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O75970 (MPDZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2070 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with HTR2C and provokes its clustering at the cell surface By similarity. Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses. Ref.10 Ref.14

Subunit structure

Interacts with CLDN5, DLG4, GRIN1, F11R/JAM, CLDN1, NG2, CRB1, MPP4 and MPP5 By similarity. Interacts with HTR2A, HTR2B, HTR2C, PLEKHA1/TAPP1, PLEKHA2/TAPP2, CXADR, SYNGAP1, CAMK2A and CAMK2B. Interacts with FAT4 (via cytoplasmic domain) By similarity. Interacts with the adenovirus type 9 E4-ORF1 protein. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 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. Cell junctionsynapse. Cell junctionsynapsesynaptosome. Note: Associated with membranes. 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. Localized mainly in the Schmidt-Lanterman incisures of myelinating Schwann cells By similarity. In the retina, localizes to the sub-apical region adjacent to the adherens junction complex at the outer limiting membrane. Enriched at the tight junctions of epithelial cells. Association to the tight junctions depends on CXADR. Ref.8 Ref.12 Ref.13

Tissue specificity

Expressed in heart, brain, placenta, liver, skeletal muscle, kidney and pancreas. Ref.8

Domain

The PDZ domain 1 binds NG2. The PDZ domains 7 and 10 bind the Ad9 E4-ORF1 oncoprotein. The PDZ domain 9 binds F11R. The PDZ domain 10 binds the C-terminus of CLDN1 and KIT and the C-terminal PDZ-binding motif of HTR2C. The PDZ domain 13 binds CXADR By similarity. The PDZ domain 2 binds CAMK2A and CAMK2B. The PDZ domains 10 and 13 bind PLEKHA1 and PLEKHA2. The PDZ domain 13 binds SYNGAP1. Ref.10 Ref.11 Ref.14

Involvement in disease

Hydrocephalus, non-syndromic, autosomal recessive 2 (HYC2) [MIM:615219]: A disease characterized by a disturbance of cerebrospinal fluid circulation causing accumulation of ventricular cerebrospinal fluid, which results in progressive ventricular dilatation with onset in utero. Affected individuals may have neurologic impairment.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Sequence similarities

Contains 1 L27 domain.

Contains 13 PDZ (DHR) domains.

Sequence caution

The sequence AAC61870.1 differs from that shown. Reason: Aberrant splicing.

The sequence BAC05409.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE06123.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAH71900.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40490.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40491.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40492.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40494.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40495.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41236.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41237.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41238.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41240.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI56786.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell junction
Cell membrane
Cell projection
Membrane
Postsynaptic cell membrane
Synapse
Synaptosome
Tight junction
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: Ensembl

myelination

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSchmidt-Lanterman incisure

Inferred from electronic annotation. Source: Ensembl

apical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

apicolateral plasma membrane

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

tight junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein C-terminus binding

Inferred from physical interaction Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75970-1)

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: O75970-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1794-1822: Missing.
Isoform 3 (identifier: O75970-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1248-1280: Missing.
Isoform 4 (identifier: O75970-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1248-1280: Missing.
     1794-1822: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20702070Multiple PDZ domain protein
PRO_0000094594

Regions

Domain1 – 6363L27
Domain137 – 22488PDZ 1
Domain257 – 33781PDZ 2
Domain377 – 46387PDZ 3
Domain553 – 63482PDZ 4
Domain700 – 78687PDZ 5
Domain1008 – 108982PDZ 6
Domain1151 – 124393PDZ 7
Domain1350 – 143384PDZ 8
Domain1483 – 156482PDZ 9
Domain1629 – 171284PDZ 10
Domain1725 – 180783PDZ 11
Domain1862 – 194887PDZ 12
Domain1987 – 207084PDZ 13
Compositional bias1818 – 184831Ser-rich

Amino acid modifications

Modified residue2301Phosphoserine Ref.15
Modified residue4831Phosphoserine Ref.17

Natural variations

Alternative sequence1248 – 128033Missing in isoform 3 and isoform 4.
VSP_040450
Alternative sequence1794 – 182229Missing in isoform 2 and isoform 4.
VSP_040451
Natural variant921S → L.
Corresponds to variant rs17273542 [ dbSNP | Ensembl ].
VAR_056115
Natural variant3511L → F.
Corresponds to variant rs3739757 [ dbSNP | Ensembl ].
VAR_056116
Natural variant7021E → K.
Corresponds to variant rs4741289 [ dbSNP | Ensembl ].
VAR_056117
Natural variant7021E → V.
Corresponds to variant rs4740548 [ dbSNP | Ensembl ].
VAR_056118
Natural variant16041T → A.
Corresponds to variant rs16930134 [ dbSNP | Ensembl ].
VAR_056119
Natural variant16631G → R.
Corresponds to variant rs2274648 [ dbSNP | Ensembl ].
VAR_056120

Experimental info

Mutagenesis147 – 1504GLGF → PSES: Loss of interaction with CAMK2A. Ref.14
Sequence conflict19501V → M in CAI56786. Ref.6

Secondary structure

......................................................................................................... 2070
Helix Strand Turn

Details...

Sequences

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

Last modified January 11, 2011. Version 2.
Checksum: A4D304C20401FD45

FASTA2,070221,618
        10         20         30         40         50         60 
MLEAIDKNRA LHAAERLQTK LRERGDVANE DKLSLLKSVL QSPLFSQILS LQTSVQQLKD 

        70         80         90        100        110        120 
QVNIATSATS NIEYAHVPHL SPAVIPTLQN ESFLLSPNNG NLEALTGPGI PHINGKPACD 

       130        140        150        160        170        180 
EFDQLIKNMA QGRHVEVFEL LKPPSGGLGF SVVGLRSENR GELGIFVQEI QEGSVAHRDG 

       190        200        210        220        230        240 
RLKETDQILA INGQALDQTI THQQAISILQ KAKDTVQLVI ARGSLPQLVS PIVSRSPSAA 

       250        260        270        280        290        300 
STISAHSNPV HWQHMETIEL VNDGSGLGFG IIGGKATGVI VKTILPGGVA DQHGRLCSGD 

       310        320        330        340        350        360 
HILKIGDTDL AGMSSEQVAQ VLRQCGNRVK LMIARGAIEE RTAPTALGIT LSSSPTSTPE 

       370        380        390        400        410        420 
LRVDASTQKG EESETFDVEL TKNVQGLGIT IAGYIGDKKL EPSGIFVKSI TKSSAVEHDG 

       430        440        450        460        470        480 
RIQIGDQIIA VDGTNLQGFT NQQAVEVLRH TGQTVLLTLM RRGMKQEAEL MSREDVTKDA 

       490        500        510        520        530        540 
DLSPVNASII KENYEKDEDF LSSTRNTNIL PTEEEGYPLL SAEIEEIEDA QKQEAALLTK 

       550        560        570        580        590        600 
WQRIMGINYE IVVAHVSKFS ENSGLGISLE ATVGHHFIRS VLPEGPVGHS GKLFSGDELL 

       610        620        630        640        650        660 
EVNGITLLGE NHQDVVNILK ELPIEVTMVC CRRTVPPTTQ SELDSLDLCD IELTEKPHVD 

       670        680        690        700        710        720 
LGEFIGSSET EDPVLAMTDA GQSTEEVQAP LAMWEAGIQH IELEKGSKGL GFSILDYQDP 

       730        740        750        760        770        780 
IDPASTVIII RSLVPGGIAE KDGRLLPGDR LMFVNDVNLE NSSLEEAVEA LKGAPSGTVR 

       790        800        810        820        830        840 
IGVAKPLPLS PEEGYVSAKE DSFLYPPHSC EEAGLADKPL FRADLALVGT NDADLVDEST 

       850        860        870        880        890        900 
FESPYSPEND SIYSTQASIL SLHGSSCGDG LNYGSSLPSS PPKDVIENSC DPVLDLHMSL 

       910        920        930        940        950        960 
EELYTQNLLQ RQDENTPSVD ISMGPASGFT INDYTPANAI EQQYECENTI VWTESHLPSE 

       970        980        990       1000       1010       1020 
VISSAELPSV LPDSAGKGSE YLLEQSSLAC NAECVMLQNV SKESFERTIN IAKGNSSLGM 

      1030       1040       1050       1060       1070       1080 
TVSANKDGLG MIVRSIIHGG AISRDGRIAI GDCILSINEE STISVTNAQA RAMLRRHSLI 

      1090       1100       1110       1120       1130       1140 
GPDIKITYVP AEHLEEFKIS LGQQSGRVMA LDIFSSYTGR DIPELPEREE GEGEESELQN 

      1150       1160       1170       1180       1190       1200 
TAYSNWNQPR RVELWREPSK SLGISIVGGR GMGSRLSNGE VMRGIFIKHV LEDSPAGKNG 

      1210       1220       1230       1240       1250       1260 
TLKPGDRIVE VDGMDLRDAS HEQAVEAIRK AGNPVVFMVQ SIINRPRKSP LPSLLHNLYP 

      1270       1280       1290       1300       1310       1320 
KYNFSSTNPF ADSLQINADK APSQSESEPE KAPLCSVPPP PPSAFAEMGS DHTQSSASKI 

      1330       1340       1350       1360       1370       1380 
SQDVDKEDEF GYSWKNIRER YGTLTGELHM IELEKGHSGL GLSLAGNKDR SRMSVFIVGI 

      1390       1400       1410       1420       1430       1440 
DPNGAAGKDG RLQIADELLE INGQILYGRS HQNASSIIKC APSKVKIIFI RNKDAVNQMA 

      1450       1460       1470       1480       1490       1500 
VCPGNAVEPL PSNSENLQNK ETEPTVTTSD AAVDLSSFKN VQHLELPKDQ GGLGIAISEE 

      1510       1520       1530       1540       1550       1560 
DTLSGVIIKS LTEHGVAATD GRLKVGDQIL AVDDEIVVGY PIEKFISLLK TAKMTVKLTI 

      1570       1580       1590       1600       1610       1620 
HAENPDSQAV PSAAGAASGE KKNSSQSLMV PQSGSPEPES IRNTSRSSTP AIFASDPATC 

      1630       1640       1650       1660       1670       1680 
PIIPGCETTI EISKGRTGLG LSIVGGSDTL LGAIIIHEVY EEGAACKDGR LWAGDQILEV 

      1690       1700       1710       1720       1730       1740 
NGIDLRKATH DEAINVLRQT PQRVRLTLYR DEAPYKEEEV CDTLTIELQK KPGKGLGLSI 

      1750       1760       1770       1780       1790       1800 
VGKRNDTGVF VSDIVKGGIA DADGRLMQGD QILMVNGEDV RNATQEAVAA LLKCSLGTVT 

      1810       1820       1830       1840       1850       1860 
LEVGRIKAGP FHSERRPSQS SQVSEGSLSS FTFPLSGSST SESLESSSKK NALASEIQGL 

      1870       1880       1890       1900       1910       1920 
RTVEMKKGPT DSLGISIAGG VGSPLGDVPI FIAMMHPTGV AAQTQKLRVG DRIVTICGTS 

      1930       1940       1950       1960       1970       1980 
TEGMTHTQAV NLLKNASGSI EMQVVAGGDV SVVTGHQQEP ASSSLSFTGL TSSSIFQDDL 

      1990       2000       2010       2020       2030       2040 
GPPQCKSITL ERGPDGLGFS IVGGYGSPHG DLPIYVKTVF AKGAASEDGR LKRGDQIIAV 

      2050       2060       2070 
NGQSLEGVTH EEAVAILKRT KGTVTLMVLS 

« Hide

Isoform 2 [UniParc].

Checksum: 03736D2490F3E2C7
Show »

FASTA2,041218,507
Isoform 3 [UniParc].

Checksum: 99D1557E87DECAE9
Show »

FASTA2,037217,915
Isoform 4 [UniParc].

Checksum: C0EBEA38A7020807
Show »

FASTA2,008214,804

References

« Hide 'large scale' references
[1]"Human homolog of MUPP1 protein."
Eng L., Krapivinsky G., Clapham D.E.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 3 AND 4).
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 573-2070 (ISOFORM 1).
Tissue: Amygdala.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1535-2070 (ISOFORM 1).
Tissue: Brain.
[8]"Cloning and characterization of MUPP1, a novel PDZ domain protein."
Ullmer C., Schmuck K., Figge A., Luebbert H.
FEBS Lett. 424:63-68(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1618-2070 (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH HTR2C, SUBCELLULAR LOCATION.
Tissue: Brain.
[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]"Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10 of the multi-PDZ domain protein MUPP1."
Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J., Luebbert H., Ullmer C.
J. Biol. Chem. 276:12974-12982(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTR2A; HTR2B AND HTR2C, DOMAIN, FUNCTION.
[11]"Evidence that the tandem-pleckstrin-homology-domain-containing protein TAPP1 interacts with Ptd(3,4)P2 and the multi-PDZ-domain-containing protein MUPP1 in vivo."
Kimber W.A., Trinkle-Mulcahy L., Cheung P.C.F., Deak M., Marsden L.J., Kieloch A., Watt S., Javier R.T., Gray A., Downes C.P., Lucocq J.M., Alessi D.R.
Biochem. J. 361:525-536(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLEKHA1 AND PLEKHA2, DOMAIN.
[12]"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, SUBCELLULAR LOCATION.
[13]"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, SUBCELLULAR LOCATION.
[14]"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation."
Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.
Neuron 43:563-574(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYNGAP1; CAMK2A AND CAMK2B, MUTAGENESIS OF 147-GLY--PHE-150, DOMAIN, FUNCTION.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Mutation in MPDZ causes severe congenital hydrocephalus."
Al-Dosari M.S., Al-Owain M., Tulbah M., Kurdi W., Adly N., Al-Hemidan A., Masoodi T.A., Albash B., Alkuraya F.S.
J. Med. Genet. 50:54-58(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HYC2.
[20]"Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions."
Elkins J.M., Papagrigoriou E., Berridge G., Yang X., Phillips C., Gileadi C., Savitsky P., Doyle D.A.
Protein Sci. 16:683-694(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 117-227, X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 373-463, X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 1148-1243, X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1625-1716, X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1722-1806, X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1859-1951, X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 1983-2070.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF093419 mRNA. Translation: AAC61870.1. Sequence problems.
AB210041 mRNA. Translation: BAE06123.1. Different initiation.
AL162386, AL161449, AL353639 Genomic DNA. Translation: CAH71899.1.
AL162386, AL161449, AL353639 Genomic DNA. Translation: CAH71900.1. Sequence problems.
AL353639, AL161449 Genomic DNA. Translation: CAI41236.1. Sequence problems.
AL353639, AL161449 Genomic DNA. Translation: CAI41237.1. Sequence problems.
AL353639, AL161449, AL162386 Genomic DNA. Translation: CAI41238.1. Sequence problems.
AL353639, AL161449, AL162386 Genomic DNA. Translation: CAI41239.1.
AL353639 Genomic DNA. Translation: CAI41240.1. Sequence problems.
AL161449, AL353639 Genomic DNA. Translation: CAI40490.1. Sequence problems.
AL161449, AL353639 Genomic DNA. Translation: CAI40491.1. Sequence problems.
AL161449, AL162386, AL353639 Genomic DNA. Translation: CAI40492.1. Sequence problems.
AL161449, AL162386, AL353639 Genomic DNA. Translation: CAI40493.1.
AL161449 Genomic DNA. Translation: CAI40494.1. Sequence problems.
AL161449 Genomic DNA. Translation: CAI40495.1. Sequence problems.
CH471071 Genomic DNA. Translation: EAW58704.1.
BC140793 mRNA. Translation: AAI40794.1.
BC144564 mRNA. Translation: AAI44565.1.
CR936648 mRNA. Translation: CAI56786.1. Sequence problems.
AK098775 mRNA. Translation: BAC05409.1. Different initiation.
AJ001319 mRNA. Translation: CAA04680.1.
CCDSCCDS47951.1. [O75970-2]
CCDS59119.1. [O75970-5]
CCDS59120.1. [O75970-3]
RefSeqNP_001248335.1. NM_001261406.1. [O75970-3]
NP_001248336.1. NM_001261407.1. [O75970-5]
NP_003820.2. NM_003829.4. [O75970-2]
XP_005251679.1. XM_005251622.2. [O75970-1]
XP_006716948.1. XM_006716885.1. [O75970-1]
XP_006716949.1. XM_006716886.1. [O75970-1]
XP_006716950.1. XM_006716887.1. [O75970-1]
XP_006716951.1. XM_006716888.1. [O75970-2]
XP_006716952.1. XM_006716889.1. [O75970-3]
XP_006716954.1. XM_006716891.1. [O75970-5]
UniGeneHs.169378.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FCFX-ray1.76A1148-1243[»]
2FNEX-ray1.83A/B/C1983-2070[»]
2IWNX-ray1.35A373-463[»]
2IWOX-ray1.70A/B1859-1951[»]
2IWPX-ray2.15A/B1859-1951[»]
2IWQX-ray1.80A1148-1243[»]
2O2TX-ray2.70A/B117-227[»]
2OPGX-ray1.50A/B1625-1716[»]
2QG1X-ray1.40A1722-1806[»]
ProteinModelPortalO75970.
SMRO75970. Positions 119-227, 373-463, 1148-1244, 1331-1446, 1625-1716, 1722-1806, 1859-1951, 1983-2070.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114307. 14 interactions.
IntActO75970. 25 interactions.
MINTMINT-275229.

PTM databases

PhosphoSiteO75970.

Proteomic databases

MaxQBO75970.
PaxDbO75970.
PRIDEO75970.

Protocols and materials databases

DNASU8777.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319217; ENSP00000320006; ENSG00000107186. [O75970-1]
ENST00000381015; ENSP00000370403; ENSG00000107186. [O75970-1]
ENST00000381022; ENSP00000370410; ENSG00000107186. [O75970-2]
ENST00000447879; ENSP00000415208; ENSG00000107186. [O75970-3]
ENST00000536827; ENSP00000444151; ENSG00000107186. [O75970-5]
ENST00000541718; ENSP00000439807; ENSG00000107186. [O75970-2]
GeneID8777.
KEGGhsa:8777.
UCSCuc003zlb.4. human. [O75970-2]
uc010mhz.4. human. [O75970-3]
uc010mia.1. human. [O75970-1]
uc011lmn.3. human.

Organism-specific databases

CTD8777.
GeneCardsGC09M013095.
H-InvDBHIX0007919.
HGNCHGNC:7208. MPDZ.
HPACAB013512.
HPA020255.
HPA026686.
MIM603785. gene.
615219. phenotype.
neXtProtNX_O75970.
Orphanet269505. Congenital communicating hydrocephalus.
PharmGKBPA30914.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG252837.
HOVERGENHBG080134.
KOK06095.
OrthoDBEOG72ZCD0.
PhylomeDBO75970.
TreeFamTF330709.

Gene expression databases

ArrayExpressO75970.
BgeeO75970.
GenevestigatorO75970.

Family and domain databases

Gene3D2.30.42.10. 13 hits.
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. SSF50156. 13 hits.
PROSITEPS51022. L27. 1 hit.
PS50106. PDZ. 13 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75970.
GeneWikiMPDZ.
GenomeRNAi8777.
NextBio32912.
PROO75970.
SOURCESearch...

Entry information

Entry nameMPDZ_HUMAN
AccessionPrimary (citable) accession number: O75970
Secondary accession number(s): A6NLC2 expand/collapse secondary AC list , B2RTS3, B7ZMI4, O43798, Q4LE30, Q5CZ80, Q5JTX3, Q5JTX6, Q5JTX7, Q5JUC3, Q5JUC4, Q5VZ62, Q8N790
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM