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Q8VBX6 (MPDZ_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multiple PDZ domain protein
Alternative name(s):
Multi-PDZ domain protein 1
Gene names
Name:Mpdz
Synonyms:Mupp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2055 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

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 the adenovirus type 9 E4-ORF1 oncoprotein. Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell projectiondendrite. Cell junctiontight junction By similarity. Cell junctionsynapse. Cell junctionsynapsesynaptosome By similarity. 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. Ref.10 Ref.11 Ref.14

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. Ref.7 Ref.12

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. Ref.10 Ref.13

Sequence similarities

Contains 1 L27 domain.

Contains 13 PDZ (DHR) domains.

Sequence caution

The sequence BAC27346.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC34766.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VBX6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8VBX6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1236-1268: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8VBX6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2054-2055: LS → SLEVTARVEAAQPLAPLLL
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8VBX6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1714-1714: Q → QLQ
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8VBX6-5)

The sequence of this isoform differs from the canonical sequence as follows:
     63-87: NIATLATAAADHAHTPQFSSAVISN → GWHHPQRPSRCSKDLVRKGSCFSTG
     88-2055: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20552055Multiple PDZ domain protein
PRO_0000094595

Regions

Domain1 – 6363L27
Domain138 – 22588PDZ 1
Domain258 – 33881PDZ 2
Domain378 – 46487PDZ 3
Domain546 – 62782PDZ 4
Domain693 – 77987PDZ 5
Domain996 – 107782PDZ 6
Domain1139 – 123193PDZ 7
Domain1338 – 142184PDZ 8
Domain1471 – 155282PDZ 9
Domain1614 – 169784PDZ 10
Domain1710 – 179283PDZ 11
Domain1847 – 193387PDZ 12
Domain1972 – 205584PDZ 13

Amino acid modifications

Modified residue2311Phosphoserine By similarity

Natural variations

Alternative sequence63 – 8725NIATL…AVISN → GWHHPQRPSRCSKDLVRKGS CFSTG in isoform 5.
VSP_014199
Alternative sequence88 – 20551968Missing in isoform 5.
VSP_014200
Alternative sequence1236 – 126833Missing in isoform 2.
VSP_014201
Alternative sequence17141Q → QLQ in isoform 4.
VSP_014202
Alternative sequence2054 – 20552LS → SLEVTARVEAAQPLAPLLL in isoform 3.
VSP_014203
Natural variant5411N → S in strain: DBA/2J and DBA1/J. Ref.2
Natural variant6911G → V in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J. Ref.2
Natural variant8011H → R in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J. Ref.2
Natural variant8591T → A in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J. Ref.2
Natural variant8801S → N in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J. Ref.2
Natural variant9141R → S in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J. Ref.2
Natural variant9771A → V in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J. Ref.2
Natural variant13381V → M in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J. Ref.2
Natural variant14331I → N in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J. Ref.2
Natural variant17671H → N in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J. Ref.2

Experimental info

Sequence conflict5831S → N in CAA10523. Ref.1
Sequence conflict5881S → N in CAA10523. Ref.1
Sequence conflict8711P → S in CAA10523. Ref.1
Sequence conflict909 – 9102PP → SS in CAA10523. Ref.1
Sequence conflict914 – 9196RPAPTS → KPTPTF in CAA10523. Ref.1
Sequence conflict9321V → G in CAA10523. Ref.1
Sequence conflict937 – 9382EC → QW in CAA10523. Ref.1
Sequence conflict9521S → N in CAA10523. Ref.1
Sequence conflict9561S → F in CAA10523. Ref.1
Sequence conflict9601P → S in CAA10523. Ref.1
Sequence conflict9631P → A in CAA10523. Ref.1
Sequence conflict9671Q → P in CAA10523. Ref.1
Sequence conflict974 – 9752SS → TF in CAA10523. Ref.1
Sequence conflict9841N → T in CAA10523. Ref.1
Sequence conflict9961T → P in CAA10523. Ref.1
Sequence conflict15321K → N in AAB57835. Ref.6
Sequence conflict15471T → I in AAB57835. Ref.6
Sequence conflict15891T → P in CAA10523. Ref.1
Sequence conflict1616 – 16172EI → GV in AAB57835. Ref.6
Sequence conflict16911L → V in AAB57835. Ref.6
Sequence conflict18441G → R in AAB57835. Ref.6
Sequence conflict19141A → V in AAH61504. Ref.5
Sequence conflict19681P → S in CAA10523. Ref.1
Sequence conflict1983 – 19853GFS → SFN in CAA10523. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 26EA94B814214B69

FASTA2,055218,711
        10         20         30         40         50         60 
MLETIDKNRA LQAAERLQSK LKERGDVANE DKLSLLKSVL QSPLFSQILN LQTSLQQLKD 

        70         80         90        100        110        120 
QVNIATLATA AADHAHTPQF SSAVISNLQS ESLLLSPNHG NLEALPGPGA PAVMDGKPTC 

       130        140        150        160        170        180 
DELDQLIKNM AQGRHVEIFE LLKPPCGGLG FSVVGLRSEN RGELGIFVQE IQEGSVAHRD 

       190        200        210        220        230        240 
GRLKETDQIL AINGQVLDQT ITHQQAISIL QKAKDTVQLV IARGSLPPVS SPRISRSPSA 

       250        260        270        280        290        300 
ASTISAHSNP MHWQHVETIE LVNDGSGLGF GIIGGKATGV IVKTILPGGV ADQHGRLCSG 

       310        320        330        340        350        360 
DHILKIGDTD LAGMSSEQVA QVLRQCGNRV KLMIARGAVE ETPASSSLGI TLSSSTSSTS 

       370        380        390        400        410        420 
EMRVDASTQK NDESETFDVE LTKNVQGLGI TIAGYIGDKK LEPSGIFVKS ITKSSAVEHD 

       430        440        450        460        470        480 
GRIQIGDQII AVDGTNLQGF TNQQAVEVLR HTGQTVRLTL MRKGASQEAE LTSRGDTAKD 

       490        500        510        520        530        540 
VDLPAENCEK DEESLSLKRN TSILPIEEEG FPLLSAELEE AEDVQQEAAL LTKWQRIMGI 

       550        560        570        580        590        600 
NYEIVVAHVS KFSENSGLGI SLEATVGHHF IRSVLPEGPV GHSGKLFSGD ELLEVNGINL 

       610        620        630        640        650        660 
LGENHQDVVN ILKELPIDVT MVCCRRTVPP IALSEMDSLD INDLELTEKP HIDLGEFIGS 

       670        680        690        700        710        720 
SETEDPMLAM SDVDQNAEEI QTPLAMWEAG GQSIELEKGS RGLGFSILDY QDPIDPANTV 

       730        740        750        760        770        780 
IVIRSLVPGG IAEKDGRLFP GDRLMFVNDI NLENSTLEEA VEALKGAPSG MVRIGVAKPL 

       790        800        810        820        830        840 
PLSPEEGYVS AKEDAFLCSP HACKESGLSD KALFRADLAL IDTPDAESIA ESRFESQFSP 

       850        860        870        880        890        900 
DNDSVYSTQA SIFSLHDGTC SDGMNYGPSL PSSPPKDVTS SSEVVLGLHL SLEELYTQNL 

       910        920        930        940        950        960 
LQRQHAGSPP TDMRPAPTSG FPISDYTTTN AVEQKYECAN PVAWPHSQLP SSLSTSELAP 

       970        980        990       1000       1010       1020 
ALPAVAQKYL TDQSSLASDA ESVNLQSMSQ EAFERTVTIA KGSSSLGMTV SANKDGLGVI 

      1030       1040       1050       1060       1070       1080 
VRSIIHGGAI SRDGRIAVGD CILSINEEST ISLTNAQARA MLRRHSLIGP DIKITYVPAE 

      1090       1100       1110       1120       1130       1140 
HLEEFRVSFG QQAGGIMALD IFSSYTGRDI PELPEREEGE GEESELQNAA YSSWSQPRRV 

      1150       1160       1170       1180       1190       1200 
ELWREPSKSL GISIVGGRGM GSRLSNGEVM RGIFIKHVLE DSPAGKNGTL KPGDRIIEVD 

      1210       1220       1230       1240       1250       1260 
GMDLRDASHE QAVEAIRKAG NPVVFMVQSI INRPRKSPLP SLPHSLYPKY SFSSTNPFAD 

      1270       1280       1290       1300       1310       1320 
SLQLTTDQAP SQSESETEKP ALCNVPPSSP SVFSEMGSDC AQPSATAVSE DEDKEDEFGY 

      1330       1340       1350       1360       1370       1380 
SWKNIQERYG SLTGQLHVIE LEKGQSGLGL SLAGNKDRTR MSVFIVGIDP TGAAGRDGRL 

      1390       1400       1410       1420       1430       1440 
QIADELLEIN GQILYGRSHQ NASSIIKCAP SKVKIIFIRN ADAVNQMAVC PGIAADSPSS 

      1450       1460       1470       1480       1490       1500 
TSDSPQNKEV EPCSTTSASA ADLSSLTDVY QLELPKDQGG LGIAICEEDT INGVMIESLT 

      1510       1520       1530       1540       1550       1560 
EHGGAAKDGR LKPGDHILAV DDEVVAGCPV EKFISLLKTA KATVKLTVRA ENPACPAVPS 

      1570       1580       1590       1600       1610       1620 
SAVTVSGERK DNSQTPAVPA PDLEPIPSTS RSSTPAVFAS DPATCPIIPG CETTIEISKG 

      1630       1640       1650       1660       1670       1680 
QTGLGLSIVG GSDTLLGAII IHEVYEEGAA CKDGRLWAGD QILEVNGIDL RKATHDEAIN 

      1690       1700       1710       1720       1730       1740 
VLRQTPQRVR LTLYRDEAPY KEEDVCDTFT IELQKRPGKG LGLSIVGKRN DTGVFVSDIV 

      1750       1760       1770       1780       1790       1800 
KGGIADADGR LMQGDQILMV NGEDVRHATQ EAVAALLKCS LGAVTLEVGR VKAAPFHSER 

      1810       1820       1830       1840       1850       1860 
RPSQSSQVSE SSLSSFTPPL SGINTSESLE SNSKKNALAS EIQGLRTVEI KKGPADSLGL 

      1870       1880       1890       1900       1910       1920 
SIAGGVGSPL GDVPIFIAMM HPNGVAAQTQ KLRVGDRIVT ICGTSTDGMT HTQAVNLMKN 

      1930       1940       1950       1960       1970       1980 
ASGSIEVQVV AGGDVSVVTG HQQELANPCL AFTGLTSSSI FPDDLGPPQS KTITLDRGPD 

      1990       2000       2010       2020       2030       2040 
GLGFSIVGGY GSPHGDLPIY VKTVFAKGAA AEDGRLKRGD QIIAVNGQSL EGVTHEEAVA 

      2050 
ILKRTKGTVT LMVLS 

« Hide

Isoform 2 [UniParc].

Checksum: 1B5D7BF3FFA7B4BA
Show »

FASTA2,022215,061
Isoform 3 [UniParc].

Checksum: CAA3A0A924541F8D
Show »

FASTA2,072220,484
Isoform 4 [UniParc].

Checksum: 7861BBC636A9C862
Show »

FASTA2,057218,953
Isoform 5 [UniParc].

Checksum: 40BB9E94036D48CB
Show »

FASTA879,845

References

« Hide 'large scale' references
[1]"Identification, sequence, and mapping of mouse multiple PDZ domain protein gene, Mpdz."
Simpson E.H., Suffolk R., Jackson I.J.
Genomics 59:102-104(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: C57BL/6 X CBA.
Tissue: Brain.
[2]"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."
Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.
J. Neurosci. 22:3730-3738(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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.
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1894-2055 (ISOFORM 3).
Strain: C57BL/6J.
Tissue: Spinal ganglion and Testis.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: FVB/N.
Tissue: Brain, Kidney and Mammary tumor.
[6]"Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein."
Lee S.S., Weiss R.S., Javier R.T.
Proc. Natl. Acad. Sci. U.S.A. 94:6670-6675(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1532-2055 (ISOFORM 4).
Tissue: Pancreas.
[7]"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."
Mancini A., Koch A., Stefan M., Niemann H., Tamura T.
FEBS Lett. 482:54-58(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIT, TISSUE SPECIFICITY.
[8]"The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the membrane-spanning proteoglycan NG2."
Barritt D.S., Pearn M.T., Zisch A.H., Lee S.S., Javier R.T., Pasquale E.B., Stallcup W.B.
J. Cell. Biochem. 79:213-224(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NG2.
[9]"Multi-PDZ domain protein MUPP1 is a cellular target for both adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6 oncoproteins."
Lee S.S., Glaunsinger B., Mantovani F., Banks L., Javier R.T.
J. Virol. 74:9680-9693(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADENOVIRUS TYPE 9 E4-ORF1 PROTEIN.
[10]"Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule."
Hamazaki Y., Itoh M., Sasaki H., Furuse M., Tsukita S.
J. Biol. Chem. 277:455-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLDN1 AND F11R, DOMAINS, SUBCELLULAR LOCATION.
[11]"Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells."
Poliak S., Matlis S., Ullmer C., Scherer S.S., Peles E.
J. Cell Biol. 159:361-372(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Expression of MUPP1 protein in mouse brain."
Sitek B., Poschmann G., Schmidtke K., Ullmer C., Maskri L., Andriske M., Stichel C.C., Zhu X.-R., Luebbert H.
Brain Res. 970:178-187(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[13]"The coxsackievirus and adenovirus receptor interacts with the multi-PDZ domain protein-1 (MUPP-1) within the tight junction."
Coyne C.B., Voelker T., Pichla S.L., Bergelson J.M.
J. Biol. Chem. 279:48079-48084(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CXADR, DOMAIN.
[14]"Crumbs homologue 1 is required for maintenance of photoreceptor cell polarization and adhesion during light exposure."
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.
J. Cell Sci. 117:4169-4177(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRB1; MPP5 AND MPP4, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ131869 mRNA. Translation: CAA10523.1.
AF326526 mRNA. Translation: AAL37372.1.
AF326527 mRNA. Translation: AAL37373.1.
AF326528 mRNA. Translation: AAL37374.1.
AF326529 mRNA. Translation: AAL37375.1.
AF326530 mRNA. Translation: AAL37376.1.
AF326531 mRNA. Translation: AAL37377.2.
AF326532 mRNA. Translation: AAL37378.1.
AF326533 mRNA. Translation: AAL37379.1.
AF326534 mRNA. Translation: AAL37380.1.
AF326535 mRNA. Translation: AAL37381.1.
AF326536 mRNA. Translation: AAL37382.1.
AF326537 mRNA. Translation: AAL37383.1.
AF326538 mRNA. Translation: AAL37384.1.
AF326539 mRNA. Translation: AAL37385.1.
AF326540 mRNA. Translation: AAL37386.1.
AF326541 mRNA. Translation: AAL37387.1.
AF326542 mRNA. Translation: AAL37388.1.
AF326543 mRNA. Translation: AAL37389.1.
AF326544 mRNA. Translation: AAL37390.1.
AK031321 mRNA. Translation: BAC27346.1. Different initiation.
AK051782 mRNA. Translation: BAC34766.1. Different initiation.
CR352325, AL670939 Genomic DNA. Translation: CAI25220.1.
AL670939, CR352325 Genomic DNA. Translation: CAI25921.1.
BC061504 mRNA. Translation: AAH61504.1.
BC145117 mRNA. Translation: AAI45118.1.
AF000168 mRNA. Translation: AAB57835.1.
IPIIPI00404052.
IPI00457729.
IPI00466594.
IPI00474705.
IPI00608031.
PIRT30259.
RefSeqNP_034950.2. NM_010820.2.
UniGeneMm.153039.

3D structure databases

ProteinModelPortalQ8VBX6.
SMRQ8VBX6. Positions 11-63, 120-466, 571-625, 684-776, 1002-1064, 1078-1232, 1270-1557, 1610-2055.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-41165N.
MINTMINT-146667.

PTM databases

PhosphoSiteQ8VBX6.

Proteomic databases

PaxDbQ8VBX6.
PRIDEQ8VBX6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102830; ENSMUSP00000099894; ENSMUSG00000028402.
GeneID17475.
KEGGmmu:17475.
UCSCuc008tjw.2. mouse.
uc008tjx.1. mouse.
uc008tjy.1. mouse.

Organism-specific databases

CTD8777.
MGIMGI:1343489. Mpdz.

Phylogenomic databases

eggNOGNOG252837.
GeneTreeENSGT00650000092901.
HOVERGENHBG080134.
KOK06095.
OrthoDBEOG44F688.

Gene expression databases

ArrayExpressQ8VBX6.
BgeeQ8VBX6.
CleanExMM_MPDZ.
GenevestigatorQ8VBX6.
GermOnlineENSMUSG00000028402. Mus musculus.

Family and domain databases

InterProIPR004172. L27.
IPR015132. L27_2.
IPR001478. PDZ.
[Graphical view]
PfamPF09045. L27_2. 1 hit.
PF00595. PDZ. 13 hits.
[Graphical view]
SMARTSM00569. L27. 1 hit.
SM00228. PDZ. 13 hits.
[Graphical view]
SUPFAMSSF50156. PDZ. 13 hits.
PROSITEPS51022. L27. 1 hit.
PS50106. PDZ. 13 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio292120.
SOURCESearch...

Entry information

Entry nameMPDZ_MOUSE
AccessionPrimary (citable) accession number: Q8VBX6
Secondary accession number(s): B7ZNA1 expand/collapse secondary AC list , O08783, Q6P7U4, Q80ZY8, Q8BKJ1, Q8C0H8, Q8VBV5, Q8VBY0, Q9Z1K3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families