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SH3 and multiple ankyrin repeat domains protein 2 (Shank2) (Cortactin-binding protein 1) (CortBP1)

 SHAN2_MOUSE             Reviewed;        1476 AA.
Q80Z38; E9QPH7; Q3UTK4; Q5DU07;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
27-SEP-2017, entry version 113.
RecName: Full=SH3 and multiple ankyrin repeat domains protein 2;
Short=Shank2;
AltName: Full=Cortactin-binding protein 1;
Short=CortBP1;
Name=Shank2; Synonyms=Cortbp1, Kiaa1022;
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 1), SUBCELLULAR LOCATION, AND
INTERACTION WITH GRID2.
PubMed=15207857; DOI=10.1016/j.mcn.2004.02.007;
Uemura T., Mori H., Mishina M.;
"Direct interaction of GluRdelta2 with Shank scaffold proteins in
cerebellar Purkinje cells.";
Mol. Cell. Neurosci. 26:330-341(2004).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-350 (ISOFORMS 1/2).
STRAIN=C57BL/6J; TISSUE=Brain cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-1476 (ISOFORM 2).
TISSUE=Fetal brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[6]
TISSUE SPECIFICITY.
PubMed=9742101; DOI=10.1128/MCB.18.10.5838;
Du Y., Weed S.A., Xiong W.-C., Marshall T.D., Parsons J.T.;
"Identification of a novel cortactin SH3 domain-binding protein and
its localization to growth cones of cultured neurons.";
Mol. Cell. Biol. 18:5838-5851(1998).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586 AND THR-903, 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]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-1292.
TISSUE=Brain;
PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
Maltby D.A., Schoepfer R., Burlingame A.L.;
"O-linked N-acetylglucosamine proteomics of postsynaptic density
preparations using lectin weak affinity chromatography and mass
spectrometry.";
Mol. Cell. Proteomics 5:923-934(2006).
[9]
INTERACTION WITH PDE4D, AND TISSUE SPECIFICITY.
PubMed=17244609; DOI=10.1074/jbc.M610857200;
Lee J.H., Richter W., Namkung W., Kim K.H., Kim E., Conti M.,
Lee M.G.;
"Dynamic regulation of cystic fibrosis transmembrane conductance
regulator by competitive interactions of molecular adaptors.";
J. Biol. Chem. 282:10414-10422(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; THR-485; SER-586;
SER-724; SER-1334 AND SER-1338, PHOSPHORYLATION [LARGE SCALE ANALYSIS]
AT SER-372 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
SER-162 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Kidney, and Pancreas;
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]
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).
[12]
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).
-!- FUNCTION: Seems to be an adapter protein in the postsynaptic
density (PSD) of excitatory synapses that interconnects receptors
of the postsynaptic membrane including NMDA-type and metabotropic
glutamate receptors, and the actin-based cytoskeleton. May play a
role in the structural and functional organization of the
dendritic spine and synaptic junction (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP.
Interacts with CTTN/cortactin SH3 domain, DLGAP1/GKAP and alpha-
latrotoxin receptor 1. Interacts with DNM2, DBNL, GRID2, BAIAP2,
SLC9A3, PLCB3 and CFTR. Interacts (via proline-rich region) with
PDE4D. Interacts with ABI1 (via SH3 domain).
{ECO:0000269|PubMed:15207857, ECO:0000269|PubMed:17244609}.
-!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}.
Cytoplasm {ECO:0000269|PubMed:15207857}. Cell junction, synapse
{ECO:0000269|PubMed:15207857}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000269|PubMed:15207857}. Cell projection, dendritic spine
{ECO:0000269|PubMed:15207857}. Cell projection, growth cone
{ECO:0000250}. Note=Colocalizes with cortactin in growth cones in
differentiating hippocampal neurons. Colocalized with PDE4D to the
apical membrane of colonic crypt cells (By similarity). Present in
the dendritic spines of cerebellar Purkinje cells. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=E;
IsoId=Q80Z38-1; Sequence=Displayed;
Name=2;
IsoId=Q80Z38-2; Sequence=VSP_020040;
Note=Contains a phosphoserine at position 372.
{ECO:0000244|PubMed:21183079};
Name=3;
IsoId=Q80Z38-3; Sequence=VSP_041614, VSP_041615, VSP_020040;
Note=Contains a phosphoserine at position 162.
{ECO:0000244|PubMed:21183079};
-!- TISSUE SPECIFICITY: Detected in brain (at protein level), where it
is highly expressed in Purkinje cells.
{ECO:0000269|PubMed:17244609, ECO:0000269|PubMed:21423165,
ECO:0000269|PubMed:9742101}.
-!- DOMAIN: The PDZ domain is required for interaction with GRID2,
PLCB3, SLC9A3 and CFTR.
-!- DISRUPTION PHENOTYPE: Mutants are viable, but with reduced body
weight and a lower survival rate compared to their wild-type
littermates. They are extremely hiperactive and display profound
autistic-like behavioral alterations including repetitive grooming
as well as abnormalities in vocal and social behaviors. Mutants
exhibit fewer dendritic spines and show reduced basal synaptic
transmission, a reduced frequency of miniature excitatory
postsynaptic currents and enhanced NMDA receptor-mediated
excitatory currents at the physiological level. They also show a
brain-region-specific up-regulation of ionotropic glutamate
receptors and increased levels of SHANK3.
{ECO:0000269|PubMed:22699619}.
-!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
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EMBL; AB099695; BAC58120.1; -; mRNA.
EMBL; AC124520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC127546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC140268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC152166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC167171; AAI67171.1; -; mRNA.
EMBL; AK139360; BAE23976.1; -; mRNA.
EMBL; AK220363; BAD90424.1; -; mRNA.
CCDS; CCDS40201.1; -. [Q80Z38-3]
CCDS; CCDS85484.1; -. [Q80Z38-2]
RefSeq; NP_001074839.2; NM_001081370.2.
RefSeq; NP_001106844.2; NM_001113373.2.
RefSeq; XP_006508596.1; XM_006508533.1. [Q80Z38-1]
UniGene; Mm.483624; -.
ProteinModelPortal; Q80Z38; -.
SMR; Q80Z38; -.
BioGrid; 229144; 6.
CORUM; Q80Z38; -.
IntAct; Q80Z38; 4.
STRING; 10090.ENSMUSP00000095542; -.
iPTMnet; Q80Z38; -.
PhosphoSitePlus; Q80Z38; -.
PaxDb; Q80Z38; -.
PeptideAtlas; Q80Z38; -.
PRIDE; Q80Z38; -.
DNASU; 210274; -.
Ensembl; ENSMUST00000105900; ENSMUSP00000101520; ENSMUSG00000037541. [Q80Z38-2]
Ensembl; ENSMUST00000146006; ENSMUSP00000146440; ENSMUSG00000037541. [Q80Z38-3]
GeneID; 210274; -.
KEGG; mmu:210274; -.
UCSC; uc009kqe.2; mouse. [Q80Z38-2]
UCSC; uc009kqf.1; mouse. [Q80Z38-3]
UCSC; uc009kqg.1; mouse. [Q80Z38-1]
CTD; 22941; -.
MGI; MGI:2671987; Shank2.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00510000046474; -.
HOGENOM; HOG000293276; -.
HOVERGEN; HBG054027; -.
InParanoid; Q80Z38; -.
KO; K15009; -.
Reactome; R-MMU-6794361; Neurexins and neuroligins.
PRO; PR:Q80Z38; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000037541; -.
CleanEx; MM_SHANK2; -.
ExpressionAtlas; Q80Z38; baseline and differential.
GO; GO:0016324; C:apical plasma membrane; ISS:BHF-UCL.
GO; GO:0031526; C:brush border membrane; ISS:BHF-UCL.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0060170; C:ciliary membrane; ISS:BHF-UCL.
GO; GO:0043197; C:dendritic spine; IDA:BHF-UCL.
GO; GO:0030426; C:growth cone; ISS:BHF-UCL.
GO; GO:0005883; C:neurofilament; IDA:CACAO.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
GO; GO:0001917; C:photoreceptor inner segment; IDA:BHF-UCL.
GO; GO:0001750; C:photoreceptor outer segment; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0014069; C:postsynaptic density of dendrite; ISS:BHF-UCL.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0048786; C:presynaptic active zone; ISO:MGI.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0030534; P:adult behavior; IMP:BHF-UCL.
GO; GO:0035640; P:exploration behavior; IMP:BHF-UCL.
GO; GO:0007612; P:learning; IMP:BHF-UCL.
GO; GO:0060292; P:long term synaptic depression; IMP:BHF-UCL.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:BHF-UCL.
GO; GO:0007613; P:memory; IMP:BHF-UCL.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:CACAO.
GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
GO; GO:0007416; P:synapse assembly; IMP:BHF-UCL.
GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
InterPro; IPR001478; PDZ.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR011511; SH3_2.
InterPro; IPR001452; SH3_domain.
Pfam; PF00595; PDZ; 1.
Pfam; PF00536; SAM_1; 1.
Pfam; PF07653; SH3_2; 1.
SMART; SM00228; PDZ; 1.
SMART; SM00454; SAM; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50106; PDZ; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Glycoprotein; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; SH3 domain;
SH3-binding; Synapse.
CHAIN 1 1476 SH3 and multiple ankyrin repeat domains
protein 2.
/FTId=PRO_0000247760.
DOMAIN 147 206 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 247 341 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1413 1476 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
MOTIF 1169 1175 SH3-binding. {ECO:0000255}.
COMPBIAS 24 27 Poly-Arg.
COMPBIAS 355 358 Poly-Pro.
COMPBIAS 513 560 Pro-rich.
COMPBIAS 1017 1020 Poly-Pro.
COMPBIAS 1169 1211 Pro-rich.
COMPBIAS 1348 1353 Poly-Pro.
MOD_RES 456 456 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 485 485 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 586 586 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 648 648 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QX74}.
MOD_RES 724 724 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 903 903 Phosphothreonine.
{ECO:0000244|PubMed:16452087}.
MOD_RES 1334 1334 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1338 1338 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 1292 1292 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:16452088}.
VAR_SEQ 1 210 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041614.
VAR_SEQ 211 238 SQAETRADRSKKLFRHYTVGSYDSFDAA -> MMSVPGGGA
ATVMMTGYNNGRYPRNSLY (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041615.
VAR_SEQ 380 383 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.5}.
/FTId=VSP_020040.
CONFLICT 1071 1071 S -> P (in Ref. 1; BAC58120 and 5;
BAD90424). {ECO:0000305}.
SEQUENCE 1476 AA; 158969 MW; 0B5B0EBDFD6BAAA7 CRC64;
MKSLLNAFTK KEVPFREAPA YSNRRRRPPN TLAAPRVLLR SNSDNNLNAG APEWAVCSAA
TSHRSLSPQL LQQTPSKPDG ATKSLGSYTP GPRSRSPSLN RLGGTAEDGK RTQPHWHVGS
PFTPGANKDS LSTFEYPGPR RKLYSAVPGR LFVAVKPYQP QVDGEIPLHR GDRVKVLSIG
EGGFWEGSAR GHIGWFPAEC VEEVQCKPRD SQAETRADRS KKLFRHYTVG SYDSFDAASD
CIIEDKTVVL QKKDNEGFGF VLRGAKADTP IEEFTPTPAF PALQYLESVD EGGVAWQAGL
RTGDFLIEVN NENVVKVGHR QVVNMIRQGG NHLILKVVTV TRNLDPDDTA RKKAPPPPKR
APTTALTLRS KSMTAELEEL GLSLVDKASV RKKKDKPEEI VPASKPSRTA ENVAIESRVA
TIKQRPTSRC FPAASDVNSV YERQGIAVMT PTVPGSPKGP FLGLPRGTMR RQKSIDSRIF
LSGITEEERQ FLAPPMLKFT RSLSMPDTSE DIPPPPQSVP PSPPPPSPTT YNCPRSPTPR
VYGTIKPAFN QNPVVAKVPP ATRSDTVATM MREKGMFYRR ELDRFSLDSE DVYSRSPAPQ
AAFRTKRGQM PENPYSEVGK IASKAVYVPA KPARRKGVLV KQSNVEDSPE KTCSIPIPTI
IVKEPSTSSS GKSSQGSSME IDPQATEPGQ LRPDDSLTVS SPFAAAIAGA VRDREKRLEA
RRNSPAFLST DLGDEDVGLG PPAPRMQASK FPEEGGFGDE DETEQPLLPT PGAAPRELEN
HFLGGGEAGA QGEAGGPLSS TSKAKGPESG PAAPLKSSSP AGPENYVHPL TGRLLDPSSP
LALALSARDR AMQESQQGHK GEAPKADLNK PLYIDTKMRP SVESGFPPVT RQNTRGPLRR
QETENKYETD LGKDRRADDK KNMLINIVDT AQQKSAGLLM VHTVDVPMAG PPLEEEEDRE
DGDTKPDHSP STVPEGVPKT EGALQISAAP EPAVAPGRTI VAAGSVEEAV ILPFRIPPPP
LASVDLDEDF LFTEPLPPPL EFANSFDIPD DRAASVPALA DLVKQKKNDT SQPPTLNSSQ
PANSTDSKKP AGISNCLPSS FLPPPESFDA VTDSGIEEVD SRSSSDHHLE TTSTISTVSS
ISTLSSEGGE SMDTCTVYAD GQAFVVDKPP VPPKPKMKPI VHKSNALYQD TLPEEDTDGF
VIPPPAPPPP PGSAQAGVAK VIQPRTSKLW GDVPEVKSPI LSGPKANVIS ELNSILQQMN
RGKSVKPGEG LELPVGAKSA NLAPRSPEVM STVSGTRSTT VTFTVRPGTS QPITLQSRPP
DYESRTSGPR RAPSPVVSPT ELSKEILPTP PPPSATAASP SPTLSDVFSL PSQSPAGDLF
GLNPAGRSRS PSPSILQQPI SNKPFTTKPV HLWTKPDVAD WLESLNLGEH KETFMDNEID
GSHLPNLQKE DLIDLGVTRV GHRMNIERAL KQLLDR


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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
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
SMC-328D SHANK2 Antibody Monoclonal, Clone number: S23b-6 Host: Mouse, Isotype: IgG1 Immunogen: Fusion protein amino acids 84-309 (SH3_PDZ domains) of rat Shank2 (SH3 and multiple ankyrin repeat domains protei 100ug
H0225 SH3 and multiple ankyrin repeat domains protein 2 (SHANK2), Rat, ELISA Kit 96T
CSB-EL021248RA Rat SH3 and multiple ankyrin repeat domains protein 2(SHANK2) ELISA kit 96T
H0224 SH3 and multiple ankyrin repeat domains protein 2 (SHANK2), Mouse, ELISA Kit 96T
CSB-EL021248RA Rat SH3 and multiple ankyrin repeat domains protein 2(SHANK2) ELISA kit SpeciesRat 96T
CSB-EL021248HU Human SH3 and multiple ankyrin repeat domains protein 2(SHANK2) ELISA kit 96T
H0223 SH3 and multiple ankyrin repeat domains protein 2 (SHANK2), Human, ELISA Kit 96T
CSB-EL021248MO Mouse SH3 and multiple ankyrin repeat domains protein 2(SHANK2) ELISA kit 96T
CSB-EL021248MO Mouse SH3 and multiple ankyrin repeat domains protein 2(SHANK2) ELISA kit SpeciesMouse 96T
SHAN2_RAT ELISA Kit FOR SH3 and multiple ankyrin repeat domains protein 2; organism: Rat; gene name: Shank2 96T
CSB-EL021248HU Human SH3 and multiple ankyrin repeat domains protein 2(SHANK2) ELISA kit SpeciesHuman 96T
SHAN2_MOUSE ELISA Kit FOR SH3 and multiple ankyrin repeat domains protein 2; organism: Mouse; gene name: Shank2 96T
SHANK2 SHANK2 Gene SH3 and multiple ankyrin repeat domains 2
CSB-EL021248RA Rat SH3 and multiple ankyrin repeat domains 2 (SHANK2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL021248HU Human SH3 and multiple ankyrin repeat domains 2 (SHANK2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL021248MO Mouse SH3 and multiple ankyrin repeat domains 2 (SHANK2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
30036 IgG,SH3 and multiple ankyrin repeat domains protein 1 0.1 mg
30037 IgG,SH3 and multiple ankyrin repeat domains protein 1 0.1 mg
GWB-CC842E Anti- SH3 and multiple ankyrin repeat domains protein 1 Antibody
GWB-C89AA1 Anti- SH3 and multiple ankyrin repeat domains protein 1 Antibody
H0222 SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), Rat, ELISA Kit 96T


 

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