Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Multiple PDZ domain protein (Multi-PDZ domain protein 1)

 MPDZ_MOUSE              Reviewed;        2055 AA.
Q8VBX6; B7ZNA1; O08783; Q6P7U4; Q80ZY8; Q8BKJ1; Q8C0H8; Q8VBV5;
Q8VBY0; Q9Z1K3;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
25-OCT-2017, entry version 137.
RecName: Full=Multiple PDZ domain protein;
AltName: Full=Multi-PDZ domain protein 1;
Name=Mpdz; Synonyms=Mupp1;
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).
STRAIN=C57BL/6 X CBA; TISSUE=Brain;
PubMed=10395806; DOI=10.1006/geno.1999.5853;
Simpson E.H., Suffolk R., Jackson I.J.;
"Identification, sequence, and mapping of mouse multiple PDZ domain
protein gene, Mpdz.";
Genomics 59:102-104(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-541; VAL-691;
ARG-801; ALA-859; ASN-880; SER-914; VAL-977; MET-1338; ASN-1433 AND
ASN-1767.
STRAIN=129/J, A/HeJ, AKR/J, BALB/cJ, C3H/J, C57BL/6J, C57BR/cdJ,
C57L/J, CBA/J, CE/J, DBA/2J, DBA1/J, PL/J, SJL/J, SWR/J, WSP1, WSP2,
WSR1, and WSR2; TISSUE=Brain;
PubMed=11978849;
Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.;
"Congenic mapping of alcohol and pentobarbital withdrawal liability
loci to a <1 centimorgan interval of murine chromosome 4:
identification of Mpdz as a candidate gene.";
J. Neurosci. 22:3730-3738(2002).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Brain, Kidney, and Mammary tumor;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1532-2055 (ISOFORM 4).
TISSUE=Pancreas;
PubMed=9192623; DOI=10.1073/pnas.94.13.6670;
Lee S.S., Weiss R.S., Javier R.T.;
"Binding of human virus oncoproteins to hDlg/SAP97, a mammalian
homolog of the Drosophila discs large tumor suppressor protein.";
Proc. Natl. Acad. Sci. U.S.A. 94:6670-6675(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-62 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Spinal ganglion, and Testis;
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).
[7]
INTERACTION WITH KIT, AND TISSUE SPECIFICITY.
PubMed=11018522; DOI=10.1016/S0014-5793(00)02036-6;
Mancini A., Koch A., Stefan M., Niemann H., Tamura T.;
"The direct association of the multiple PDZ domain containing proteins
(MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine
kinase activity.";
FEBS Lett. 482:54-58(2000).
[8]
INTERACTION WITH NG2.
PubMed=10967549;
DOI=10.1002/1097-4644(20001101)79:2<213::AID-JCB50>3.0.CO;2-G;
Barritt D.S., Pearn M.T., Zisch A.H., Lee S.S., Javier R.T.,
Pasquale E.B., Stallcup W.B.;
"The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the
membrane-spanning proteoglycan NG2.";
J. Cell. Biochem. 79:213-224(2000).
[9]
INTERACTION WITH ADENOVIRUS TYPE 9 E4-ORF1 PROTEIN.
PubMed=11000240; DOI=10.1128/JVI.74.20.9680-9693.2000;
Lee S.S., Glaunsinger B., Mantovani F., Banks L., Javier R.T.;
"Multi-PDZ domain protein MUPP1 is a cellular target for both
adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6
oncoproteins.";
J. Virol. 74:9680-9693(2000).
[10]
INTERACTION WITH CLDN1 AND F11R, DOMAINS, AND SUBCELLULAR LOCATION.
PubMed=11689568; DOI=10.1074/jbc.M109005200;
Hamazaki Y., Itoh M., Sasaki H., Furuse M., Tsukita S.;
"Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions
through its possible interaction with claudin-1 and junctional
adhesion molecule.";
J. Biol. Chem. 277:455-461(2002).
[11]
SUBCELLULAR LOCATION.
PubMed=12403818; DOI=10.1083/jcb.200207050;
Poliak S., Matlis S., Ullmer C., Scherer S.S., Peles E.;
"Distinct claudins and associated PDZ proteins form different
autotypic tight junctions in myelinating Schwann cells.";
J. Cell Biol. 159:361-372(2002).
[12]
TISSUE SPECIFICITY.
PubMed=12706259; DOI=10.1016/S0006-8993(03)02338-2;
Sitek B., Poschmann G., Schmidtke K., Ullmer C., Maskri L.,
Andriske M., Stichel C.C., Zhu X.-R., Luebbert H.;
"Expression of MUPP1 protein in mouse brain.";
Brain Res. 970:178-187(2003).
[13]
INTERACTION WITH DLL1.
PubMed=15509766; DOI=10.1242/dev.01417;
Wright G.J., Leslie J.D., Ariza-McNaughton L., Lewis J.;
"Delta proteins and MAGI proteins: an interaction of Notch ligands
with intracellular scaffolding molecules and its significance for
zebrafish development.";
Development 131:5659-5669(2004).
[14]
INTERACTION WITH CXADR, AND DOMAIN.
PubMed=15364909; DOI=10.1074/jbc.M409061200;
Coyne C.B., Voelker T., Pichla S.L., Bergelson J.M.;
"The coxsackievirus and adenovirus receptor interacts with the multi-
PDZ domain protein-1 (MUPP-1) within the tight junction.";
J. Biol. Chem. 279:48079-48084(2004).
[15]
INTERACTION WITH CRB1; MPP5 AND MPP4, AND SUBCELLULAR LOCATION.
PubMed=15316081; DOI=10.1242/jcs.01301;
van de Pavert S.A., Kantardzhieva A., Malysheva A., Meuleman J.,
Versteeg I., Levelt C., Klooster J., Geiger S., Seeliger M.W.,
Rashbass P., Le Bivic A., Wijnholds J.;
"Crumbs homologue 1 is required for maintenance of photoreceptor cell
polarization and adhesion during light exposure.";
J. Cell Sci. 117:4169-4177(2004).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[17]
INTERACTION WITH FAT4.
PubMed=19506035; DOI=10.1083/jcb.200811030;
Ishiuchi T., Misaki K., Yonemura S., Takeichi M., Tanoue T.;
"Mammalian Fat and Dachsous cadherins regulate apical membrane
organization in the embryonic cerebral cortex.";
J. Cell Biol. 185:959-967(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, and Lung;
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).
[19]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1158, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Interacts with HTR2C and provokes its clustering at the
cell surface. Member of the NMDAR signaling complex that may play
a role in control of AMPAR potentiation and synaptic plasticity in
excitatory synapses (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with CLDN5, DLG4, GRIN1, SYNGAP1, CAMK2A and
CAMK2B, HTR2A, HTR2B, HTR2C, PLEKHA1/TAPP1 and PLEKHA2/TAPP2 (By
similarity). Interacts with F11R/JAM, CLDN1, NG2, CXADR, CRB1,
MPP4 and MPP5. Interacts with FAT4 (via cytoplasmic domain).
Interacts with the adenovirus type 9 E4-ORF1 oncoprotein.
Interacts with DLL1 (PubMed:15509766). {ECO:0000250,
ECO:0000269|PubMed:10967549, ECO:0000269|PubMed:11000240,
ECO:0000269|PubMed:11018522, ECO:0000269|PubMed:11689568,
ECO:0000269|PubMed:15316081, ECO:0000269|PubMed:15364909,
ECO:0000269|PubMed:15509766, ECO:0000269|PubMed:19506035}.
-!- INTERACTION:
O88551:Cldn1; NbExp=2; IntAct=EBI-8026435, EBI-7158428;
P10721:KIT (xeno); NbExp=4; IntAct=EBI-8026435, EBI-1379503;
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
Cytoplasmic side. Apical cell membrane; Peripheral membrane
protein; Cytoplasmic side. Cell junction, synapse, postsynaptic
cell membrane, postsynaptic density. Cell projection, dendrite.
Cell junction, tight junction {ECO:0000250}. Cell junction,
synapse. Cell junction, synapse, synaptosome {ECO:0000250}.
Note=Colocalizes with HTR2C on the apical membrane of epithelial
choroid plexus cells. Highly enriched in postsynaptic densities
(PSD). Localized to punctae on dendrites of hippocampal neurons
and colocalizes with the synaptic marker DLG4. Enriched at the
tight junctions of epithelial cells. Association to the tight
junctions depends on CXADR (By similarity). In the retina,
localizes to the sub-apical region adjacent to the adherens
junction complex at the outer limiting membrane. Localized mainly
in the Schmidt-Lanterman incisures of myelinating Schwann cells.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8VBX6-1; Sequence=Displayed;
Name=2;
IsoId=Q8VBX6-2; Sequence=VSP_014201;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8VBX6-3; Sequence=VSP_058771;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q8VBX6-4; Sequence=VSP_014202;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: In the brain, it is strongly expressed in the
choroid plexus. Within the hippocampal formation, strongest
expression was seen in the soma of CA1-4 pyramidal cells.
Expressed in most neocortical regions with the strongest
expression in piriform cortex and amygdaloid nuclei but also
detected in the subiculum and olfactory bulb. In the cerebellum,
the highest level of expression was found in Purkinje cells.
Moderately expressed in the granular layer and molecular layer.
Expressed in the pontine nuclei, parts of spinal trigeminal
nuclei, and the principal sensory trigeminal nuclei of the
metencephalon. Expressed in all thalamic and hypothalamic nuclei,
and the substantia nigra (at protein level). Ubiquitously
expressed. {ECO:0000269|PubMed:11018522,
ECO:0000269|PubMed:12706259}.
-!- DOMAIN: The PDZ domain 2 mainly binds CAMK2A and CAMK2B. The PDZ
domains 7 and 10 bind the Ad9 E4-ORF1 oncoprotein. The PDZ domain
10 binds the C-terminal PDZ-binding motif of HTR2C. The PDZ
domains 10 and 13 bind PLEKHA1 and PLEKHA2. The PDZ domain 13
binds SYNGAP1 (By similarity). The PDZ domain 1 binds NG2. The PDZ
domain 9 binds F11R. The PDZ domain 10 binds the C-terminus of
CLDN1 and KIT. The PDZ domain 13 binds CXADR. {ECO:0000250,
ECO:0000269|PubMed:11689568, ECO:0000269|PubMed:15364909}.
-!- SEQUENCE CAUTION:
Sequence=BAC27346.1; Type=Frameshift; Positions=2054; Evidence={ECO:0000305};
Sequence=BAC34766.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ131869; CAA10523.1; -; mRNA.
EMBL; AF326526; AAL37372.1; -; mRNA.
EMBL; AF326527; AAL37373.1; -; mRNA.
EMBL; AF326528; AAL37374.1; -; mRNA.
EMBL; AF326529; AAL37375.1; -; mRNA.
EMBL; AF326530; AAL37376.1; -; mRNA.
EMBL; AF326531; AAL37377.2; -; mRNA.
EMBL; AF326532; AAL37378.1; -; mRNA.
EMBL; AF326533; AAL37379.1; -; mRNA.
EMBL; AF326534; AAL37380.1; -; mRNA.
EMBL; AF326535; AAL37381.1; -; mRNA.
EMBL; AF326536; AAL37382.1; -; mRNA.
EMBL; AF326537; AAL37383.1; -; mRNA.
EMBL; AF326538; AAL37384.1; -; mRNA.
EMBL; AF326539; AAL37385.1; -; mRNA.
EMBL; AF326540; AAL37386.1; -; mRNA.
EMBL; AF326541; AAL37387.1; -; mRNA.
EMBL; AF326542; AAL37388.1; -; mRNA.
EMBL; AF326543; AAL37389.1; -; mRNA.
EMBL; AF326544; AAL37390.1; -; mRNA.
EMBL; CR352325; CAI25220.1; -; Genomic_DNA.
EMBL; AL670939; CAI25220.1; JOINED; Genomic_DNA.
EMBL; AL670939; CAI25921.1; -; Genomic_DNA.
EMBL; CR352325; CAI25921.1; JOINED; Genomic_DNA.
EMBL; BC061504; AAH61504.1; -; mRNA.
EMBL; BC145117; AAI45118.1; -; mRNA.
EMBL; AF000168; AAB57835.1; -; mRNA.
EMBL; AK031321; BAC27346.1; ALT_FRAME; mRNA.
EMBL; AK051782; BAC34766.1; ALT_SEQ; mRNA.
CCDS; CCDS18292.1; -. [Q8VBX6-1]
PIR; T30259; T30259.
RefSeq; NP_001292213.1; NM_001305284.1.
RefSeq; NP_001292215.1; NM_001305286.1. [Q8VBX6-2]
RefSeq; NP_034950.2; NM_010820.3. [Q8VBX6-1]
UniGene; Mm.153039; -.
PDB; 4XH7; X-ray; 1.65 A; A=521-665.
PDBsum; 4XH7; -.
ProteinModelPortal; Q8VBX6; -.
SMR; Q8VBX6; -.
BioGrid; 201476; 8.
CORUM; Q8VBX6; -.
DIP; DIP-41165N; -.
IntAct; Q8VBX6; 7.
MINT; MINT-146667; -.
STRING; 10090.ENSMUSP00000099894; -.
ChEMBL; CHEMBL2176783; -.
iPTMnet; Q8VBX6; -.
PhosphoSitePlus; Q8VBX6; -.
EPD; Q8VBX6; -.
PaxDb; Q8VBX6; -.
PRIDE; Q8VBX6; -.
Ensembl; ENSMUST00000102830; ENSMUSP00000099894; ENSMUSG00000028402. [Q8VBX6-1]
Ensembl; ENSMUST00000107258; ENSMUSP00000102879; ENSMUSG00000028402. [Q8VBX6-2]
GeneID; 17475; -.
KEGG; mmu:17475; -.
UCSC; uc008tjw.3; mouse. [Q8VBX6-2]
UCSC; uc008tjx.2; mouse. [Q8VBX6-1]
CTD; 8777; -.
MGI; MGI:1343489; Mpdz.
eggNOG; KOG3528; Eukaryota.
eggNOG; ENOG4110362; LUCA.
GeneTree; ENSGT00760000119017; -.
HOVERGEN; HBG080134; -.
InParanoid; Q8VBX6; -.
KO; K06095; -.
TreeFam; TF330709; -.
PRO; PR:Q8VBX6; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028402; -.
CleanEx; MM_MPDZ; -.
ExpressionAtlas; Q8VBX6; baseline and differential.
Genevisible; Q8VBX6; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0016327; C:apicolateral plasma membrane; ISO:MGI.
GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0007155; P:cell adhesion; IDA:MGI.
Gene3D; 1.10.287.650; -; 1.
InterPro; IPR015132; L27_2.
InterPro; IPR004172; L27_dom.
InterPro; IPR036892; L27_dom_sf.
InterPro; IPR032078; MPDZ.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
Pfam; PF09045; L27_2; 1.
Pfam; PF16667; MPDZ_u10; 1.
Pfam; PF00595; PDZ; 12.
SMART; SM00569; L27; 1.
SMART; SM00228; PDZ; 13.
SUPFAM; SSF101288; SSF101288; 1.
SUPFAM; SSF50156; SSF50156; 13.
PROSITE; PS51022; L27; 1.
PROSITE; PS50106; PDZ; 13.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Complete proteome; Membrane; Methylation;
Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
Repeat; Synapse; Synaptosome; Tight junction.
CHAIN 1 2055 Multiple PDZ domain protein.
/FTId=PRO_0000094595.
DOMAIN 1 63 L27. {ECO:0000255|PROSITE-
ProRule:PRU00365}.
DOMAIN 138 225 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 258 338 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 378 464 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 546 627 PDZ 4. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 693 779 PDZ 5. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 996 1077 PDZ 6. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1139 1231 PDZ 7. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1338 1421 PDZ 8. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1471 1552 PDZ 9. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1614 1697 PDZ 10. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1710 1792 PDZ 11. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1847 1933 PDZ 12. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1972 2055 PDZ 13. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000250|UniProtKB:O75970}.
MOD_RES 783 783 Phosphoserine.
{ECO:0000250|UniProtKB:O75970}.
MOD_RES 1066 1066 Phosphoserine.
{ECO:0000250|UniProtKB:O75970}.
MOD_RES 1158 1158 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1803 1803 Phosphoserine.
{ECO:0000250|UniProtKB:O75970}.
MOD_RES 1809 1809 Phosphoserine.
{ECO:0000250|UniProtKB:O55164}.
VAR_SEQ 1 1908 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_058771.
VAR_SEQ 1236 1268 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014201.
VAR_SEQ 1714 1714 Q -> QLQ (in isoform 4).
{ECO:0000303|PubMed:9192623}.
/FTId=VSP_014202.
VARIANT 541 541 N -> S (in strain: DBA/2J and DBA1/J).
{ECO:0000269|PubMed:11978849}.
VARIANT 691 691 G -> V (in strain: DBA/2J, DBA1/J, CE/J,
A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
and 129/J).
{ECO:0000269|PubMed:11978849}.
VARIANT 801 801 H -> R (in strain: DBA/2J, DBA1/J, CE/J,
A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
and 129/J).
{ECO:0000269|PubMed:11978849}.
VARIANT 859 859 T -> A (in strain: DBA/2J, DBA1/J, CE/J,
A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
and 129/J).
{ECO:0000269|PubMed:11978849}.
VARIANT 880 880 S -> N (in strain: DBA/2J, DBA1/J, CE/J,
A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
and 129/J).
{ECO:0000269|PubMed:11978849}.
VARIANT 914 914 R -> S (in strain: DBA/2J, DBA1/J, CE/J,
A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
and 129/J).
{ECO:0000269|PubMed:11978849}.
VARIANT 977 977 A -> V (in strain: DBA/2J, DBA1/J, CE/J,
A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
and 129/J).
{ECO:0000269|PubMed:11978849}.
VARIANT 1338 1338 V -> M (in strain: DBA/2J, DBA1/J, CE/J,
A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
and 129/J).
{ECO:0000269|PubMed:11978849}.
VARIANT 1433 1433 I -> N (in strain: DBA/2J, DBA1/J, CE/J,
A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
and 129/J).
{ECO:0000269|PubMed:11978849}.
VARIANT 1767 1767 H -> N (in strain: DBA/2J, DBA1/J, CE/J,
A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
and 129/J).
{ECO:0000269|PubMed:11978849}.
CONFLICT 583 583 S -> N (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 588 588 S -> N (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 871 871 P -> S (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 909 910 PP -> SS (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 914 919 RPAPTS -> KPTPTF (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 932 932 V -> G (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 937 938 EC -> QW (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 952 952 S -> N (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 956 956 S -> F (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 960 960 P -> S (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 963 963 P -> A (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 967 967 Q -> P (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 974 975 SS -> TF (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 984 984 N -> T (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 996 996 T -> P (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 1532 1532 K -> N (in Ref. 5; AAB57835).
{ECO:0000305}.
CONFLICT 1547 1547 T -> I (in Ref. 5; AAB57835).
{ECO:0000305}.
CONFLICT 1589 1589 T -> P (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 1616 1617 EI -> GV (in Ref. 5; AAB57835).
{ECO:0000305}.
CONFLICT 1691 1691 L -> V (in Ref. 5; AAB57835).
{ECO:0000305}.
CONFLICT 1844 1844 G -> R (in Ref. 5; AAB57835).
{ECO:0000305}.
CONFLICT 1914 1914 A -> V (in Ref. 4; AAH61504).
{ECO:0000305}.
CONFLICT 1968 1968 P -> S (in Ref. 1; CAA10523).
{ECO:0000305}.
CONFLICT 1983 1985 GFS -> SFN (in Ref. 1; CAA10523).
{ECO:0000305}.
HELIX 521 538 {ECO:0000244|PDB:4XH7}.
STRAND 542 550 {ECO:0000244|PDB:4XH7}.
STRAND 559 565 {ECO:0000244|PDB:4XH7}.
STRAND 568 574 {ECO:0000244|PDB:4XH7}.
HELIX 579 583 {ECO:0000244|PDB:4XH7}.
STRAND 591 595 {ECO:0000244|PDB:4XH7}.
HELIX 605 613 {ECO:0000244|PDB:4XH7}.
STRAND 617 626 {ECO:0000244|PDB:4XH7}.
SEQUENCE 2055 AA; 218711 MW; 26EA94B814214B69 CRC64;
MLETIDKNRA LQAAERLQSK LKERGDVANE DKLSLLKSVL QSPLFSQILN LQTSLQQLKD
QVNIATLATA AADHAHTPQF SSAVISNLQS ESLLLSPNHG NLEALPGPGA PAVMDGKPTC
DELDQLIKNM AQGRHVEIFE LLKPPCGGLG FSVVGLRSEN RGELGIFVQE IQEGSVAHRD
GRLKETDQIL AINGQVLDQT ITHQQAISIL QKAKDTVQLV IARGSLPPVS SPRISRSPSA
ASTISAHSNP MHWQHVETIE LVNDGSGLGF GIIGGKATGV IVKTILPGGV ADQHGRLCSG
DHILKIGDTD LAGMSSEQVA QVLRQCGNRV KLMIARGAVE ETPASSSLGI TLSSSTSSTS
EMRVDASTQK NDESETFDVE LTKNVQGLGI TIAGYIGDKK LEPSGIFVKS ITKSSAVEHD
GRIQIGDQII AVDGTNLQGF TNQQAVEVLR HTGQTVRLTL MRKGASQEAE LTSRGDTAKD
VDLPAENCEK DEESLSLKRN TSILPIEEEG FPLLSAELEE AEDVQQEAAL LTKWQRIMGI
NYEIVVAHVS KFSENSGLGI SLEATVGHHF IRSVLPEGPV GHSGKLFSGD ELLEVNGINL
LGENHQDVVN ILKELPIDVT MVCCRRTVPP IALSEMDSLD INDLELTEKP HIDLGEFIGS
SETEDPMLAM SDVDQNAEEI QTPLAMWEAG GQSIELEKGS RGLGFSILDY QDPIDPANTV
IVIRSLVPGG IAEKDGRLFP GDRLMFVNDI NLENSTLEEA VEALKGAPSG MVRIGVAKPL
PLSPEEGYVS AKEDAFLCSP HACKESGLSD KALFRADLAL IDTPDAESIA ESRFESQFSP
DNDSVYSTQA SIFSLHDGTC SDGMNYGPSL PSSPPKDVTS SSEVVLGLHL SLEELYTQNL
LQRQHAGSPP TDMRPAPTSG FPISDYTTTN AVEQKYECAN PVAWPHSQLP SSLSTSELAP
ALPAVAQKYL TDQSSLASDA ESVNLQSMSQ EAFERTVTIA KGSSSLGMTV SANKDGLGVI
VRSIIHGGAI SRDGRIAVGD CILSINEEST ISLTNAQARA MLRRHSLIGP DIKITYVPAE
HLEEFRVSFG QQAGGIMALD IFSSYTGRDI PELPEREEGE GEESELQNAA YSSWSQPRRV
ELWREPSKSL GISIVGGRGM GSRLSNGEVM RGIFIKHVLE DSPAGKNGTL KPGDRIIEVD
GMDLRDASHE QAVEAIRKAG NPVVFMVQSI INRPRKSPLP SLPHSLYPKY SFSSTNPFAD
SLQLTTDQAP SQSESETEKP ALCNVPPSSP SVFSEMGSDC AQPSATAVSE DEDKEDEFGY
SWKNIQERYG SLTGQLHVIE LEKGQSGLGL SLAGNKDRTR MSVFIVGIDP TGAAGRDGRL
QIADELLEIN GQILYGRSHQ NASSIIKCAP SKVKIIFIRN ADAVNQMAVC PGIAADSPSS
TSDSPQNKEV EPCSTTSASA ADLSSLTDVY QLELPKDQGG LGIAICEEDT INGVMIESLT
EHGGAAKDGR LKPGDHILAV DDEVVAGCPV EKFISLLKTA KATVKLTVRA ENPACPAVPS
SAVTVSGERK DNSQTPAVPA PDLEPIPSTS RSSTPAVFAS DPATCPIIPG CETTIEISKG
QTGLGLSIVG GSDTLLGAII IHEVYEEGAA CKDGRLWAGD QILEVNGIDL RKATHDEAIN
VLRQTPQRVR LTLYRDEAPY KEEDVCDTFT IELQKRPGKG LGLSIVGKRN DTGVFVSDIV
KGGIADADGR LMQGDQILMV NGEDVRHATQ EAVAALLKCS LGAVTLEVGR VKAAPFHSER
RPSQSSQVSE SSLSSFTPPL SGINTSESLE SNSKKNALAS EIQGLRTVEI KKGPADSLGL
SIAGGVGSPL GDVPIFIAMM HPNGVAAQTQ KLRVGDRIVT ICGTSTDGMT HTQAVNLMKN
ASGSIEVQVV AGGDVSVVTG HQQELANPCL AFTGLTSSSI FPDDLGPPQS KTITLDRGPD
GLGFSIVGGY GSPHGDLPIY VKTVFAKGAA AEDGRLKRGD QIIAVNGQSL EGVTHEEAVA
ILKRTKGTVT LMVLS


Related products :

Catalog number Product name Quantity
EIAAB25252 Homo sapiens,Human,MPDZ,Multi-PDZ domain protein 1,Multiple PDZ domain protein,MUPP1
EIAAB25253 Mpdz,Multi-PDZ domain protein 1,Multiple PDZ domain protein,Mupp1,Rat,Rattus norvegicus
EIAAB25254 Mouse,Mpdz,Multi-PDZ domain protein 1,Multiple PDZ domain protein,Mupp1,Mus musculus
EIAAB39471 Adapter protein TKS5,FISH,Five SH3 domain-containing protein,Homo sapiens,Human,KIAA0418,SH3 and PX domain-containing protein 2A,SH3 multiple domains protein 1,SH3MD1,SH3PXD2A,TKS5,Tyrosine kinase sub
EIAAB39470 Fish,Five SH3 domain-containing protein,Mouse,Mus musculus,SH3 and PX domain-containing protein 2A,SH3 multiple domains protein 1,Sh3md1,Sh3pxd2a,Tks5,Tyrosine kinase substrate with five SH3 domains
EIAAB27933 Homo sapiens,Human,KIAA1090,MMSET,Multiple myeloma SET domain-containing protein,NSD2,Nuclear SET domain-containing protein 2,Probable histone-lysine N-methyltransferase NSD2,Protein trithorax-5,TRX5,
18-003-43746 EGF-like domain-containing protein 8 - Epidermal growth factor-like protein 8; Multiple EGF-like domain protein 8; Vascular endothelial-statin 2; VE-statin-2 Polyclonal 0.1 mg Protein A
25-097 PRDM5 is a transcription factor of the PR-domain protein family. It contains a PR-domain and multiple zinc finger motifs. Transcription factors of the PR-domain family are known to be involved in cell 0.05 mg
28-082 LIM domain only 6 is a three LIM domain-containing protein. The LIM domain is a cysteine-rich sequence motif that binds zinc atoms to form a specific protein-binding interface for protein-protein inte 0.05 mg
EIAAB37261 Mouse,Mus musculus,SAM domain, SH3 domain and nuclear localization signals protein 1,SAM domain-containing protein SAMSN-1,Samsn1,SH3 protein expressed in lymphocytes 2,SH3-lymphocyte protein 2,SLy2
25-203 LIM domain only 6 is a three LIM domain-containing protein. The LIM domain is a cysteine-rich sequence motif that binds zinc atoms to form a specific protein-binding interface for protein-protein inte 0.05 mg
EIAAB34704 ARHGAP27,CAMGAP1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Homo sapiens,Human,PP905,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27,SH3 domain-con
25-095 TCERG1 is a nuclear protein that regulates transcriptional elongation and pre-mRNA splicing. TCERG1 interacts with the hyperphosphorylated C-terminal domain of RNA polymerase II via multiple FF domain 0.05 mg
EIAAB30394 CLIM1,CLP36,C-terminal LIM domain protein 1,Elfin,Homo sapiens,Human,LIM domain protein CLP-36,PDLIM1,PDZ and LIM domain protein 1
EIAAB37228 Major retinal SAM domain-containing protein,Mouse,Mr-s,Mus musculus,SAM domain-containing protein 11,Samd11,Sterile alpha motif domain-containing protein 11
EIAAB45821 C10orf23,Cerebral protein 9,Homo sapiens,hucep-9,Human,KIAA1768,Kinase non-catalytic C-lobe domain-containing protein 1,KIND domain-containing protein 1,KNDC1,Protein very KIND,Ras-GEF domain-containi
EIAAB30395 Clim1,Clp36,C-terminal LIM domain protein 1,Elfin,LIM domain protein CLP-36,Pdlim1,PDZ and LIM domain protein 1,Rat,Rattus norvegicus
EIAAB30393 Clim1,C-terminal LIM domain protein 1,Elfin,LIM domain protein CLP-36,Mouse,Mus musculus,Pdlim1,PDZ and LIM domain protein 1
25-850 LONRF3 contains a RING finger domain, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. Multiple alternatively sp 0.05 mg
EIAAB32313 Gm92,Mouse,Mus musculus,PR domain zinc finger protein 6,PR domain-containing protein 6,PR domain-containing protein in smooth muscle,Prdm6,Prism,Putative histone-lysine N-methyltransferase PRDM6
EIAAB45822 Kiaa1768,Kinase non-catalytic C-lobe domain-containing protein 1,KIND domain-containing protein 1,Kndc1,Mouse,Mus musculus,Protein very KIND,Ras-GEF domain-containing family member 2,Rasgef2,Vkind
25-305 The PR domain is a protein-protein interaction module of about 100 amino acids. PR domain-containing proteins, such as PRDM9, are often involved in transcriptional regulation.The PR domain is a protei 0.05 mg
25-803 This gene is a member of the PAR6 family and encodes a protein with a PSD95_Discs-large_ZO1 (PDZ) domain, an OPR domain and a semi-Cdc42_Rac interactive binding (CRIB) domain. This cytoplasmic protein 0.05 mg
EIAAB31275 Evectin-1,Evt1,Mouse,Mus musculus,PH domain-containing family B member 1,PH domain-containing protein in retina 1,Phr1,PHRET1,Pleckstrin homology domain retinal protein 1,Pleckstrin homology domain-co
EIAAB37262 HACS1,Hematopoietic adaptor containing SH3 and SAM domains 1,Homo sapiens,Human,Nash1,SAM domain, SH3 domain and nuclear localization signals protein 1,SAM domain-containing protein SAMSN-1,SAMSN1,SH3


 

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