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Disks large homolog 2 (Channel-associated protein of synapse-110) (Chapsyn-110) (Postsynaptic density protein PSD-93)

 DLG2_RAT                Reviewed;         852 AA.
Q63622; P70548; Q62939;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 157.
RecName: Full=Disks large homolog 2;
AltName: Full=Channel-associated protein of synapse-110;
Short=Chapsyn-110 {ECO:0000303|PubMed:11997254};
AltName: Full=Postsynaptic density protein PSD-93;
Name=Dlg2; Synonyms=Dlgh2;
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).
PubMed=8755482; DOI=10.1016/S0896-6273(00)80284-6;
Kim E., Cho K.-O., Rothschild A., Sheng M.;
"Heteromultimerization and NMDA receptor-clustering activity of
Chapsyn-110, a member of the PSD-95 family of proteins.";
Neuron 17:103-113(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
PubMed=8625413; DOI=10.1016/S0092-8674(00)81053-3;
Brenman J.E., Chao D.S., Gee S.H., McGee A.W., Craven S.E.,
Santillano D.R., Wu Z., Huang F., Xia H., Peters M.F., Froehner S.C.,
Bredt D.S.;
"Interaction of nitric oxide synthase with the postsynaptic density
protein PSD-95 and alpha1-syntrophin mediated by PDZ domains.";
Cell 84:757-767(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Irie M., Hata Y., Takai Y.;
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[4]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE
SPECIFICITY.
PubMed=15304517; DOI=10.1074/jbc.M407575200;
Leyland M.L., Dart C.;
"An alternatively spliced isoform of PSD-93/chapsyn 110 binds to the
inwardly rectifying potassium channel, Kir2.1.";
J. Biol. Chem. 279:43427-43436(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5), SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION
WITH NOS1.
PubMed=8922396;
Brenman J.E., Christopherson K.S., Craven S.E., McGee A.W.,
Bredt D.S.;
"Cloning and characterization of postsynaptic density 93, a nitric
oxide synthase interacting protein.";
J. Neurosci. 16:7407-7415(1996).
[6]
MUTAGENESIS OF CYS-5 AND CYS-7, AND PALMITOYLATION AT CYS-5 AND CYS-7.
PubMed=10779526; DOI=10.1074/jbc.M909919199;
El-Husseini A.E., Topinka J.R., Lehrer-Graiwer J.E., Firestein B.L.,
Craven S.E., Aoki C., Bredt D.S.;
"Ion channel clustering by membrane-associated guanylate kinases.
Differential regulation by N-terminal lipid and metal binding
motifs.";
J. Biol. Chem. 275:23904-23910(2000).
[7]
SUBCELLULAR LOCATION.
PubMed=11095503; DOI=10.1097/00001756-200011090-00016;
Firestein B.L., Craven S.E., Bredt D.S.;
"Postsynaptic targeting of MAGUKs mediated by distinct N-terminal
domains.";
NeuroReport 11:3479-3484(2000).
[8]
INTERACTION WITH KCNJ4, AND SUBCELLULAR LOCATION.
PubMed=11997254; DOI=10.1152/ajpcell.00615.2001;
Inanobe A., Fujita A., Ito M., Tomoike H., Inageda K., Kurachi Y.;
"Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic
membrane of excitatory synapses.";
Am. J. Physiol. 282:C1396-C1403(2002).
[9]
INTERACTION WITH LRFN1.
PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H.,
Kaang B.-K., Kim E.;
"SALM synaptic cell adhesion-like molecules regulate the
differentiation of excitatory synapses.";
Neuron 50:233-245(2006).
[10]
INTERACTION WITH FRMPD4.
PubMed=19118189; DOI=10.1523/JNEUROSCI.3112-08.2008;
Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y.,
Kang G.B., Eom S.H., Kim H., Kim E.;
"Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
regulates dendritic spine morphogenesis.";
J. Neurosci. 28:14546-14556(2008).
[11]
INTERACTION WITH ADAM22, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=20089912; DOI=10.1523/JNEUROSCI.4661-09.2010;
Ogawa Y., Oses-Prieto J., Kim M.Y., Horresh I., Peles E.,
Burlingame A.L., Trimmer J.S., Meijer D., Rasband M.N.;
"ADAM22, a Kv1 channel-interacting protein, recruits membrane-
associated guanylate kinases to juxtaparanodes of myelinated axons.";
J. Neurosci. 30:1038-1048(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-365; SER-406;
SER-414; SER-528 AND SER-530, 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).
-!- FUNCTION: Required for perception of chronic pain through NMDA
receptor signaling. Regulates surface expression of NMDA receptors
in dorsal horn neurons of the spinal cord. Interacts with the
cytoplasmic tail of NMDA receptor subunits as well as inward
rectifying potassium channels. Involved in regulation of synaptic
stability at cholinergic synapses. Part of the postsynaptic
protein scaffold of excitatory synapses (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts through its PDZ domains with NETO1. Interacts
with NOS1/nNOS through second PDZ domain (PubMed:8922396).
Interacts with KCNJ2/Kir2.1 (via C-terminus) through one of its
PDZ domains (By similarity). Interacts with KCNJ4 (By similarity).
Interacts with FRMPD4 (via C-terminus) (PubMed:19118189).
Interacts with LRFN1 (PubMed:16630835). Interacts with LRFN2 and
LRFN4. Interacts with FASLG (By similarity). Interacts with ADAM22
(PubMed:20089912). {ECO:0000250|UniProtKB:Q15700,
ECO:0000250|UniProtKB:Q91XM9, ECO:0000269|PubMed:11997254,
ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:19118189,
ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:8922396}.
-!- INTERACTION:
Q01814-1:ATP2B2 (xeno); NbExp=2; IntAct=EBI-396947, EBI-1174262;
P23634-6:ATP2B4 (xeno); NbExp=2; IntAct=EBI-396947, EBI-1174437;
Q810C5:Dgki; NbExp=3; IntAct=EBI-396947, EBI-8523614;
O08560:Dgkz; NbExp=4; IntAct=EBI-396947, EBI-8570505;
O60333-3:KIF1B (xeno); NbExp=3; IntAct=EBI-396947, EBI-465669;
P34926:Map1a; NbExp=4; IntAct=EBI-396947, EBI-631571;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10779526};
Lipid-anchor {ECO:0000269|PubMed:10779526}. Cell junction,
synapse, postsynaptic cell membrane, postsynaptic density
{ECO:0000269|PubMed:11095503}. Cell junction, synapse. Cell
projection, axon {ECO:0000269|PubMed:20089912}. Membrane
{ECO:0000269|PubMed:11997254, ECO:0000269|PubMed:20089912}.
Note=Concentrated in soma and postsynaptic density of a subset of
neurons (PubMed:11095503). {ECO:0000269|PubMed:11095503}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=PSD-93b;
IsoId=Q63622-1; Sequence=Displayed;
Name=2; Synonyms=PSD-93a;
IsoId=Q63622-2; Sequence=VSP_015528;
Name=3; Synonyms=PSD-93c;
IsoId=Q63622-3; Sequence=VSP_015527, VSP_015529, VSP_015530;
Name=4; Synonyms=PSD-93-delta;
IsoId=Q63622-4; Sequence=VSP_015526;
Name=5; Synonyms=PSD-93d;
IsoId=Q63622-5; Sequence=VSP_015525;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q63622-6; Sequence=VSP_015531, VSP_015533;
Name=7;
IsoId=Q63622-7; Sequence=VSP_015532;
-!- TISSUE SPECIFICITY: Detected in juxtaparanodal zones in the
central nervous system and at nerve terminal plexuses of basket
cells in the cerebellum (at protein level) (PubMed:20089912).
Brain. High levels in cerebellar Purkinje cells. Expressed in
pyramidal cells of the Ammons's horn and granular cells of the
dentate gyrus in the hippocampus as well as cerebral cortex and
striatum. High levels in dorsal horn of spinal cord.
{ECO:0000269|PubMed:15304517, ECO:0000269|PubMed:20089912,
ECO:0000269|PubMed:8922396}.
-!- DEVELOPMENTAL STAGE: High levels in developing brain and spinal
chord, sensory neurons of dorsal root and trigeminal ganglia,
myenteric neurons of the intestine as well as in non-neuronal
cells of adrenal, thymus and submandibular glands of E15 embryos.
{ECO:0000269|PubMed:8922396}.
-!- PTM: Palmitoylation of isoform 1 and isoform 2 is not required for
targeting to postsynaptic density. {ECO:0000269|PubMed:10779526}.
-!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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EMBL; U49049; AAB53243.1; -; mRNA.
EMBL; U50717; AAC52643.1; -; mRNA.
EMBL; U53368; AAB48562.1; -; mRNA.
PIR; T10811; T10811.
RefSeq; NP_071618.1; NM_022282.1.
UniGene; Rn.202966; -.
PDB; 4H11; X-ray; 1.67 A; A/B=93-188.
PDBsum; 4H11; -.
ProteinModelPortal; Q63622; -.
SMR; Q63622; -.
BioGrid; 248965; 8.
IntAct; Q63622; 15.
MINT; MINT-155119; -.
STRING; 10116.ENSRNOP00000052268; -.
iPTMnet; Q63622; -.
PhosphoSitePlus; Q63622; -.
PaxDb; Q63622; -.
PRIDE; Q63622; -.
GeneID; 64053; -.
KEGG; rno:64053; -.
UCSC; RGD:619895; rat. [Q63622-1]
CTD; 1740; -.
RGD; 619895; Dlg2.
eggNOG; KOG0708; Eukaryota.
eggNOG; COG0194; LUCA.
HOGENOM; HOG000232102; -.
HOVERGEN; HBG107814; -.
InParanoid; Q63622; -.
KO; K12075; -.
PRO; PR:Q63622; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; ISO:RGD.
GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IBA:GO_Central.
GO; GO:0019900; F:kinase binding; ISO:RGD.
GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
GO; GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB.
GO; GO:0045161; P:neuronal ion channel clustering; IMP:RGD.
GO; GO:0043113; P:receptor clustering; IMP:RGD.
GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
CDD; cd12032; SH3_DLG2; 1.
InterPro; IPR016313; DLG1-like.
InterPro; IPR019590; DLG1_PEST_dom.
InterPro; IPR035759; DLG2_SH3.
InterPro; IPR008145; GK/Ca_channel_bsu.
InterPro; IPR008144; Guanylate_kin-like_dom.
InterPro; IPR020590; Guanylate_kinase_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001478; PDZ.
InterPro; IPR019583; PDZ_assoc.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF00625; Guanylate_kin; 1.
Pfam; PF10608; MAGUK_N_PEST; 2.
Pfam; PF00595; PDZ; 3.
Pfam; PF10600; PDZ_assoc; 1.
Pfam; PF07653; SH3_2; 1.
PIRSF; PIRSF001741; MAGUK_DLGH; 1.
SMART; SM00072; GuKc; 1.
SMART; SM01277; MAGUK_N_PEST; 1.
SMART; SM00228; PDZ; 3.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 2.
SUPFAM; SSF50156; SSF50156; 3.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PROSITE; PS50106; PDZ; 3.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Complete proteome; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
Repeat; SH3 domain; Synapse.
CHAIN 1 852 Disks large homolog 2.
/FTId=PRO_0000094555.
DOMAIN 98 184 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 193 279 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 421 501 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 536 606 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 662 837 Guanylate kinase-like.
{ECO:0000255|PROSITE-ProRule:PRU00100}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000250|UniProtKB:Q91XM9}.
MOD_RES 58 58 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q91XM9}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000250|UniProtKB:Q91XM9}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000250|UniProtKB:Q91XM9}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000250|UniProtKB:Q91XM9}.
MOD_RES 360 360 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 414 414 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 505 505 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q91XM9}.
MOD_RES 528 528 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 553 553 Phosphoserine.
{ECO:0000250|UniProtKB:Q91XM9}.
MOD_RES 732 732 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q91XM9}.
MOD_RES 737 737 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q91XM9}.
LIPID 5 5 S-palmitoyl cysteine.
{ECO:0000269|PubMed:10779526}.
LIPID 7 7 S-palmitoyl cysteine.
{ECO:0000269|PubMed:10779526}.
VAR_SEQ 1 246 Missing (in isoform 5).
{ECO:0000303|PubMed:8922396}.
/FTId=VSP_015525.
VAR_SEQ 1 68 MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPEL
VHVSEKNLSQIENVHGYVLQSHISPLK -> MNAYLTKQHS
CSRGSDGMDAGRGVPTLIRDAHCACGWQRNAQGLGYSSQTM
PSSGPGGPASNRTKLVTLWDSVRKSPHKTSTKGKGNCGERC
ACPHGWFSPAQ (in isoform 4).
{ECO:0000305}.
/FTId=VSP_015526.
VAR_SEQ 1 61 Missing (in isoform 3).
{ECO:0000303|PubMed:8922396}.
/FTId=VSP_015527.
VAR_SEQ 1 13 MFFACYCALRTNV -> MICHCKVACTNNTLSLMFGC (in
isoform 2). {ECO:0000303|PubMed:8922396}.
/FTId=VSP_015528.
VAR_SEQ 62 68 SHISPLK -> MQHAFIP (in isoform 3).
{ECO:0000303|PubMed:8922396}.
/FTId=VSP_015529.
VAR_SEQ 341 392 Missing (in isoform 3).
{ECO:0000303|PubMed:8922396}.
/FTId=VSP_015530.
VAR_SEQ 450 454 Missing (in isoform 6).
{ECO:0000303|PubMed:8625413}.
/FTId=VSP_015531.
VAR_SEQ 626 641 Missing (in isoform 6).
{ECO:0000303|PubMed:8625413}.
/FTId=VSP_015533.
VAR_SEQ 626 641 GDIPGLGDDGYGTKTL -> GSFNDKRKKSFIFSRKFPFYK
NKEQSEQETSDPE (in isoform 7).
{ECO:0000305}.
/FTId=VSP_015532.
MUTAGEN 5 5 C->S: Loss of palmitoylation and
targeting to postsynaptic density.
{ECO:0000269|PubMed:10779526}.
MUTAGEN 7 7 C->S: Loss of palmitoylation and
targeting to postsynaptic density.
{ECO:0000269|PubMed:10779526}.
CONFLICT 181 182 VR -> IL (in Ref. 2; AAC52643).
{ECO:0000305}.
CONFLICT 228 228 I -> M (in Ref. 2; AAC52643).
{ECO:0000305}.
CONFLICT 326 326 R -> K (in Ref. 2; AAC52643).
{ECO:0000305}.
CONFLICT 339 339 D -> E (in Ref. 3; AAB48562).
{ECO:0000305}.
CONFLICT 464 465 GD -> RK (in Ref. 2; AAC52643).
{ECO:0000305}.
CONFLICT 474 474 D -> H (in Ref. 2). {ECO:0000305}.
CONFLICT 476 476 R -> P (in Ref. 2). {ECO:0000305}.
CONFLICT 478 478 A -> D (in Ref. 2). {ECO:0000305}.
CONFLICT 484 486 AAA -> LP (in Ref. 2; AAC52643).
{ECO:0000305}.
CONFLICT 506 506 A -> S (in Ref. 2; AAC52643).
{ECO:0000305}.
CONFLICT 569 569 H -> N (in Ref. 2; AAC52643).
{ECO:0000305}.
CONFLICT 586 586 L -> Q (in Ref. 2; AAC52643).
{ECO:0000305}.
CONFLICT 627 630 DIPG -> TSR (in Ref. 5). {ECO:0000305}.
CONFLICT 639 639 K -> A (in Ref. 3; AAB48562).
{ECO:0000305}.
CONFLICT 726 726 F -> L (in Ref. 1; AAB53243).
{ECO:0000305}.
CONFLICT 733 733 N -> Y (in Ref. 2; AAC52643).
{ECO:0000305}.
CONFLICT 749 749 E -> V (in Ref. 1; AAB53243).
{ECO:0000305}.
CONFLICT 756 756 L -> H (in Ref. 2; AAC52643).
{ECO:0000305}.
CONFLICT 791 792 KR -> NG (in Ref. 2). {ECO:0000305}.
CONFLICT 794 794 T -> M (in Ref. 2). {ECO:0000305}.
STRAND 93 102 {ECO:0000244|PDB:4H11}.
STRAND 109 113 {ECO:0000244|PDB:4H11}.
HELIX 121 123 {ECO:0000244|PDB:4H11}.
STRAND 127 132 {ECO:0000244|PDB:4H11}.
HELIX 137 141 {ECO:0000244|PDB:4H11}.
STRAND 149 153 {ECO:0000244|PDB:4H11}.
HELIX 163 172 {ECO:0000244|PDB:4H11}.
STRAND 175 184 {ECO:0000244|PDB:4H11}.
SEQUENCE 852 AA; 94934 MW; F8D414A8B9CF5B09 CRC64;
MFFACYCALR TNVKKYRYQD EDGPHDHSLP RLTHEVRGPE LVHVSEKNLS QIENVHGYVL
QSHISPLKAS PAPIIVNTDT LDTIPYVNGT EIEYEFEEIT LERGNSGLGF SIAGGTDNPH
IGDDPGIFIT KIIPGGAAAE DGRLRVNDCI LRVNEVDVSE VSHSKAVEAL KEAGSIVRLY
VRRRRPILET VVEIKLFKGP KGLGFSIAGG VGNQHIPGDN SIYVTKIIDG GAAQKDGRLQ
VGDRLLMVNN YSLEEVTHEE AVAILKNTSD VVYLKVGKPT TIYMTDPYGP PDITHSYSPP
MENHLLSGNN GTLEYKTSLP PISPGRYSPI PKHMLVEDDY TRPPEPVYST VNKLCDKPAS
PRHYSPVECD KSFLLSTPYP HYHLGLLPDS DMTSHSQHST ATRQPSVTLQ RAISLEGEPR
KVVLHKGSTG LGFNIVGGED GEGIFVSFIL AGGPADLSGE LQRGDQILSV NGIDLRGASH
EQAAAALKGA GQTVTIIAQY QPEDYARFEA KIHDLREQMM NHSMSSGSGS LRTNQKRSLY
VRAMFDYDKS KDSGLPSQGL SFKYGDILHV INASDDEWWQ ARRVILDGDS EEMGVIPSKR
RVERKERARL KTVKFNAKPG VIDSKGDIPG LGDDGYGTKT LRGQEDLILS YEPVTRQEIN
YTRPVIILGP MKDRINDDLI SEFPDKFGSC VPHTTRPKRD YEVDGRDYHF VISREQMEKD
IQEHKFIEAG QYNDNLYGTS VQSVRFVAER GKHCILDVSG NAIKRLQVAQ LYPIAIFIKP
KSLEPLMEMN KRLTEEQAKK TYDRAIKLEQ EFGEYFTAIV QGDTLEDIYN QCKLVIEEQS
GPFIWIPSKE KL


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EIAAB11405 DAP-5,Discs large homolog 7,Disks large-associated protein 5,Disks large-associated protein DLG7,Dlg7,Dlgap5,Hepatoma up-regulated protein homolog,HURP,Kiaa0008,Mouse,Mus musculus
EIAAB11386 Disks large homolog 3,Dlg3,Dlgh3,Mouse,Mus musculus,SAP102,SAP-102,Synapse-associated protein 102
EIAAB11379 Disks large homolog 1,Dlg1,Dlgh1,Rat,Rattus norvegicus,SAP97,SAP-97,Synapse-associated protein 97
EIAAB11381 Disks large homolog 1,DLG1,hDlg,Homo sapiens,Human,SAP97,SAP-97,Synapse-associated protein 97
EIAAB11404 DAP-5,Discs large homolog 7,Disks large-associated protein 5,Disks large-associated protein DLG7,DLG7,DLGAP5,Hepatoma up-regulated protein,Homo sapiens,Human,HURP,KIAA0008
EIAAB11387 Disks large homolog 3,DLG3,Homo sapiens,Human,KIAA1232,Neuroendocrine-DLG,SAP102,SAP-102,Synapse-associated protein 102,XLMR
EIAAB11391 Discs large protein P-dlg,Disks large homolog 5,DLG5,Homo sapiens,Human,KIAA0583,PDLG,Placenta and prostate DLG
EIAAB33773 43 kDa postsynaptic protein,43 kDa receptor-associated protein of the synapse,Acetylcholine receptor-associated 43 kDa protein,Homo sapiens,Human,RAPSN,RAPsyn,RING finger protein 205,RNF205
EIAAB33771 43 kDa postsynaptic protein,43 kDa receptor-associated protein of the synapse,Acetylcholine receptor-associated 43 kDa protein,Mouse,Mus musculus,Rapsn,RAPsyn
EIAAB33772 43 kDa postsynaptic protein,43 kDa receptor-associated protein of the synapse,Acetylcholine receptor-associated 43 kDa protein,Chicken,Gallus gallus,RAPSN,RAPsyn
GWB-E5E9C0 Anti- DLG2 (discs. large homolog 2. chapsyn-110 (Drosophila)) Antibody
EIAAB11392 DAP-1,Disks large-associated protein 1,Dlgap1,Guanylate kinase-associated protein,Kiaa4162,Mouse,Mus musculus,PSD-95_SAP90-binding protein 1,SAP90_PSD-95-associated protein 1,SAPAP1
EIAAB11394 DAP-1,Disks large-associated protein 1,Dlgap1,Gkap,Guanylate kinase-associated protein,PSD-95_SAP90-binding protein 1,Rat,Rattus norvegicus,rGKAP,SAP90_PSD-95-associated protein 1,SAPAP1
EIAAB11393 DAP1,DAP-1,Disks large-associated protein 1,DLGAP1,GKAP,Guanylate kinase-associated protein,hGKAP,Homo sapiens,Human,PSD-95_SAP90-binding protein 1,SAP90_PSD-95-associated protein 1,SAPAP1
SMC-325D CHAPSYN-110 (PSD93) MAGUK, S18-30 Monoclonals AntibodiesS18-30 Fusion protein amino acids 1-852 of rat Chapsyn-110; accession number Q63622 100ug
EIAAB11399 Dap3,DAP-3,Disks large-associated protein 3,Dlgap3,Mouse,Mus musculus,PSD-95_SAP90-binding protein 3,SAP90_PSD-95-associated protein 3,SAPAP3


 

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