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)

 SHAN3_HUMAN             Reviewed;        1731 AA.
Q9BYB0; D7UT47; Q8TET3;
26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
19-FEB-2014, sequence version 3.
22-NOV-2017, entry version 145.
RecName: Full=SH3 and multiple ankyrin repeat domains protein 3;
Short=Shank3;
AltName: Full=Proline-rich synapse-associated protein 2;
Short=ProSAP2;
Name=SHANK3; Synonyms=KIAA1650, PROSAP2, PSAP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Uchino S., Waga C., Kohsaka S.;
"Novel veriants of human SHANK3 gene.";
Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 935-1731 (ISOFORMS 1/2).
PubMed=11258795; DOI=10.1093/dnares/8.1.1;
Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
"Identification of novel transcribed sequences on human chromosome 22
by expressed sequence tag mapping.";
DNA Res. 8:1-9(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 962-1731 (ISOFORMS 1/2).
TISSUE=Spleen;
Ohara O., Nagase T., Kikuno R., Okumura K.;
"The nucleotide sequence of a long cDNA clone isolated from human
spleen.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1158 AND SER-1162, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1234 AND SER-1253, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[7]
ALTERNATIVE SPLICING (ISOFORM 2), AND INVOLVEMENT IN NEUROPSYCHIATRIC
DISORDERS.
PubMed=24186872; DOI=10.1093/hmg/ddt547;
Zhu L., Wang X., Li X.L., Towers A., Cao X., Wang P., Bowman R.,
Yang H., Goldstein J., Li Y.J., Jiang Y.H.;
"Epigenetic dysregulation of SHANK3 in brain tissues from individuals
with autism spectrum disorders.";
Hum. Mol. Genet. 23:1563-1578(2014).
[8]
CHROMOSOMAL TRANSLOCATION WITH APPL2.
PubMed=11431708; DOI=10.1086/321293;
Bonaglia M.C., Giorda R., Borgatti R., Felisari G., Gagliardi C.,
Selicorni A., Zuffardi O.;
"Disruption of the ProSAP2 gene in a t(12;22)(q24.1;q13.3) is
associated with the 22q13.3 deletion syndrome.";
Am. J. Hum. Genet. 69:261-268(2001).
[9]
REVIEW.
PubMed=10806096;
Sheng M., Kim E.;
"The Shank family of scaffold proteins.";
J. Cell Sci. 113:1851-1856(2000).
[10]
INTERACTION WITH BAIAP2.
PubMed=12504591; DOI=10.1006/mcne.2002.1201;
Soltau M., Richter D., Kreienkamp H.-J.;
"The insulin receptor substrate IRSp53 links postsynaptic shank1 to
the small G-protein cdc42.";
Mol. Cell. Neurosci. 21:575-583(2002).
[11]
INVOLVEMENT IN NEUROPSYCHIATRIC DISORDERS.
PubMed=22922660; DOI=10.1016/j.ejmg.2012.07.009;
Vucurovic K., Landais E., Delahaigue C., Eutrope J., Schneider A.,
Leroy C., Kabbaj H., Motte J., Gaillard D., Rolland A.C.,
Doco-Fenzy M.;
"Bipolar affective disorder and early dementia onset in a male patient
with SHANK3 deletion.";
Eur. J. Med. Genet. 55:625-629(2012).
[12]
INVOLVEMENT IN PHMDS.
PubMed=23758760; DOI=10.1186/2040-2392-4-18;
Soorya L., Kolevzon A., Zweifach J., Lim T., Dobry Y., Schwartz L.,
Frank Y., Wang A.T., Cai G., Parkhomenko E., Halpern D., Grodberg D.,
Angarita B., Willner J.P., Yang A., Canitano R., Chaplin W.,
Betancur C., Buxbaum J.D.;
"Prospective investigation of autism and genotype-phenotype
correlations in 22q13 deletion syndrome and SHANK3 deficiency.";
Mol. Autism 4:18-18(2013).
[13]
INVOLVEMENT IN NEUROPSYCHIATRIC DISORDERS.
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).
[14]
INVOLVEMENT IN PHMDS, FUNCTION IN SYNAPSE FORMATION, AND SUBCELLULAR
LOCATION.
PubMed=24132240; DOI=10.1038/nature12618;
Shcheglovitov A., Shcheglovitova O., Yazawa M., Portmann T., Shu R.,
Sebastiano V., Krawisz A., Froehlich W., Bernstein J.A.,
Hallmayer J.F., Dolmetsch R.E.;
"SHANK3 and IGF1 restore synaptic deficits in neurons from 22q13
deletion syndrome patients.";
Nature 503:267-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-913; THR-1234; SER-1253;
SER-1636 AND SER-1638, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
VARIANTS ARG-321; LEU-341; SER-970; THR-1173; LEU-1263; VAL-1406;
THR-1443; SER-1557 AND THR-1654, AND INVOLVEMENT IN NEUROPSYCHIATRIC
DISORDERS.
PubMed=17999366; DOI=10.1086/522590;
Moessner R., Marshall C.R., Sutcliffe J.S., Skaug J., Pinto D.,
Vincent J., Zwaigenbaum L., Fernandez B., Roberts W., Szatmari P.,
Scherer S.W.;
"Contribution of SHANK3 mutations to autism spectrum disorder.";
Am. J. Hum. Genet. 81:1289-1297(2007).
[17]
VARIANTS CYS-12; GLY-198; THR-224; CYS-300; GLY-963; VAL-1011;
HIS-1231; GLY-1566 AND THR-1654, INVOLVEMENT IN NEUROPSYCHIATRIC
DISORDERS, AND CHARACTERIZATION OF VARIANTS CYS-12 AND CYS-300.
PubMed=17173049; DOI=10.1038/ng1933;
Durand C.M., Betancur C., Boeckers T.M., Bockmann J., Chaste P.,
Fauchereau F., Nygren G., Rastam M., Gillberg I.C., Anckarsaeter H.,
Sponheim E., Goubran-Botros H., Delorme R., Chabane N.,
Mouren-Simeoni M.-C., de Mas P., Bieth E., Roge B., Heron D.,
Burglen L., Gillberg C., Leboyer M., Bourgeron T.;
"Mutations in the gene encoding the synaptic scaffolding protein
SHANK3 are associated with autism spectrum disorders.";
Nat. Genet. 39:25-27(2007).
[18]
VARIANT SCZD15 TRP-536, AND VARIANTS THR-245; GLN-493; THR-720;
THR-952; VAL-1010; LYS-1298; GLY-1333; VAL-1546 AND THR-1645.
PubMed=20385823; DOI=10.1073/pnas.0906232107;
Gauthier J., Champagne N., Lafreniere R.G., Xiong L., Spiegelman D.,
Brustein E., Lapointe M., Peng H., Cote M., Noreau A., Hamdan F.F.,
Addington A.M., Rapoport J.L., Delisi L.E., Krebs M.O., Joober R.,
Fathalli F., Mouaffak F., Haghighi A.P., Neri C., Dube M.P.,
Samuels M.E., Marineau C., Stone E.A., Awadalla P., Barker P.A.,
Carbonetto S., Drapeau P., Rouleau G.A.;
"De novo mutations in the gene encoding the synaptic scaffolding
protein SHANK3 in patients ascertained for schizophrenia.";
Proc. Natl. Acad. Sci. U.S.A. 107:7863-7868(2010).
[19]
VARIANTS PHMDS ALA-141 AND SER-1452.
PubMed=22892527; DOI=10.1038/ejhg.2012.175;
Boccuto L., Lauri M., Sarasua S.M., Skinner C.D., Buccella D.,
Dwivedi A., Orteschi D., Collins J.S., Zollino M., Visconti P.,
Dupont B., Tiziano D., Schroer R.J., Neri G., Stevenson R.E.,
Gurrieri F., Schwartz C.E.;
"Prevalence of SHANK3 variants in patients with different subtypes of
autism spectrum disorders.";
Eur. J. Hum. Genet. 21:310-316(2013).
-!- 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:24132240}.
-!- 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 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
P62993:GRB2; NbExp=2; IntAct=EBI-1752330, EBI-401755;
P16333:NCK1; NbExp=4; IntAct=EBI-1752330, EBI-389883;
P19174:PLCG1; NbExp=2; IntAct=EBI-1752330, EBI-79387;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24132240}.
Cell junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000269|PubMed:24132240}. Cell projection, dendritic
spine {ECO:0000250}. Note=In neuronal cells, extends into the
region subjacent to the postsynaptic density (PSD). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Comment=Additional isoforms seem to exist. These isoforms may be
the product of multiple intragenic promoter and/or alternative
splicing.;
Name=1; Synonyms=A;
IsoId=Q9BYB0-1; Sequence=Displayed;
Note=Primarily expressed in neurons.;
Name=2; Synonyms=B;
IsoId=Q9BYB0-3; Sequence=VSP_053605;
Note=Produced by alternative promoter usage.;
-!- TISSUE SPECIFICITY: Expressed in the cerebral cortex and the
cerebellum.
-!- 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}.
-!- DISEASE: Note=A chromosomal aberration involving SHANK3 is found
in patients with chromosome 22q13.3 deletion syndrome.
Translocation t(12;22)(q24.1;q13.3) with APPL2/DIP13B.
{ECO:0000269|PubMed:11431708}.
-!- DISEASE: Note=Defects in SHANK3 are associated with
neuropsychiatric disorders such as autism spectrum disorders
(ASD), bipolar affective disorders and early dementia onset. ASD
are characterized by impairments in reciprocal social interaction
and communication as well as restricted and stereotyped patterns
of interest and activities. ASD include forms with moderate to
severe cognitive impairment and milder forms with higher cognitive
ability (Asperger syndrome). Gene duplication is associated with
hyperkinetic neuropsychiatric disorders (PubMed:24153177) such as
hyperactivity, auditory overstimulation, epilepsy and bipolar
affective disorders, among others. {ECO:0000269|PubMed:24153177}.
-!- DISEASE: Phelan-McDermid syndrome (PHMDS) [MIM:606232]: A
developmental disorder with variable features. Common features
include neonatal hypotonia, global developmental delay, normal to
accelerated growth, absent to severely delayed speech, autistic
behavior, and minor dysmorphic features.
{ECO:0000269|PubMed:22892527, ECO:0000269|PubMed:23758760,
ECO:0000269|PubMed:24132240}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Schizophrenia 15 (SCZD15) [MIM:613950]: A complex,
multifactorial psychotic disorder or group of disorders
characterized by disturbances in the form and content of thought
(e.g. delusions, hallucinations), in mood (e.g. inappropriate
affect), in sense of self and relationship to the external world
(e.g. loss of ego boundaries, withdrawal), and in behavior (e.g
bizarre or apparently purposeless behavior). Although it affects
emotions, it is distinguished from mood disorders in which such
disturbances are primary. Similarly, there may be mild impairment
of cognitive function, and it is distinguished from the dementias
in which disturbed cognitive function is considered primary. Some
patients manifest schizophrenic as well as bipolar disorder
symptoms and are often given the diagnosis of schizoaffective
disorder. {ECO:0000269|PubMed:20385823}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC000050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC000036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB051437; BAB33320.1; -; mRNA.
EMBL; AK074038; BAB84864.1; -; mRNA.
EMBL; AB569469; BAJ09793.1; -; mRNA.
RefSeq; NP_277052.1; NM_033517.1. [Q9BYB0-1]
UniGene; Hs.149035; -.
ProteinModelPortal; Q9BYB0; -.
SMR; Q9BYB0; -.
BioGrid; 124487; 16.
CORUM; Q9BYB0; -.
DIP; DIP-52267N; -.
IntAct; Q9BYB0; 29.
MINT; MINT-4134553; -.
STRING; 9606.ENSP00000442518; -.
iPTMnet; Q9BYB0; -.
PhosphoSitePlus; Q9BYB0; -.
BioMuta; SHANK3; -.
DMDM; 148887434; -.
PaxDb; Q9BYB0; -.
PeptideAtlas; Q9BYB0; -.
PRIDE; Q9BYB0; -.
Ensembl; ENST00000635818; ENSP00000490818; ENSG00000283243. [Q9BYB0-1]
GeneID; 85358; -.
KEGG; hsa:85358; -.
CTD; 85358; -.
DisGeNET; 85358; -.
GeneCards; SHANK3; -.
GeneReviews; SHANK3; -.
HGNC; HGNC:14294; SHANK3.
HPA; HPA003446; -.
MalaCards; SHANK3; -.
MIM; 606230; gene.
MIM; 606232; phenotype.
MIM; 613950; phenotype.
neXtProt; NX_Q9BYB0; -.
Orphanet; 106; Autism.
Orphanet; 48652; Monosomy 22q13.
Orphanet; 3140; Schizophrenia.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4375; Eukaryota.
eggNOG; COG0666; LUCA.
HOVERGEN; HBG054027; -.
InParanoid; Q9BYB0; -.
KO; K15009; -.
Reactome; R-HSA-6794361; Neurexins and neuroligins.
Reactome; R-HSA-8853659; RET signaling.
SignaLink; Q9BYB0; -.
ChiTaRS; SHANK3; human.
GeneWiki; SHANK3; -.
GenomeRNAi; 85358; -.
PRO; PR:Q9BYB0; -.
Proteomes; UP000005640; Unplaced.
CleanEx; HS_SHANK3; -.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0060170; C:ciliary membrane; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
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; 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; ISS:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; ISS:BHF-UCL.
GO; GO:0043621; F:protein self-association; ISS:BHF-UCL.
GO; GO:0097110; F:scaffold protein binding; ISS: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; IMP:BHF-UCL.
GO; GO:0097113; P:AMPA glutamate receptor clustering; ISS:BHF-UCL.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
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; IMP:BHF-UCL.
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: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; ISS:BHF-UCL.
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:0061001; P:regulation of dendritic spine morphogenesis; 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; IMP: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:0042297; P:vocal learning; IMP:BHF-UCL.
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_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF12796; Ank_2; 2.
Pfam; PF16511; FERM_f0; 1.
Pfam; PF00595; PDZ; 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;
Actin-binding; Alternative promoter usage; ANK repeat;
Autism spectrum disorder; Cell junction; Cell membrane;
Cell projection; Chromosomal rearrangement; Coiled coil;
Complete proteome; Cytoplasm; Disease mutation; Membrane; Methylation;
Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
Reference proteome; Repeat; Schizophrenia; SH3 domain; SH3-binding;
Synapse.
CHAIN 1 1731 SH3 and multiple ankyrin repeat domains
protein 3.
/FTId=PRO_0000174675.
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 471 530 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 571 665 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1668 1731 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
REGION 1 75 Intramolecular interaction with the ANK
repeats. {ECO:0000250}.
REGION 678 685 Required for interaction with ABI1.
{ECO:0000250}.
COILED 1494 1514 {ECO:0000255}.
MOTIF 1410 1416 SH3-binding. {ECO:0000255}.
COMPBIAS 678 681 Poly-Pro.
COMPBIAS 719 722 Poly-Ala.
COMPBIAS 814 930 Pro-rich.
COMPBIAS 1232 1349 Pro-rich.
MOD_RES 122 122 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JLU4}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 556 556 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 782 782 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 791 791 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 802 802 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:0000244|PubMed:24275569}.
MOD_RES 931 931 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9JLU4}.
MOD_RES 966 966 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1129 1129 Phosphothreonine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1133 1133 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1158 1158 Phosphoserine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 1162 1162 Phosphoserine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 1165 1165 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1234 1234 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 1253 1253 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 1420 1420 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JLU4}.
MOD_RES 1510 1510 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1521 1521 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1529 1529 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1539 1539 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1634 1634 Phosphoserine.
{ECO:0000250|UniProtKB:Q4ACU6}.
MOD_RES 1636 1636 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1638 1638 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 119 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_053605.
VARIANT 12 12 R -> C (found in patients with
neuropsychiatric disorders; unknown
pathological significance; disrupts
synaptic localization).
{ECO:0000269|PubMed:17173049}.
/FTId=VAR_032804.
VARIANT 141 141 P -> A (in PHMDS; dbSNP:rs397514705).
{ECO:0000269|PubMed:22892527}.
/FTId=VAR_070259.
VARIANT 198 198 A -> G. {ECO:0000269|PubMed:17173049}.
/FTId=VAR_032805.
VARIANT 224 224 A -> T (in dbSNP:rs766856815).
{ECO:0000269|PubMed:17173049}.
/FTId=VAR_032806.
VARIANT 245 245 I -> T (in dbSNP:rs9616915).
{ECO:0000269|PubMed:20385823}.
/FTId=VAR_032807.
VARIANT 300 300 R -> C (found in patients with
neuropsychiatric disorders; unknown
pathological significance; disrupts
synaptic localization;
dbSNP:rs376862893).
{ECO:0000269|PubMed:17173049}.
/FTId=VAR_032808.
VARIANT 321 321 Q -> R (found in a patient with
neuropsychiatric disorders; unknown
pathological significance).
{ECO:0000269|PubMed:17999366}.
/FTId=VAR_070260.
VARIANT 341 341 S -> L (found in patient with
neuropsychiatric disorders; unknown
pathological significance).
{ECO:0000269|PubMed:17999366}.
/FTId=VAR_070261.
VARIANT 493 493 H -> Q. {ECO:0000269|PubMed:20385823}.
/FTId=VAR_065799.
VARIANT 536 536 R -> W (in SCZD15; dbSNP:rs387906933).
{ECO:0000269|PubMed:20385823}.
/FTId=VAR_065800.
VARIANT 720 720 A -> T. {ECO:0000269|PubMed:20385823}.
/FTId=VAR_065801.
VARIANT 952 952 S -> T. {ECO:0000269|PubMed:20385823}.
/FTId=VAR_065802.
VARIANT 963 963 A -> G. {ECO:0000269|PubMed:17173049}.
/FTId=VAR_070262.
VARIANT 970 970 A -> S (found in a patient with
neuropsychiatric disorders; unknown
pathological significance;
dbSNP:rs530255181).
{ECO:0000269|PubMed:17999366}.
/FTId=VAR_070263.
VARIANT 1010 1010 G -> V. {ECO:0000269|PubMed:20385823}.
/FTId=VAR_065803.
VARIANT 1011 1011 G -> V (in dbSNP:rs767058690).
{ECO:0000269|PubMed:17173049}.
/FTId=VAR_070264.
VARIANT 1134 1134 P -> H (in dbSNP:rs769454362).
/FTId=VAR_065804.
VARIANT 1173 1173 A -> T (found in a patient with
neuropsychiatric disorders; unknown
pathological significance;
dbSNP:rs139686326).
{ECO:0000269|PubMed:17999366}.
/FTId=VAR_070265.
VARIANT 1231 1231 R -> H (in dbSNP:rs750186589).
{ECO:0000269|PubMed:17173049}.
/FTId=VAR_070266.
VARIANT 1263 1263 P -> L (found in a patient with
neuropsychiatric disorders; unknown
pathological significance;
dbSNP:rs757572910).
{ECO:0000269|PubMed:17999366}.
/FTId=VAR_070267.
VARIANT 1298 1298 R -> K (in dbSNP:rs201483867).
{ECO:0000269|PubMed:20385823}.
/FTId=VAR_065805.
VARIANT 1333 1333 V -> G (in dbSNP:rs200087210).
{ECO:0000269|PubMed:20385823}.
/FTId=VAR_065806.
VARIANT 1406 1406 L -> V (found in a patient with
neuropsychiatric disorders; unknown
pathological significance;
dbSNP:rs201973139).
{ECO:0000269|PubMed:17999366}.
/FTId=VAR_070268.
VARIANT 1443 1443 M -> T (found in a patient with
neuropsychiatric disorders; unknown
pathological significance;
dbSNP:rs773395828).
{ECO:0000269|PubMed:17999366}.
/FTId=VAR_070269.
VARIANT 1452 1452 A -> S (in PHMDS).
{ECO:0000269|PubMed:22892527}.
/FTId=VAR_070270.
VARIANT 1546 1546 I -> V. {ECO:0000269|PubMed:20385823}.
/FTId=VAR_065807.
VARIANT 1557 1557 G -> S (found in a patient with
neuropsychiatric disorders; unknown
pathological significance).
{ECO:0000269|PubMed:17999366}.
/FTId=VAR_070271.
VARIANT 1566 1566 S -> G. {ECO:0000269|PubMed:17173049}.
/FTId=VAR_070272.
VARIANT 1645 1645 P -> T. {ECO:0000269|PubMed:20385823}.
/FTId=VAR_065808.
VARIANT 1654 1654 P -> T (found in patients with
neuropsychiatric disorders; unknown
pathological significance;
dbSNP:rs749130556).
{ECO:0000269|PubMed:17173049,
ECO:0000269|PubMed:17999366}.
/FTId=VAR_070273.
SEQUENCE 1731 AA; 184667 MW; 781936CE60988D08 CRC64;
MDGPGASAVV VRVGIPDLQQ TKCLRLDPAA PVWAAKQRVL CALNHSLQDA LNYGLFQPPS
RGRAGKFLDE ERLLQEYPPN LDTPLPYLEF RYKRRVYAQN LIDDKQFAKL HTKANLKKFM
DYVQLHSTDK VARLLDKGLD PNFHDPDSGE CPLSLAAQLD NATDLLKVLK NGGAHLDFRT
RDGLTAVHCA TRQRNAAALT TLLDLGASPD YKDSRGLTPL YHSALGGGDA LCCELLLHDH
AQLGITDENG WQEIHQACRF GHVQHLEHLL FYGADMGAQN ASGNTALHIC ALYNQESCAR
VLLFRGANRD VRNYNSQTAF QVAIIAGNFE LAEVIKTHKD SDVVPFRETP SYAKRRRLAG
PSGLASPRPL QRSASDINLK GEAQPAASPG PSLRSLPHQL LLQRLQEEKD RDRDADQESN
ISGPLAGRAG QSKISPSGPG GPGPAPGPGP APPAPPAPPP RGPKRKLYSA VPGRKFIAVK
AHSPQGEGEI PLHRGEAVKV LSIGEGGFWE GTVKGRTGWF PADCVEEVQM RQHDTRPETR
EDRTKRLFRH YTVGSYDSLT SHSDYVIDDK VAVLQKRDHE GFGFVLRGAK AETPIEEFTP
TPAFPALQYL ESVDVEGVAW RAGLRTGDFL IEVNGVNVVK VGHKQVVALI RQGGNRLVMK
VVSVTRKPEE DGARRRAPPP PKRAPSTTLT LRSKSMTAEL EELASIRRRK GEKLDEMLAA
AAEPTLRPDI ADADSRAATV KQRPTSRRIT PAEISSLFER QGLPGPEKLP GSLRKGIPRT
KSVGEDEKLA SLLEGRFPRS TSMQDPVREG RGIPPPPQTA PPPPPAPYYF DSGPPPAFSP
PPPPGRAYDT VRSSFKPGLE ARLGAGAAGL YEPGAALGPL PYPERQKRAR SMIILQDSAP
ESGDAPRPPP AATPPERPKR RPRPPGPDSP YANLGAFSAS LFAPSKPQRR KSPLVKQLQV
EDAQERAALA VGSPGPGGGS FAREPSPTHR GPRPGGLDYG AGDGPGLAFG GPGPAKDRRL
EERRRSTVFL SVGAIEGSAP GADLPSLQPS RSIDERLLGT GPTAGRDLLL PSPVSALKPL
VSGPSLGPSG STFIHPLTGK PLDPSSPLAL ALAARERALA SQAPSRSPTP VHSPDADRPG
PLFVDVQARD PERGSLASPA FSPRSPAWIP VPARREAEKV PREERKSPED KKSMILSVLD
TSLQRPAGLI VVHATSNGQE PSRLGGAEEE RPGTPELAPA PMQSAAVAEP LPSPRAQPPG
GTPADAGPGQ GSSEEEPELV FAVNLPPAQL SSSDEETREE LARIGLVPPP EEFANGVLLA
TPLAGPGPSP TTVPSPASGK PSSEPPPAPE SAADSGVEEA DTRSSSDPHL ETTSTISTVS
SMSTLSSESG ELTDTHTSFA DGHTFLLEKP PVPPKPKLKS PLGKGPVTFR DPLLKQSSDS
ELMAQQHHAA SAGLASAAGP ARPRYLFQRR SKLWGDPVES RGLPGPEDDK PTVISELSSR
LQQLNKDTRS LGEEPVGGLG SLLDPAKKSP IAAARLFSSL GELSSISAQR SPGGPGGGAS
YSVRPSGRYP VARRAPSPVK PASLERVEGL GAGAGGAGRP FGLTPPTILK SSSLSIPHEP
KEVRFVVRSV SARSRSPSPS PLPSPASGPG PGAPGPRRPF QQKPLQLWSK FDVGDWLESI
HLGEHRDRFE DHEIEGAHLP ALTKDDFVEL GVTRVGHRMN IERALRQLDG S


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
CSB-EL021249RA Rat SH3 and multiple ankyrin repeat domains 3 (SHANK3) ELISA kit, Species Rat, 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
CSB-EL021249MO Mouse SH3 and multiple ankyrin repeat domains 3 (SHANK3) ELISA kit, Species Mouse, 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
GWB-CC842E Anti- SH3 and multiple ankyrin repeat domains protein 1 Antibody
GWB-C89AA1 Anti- SH3 and multiple ankyrin repeat domains protein 1 Antibody


 

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