:BHF-UCL.
GO; GO:0043621; F:protein self-association; IDA:RGD.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
GO; GO:0098919; F:structural constituent of postsynaptic density; IC:SynGO.
GO; GO:0008270; F:zinc ion binding; IDA:RGD.
GO; GO:0097113; P:AMPA glutamate receptor clustering; ISS:BHF-UCL.
GO; GO:0048854; P:brain morphogenesis; ISS:BHF-UCL.
GO; GO:0060997; P:dendritic spine morphogenesis; ISS:BHF-UCL.
GO; GO:0097117; P:guanylate kinase-associated protein clustering; ISS:BHF-UCL.
GO; GO:0007612; P:learning; ISS:BHF-UCL.
GO; GO:0035641; P:locomotory exploration behavior; ISS:BHF-UCL.
GO; GO:0099562; P:maintenance of postsynaptic density structure; IC:SynGO.
GO; GO:0000165; P:MAPK cascade; ISS:BHF-UCL.
GO; GO:0007613; P:memory; ISS:BHF-UCL.
GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISS:BHF-UCL.
GO; GO:0045794; P:negative regulation of cell volume; ISS:BHF-UCL.
GO; GO:0050885; P:neuromuscular process controlling balance; ISS:BHF-UCL.
GO; GO:0097114; P:NMDA glutamate receptor clustering; ISS:BHF-UCL.
GO; GO:2000969; P:positive regulation of AMPA receptor activity; ISS:BHF-UCL.
GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:BHF-UCL.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
GO; GO:1900451; P:positive regulation of glutamate receptor signaling pathway; IMP:RGD.
GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISS:BHF-UCL.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:BHF-UCL.
GO; GO:0051835; P:positive regulation of synapse structural plasticity; ISS:BHF-UCL.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
GO; GO:0097107; P:postsynaptic density assembly; ISS:BHF-UCL.
GO; GO:0051259; P:protein oligomerization; IDA:RGD.
GO; GO:2000822; P:regulation of behavioral fear response; ISS:BHF-UCL.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:BHF-UCL.
GO; GO:2000821; P:regulation of grooming behavior; ISS:BHF-UCL.
GO; GO:1900452; P:regulation of long term synaptic depression; ISS:BHF-UCL.
GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISS:BHF-UCL.
GO; GO:0035176; P:social behavior; ISS:BHF-UCL.
GO; GO:0021773; P:striatal medium spiny neuron differentiation; ISS:BHF-UCL.
GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
GO; GO:0071625; P:vocalization behavior; ISS:BHF-UCL.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR032425; FERM_f0.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
Pfam; PF12796; Ank_2; 1.
Pfam; PF16511; FERM_f0; 1.
Pfam; PF00536; SAM_1; 1.
Pfam; PF07653; SH3_2; 1.
SMART; SM00248; ANK; 5.
SMART; SM00228; PDZ; 1.
SMART; SM00454; SAM; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 4.
PROSITE; PS50106; PDZ; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative promoter usage;
Alternative splicing; ANK repeat; Cell junction; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm; Membrane;
Methylation; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; SH3 domain; SH3-binding; Synapse.
CHAIN 1 1740 SH3 and multiple ankyrin repeat domains
protein 3.
/FTId=PRO_0000174676.
REPEAT 148 181 ANK 1.
REPEAT 182 214 ANK 2.
REPEAT 215 245 ANK 3.
REPEAT 249 278 ANK 4.
REPEAT 282 311 ANK 5.
REPEAT 315 345 ANK 6.
DOMAIN 470 529 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 570 664 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1677 1740 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
REGION 1 75 Intramolecular interaction with the ANK
repeats.
REGION 677 684 Required for interaction with ABI1.
{ECO:0000269|PubMed:17304222}.
COILED 1495 1515 {ECO:0000255}.
MOTIF 1411 1417 SH3-binding. {ECO:0000255}.
COMPBIAS 820 826 Poly-Pro.
COMPBIAS 839 844 Poly-Pro.
MOD_RES 122 122 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 387 387 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 555 555 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 694 694 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 801 801 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 891 891 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 898 898 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 913 913 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9BYB0}.
MOD_RES 931 931 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 966 966 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1131 1131 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1135 1135 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1160 1160 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1164 1164 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYB0}.
MOD_RES 1167 1167 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1235 1235 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1254 1254 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1421 1421 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1511 1511 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1522 1522 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1530 1530 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1549 1549 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1644 1644 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1646 1646 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYB0}.
MOD_RES 1648 1648 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYB0}.
VAR_SEQ 1129 1136 SPTPVHSP -> PRRRAGMV (in isoform 3).
{ECO:0000305}.
/FTId=VSP_006087.
VAR_SEQ 1137 1740 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_006088.
VAR_SEQ 1537 1545 Missing (in isoform 1).
{ECO:0000303|PubMed:10433268,
ECO:0000303|PubMed:10527873}.
/FTId=VSP_006089.
MUTAGEN 12 12 R->C: Disrupts postsynaptic AMPA and NMDA
receptor-mediated synaptic transmission
as well as transsynaptic signaling and
spine maturation.
{ECO:0000269|PubMed:21606927,
ECO:0000269|PubMed:23100419}.
MUTAGEN 68 68 L->P: Slightly increases interaction with
SHARPIN and SPTAN1. No effect on
localization.
{ECO:0000269|PubMed:23897824}.
MUTAGEN 300 300 R->C: Disrupts postsynaptic AMPA and NMDA
receptor-mediated synaptic transmission
as well as transsynaptic signaling and
spine maturation. Slightly decreases
interaction with SHARPIN and SPTAN1. No
effect on localization.
{ECO:0000269|PubMed:21606927,
ECO:0000269|PubMed:23100419,
ECO:0000269|PubMed:23897824}.
MUTAGEN 321 321 Q->R: Disrupts postsynaptic AMPA and NMDA
receptor-mediated synaptic transmission
as well as transsynaptic signaling and
spine maturation. Disrupts axonal growth
cone motility. Slightly increases
interaction with SHARPIN and SPTAN1. No
effect on localization.
{ECO:0000269|PubMed:21606927,
ECO:0000269|PubMed:23100419,
ECO:0000269|PubMed:23897824}.
MUTAGEN 677 677 P->A: Strongly decreases interaction with
ABI1. {ECO:0000269|PubMed:17304222}.
MUTAGEN 678 678 P->A: Almost abolishes interaction with
ABI1. {ECO:0000269|PubMed:17304222}.
MUTAGEN 679 679 P->A: Abolishes interaction with ABI1.
{ECO:0000269|PubMed:17304222}.
MUTAGEN 680 680 P->A: Abolishes interaction with ABI1.
{ECO:0000269|PubMed:17304222}.
MUTAGEN 684 684 P->A: Abolishes interaction with ABI1.
{ECO:0000269|PubMed:17304222}.
MUTAGEN 1311 1311 P->L: Abolishes interaction with HOMER1
isoform 3. {ECO:0000269|PubMed:10433269}.
MUTAGEN 1314 1314 F->C: Abolishes interaction with HOMER1
isoform 3. {ECO:0000269|PubMed:10433269}.
CONFLICT 397 397 H -> L (in Ref. 3; AAD42976).
{ECO:0000305}.
CONFLICT 706 706 R -> G (in Ref. 3; AAD42976).
{ECO:0000305}.
CONFLICT 827 832 YYFDSG -> ILRLR (in Ref. 3; AAD42976).
{ECO:0000305}.
CONFLICT 837 842 FSPPPP -> SHHGHQ (in Ref. 3; AAD42976).
{ECO:0000305}.
CONFLICT 846 846 R -> G (in Ref. 3; AAD42976).
{ECO:0000305}.
CONFLICT 888 888 R -> G (in Ref. 3; AAD42976).
{ECO:0000305}.
CONFLICT 1040 1040 S -> N (in Ref. 2; AAF61375).
{ECO:0000305}.
CONFLICT 1087 1087 S -> N (in Ref. 2; AAF61375).
{ECO:0000305}.
CONFLICT 1092 1092 G -> S (in Ref. 2; AAF61375).
{ECO:0000305}.
CONFLICT 1262 1262 S -> N (in Ref. 2; AAF61375).
{ECO:0000305}.
CONFLICT 1270 1270 G -> S (in Ref. 2; AAF61375).
{ECO:0000305}.
CONFLICT 1273 1273 S -> N (in Ref. 2; AAF61375).
{ECO:0000305}.
CONFLICT 1279 1279 E -> K (in Ref. 2; AAF61375).
{ECO:0000305}.
CONFLICT 1294 1294 S -> N (in Ref. 2; AAF61375).
{ECO:0000305}.
CONFLICT 1432 1432 D -> G (in Ref. 2; AAF61375).
{ECO:0000305}.
CONFLICT 1640 1640 V -> A (in Ref. 2; AAF61375).
{ECO:0000305}.
STRAND 9 15 {ECO:0000244|PDB:5G4X}.
HELIX 16 18 {ECO:0000244|PDB:5G4X}.
STRAND 20 26 {ECO:0000244|PDB:5G4X}.
HELIX 32 43 {ECO:0000244|PDB:5G4X}.
HELIX 50 52 {ECO:0000244|PDB:5G4X}.
STRAND 53 57 {ECO:0000244|PDB:5G4X}.
HELIX 74 76 {ECO:0000244|PDB:5G4X}.
STRAND 87 92 {ECO:0000244|PDB:5G4X}.
HELIX 104 110 {ECO:0000244|PDB:5G4X}.
HELIX 113 124 {ECO:0000244|PDB:5G4X}.
HELIX 128 136 {ECO:0000244|PDB:5G4X}.
TURN 146 148 {ECO:0000244|PDB:5G4X}.
HELIX 152 156 {ECO:0000244|PDB:5G4X}.
HELIX 163 171 {ECO:0000244|PDB:5G4X}.
HELIX 186 192 {ECO:0000244|PDB:5G4X}.
HELIX 196 204 {ECO:0000244|PDB:5G4X}.
HELIX 219 226 {ECO:0000244|PDB:5G4X}.
HELIX 231 238 {ECO:0000244|PDB:5G4X}.
HELIX 253 260 {ECO:0000244|PDB:5G4X}.
HELIX 263 271 {ECO:0000244|PDB:5G4X}.
HELIX 286 293 {ECO:0000244|PDB:5G4X}.
HELIX 296 304 {ECO:0000244|PDB:5G4X}.
HELIX 319 325 {ECO:0000244|PDB:5G4X}.
HELIX 329 337 {ECO:0000244|PDB:5G4X}.
HELIX 1674 1676 {ECO:0000244|PDB:2F3N}.
HELIX 1679 1688 {ECO:0000244|PDB:2F3N}.
HELIX 1692 1694 {ECO:0000244|PDB:2F3N}.
HELIX 1695 1700 {ECO:0000244|PDB:2F3N}.
HELIX 1705 1710 {ECO:0000244|PDB:2F3N}.
HELIX 1713 1718 {ECO:0000244|PDB:2F3N}.
HELIX 1724 1735 {ECO:0000244|PDB:2F3N}.
SEQUENCE 1740 AA; 186376 MW; A9F486E893EA5AA0 CRC64;
MDGPGASAVV VRVGIPDLQQ TKCLRLDPTA PVWAAKQRVL CALNHSLQDA LNYGLFQPPS
RGRAGKFLDE ERLLQDYPPN LDTPLPYLEF RYKRRVYAQN LIDDKQFAKL HTKANLKKFM
DYVQLHSTDK VARLLDKGLD PNFHDPDSGE CPLSLAAQLD NATDLLKVLR NGGAHLDFRT
RDGLTAVHCA TRQRNAGALT TLLDLGASPD YKDSRGLTPL YHSALGGGDA LCCELLLHDH
AQLGTTDENG WQEIHQACRF GHVQHLEHLL FYGANMGAQN ASGNTALHIC ALYNQESCAR
VLLFRGANKD VRNYNSQTAF QVAIIAGNFE LAEVIKTHKD SDVVPFRETP SYAKRRRLAG
PSGLASPRPL QRSASDINLK GDQPAASPGP TLRSLPHQLL LQRLQEEKDR DRDGEQENDI
SGPSAGRGGH SKISPSGPGG SGPAPGPGPA SPAPPAPPPR GPKRKLYSAV PGRKFIAVKA
HSPQGEGEIP LHRGEAVKVL SIGEGGFWEG TVKGRTGWFP ADCVEEVQMR QYDTRHETRE
DRTKRLFRHY TVGSYDSLTS HSDYVIDDKV AILQKRDHEG FGFVLRGAKA ETPIEEFTPT
PAFPALQYLE SVDVEGVAWK AGLRTGDFLI EVNGVNVVKV GHKQVVGLIR QGGNRLVMKV
VSVTRKPEED SARRRAPPPP KRAPSTTLTL RSKSMTAELE ELASIRRRKG EKLDEILAVA
AEPTLRPDIA DADSRAATVK QRPTSRRITP AEISSLFERQ GLPGPEKLPG SLRKGIPRTK
SVGEDEKLAS LLEGRFPRST SMQDTVREGR GIPPPPQTAP PPPPAPYYFD SGPPPTFSPP
PPPPGRAYDT VRSSFKPGLE ARLGAGAAGL YDSGTPLGPL PYPERQKRAR SMIILQDSAP
EVGDVPRPAP AATPPERPKR RPRPSGPDSP YANLGAFSAS LFAPSKPQRR KSPLVKQLQV
EDAQERAALA VGSPGPVGGS FAREPSPTHR GPRPGGLDYS SGEGLGLTFG GPSPGPVKER
RLEERRRSTV FLSVGAIEGS PPSADLPSLQ PSRSIDERLL GTGATTGRDL LLPSPVSALK
PLVGGPSLGP SGSTFIHPLT GKPLDPSSPL ALALAARERA LASQTPSRSP TPVHSPDADR
PGPLFVDVQT RDSERGPLAS PAFSPRSPAW IPVPARREAE KPTREERKSP EDKKSMILSV
LDTSLQRPAG LIVVHATSNG QEPNRLGAEE ERPGTPELAP TPMQAAAVAE PMPSPRAQPP
GSIPADPGPG QGSSEEEPEL VFAVNLPPAQ LSSSDEETRE ELARIGLVPP PEEFANGILL
ATPPPGPGPL PTTVPSPASG KPSSELPPAP ESAADSGVEE ADTRSSSDPH LETTSTISTV
SSMSTLSSES GELTDTHTSF ADGHTFLLEK PPVPPKPKLK SPLGKGPVTF RDPLLKQSSD
SELMAQQHHA TSTGLTSAAG PARPRYLFQR RSKLWGDPVE SRGLPGPEDD KPTVISELSS
RLQQLNKDTR SLGEEPVGGL GSLLDPAKKS PIAAARCAVV PSAGWLFSSL GELSTISAQR
SPGGPGGGAS YSVRPSGRYP VARRAPSPVK PASLERVEGL GAGVGGAGRP FGLTPPTILK
SSSLSIPHEP KEVRFVVRSV SARSRSPSPS PLPSPSPGSG PSAGPRRPFQ QKPLQLWSKF
DVGDWLESIH LGEHRDRFED HEIEGAHLPA LTKEDFVELG VTRVGHRMNI ERALRQLDGS


Related products :

Catalog number Product name Quantity
EIAAB38260 Proline-rich synapse-associated protein 2,ProSAP2,Rat,Rattus norvegicus,SH3 and multiple ankyrin repeat domains protein 3,Shank3,Shank3,SPANK-2
EIAAB38261 Kiaa1650,Mouse,Mus musculus,Proline-rich synapse-associated protein 2,ProSAP2,SH3 and multiple ankyrin repeat domains protein 3,Shank3,Shank3,SPANK-2
EIAAB38262 Homo sapiens,Human,KIAA1650,Proline-rich synapse-associated protein 2,ProSAP2,PSAP2,SH3 and multiple ankyrin repeat domains protein 3,Shank3,SHANK3
EIAAB38258 Cortactin-binding protein 1,CortBP1,Cortbp1,GKAP_SAPAP-interacting protein,Proline-rich synapse-associated protein 1,ProSAP1,Rat,Rattus norvegicus,SH3 and multiple ankyrin repeat domains protein 2,Sha
EIAAB38257 Cortactin-binding protein 1,CortBP1,CORTBP1,Homo sapiens,Human,KIAA1022,Proline-rich synapse-associated protein 1,PROSAP1,SH3 and multiple ankyrin repeat domains protein 2,Shank2,SHANK2
H0228 SH3 and multiple ankyrin repeat domains protein 3 (SHANK3), Rat, ELISA Kit 96T
CSB-EL021249RA Rat SH3 and multiple ankyrin repeat domains protein 3(SHANK3) ELISA kit 96T
CSB-EL021249RA Rat SH3 and multiple ankyrin repeat domains protein 3(SHANK3) ELISA kit SpeciesRat 96T
CSB-EL021249MO Mouse SH3 and multiple ankyrin repeat domains protein 3(SHANK3) ELISA kit 96T
H0226 SH3 and multiple ankyrin repeat domains protein 3 (SHANK3), Human, ELISA Kit 96T
CSB-EL021249HU Human SH3 and multiple ankyrin repeat domains protein 3(SHANK3) ELISA kit 96T
H0227 SH3 and multiple ankyrin repeat domains protein 3 (SHANK3), Mouse, ELISA Kit 96T
SHAN3_RAT ELISA Kit FOR SH3 and multiple ankyrin repeat domains protein 3; organism: Rat; gene name: Shank3 96T
CSB-EL021249MO Mouse SH3 and multiple ankyrin repeat domains protein 3(SHANK3) ELISA kit SpeciesMouse 96T
CSB-EL021249HU Human SH3 and multiple ankyrin repeat domains protein 3(SHANK3) ELISA kit SpeciesHuman 96T
SHANK3 SHANK3 Gene SH3 and multiple ankyrin repeat domains 3
SHAN3_MOUSE ELISA Kit FOR SH3 and multiple ankyrin repeat domains protein 3; organism: Mouse; gene name: Shank3 96T
EIAAB38255 GKAP_SAPAP-interacting protein,Rat,Rattus norvegicus,SH3 and multiple ankyrin repeat domains protein 1,Shank1,Shank1,Somatostatin receptor-interacting protein,SPANK-1,SSTR-interacting protein,SSTRIP,S
CSB-EL021249RA Rat SH3 and multiple ankyrin repeat domains 3 (SHANK3) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL021249MO Mouse SH3 and multiple ankyrin repeat domains 3 (SHANK3) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL021249HU Human SH3 and multiple ankyrin repeat domains 3 (SHANK3) ELISA kit, Species Human, Sample Type serum, plasma 96T
30037 IgG,SH3 and multiple ankyrin repeat domains protein 1 0.1 mg
30036 IgG,SH3 and multiple ankyrin repeat domains protein 1 0.1 mg
SMC-328D SHANK2, S23b-6 Monoclonals AntibodiesS23b-6 Fusion protein amino acids 84-309 (SH3_PDZ domains) of rat Shank2 (SH3 and multiple ankyrin repeat domains protein 2 (accession number Q9QX74) 100ug
H0222 SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), Rat, ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur