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

 SHAN3_MOUSE             Reviewed;        1730 AA.
Q4ACU6; F8S0X0; F8S0X2; F8S0X3; F8S0X5; F8S0X6; Q69ZD8; Q9JJZ3;
S6BMD3; S6CCV8;
12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
19-FEB-2014, sequence version 3.
25-OCT-2017, entry version 122.
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=Kiaa1650, Prosap2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57B16/J; TISSUE=Kidney;
Dehmelt L., Nalbant P., Werner A.;
"Interaction of the Na+/Phosphate cotransporter type II with rSHANK.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH GRIA1, AND
SUBCELLULAR LOCATION.
PubMed=16606358; DOI=10.1111/j.1471-4159.2006.03831.x;
Uchino S., Wada H., Honda S., Nakamura Y., Ondo Y., Uchiyama T.,
Tsutsumi M., Suzuki E., Hirasawa T., Kohsaka S.;
"Direct interaction of post-synaptic density-95/Dlg/ZO-1 domain-
containing synaptic molecule Shank3 with GluR1 alpha-amino-3-hydroxy-
5-methyl-4-isoxazole propionic acid receptor.";
J. Neurochem. 97:1203-1214(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING,
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=24164323; DOI=10.1111/jnc.12505;
Waga C., Asano H., Sanagi T., Suzuki E., Nakamura Y., Tsuchiya A.,
Itoh M., Goto Y.I., Kohsaka S., Uchino S.;
"Identification of two novel Shank3 transcripts in the developing
mouse neocortex.";
J. Neurochem. 128:280-293(2014).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 875-1730.
TISSUE=Brain;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 6; 7; 8 AND 9),
ALTERNATIVE SPLICING, FUNCTION, DISRUPTION PHENOTYPE, TISSUE
SPECIFICITY, AND INTERACTION WITH HOMER1.
PubMed=21558424; DOI=10.1093/hmg/ddr212;
Wang X., McCoy P.A., Rodriguiz R.M., Pan Y., Je H.S., Roberts A.C.,
Kim C.J., Berrios J., Colvin J.S., Bousquet-Moore D., Lorenzo I.,
Wu G., Weinberg R.J., Ehlers M.D., Philpot B.D., Beaudet A.L.,
Wetsel W.C., Jiang Y.H.;
"Synaptic dysfunction and abnormal behaviors in mice lacking major
isoforms of Shank3.";
Hum. Mol. Genet. 20:3093-3108(2011).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1634, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122 AND TYR-555, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-375; SER-387;
SER-694; SER-781; SER-790; SER-801; SER-890; SER-897; SER-995;
THR-1130; SER-1134; SER-1159; SER-1166; THR-1234; SER-1510; SER-1521;
SER-1529; SER-1539; SER-1634 AND SER-1636, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
ALTERNATIVE PROMOTER USAGE.
PubMed=20613842; DOI=10.1038/nature09165;
Maunakea A.K., Nagarajan R.P., Bilenky M., Ballinger T.J., D'Souza C.,
Fouse S.D., Johnson B.E., Hong C., Nielsen C., Zhao Y., Turecki G.,
Delaney A., Varhol R., Thiessen N., Shchors K., Heine V.M.,
Rowitch D.H., Xing X., Fiore C., Schillebeeckx M., Jones S.J.,
Haussler D., Marra M.A., Hirst M., Wang T., Costello J.F.;
"Conserved role of intragenic DNA methylation in regulating
alternative promoters.";
Nature 466:253-257(2010).
[12]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=21423165; DOI=10.1038/nature09965;
Peca J., Feliciano C., Ting J.T., Wang W., Wells M.F.,
Venkatraman T.N., Lascola C.D., Fu Z., Feng G.;
"Shank3 mutant mice display autistic-like behaviours and striatal
dysfunction.";
Nature 472:437-442(2011).
[13]
DISRUPTION PHENOTYPE.
PubMed=22699619; DOI=10.1038/nature11015;
Schmeisser M.J., Ey E., Wegener S., Bockmann J., Stempel A.V.,
Kuebler A., Janssen A.L., Udvardi P.T., Shiban E., Spilker C.,
Balschun D., Skryabin B.V., Dieck S.T., Smalla K.H., Montag D.,
Leblond C.S., Faure P., Torquet N., Le Sourd A.M., Toro R.,
Grabrucker A.M., Shoichet S.A., Schmitz D., Kreutz M.R., Bourgeron T.,
Gundelfinger E.D., Boeckers T.M.;
"Autistic-like behaviours and hyperactivity in mice lacking
ProSAP1/Shank2.";
Nature 486:256-260(2012).
[14]
FUNCTION IN AMPA RECEPTOR SIGNALING, AND INTERACTION WITH ARHGAP44.
PubMed=23739967; DOI=10.1523/JNEUROSCI.2725-12.2013;
Raynaud F., Janossy A., Dahl J., Bertaso F., Perroy J., Varrault A.,
Vidal M., Worley P.F., Boeckers T.M., Bockaert J., Marin P., Fagni L.,
Homburger V.;
"Shank3-Rich2 interaction regulates AMPA receptor recycling and
synaptic long-term potentiation.";
J. Neurosci. 33:9699-9715(2013).
[15]
DISRUPTION PHENOTYPE.
PubMed=24259569; DOI=10.1523/JNEUROSCI.3017-13.2013;
Kouser M., Speed H.E., Dewey C.M., Reimers J.M., Widman A.J.,
Gupta N., Liu S., Jaramillo T.C., Bangash M., Xiao B., Worley P.F.,
Powell C.M.;
"Loss of predominant shank3 isoforms results in hippocampus-dependent
impairments in behavior and synaptic transmission.";
J. Neurosci. 33:18448-18468(2013).
[16]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ACTIN-BINDING, AND
INTERACTION WITH ARPC2; CYFIP2; DLG4; GKAP1; HOMER1 AND SLC17A7.
PubMed=24153177; DOI=10.1038/nature12630;
Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H.,
Tang J., Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M.,
Patel A., Lu H.C., Zoghbi H.Y.;
"SHANK3 overexpression causes manic-like behaviour with unique
pharmacogenetic properties.";
Nature 503:72-77(2013).
[17]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-965, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- 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:21423165,
ECO:0000269|PubMed:21558424, ECO:0000269|PubMed:23739967,
ECO:0000269|PubMed:24153177}.
-!- 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:16606358, ECO:0000269|PubMed:21558424,
ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:24153177}.
-!- INTERACTION:
O60741:HCN1 (xeno); NbExp=4; IntAct=EBI-16201983, EBI-11173743;
Q9UL51:HCN2 (xeno); NbExp=3; IntAct=EBI-16201983, EBI-1751885;
Q9P1Z3:HCN3 (xeno); NbExp=3; IntAct=EBI-16201983, EBI-11178054;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density. Cell projection, dendritic spine {ECO:0000250}. Note=In
neuronal cells, extends into the region subjacent to the
postsynaptic density (PSD).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=10;
Comment=Additional isoform seem to exist. These isoforms may be
the product of multiple intragenic promoter and/or alternative
splicing. {ECO:0000269|PubMed:21558424,
ECO:0000269|PubMed:24164323};
Name=1; Synonyms=A, Alpha;
IsoId=Q4ACU6-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=Q4ACU6-2; Sequence=VSP_053612, VSP_053613, VSP_053614,
VSP_053615;
Note=Produced by alternative promoter usage and alternative
splicing.;
Name=4; Synonyms=C3, Beta;
IsoId=Q4ACU6-3; Sequence=VSP_053611;
Note=Produced by alternative splicing of isoform 3.;
Name=5; Synonyms=C4;
IsoId=Q4ACU6-6; Sequence=VSP_053611, VSP_053614, VSP_053615;
Note=Produced by alternative splicing of isoform 3.;
Name=6; Synonyms=D1;
IsoId=Q4ACU6-7; Sequence=VSP_053609;
Note=Produced by alternative promoter usage.;
Name=7; Synonyms=D2;
IsoId=Q4ACU6-8; Sequence=VSP_053608;
Note=Produced by alternative splicing of isoform 6.;
Name=8; Synonyms=E1;
IsoId=Q4ACU6-9; Sequence=VSP_053607;
Note=Produced by alternative promoter usage.;
Name=9; Synonyms=E2;
IsoId=Q4ACU6-10; Sequence=VSP_053607, VSP_053613;
Note=Produced by alternative splicing of isoform 8.;
Name=3; Synonyms=C1;
IsoId=Q4ACU6-11; Sequence=VSP_053610;
Note=Produced by alternative promoter usage.;
Name=10; Synonyms=F;
IsoId=Q4ACU6-12; Sequence=VSP_053606;
Note=Produced by alternative promoter usage.;
-!- TISSUE SPECIFICITY: In brain, highly expressed in striatum,
thalamus, hippocampus and granule cells of the cerebellum.
{ECO:0000269|PubMed:21423165, ECO:0000269|PubMed:21558424,
ECO:0000269|PubMed:24153177}.
-!- DEVELOPMENTAL STAGE: Isoform 3 is weakly expressed at 17 dpc but
its expression increases after birth.
{ECO:0000269|PubMed:24164323}.
-!- 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:0000250}.
-!- DISRUPTION PHENOTYPE: Animals deficient for isoforms 1-7 exhibit
self-injourious repetitive grooming and deficits in social
interaction. They show defects at striatal synapses and cortico-
striatal circuits with an increase in striatal volume, dendritic
length, and surface area and a decrease of spine density, length
and thickness of PSD. They seem to have an altered molecular
composition of postsynaptic machinery in the striatum
(PubMed:21423165). In contrast, animals deficient for isoforms 1
and 2 exhibit a normal initiation of social interaction with a
perturbed recognition of social novelty (PubMed:21423165). In
PubMed:21558424, animals deficient for isoforms 1 and 2 show
abnormal social behaviors, communication patterns, repetitive
behaviors, learning and memory. In CA1 hippocampus, the synaptic
plasticity is impaired with longer dendritic spines, decreased
spine density and deficient long-term potentiation. The expression
of specific synaptic scaffolding proteins and receptor subunits
are altered. Animals deficient for isoforms 1-5 exhibit self-
injourious repetitive grooming, brain-region-specific up-
regulation of ionotropic glutamate receptors and increased levels
of SHANK2 (PubMed:22699619). Animals deficient for predominant
isoforms containing exon 21 exhibit motor-coordination deficits,
hypersensitivity to heat, novelty avoidance, altered locomotor
response to novelty and minimal social abnormalities. They show a
decrease in NMDA-AMPA excitatory postsynaptic current ratio in
hippocampal CA1, reduced long-term potentiation and deficits in
hippocampus-dependent spatial learning and memory
(PubMed:24259569). {ECO:0000269|PubMed:21423165,
ECO:0000269|PubMed:21558424, ECO:0000269|PubMed:22699619,
ECO:0000269|PubMed:24259569}.
-!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
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EMBL; AJ245904; CAB89816.1; -; mRNA.
EMBL; AB841411; BAN67189.1; -; mRNA.
EMBL; AB841412; BAN67190.1; -; mRNA.
EMBL; AC122401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC137513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB231013; BAE16756.1; -; mRNA.
EMBL; AK173228; BAD32506.1; -; mRNA.
EMBL; HQ405757; AEB77764.1; -; mRNA.
EMBL; HQ405758; AEB77765.1; -; mRNA.
EMBL; HQ405759; AEB77766.1; -; mRNA.
EMBL; HQ405760; AEB77767.1; -; mRNA.
EMBL; HQ405761; AEB77768.1; -; mRNA.
EMBL; HQ405762; AEB77769.1; -; mRNA.
EMBL; HQ405763; AEB77770.1; -; mRNA.
CCDS; CCDS27754.1; -. [Q4ACU6-1]
RefSeq; NP_067398.2; NM_021423.3. [Q4ACU6-1]
UniGene; Mm.146855; -.
PDB; 3O5N; X-ray; 1.83 A; A/B/C/D/E/F/G/H=562-669.
PDB; 5IZU; X-ray; 2.49 A; A/C=533-665.
PDBsum; 3O5N; -.
PDBsum; 5IZU; -.
ProteinModelPortal; Q4ACU6; -.
SMR; Q4ACU6; -.
BioGrid; 208407; 161.
DIP; DIP-32262N; -.
IntAct; Q4ACU6; 8.
STRING; 10090.ENSMUSP00000048062; -.
iPTMnet; Q4ACU6; -.
PhosphoSitePlus; Q4ACU6; -.
PaxDb; Q4ACU6; -.
PeptideAtlas; Q4ACU6; -.
PRIDE; Q4ACU6; -.
Ensembl; ENSMUST00000039074; ENSMUSP00000048062; ENSMUSG00000022623. [Q4ACU6-1]
Ensembl; ENSMUST00000066545; ENSMUSP00000064477; ENSMUSG00000022623. [Q4ACU6-2]
GeneID; 58234; -.
KEGG; mmu:58234; -.
UCSC; uc007xha.2; mouse. [Q4ACU6-1]
UCSC; uc007xhb.2; mouse. [Q4ACU6-2]
UCSC; uc033gwe.1; mouse. [Q4ACU6-3]
UCSC; uc033gwf.1; mouse. [Q4ACU6-6]
UCSC; uc056zac.1; mouse. [Q4ACU6-10]
CTD; 85358; -.
MGI; MGI:1930016; Shank3.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4375; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00510000046474; -.
HOGENOM; HOG000293276; -.
HOVERGEN; HBG054027; -.
InParanoid; Q4ACU6; -.
KO; K15009; -.
PhylomeDB; Q4ACU6; -.
TreeFam; TF324593; -.
ChiTaRS; Shank3; mouse.
EvolutionaryTrace; Q4ACU6; -.
PRO; PR:Q4ACU6; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022623; -.
CleanEx; MM_SHANK3; -.
ExpressionAtlas; Q4ACU6; baseline and differential.
Genevisible; Q4ACU6; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0060170; C:ciliary membrane; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0060076; C:excitatory synapse; IC:BHF-UCL.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0044309; C:neuron spine; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0014069; C:postsynaptic density; ISS:BHF-UCL.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0030160; F:GKAP/Homer scaffold activity; ISS:BHF-UCL.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:BHF-UCL.
GO; GO:0043621; F:protein self-association; ISS:BHF-UCL.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; ISS:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; ISS:BHF-UCL.
GO; GO:0030534; P:adult behavior; ISO:MGI.
GO; GO:0097113; P:AMPA glutamate receptor clustering; IMP:BHF-UCL.
GO; GO:0048854; P:brain morphogenesis; IMP:BHF-UCL.
GO; GO:0060997; P:dendritic spine morphogenesis; IMP:BHF-UCL.
GO; GO:0001838; P:embryonic epithelial tube formation; IGI:MGI.
GO; GO:0035640; P:exploration behavior; IMP:CACAO.
GO; GO:0097117; P:guanylate kinase-associated protein clustering; IMP:BHF-UCL.
GO; GO:0007612; P:learning; IMP:BHF-UCL.
GO; GO:0007611; P:learning or memory; IMP:MGI.
GO; GO:0040011; P:locomotion; IMP:CACAO.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0035641; P:locomotory exploration behavior; IMP:BHF-UCL.
GO; GO:0060292; P:long term synaptic depression; IMP:CACAO.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:CACAO.
GO; GO:0000165; P:MAPK cascade; IGI:MGI.
GO; GO:0007613; P:memory; IMP:BHF-UCL.
GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IDA:MGI.
GO; GO:0045794; P:negative regulation of cell volume; IMP:BHF-UCL.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
GO; GO:0097114; P:NMDA glutamate receptor clustering; IMP:BHF-UCL.
GO; GO:2000969; P:positive regulation of AMPA receptor activity; IMP:BHF-UCL.
GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:BHF-UCL.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:BHF-UCL.
GO; GO:1900451; P:positive regulation of glutamate receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IMP:BHF-UCL.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:BHF-UCL.
GO; GO:0051835; P:positive regulation of synapse structural plasticity; IMP:BHF-UCL.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:BHF-UCL.
GO; GO:0097107; P:postsynaptic density assembly; IMP:BHF-UCL.
GO; GO:1904717; P:regulation of AMPA glutamate receptor clustering; IMP:MGI.
GO; GO:2000822; P:regulation of behavioral fear response; IMP:BHF-UCL.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:BHF-UCL.
GO; GO:2000821; P:regulation of grooming behavior; IMP:BHF-UCL.
GO; GO:1900452; P:regulation of long term synaptic depression; IMP:BHF-UCL.
GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:BHF-UCL.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
GO; GO:0021773; P:striatal medium spiny neuron differentiation; IMP:BHF-UCL.
GO; GO:0007416; P:synapse assembly; IMP:BHF-UCL.
GO; GO:0042297; P:vocal learning; ISO:MGI.
GO; GO:0071625; P:vocalization behavior; IMP: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; Synapse.
CHAIN 1 1730 SH3 and multiple ankyrin repeat domains
protein 3.
/FTId=PRO_0000291257.
REPEAT 148 178 ANK 1.
REPEAT 182 211 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 1667 1730 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
REGION 1 75 Intramolecular interaction with the ANK
repeats. {ECO:0000250}.
REGION 677 684 Required for interaction with ABI1.
{ECO:0000250}.
COILED 1494 1514 {ECO:0000255}.
MOTIF 1410 1416 SH3-binding. {ECO:0000255}.
COMPBIAS 435 462 Pro-rich.
COMPBIAS 677 680 Poly-Pro.
COMPBIAS 813 1349 Pro-rich.
MOD_RES 122 122 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 387 387 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JLU4}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000244|PubMed:16452087}.
MOD_RES 555 555 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 694 694 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 801 801 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 897 897 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 912 912 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9BYB0}.
MOD_RES 930 930 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9JLU4}.
MOD_RES 965 965 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 995 995 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1130 1130 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1134 1134 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1159 1159 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1163 1163 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYB0}.
MOD_RES 1166 1166 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1234 1234 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1253 1253 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYB0}.
MOD_RES 1420 1420 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JLU4}.
MOD_RES 1510 1510 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1521 1521 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1529 1529 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1539 1539 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1634 1634 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1636 1636 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1638 1638 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYB0}.
VAR_SEQ 1 890 Missing (in isoform 10). {ECO:0000305}.
/FTId=VSP_053606.
VAR_SEQ 1 675 MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLC
ALNHSLQDALNYGLFQPPSRGRAGKFLDEERLLQDYPPNLD
TPLPYLEFRYKRRVYAQNLIDDKQFAKLHTKANLKKFMDYV
QLHSTDKVARLLDKGLDPNFHDPDSGECPLSLAAQLDNATD
LLKVLRNGGAHLDFRTRDGLTAVHCATRQRNAGALTTLLDL
GASPDYKDSRGLTPLYHSALGGGDALCCELLLHDHAQLGTT
DENGWQEIHQACRFGHVQHLEHLLFYGANMGAQNASGNTAL
HICALYNQESCARVLLFRGANKDVRNYNSQTAFQVAIIAGN
FELAEVIKTHKDSDVVPFRETPSYAKRRRLAGPSGLASPRP
LQRSASDINLKGDQPAASPGPTLRSLPHQLLLQRLQEEKDR
DRDGELENDISGPSAGRGGHNKISPSGPGGSGPAPGPGPAS
PAPPAPPPRGPKRKLYSAVPGRKFIAVKAHSPQGEGEIPLH
RGEAVKVLSIGEGGFWEGTVKGRTGWFPADCVEEVQMRQYD
TRHETREDRTKRLFRHYTVGSYDSLTSHSDYVIDDKVAILQ
KRDHEGFGFVLRGAKAETPIEEFTPTPAFPALQYLESVDVE
GVAWRAGLRTGDFLIEVNGVNVVKVGHKQVVGLIRQGGNRL
VMKVVSVTRKPEEDGARRR -> MKKFASSRSLNKILAQCD
SSSREYEEVQAVERKWHLHLATPRRLLLDRRAKASLFFA
(in isoform 8 and isoform 9).
{ECO:0000305}.
/FTId=VSP_053607.
VAR_SEQ 1 589 MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLC
ALNHSLQDALNYGLFQPPSRGRAGKFLDEERLLQDYPPNLD
TPLPYLEFRYKRRVYAQNLIDDKQFAKLHTKANLKKFMDYV
QLHSTDKVARLLDKGLDPNFHDPDSGECPLSLAAQLDNATD
LLKVLRNGGAHLDFRTRDGLTAVHCATRQRNAGALTTLLDL
GASPDYKDSRGLTPLYHSALGGGDALCCELLLHDHAQLGTT
DENGWQEIHQACRFGHVQHLEHLLFYGANMGAQNASGNTAL
HICALYNQESCARVLLFRGANKDVRNYNSQTAFQVAIIAGN
FELAEVIKTHKDSDVVPFRETPSYAKRRRLAGPSGLASPRP
LQRSASDINLKGDQPAASPGPTLRSLPHQLLLQRLQEEKDR
DRDGELENDISGPSAGRGGHNKISPSGPGGSGPAPGPGPAS
PAPPAPPPRGPKRKLYSAVPGRKFIAVKAHSPQGEGEIPLH
RGEAVKVLSIGEGGFWEGTVKGRTGWFPADCVEEVQMRQYD
TRHETREDRTKRLFRHYTVGSYDSLTSHSDYVIDDKVAILQ
KRDHEGFGFVLRGAK -> MLVNAFYLALPA (in
isoform 7). {ECO:0000305}.
/FTId=VSP_053608.
VAR_SEQ 1 536 MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLC
ALNHSLQDALNYGLFQPPSRGRAGKFLDEERLLQDYPPNLD
TPLPYLEFRYKRRVYAQNLIDDKQFAKLHTKANLKKFMDYV
QLHSTDKVARLLDKGLDPNFHDPDSGECPLSLAAQLDNATD
LLKVLRNGGAHLDFRTRDGLTAVHCATRQRNAGALTTLLDL
GASPDYKDSRGLTPLYHSALGGGDALCCELLLHDHAQLGTT
DENGWQEIHQACRFGHVQHLEHLLFYGANMGAQNASGNTAL
HICALYNQESCARVLLFRGANKDVRNYNSQTAFQVAIIAGN
FELAEVIKTHKDSDVVPFRETPSYAKRRRLAGPSGLASPRP
LQRSASDINLKGDQPAASPGPTLRSLPHQLLLQRLQEEKDR
DRDGELENDISGPSAGRGGHNKISPSGPGGSGPAPGPGPAS
PAPPAPPPRGPKRKLYSAVPGRKFIAVKAHSPQGEGEIPLH
RGEAVKVLSIGEGGFWEGTVKGRTGWFPADCVEEVQMRQYD
TRH -> MLPA (in isoform 6).
{ECO:0000305}.
/FTId=VSP_053609.
VAR_SEQ 1 528 Missing (in isoform 3).
{ECO:0000303|PubMed:24164323}.
/FTId=VSP_053610.
VAR_SEQ 1 433 MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLC
ALNHSLQDALNYGLFQPPSRGRAGKFLDEERLLQDYPPNLD
TPLPYLEFRYKRRVYAQNLIDDKQFAKLHTKANLKKFMDYV
QLHSTDKVARLLDKGLDPNFHDPDSGECPLSLAAQLDNATD
LLKVLRNGGAHLDFRTRDGLTAVHCATRQRNAGALTTLLDL
GASPDYKDSRGLTPLYHSALGGGDALCCELLLHDHAQLGTT
DENGWQEIHQACRFGHVQHLEHLLFYGANMGAQNASGNTAL
HICALYNQESCARVLLFRGANKDVRNYNSQTAFQVAIIAGN
FELAEVIKTHKDSDVVPFRETPSYAKRRRLAGPSGLASPRP
LQRSASDINLKGDQPAASPGPTLRSLPHQLLLQRLQEEKDR
DRDGELENDISGPSAGRGGHNKI -> MEAPGAGFACPLPP
GIASVTYVFVY (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:24164323}.
/FTId=VSP_053611.
VAR_SEQ 1 89 MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLC
ALNHSLQDALNYGLFQPPSRGRAGKFLDEERLLQDYPPNLD
TPLPYLE -> MGLCGSLLPTFSLSEQ (in isoform
2). {ECO:0000303|Ref.1}.
/FTId=VSP_053612.
VAR_SEQ 703 710 Missing (in isoform 2 and isoform 9).
{ECO:0000303|Ref.1}.
/FTId=VSP_053613.
VAR_SEQ 784 790 EDEKLAS -> SSAASVS (in isoform 2 and
isoform 5). {ECO:0000303|Ref.1}.
/FTId=VSP_053614.
VAR_SEQ 791 1730 Missing (in isoform 2 and isoform 5).
{ECO:0000303|Ref.1}.
/FTId=VSP_053615.
STRAND 544 552 {ECO:0000244|PDB:5IZU}.
STRAND 555 560 {ECO:0000244|PDB:5IZU}.
STRAND 564 574 {ECO:0000244|PDB:3O5N}.
STRAND 577 579 {ECO:0000244|PDB:5IZU}.
STRAND 582 586 {ECO:0000244|PDB:3O5N}.
STRAND 601 603 {ECO:0000244|PDB:3O5N}.
STRAND 608 612 {ECO:0000244|PDB:3O5N}.
STRAND 614 617 {ECO:0000244|PDB:3O5N}.
HELIX 618 621 {ECO:0000244|PDB:3O5N}.
STRAND 628 632 {ECO:0000244|PDB:3O5N}.
HELIX 643 651 {ECO:0000244|PDB:3O5N}.
TURN 652 654 {ECO:0000244|PDB:3O5N}.
STRAND 655 665 {ECO:0000244|PDB:3O5N}.
SEQUENCE 1730 AA; 185397 MW; 1343F857BE3EECD8 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 DRDGELENDI
SGPSAGRGGH NKISPSGPGG SGPAPGPGPA SPAPPAPPPR GPKRKLYSAV PGRKFIAVKA
HSPQGEGEIP LHRGEAVKVL SIGEGGFWEG TVKGRTGWFP ADCVEEVQMR QYDTRHETRE
DRTKRLFRHY TVGSYDSLTS HSDYVIDDKV AILQKRDHEG FGFVLRGAKA ETPIEEFTPT
PAFPALQYLE SVDVEGVAWR AGLRTGDFLI EVNGVNVVKV GHKQVVGLIR QGGNRLVMKV
VSVTRKPEED GARRRAPPPP KRAPSTTLTL RSKSMTAELE ELASIRRRKG EKLDEILAVA
AEPTLRPDIA DADSRAATVK QRPTSRRITP AEISSLFERQ GLPGPEKLPG SLRKGIPRTK
SVGEDEKLAS LLEGRFPRST SMQDTVREGR GIPPPPQTAP PPPPAPYYFD SGPPPTFSPP
PPPGRAYDTV RSSFKPGLEA RLGAGAAGLY DPSTPLGPLP YPERQKRARS MIILQDSAPE
VGDVPRPAPA ATPPERPKRR PRPSGPDSPY ANLGAFSASL FAPSKPQRRK SPLVKQLQVE
DAQERAALAV GSPGPVGGSF AREPSPTHRG PRPGSLDYSS GEGLGLTFGG PSPGPVKERR
LEERRRSTVF LSVGAIEGSP PSADLPSLQP SRSIDERLLG TGATTGRDLL LPSPVSALKP
LVGGPSLGPS GSTFIHPLTG KPLDPSSPLA LALAARERAL ASQTPSRSPT PVHSPDADRP
GPLFVDVQTR DSERGPLASP AFSPRSPAWI PVPARREAEK PPREERKSPE DKKSMILSVL
DTSLQRPAGL IVVHATSNGQ EPSRLGAEEE RPGTPELAPA PMQAAAVAEP MPSPRAQPPG
SIPADPGPGQ GSSEEEPELV FAVNLPPAQL SSSDEETREE LARIGLVPPP EEFANGILLT
TPPPGPGPLP TTVPSPASGK PSSELPPAPE SAADSGVEEA DTRSSSDPHL ETTSTISTVS
SMSTLSSESG ELTDTHTSFA DGHTFLLEKP PVPPKPKLKS PLGKGPVTFR DPLLKQSSDS
ELMAQQHHAA STGLASAAGP ARPRYLFQRR SKLWGDPVES RGLPGPEDDK PTVISELSSR
LQQLNKDTRS LGEEPVGGLG SLLDPAKKSP IAAARLFSSL GELSTISAQR SPGGPGGGAS
YSVRPSGRYP VARRAPSPVK PASLERVEGL GAGVGGAGRP FGLTPPTILK SSSLSIPHEP
KEVRFVVRSV SARSRSPSPS PLPSPSPGSG PSAGPRRPFQ QKPLQLWSKF DVGDWLESIH
LGEHRDRFED HEIEGAHLPA LTKEDFVELG VTRVGHRMNI ERALRQLDGS


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