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 1 (Shank1) (GKAP/SAPAP-interacting protein) (SPANK-1) (Somatostatin receptor-interacting protein) (SSTR-interacting protein) (SSTRIP) (Synamon)

 SHAN1_RAT               Reviewed;        2167 AA.
Q9WV48; Q9QZZ8; Q9WU13; Q9WUE8;
26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 168.
RecName: Full=SH3 and multiple ankyrin repeat domains protein 1;
Short=Shank1;
AltName: Full=GKAP/SAPAP-interacting protein;
AltName: Full=SPANK-1;
AltName: Full=Somatostatin receptor-interacting protein;
Short=SSTR-interacting protein;
Short=SSTRIP;
AltName: Full=Synamon;
Name=Shank1;
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] (ISOFORMS 1 AND 3), AND INTERACTION WITH
DLGAP1 AND DLG4.
TISSUE=Brain;
PubMed=10488079; DOI=10.1074/jbc.274.39.27463;
Yao I., Hata Y., Hirao K., Deguchi M., Ide N., Takeuchi M., Takai Y.;
"Synamon, a novel neuronal protein interacting with synapse-associated
protein 90/postsynaptic density-95-associated protein.";
J. Biol. Chem. 274:27463-27466(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND INTERACTION WITH DLGAP1.
STRAIN=Sprague-Dawley;
PubMed=10433268; DOI=10.1016/S0896-6273(00)80809-0;
Naisbitt S., Kim E., Tu J.C., Xiao B., Sala C., Valtschanoff J.,
Weinberg R.J., Worley P.F., Sheng M.;
"Shank, a novel family of postsynaptic density proteins that binds to
the NMDA receptor/PSD-95/GKAP complex and cortactin.";
Neuron 23:569-582(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10958799; DOI=10.1074/jbc.M006448200;
Tobaben S., Suedhof T.C., Stahl B.;
"The G protein-coupled receptor CL1 interacts directly with proteins
of the Shank family.";
J. Biol. Chem. 275:36204-36210(2000).
[4]
PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3; 4 AND 5), AND
DEVELOPMENTAL STAGE.
TISSUE=Brain;
PubMed=10506216; DOI=10.1074/jbc.274.41.29510;
Lim S., Naisbitt S., Yoon J., Hwang J.-I., Suh P.-G., Sheng M.,
Kim E.;
"Characterization of the shank family of synaptic proteins. Multiple
genes, alternative splicing, and differential expression in brain and
development.";
J. Biol. Chem. 274:29510-29518(1999).
[5]
PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 4).
TISSUE=Brain;
PubMed=10551867; DOI=10.1074/jbc.274.46.32997;
Zitzer H., Hoenck H.-H., Baechner D., Richter D., Kreienkamp H.-J.;
"Somatostatin receptor interacting protein defines a novel family of
multidomain proteins present in human and rodent brain.";
J. Biol. Chem. 274:32997-33001(1999).
[6]
INTERACTION WITH HOMER1, AND SUBCELLULAR LOCATION.
PubMed=10433269; DOI=10.1016/S0896-6273(00)80810-7;
Tu J.C., Xiao B., Naisbitt S., Yuan J.P., Petralia R.S., Brakeman P.,
Doan A., Aakalu V.K., Lanahan A.A., Sheng M., Worley P.F.;
"Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of
postsynaptic density proteins.";
Neuron 23:583-592(1999).
[7]
INTERACTION WITH SPTAN1.
PubMed=11509555; DOI=10.1074/jbc.M102454200;
Bockers T.M., Mameza M.G., Kreutz M.R., Bockmann J., Weise C.,
Buck F., Richter D., Gundelfinger E.D., Kreienkamp H.-J.;
"Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the
multidomain Shank protein family interact with the cytoskeletal
protein alpha-fodrin.";
J. Biol. Chem. 276:40104-40112(2001).
[8]
INTERACTION WITH SHARPIN.
PubMed=11178875; DOI=10.1006/mcne.2000.0940;
Lim S., Sala C., Yoon J., Park S., Kuroda S., Sheng M., Kim E.;
"Sharpin, a novel postsynaptic density protein that directly interacts
with the shank family of proteins.";
Mol. Cell. Neurosci. 17:385-397(2001).
[9]
FUNCTION.
PubMed=11498055; DOI=10.1016/S0896-6273(01)00339-7;
Sala C., Piech V., Wilson N.R., Passafaro M., Liu G., Sheng M.;
"Regulation of dendritic spine morphology and synaptic function by
Shank and Homer.";
Neuron 31:115-130(2001).
[10]
REVIEW.
PubMed=10806096;
Sheng M., Kim E.;
"The Shank family of scaffold proteins.";
J. Cell Sci. 113:1851-1856(2000).
[11]
INTERACTION WITH IGSF9.
PubMed=15340156; DOI=10.1073/pnas.0405371101;
Shi S.-H., Cheng T., Jan L.Y., Jan Y.-N.;
"The immunoglobulin family member dendrite arborization and synapse
maturation 1 (Dasm1) controls excitatory synapse maturation.";
Proc. Natl. Acad. Sci. U.S.A. 101:13346-13351(2004).
[12]
FUNCTION.
PubMed=18287537; DOI=10.1091/mbc.E07-08-0802;
Arstikaitis P., Gauthier-Campbell C., Carolina Gutierrez Herrera R.,
Huang K., Levinson J.N., Murphy T.H., Kilimann M.W., Sala C.,
Colicos M.A., El-Husseini A.;
"Paralemmin-1, a modulator of filopodia induction is required for
spine maturation.";
Mol. Biol. Cell 19:2026-2038(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540; SER-898; SER-1291
AND SER-1442, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638 AND
SER-641 (ISOFORM 3), 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).
[14]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 654-762 IN COMPLEX WITH
DLGAP1, AND SUBUNIT.
PubMed=12954649; DOI=10.1074/jbc.M306919200;
Im Y.J., Lee J.H., Park S.H., Park S.J., Rho S.-H., Kang G.B., Kim E.,
Eom S.H.;
"Crystal structure of the Shank PDZ-ligand complex reveals a class I
PDZ interaction and a novel PDZ-PDZ dimerization.";
J. Biol. Chem. 278:48099-48104(2003).
-!- 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. Plays a
role in the structural and functional organization of the
dendritic spine and synaptic junction. Overexpression promotes
maturation of dendritic spines and the enlargement of spine heads
via its ability to recruit Homer to postsynaptic sites, and
enhances presynaptic function. {ECO:0000269|PubMed:11498055,
ECO:0000269|PubMed:18287537}.
-!- SUBUNIT: May homomultimerize via its SAM domain. Interacts with
the C-terminus of SSTR2 via the PDZ domain. Interacts with
SHARPIN, SPTAN1, HOMER1 and DLGAP1/GKAP. Part of a complex with
DLG4/PSD-95 and DLGAP1/GKAP. Interacts with BAIAP2 (By
similarity). Interacts with IGSF9. {ECO:0000250,
ECO:0000269|PubMed:10433268, ECO:0000269|PubMed:10433269,
ECO:0000269|PubMed:10488079, ECO:0000269|PubMed:11178875,
ECO:0000269|PubMed:11509555, ECO:0000269|PubMed:12954649,
ECO:0000269|PubMed:15340156}.
-!- INTERACTION:
Q9ES28-2:Arhgef7 (xeno); NbExp=6; IntAct=EBI-80909, EBI-8620514;
P31016:Dlg4; NbExp=3; IntAct=EBI-80909, EBI-375655;
P97836:Dlgap1; NbExp=6; IntAct=EBI-80909, EBI-80901;
P97836-5:Dlgap1; NbExp=2; IntAct=EBI-80909, EBI-6269434;
Q9Z214-2:Homer1; NbExp=4; IntAct=EBI-80909, EBI-2338999;
Q9EQL9:Sharpin; NbExp=7; IntAct=EBI-80909, EBI-1394695;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10433269}.
Cell junction, synapse {ECO:0000269|PubMed:10433269}. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000269|PubMed:10433269}. Note=Colocalizes with
alpha-latrotoxin receptor 1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9WV48-1; Sequence=Displayed;
Name=2;
IsoId=Q9WV48-2; Sequence=VSP_006072, VSP_006073;
Name=3;
IsoId=Q9WV48-3; Sequence=VSP_006074;
Note=Contains a phosphoserine at position 638. Contains a
phosphoserine at position 641. {ECO:0000244|PubMed:22673903};
Name=4; Synonyms=A;
IsoId=Q9WV48-4; Sequence=VSP_006075;
Name=5;
IsoId=Q9WV48-5; Sequence=VSP_006076, VSP_006077;
-!- TISSUE SPECIFICITY: Expressed only in brain (neuropil of cortex,
CA1 region hippocampus and molecular layer of cerebellum).
-!- DEVELOPMENTAL STAGE: Expression increases from low levels at birth
to high levels at 3-4 weeks before dropping slightly in adulthood.
Expressed in the cortex and the molecular layer of the cerebellum
at postnatal day 7. Isoform 2 expression does not change during
development of both cortex and cerebellum. Isoform 4 expression
decreases significantly during development of cortex but not
cerebellum. {ECO:0000269|PubMed:10506216}.
-!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD29417.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAF02498.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF102855; AAD04569.2; -; mRNA.
EMBL; AF131951; AAD29417.1; ALT_INIT; mRNA.
EMBL; AF159046; AAD42975.1; -; mRNA.
EMBL; AF141904; AAF02498.1; ALT_INIT; mRNA.
RefSeq; NP_113939.2; NM_031751.3. [Q9WV48-1]
RefSeq; XP_017445247.1; XM_017589758.1. [Q9WV48-1]
RefSeq; XP_017445248.1; XM_017589759.1. [Q9WV48-4]
RefSeq; XP_017445249.1; XM_017589760.1. [Q9WV48-3]
RefSeq; XP_017445250.1; XM_017589761.1. [Q9WV48-5]
UniGene; Rn.225968; -.
PDB; 1Q3O; X-ray; 1.80 A; A/B=654-762.
PDB; 1Q3P; X-ray; 2.25 A; A/B=654-762.
PDB; 3L4F; X-ray; 2.80 A; D=653-765.
PDB; 3QJM; X-ray; 2.31 A; A/B=654-768.
PDB; 3QJN; X-ray; 2.71 A; A/B/C/D/E/F/G/H=654-768.
PDBsum; 1Q3O; -.
PDBsum; 1Q3P; -.
PDBsum; 3L4F; -.
PDBsum; 3QJM; -.
PDBsum; 3QJN; -.
ProteinModelPortal; Q9WV48; -.
SMR; Q9WV48; -.
BioGrid; 249365; 5.
CORUM; Q9WV48; -.
ELM; Q9WV48; -.
IntAct; Q9WV48; 17.
MINT; MINT-101286; -.
STRING; 10116.ENSRNOP00000026100; -.
iPTMnet; Q9WV48; -.
PhosphoSitePlus; Q9WV48; -.
PaxDb; Q9WV48; -.
PRIDE; Q9WV48; -.
Ensembl; ENSRNOT00000026100; ENSRNOP00000026100; ENSRNOG00000019207. [Q9WV48-1]
Ensembl; ENSRNOT00000044257; ENSRNOP00000039860; ENSRNOG00000019207. [Q9WV48-3]
Ensembl; ENSRNOT00000092327; ENSRNOP00000075838; ENSRNOG00000019207. [Q9WV48-4]
GeneID; 78957; -.
KEGG; rno:78957; -.
UCSC; RGD:621011; rat. [Q9WV48-1]
CTD; 50944; -.
RGD; 621011; Shank1.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4375; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00510000046474; -.
HOGENOM; HOG000293276; -.
HOVERGEN; HBG079186; -.
InParanoid; Q9WV48; -.
KO; K15009; -.
OMA; DHPLETI; -.
OrthoDB; EOG091G00OW; -.
PhylomeDB; Q9WV48; -.
Reactome; R-RNO-6794361; Neurexins and neuroligins.
EvolutionaryTrace; Q9WV48; -.
PRO; PR:Q9WV48; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000019207; -.
Genevisible; Q9WV48; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0043197; C:dendritic spine; IDA:BHF-UCL.
GO; GO:0060076; C:excitatory synapse; ISS:BHF-UCL.
GO; GO:0005622; C:intracellular; NAS:UniProtKB.
GO; GO:0008328; C:ionotropic glutamate receptor complex; IEA:Ensembl.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043005; C:neuron projection; 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; IDA:RGD.
GO; GO:0045202; C:synapse; IDA:BHF-UCL.
GO; GO:0071532; F:ankyrin repeat binding; IPI:BHF-UCL.
GO; GO:0030160; F:GKAP/Homer scaffold activity; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0030159; F:receptor signaling complex scaffold activity; IDA:RGD.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
GO; GO:0031877; F:somatostatin receptor binding; IPI:UniProtKB.
GO; GO:0030534; P:adult behavior; ISO:RGD.
GO; GO:0008306; P:associative learning; ISS:BHF-UCL.
GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; NAS:UniProtKB.
GO; GO:0060997; P:dendritic spine morphogenesis; ISS:BHF-UCL.
GO; GO:0050894; P:determination of affect; ISO:RGD.
GO; GO:0046959; P:habituation; ISS:BHF-UCL.
GO; GO:0007616; P:long-term memory; ISS:BHF-UCL.
GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISS:BHF-UCL.
GO; GO:0050885; P:neuromuscular process controlling balance; ISS:BHF-UCL.
GO; GO:0042048; P:olfactory behavior; ISS:BHF-UCL.
GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:UniProtKB.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
GO; GO:0006461; P:protein complex assembly; IDA:BHF-UCL.
GO; GO:0035418; P:protein localization to synapse; ISS:BHF-UCL.
GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL.
GO; GO:0060013; P:righting reflex; ISS:BHF-UCL.
GO; GO:0035176; P:social behavior; ISO:RGD.
GO; GO:0060074; P:synapse maturation; IDA:UniProtKB.
GO; GO:0071625; P:vocalization behavior; ISO:RGD.
CDD; cd00204; ANK; 2.
CDD; cd11982; SH3_Shank1; 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.
InterPro; IPR035735; Shank1_SH3.
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; 6.
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; 3.
PROSITE; PS50106; PDZ; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; Cell junction;
Cell membrane; Complete proteome; Cytoplasm; Differentiation;
Membrane; Methylation; Neurogenesis; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Repeat; SH3 domain;
Synapse.
CHAIN 1 2167 SH3 and multiple ankyrin repeat domains
protein 1.
/FTId=PRO_0000174672.
REPEAT 195 210 ANK 1.
REPEAT 212 245 ANK 2.
REPEAT 246 278 ANK 3.
REPEAT 279 312 ANK 4.
REPEAT 313 345 ANK 5.
REPEAT 346 378 ANK 6.
REPEAT 379 395 ANK 7.
DOMAIN 554 613 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 663 757 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 2104 2167 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
COMPBIAS 929 932 Poly-Pro.
COMPBIAS 1010 1015 Poly-His.
COMPBIAS 1022 1027 Poly-His.
COMPBIAS 1194 1199 Poly-Gly.
COMPBIAS 1850 1860 Poly-Pro.
MOD_RES 43 43 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 186 186 Phosphotyrosine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 540 540 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 544 544 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 791 791 Phosphoserine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 898 898 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 958 958 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 1059 1059 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 1098 1098 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 1109 1109 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 1257 1257 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 1291 1291 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1429 1429 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 1442 1442 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1901 1901 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 2022 2022 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 2042 2042 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
MOD_RES 2080 2080 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:D3YZU1}.
VAR_SEQ 1 614 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_006072.
VAR_SEQ 615 654 SQEGRQESRSDKAKRLFRHYTVGSYDSFDAPSLIDGIDSG
-> MALSAVGGGPGGGALPQPPPALSSSWPALGPRRRSVWY
IY (in isoform 2). {ECO:0000305}.
/FTId=VSP_006073.
VAR_SEQ 646 654 Missing (in isoform 3).
{ECO:0000303|PubMed:10488079}.
/FTId=VSP_006074.
VAR_SEQ 797 804 Missing (in isoform 4).
{ECO:0000303|PubMed:10433268}.
/FTId=VSP_006075.
VAR_SEQ 1930 1943 LSEDSQTSLLSKPS -> QYRIVVKSSDFGDF (in
isoform 5). {ECO:0000305}.
/FTId=VSP_006076.
VAR_SEQ 1944 2167 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_006077.
CONFLICT 1141 1141 S -> T (in Ref. 1; AAD04569).
{ECO:0000305}.
CONFLICT 1174 1174 S -> N (in Ref. 2; AAD29417).
{ECO:0000305}.
CONFLICT 1246 1246 R -> K (in Ref. 1; AAD04569).
{ECO:0000305}.
CONFLICT 1323 1323 A -> T (in Ref. 1; AAD04569).
{ECO:0000305}.
CONFLICT 1331 1331 S -> D (in Ref. 1; AAD04569).
{ECO:0000305}.
CONFLICT 1726 1726 S -> N (in Ref. 2; AAD29417).
{ECO:0000305}.
STRAND 657 667 {ECO:0000244|PDB:1Q3O}.
STRAND 670 672 {ECO:0000244|PDB:1Q3P}.
STRAND 675 682 {ECO:0000244|PDB:1Q3O}.
STRAND 694 696 {ECO:0000244|PDB:1Q3P}.
STRAND 698 705 {ECO:0000244|PDB:1Q3O}.
HELIX 710 713 {ECO:0000244|PDB:1Q3O}.
STRAND 721 725 {ECO:0000244|PDB:1Q3O}.
HELIX 735 744 {ECO:0000244|PDB:1Q3O}.
TURN 745 747 {ECO:0000244|PDB:1Q3O}.
STRAND 748 757 {ECO:0000244|PDB:1Q3O}.
SEQUENCE 2167 AA; 226335 MW; 3F478B5A7B18BA86 CRC64;
MTHSPATSED EERHSASECP EGGSESDSSP DGPGRGPQGT RGRGSGAPGN LASTRGLQGR
SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF
QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL
KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI
DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL
LYNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKE
TCARILLYRG ANKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR
RGPPGAGLTV PPALLRANSD TSMALPDWMV FSAPGASSSG TPGPTSGPQG QSQPSAPSTK
LSSGTLRSAS SPRGARARSP SRGRHPEDAK RQPRGRPSSS GTPRDGPAGG TGGSGGPGGS
LGSRGRRRKL YSAVPGRSFM AVKSYQAQGE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV
GWFPSDCLEE VANRSQEGRQ ESRSDKAKRL FRHYTVGSYD SFDAPSLIDG IDSGSDYIIK
EKTVLLQKKD SEGFGFVLRG AKAQTPIEEF TPTPAFPALQ YLESVDEGGV AWRAGLRMGD
FLIEVNGQNV VKVGHRQVVN MIRQGGNTLM VKVVMVTRHP DMDEAVHKKA SQQAKRLPPP
AISLRSKSMT SELEEMVSPW KKKIEYEQQP AAVPSMEKKR TVYQMALNKL DEILAAAQQT
ISASESPGPG GLASLGKHRP KGFFATESSF DPHHRSQPSY DRPSFLPPGP GLMLRQKSIG
AAEDDRPYLA PPAMKFSRSL SVPGSEDIPP PPTTSPPEPP YSTPPAPSSS GRLTPSPRGG
PFNPSSGGPL PASSPSSFDG PSPPDTRGGG REKSLYHSAA LPPAHHHPPH HHHHHAPPPQ
PHHHHAHPPH PPEMETGGSP DDPPPRLALG PQPSLRGWRG GGPSPTSGAP SPSHHSSSGG
SSGPTQAPAL RYFQLPPRAA SAAMYVPARS GRGRKGPLVK QTKVEGEPQK GSIPSASSPT
SPALPRSEPP PAGPSEKNSI PIPTIIIKAP STSSSGRSSQ GSSTEAEPPT QPDGAGGGGS
SPSPAPATSP VPPSPSPVPT PASPSGPATL DFTSQFGAAL VGAARREGGW QNEARRRSTL
FLSTDAGDED GGDSGLGPGG PPGPRLRHSK SIDEGMFSAE PYLRLESGGS SGGYGAYAAG
SRAYGGSGSS SAFTSFLPPR PLVHPLTGKA LDPASPLGLA LAARERALKE SSEGGGTPQP
PPRPPSPRYD APPPTLHHHS PHSPHSPHAR HEPVLRLWGD PARRELGYRA GLGSQEKALT
ASPPAARRSL LHRLPPTAPG VGPLLLQLGP EPPTPHPGVS KAWRTAAPEE PERLPLHVRF
LENCQARPPP AGTRGSSTED GPGVPPPSPR RVLPTSPTSP RGNEENGLPL LVLPPPAPSV
DVDDGEFLFA EPLPPPLEFS NSFEKPESPL TPGPPHPLPD PPSPATPLPA APPPAVAAAP
PTLDSTASSL TSYDSEVATL TQGAPAAPGD PPAPGPPAPA APAPPAPQPG PDPPPGTDSG
IEEVDSRSSS DHPLETISSA STLSSLSAEG GGNTGGVAGG GAGVASGTEL LDTYVAYLDG
QAFGGSGTPG PPYPPQLMTP SKLRGRALGT SGNLRPGPSG GLRDPVTPTS PTVSVTGAGT
DGLLALSACP GPSTAGVAGG PVAVEPEVPP VPLPAASSLP RKLLPWEEGP GPPPPPLPGP
LSQPQASALA TVKASIISEL SSKLQQFGGS STAGGALPWA RGGSGGSTDS HHGGASYIPE
RTSSLQRQRL SEDSQTSLLS KPSSSIFQNW PKPPLPPLPT GSGVSSSTAA APGATSPSAS
SASASTRHLQ GVEFEMRPPL LRRAPSPSLL PASDHKVSPA PRPSSLPILP SGPIYPGLFD
IRSSPTGGAG GSTDPFAPVF VPPHPGISGG LGGALSGASR SLSPTRLLSL PPDKPFGAKP
LGFWTKFDVA DWLEWLGLSE HRAQFLDHEI DGSHLPALTK EDYVDLGVTR VGHRMNIDRA
LKFFLER


Related products :

Catalog number Product name Quantity
EIAAB38255 GKAP_SAPAP-interacting protein,Rat,Rattus norvegicus,SH3 and multiple ankyrin repeat domains protein 1,Shank1,Shank1,Somatostatin receptor-interacting protein,SPANK-1,SSTR-interacting protein,SSTRIP,S
EIAAB38256 Homo sapiens,Human,SH3 and multiple ankyrin repeat domains protein 1,Shank1,SHANK1,Somatostatin receptor-interacting protein,SSTR-interacting protein,SSTRIP
18-001-30036 SH3 and multiple ankyrin repeat domains protein 1 - Shank1; Somatostatin receptor-interacting protein; SSTR-interacting protein; SSTRIP Polyclonal 0.1 mg
18-001-30037 SH3 and multiple ankyrin repeat domains protein 1 - Shank1; Somatostatin receptor-interacting protein; SSTR-interacting protein; SSTRIP Polyclonal 0.1 mg
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
EIAAB31218 Homo sapiens,hPIP1,Human,p21-activated protein kinase-interacting protein 1,PAK_PLC-interacting protein 1,PAK1-interacting protein 1,PAK1IP1,PIP1,WD repeat-containing protein 84,WDR84
EIAAB34872 ANKRD3,Ankyrin repeat domain-containing protein 3,DIK,Homo sapiens,Human,PKC-delta-interacting protein kinase,Receptor-interacting serine_threonine-protein kinase 4,RIPK4
EIAAB07420 Cdc42-interacting protein 4,CIP4,Homo sapiens,hSTP,Human,Protein Felic,Salt tolerant protein,STOT,STP,Thyroid receptor-interacting protein 10,TR-interacting protein 10,TRIP10,TRIP-10
EIAAB27017 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Homo sapiens,Human,NFATC2-interacting protein,NFATC2IP,NIP45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB27018 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Mouse,Mus musculus,NFATC2-interacting protein,Nfatc2ip,Nip45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB07421 Cdc42-interacting protein 4,Cip4,Rat,Rattus norvegicus,Salt tolerant protein,Stp,Thyroid receptor-interacting protein 10,TR-interacting protein 10,Trip10,TRIP-10
EIAAB44012 Homo sapiens,Human,OIP1,OIP-1,Opa-interacting protein 1,Thyroid receptor-interacting protein 6,TR-interacting protein 6,TRIP6,TRIP-6,ZRP-1,Zyxin-related protein 1
EIAAB31033 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Miz1,Mouse,Msx-interacting zinc finger protein,Mus musculus,Pias2,Piasx,Protein inhibitor of act
EIAAB31032 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Miz1,Msx-interacting-zinc finger protein,Pias2,Piasx,Protein inhibitor of activated STAT x,Prote
EIAAB38254 Mouse,Mus musculus,SH3 and multiple ankyrin repeat domains protein 1,Shank1,Shank1
EIAAB07419 Cdc42-interacting protein 4,Cip4,Mouse,Mus musculus,Thyroid receptor-interacting protein 10,TR-interacting protein 10,Trip10,TRIP-10
EIAAB39347 Mouse,Mus musculus,Spata24,Spermatogenesis-associated protein 24,TATA-binding protein-like factor-interacting protein,Testis protein T6441 homolog,Tipt,Tipt2,TLF-interacting protein,TRF2-interacting p
EIAAB46349 Homo sapiens,Human,Protein PRPL-2,WAS_WASL-interacting protein family member 1,WASP-interacting protein,WASPIP,WIP,WIPF1,Wiskott-Aldrich syndrome protein-interacting protein
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
EIAAB39604 54 kDa VacA-interacting protein,54 kDa vimentin-interacting protein,90 kDa SH3 protein interacting with Nck,AF3p21,AF3P21,Dia-interacting protein 1,Diaphanous protein-interacting protein,DIP-1,Homo sa
EIAAB39603 54 kDa VacA-interacting protein,90 kDa N-WASP-interacting protein,90 kDa SH3 protein interacting with Nck,Mouse,Mus musculus,NCK-interacting protein with SH3 domain,Nckipsd,N-WASP-binding protein,SH3
EIAAB46351 Rat,Rattus norvegicus,WAS_WASL-interacting protein family member 1,WASP-interacting protein,Waspip,Wip,Wipf1,Wiskott-Aldrich syndrome protein-interacting protein
EIAAB30253 Aip1,ALG-2-interacting protein 1,ALG-2-interacting protein X,Alix,E2F1-inducible protein,Eig2,Mouse,Mus musculus,Pdcd6ip,Programmed cell death 6-interacting protein


 

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