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

 MPDZ_HUMAN              Reviewed;        2070 AA.
O75970; A6NLC2; B2RTS3; B7ZMI4; O43798; Q4LE30; Q5CZ80; Q5JTX3;
Q5JTX6; Q5JTX7; Q5JUC3; Q5JUC4; Q5VZ62; Q8N790;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
12-SEP-2018, entry version 161.
RecName: Full=Multiple PDZ domain protein;
AltName: Full=Multi-PDZ domain protein 1;
Name=MPDZ; Synonyms=MUPP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Eng L., Krapivinsky G., Clapham D.E.;
"Human homolog of MUPP1 protein.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
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., 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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 573-2070 (ISOFORM 1).
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1535-2070 (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1618-2070 (ISOFORM 1), TISSUE
SPECIFICITY, INTERACTION WITH HTR2C, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=9537516; DOI=10.1016/S0014-5793(98)00141-0;
Ullmer C., Schmuck K., Figge A., Luebbert H.;
"Cloning and characterization of MUPP1, a novel PDZ domain protein.";
FEBS Lett. 424:63-68(1998).
[9]
INTERACTION WITH HUMAN ADENOVIRUS TYPE 9 E4-ORF1 PROTEIN (MICROBIAL
INFECTION) AND HUMAN PAPILLOMAVIRUS 18/HPV18 PROTEIN E6 (MICROBIAL
INFECTION).
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 HTR2A; HTR2B AND HTR2C, DOMAIN, AND FUNCTION.
PubMed=11150294; DOI=10.1074/jbc.M008089200;
Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J.,
Luebbert H., Ullmer C.;
"Interaction of serotonin 5-hydroxytryptamine type 2C receptors with
PDZ10 of the multi-PDZ domain protein MUPP1.";
J. Biol. Chem. 276:12974-12982(2001).
[11]
INTERACTION WITH PLEKHA1 AND PLEKHA2, AND DOMAIN.
PubMed=11802782; DOI=10.1042/0264-6021:3610525;
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.;
"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.";
Biochem. J. 361:525-536(2002).
[12]
INTERACTION WITH CXADR, AND SUBCELLULAR LOCATION.
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).
[13]
INTERACTION WITH CRB1, 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).
[14]
INTERACTION WITH SYNGAP1; CAMK2A AND CAMK2B, MUTAGENESIS OF
147-GLY--PHE-150, DOMAIN, AND FUNCTION.
PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase
activity and NMDA receptor-dependent synaptic AMPA receptor
potentiation.";
Neuron 43:563-574(2004).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
INVOLVEMENT IN HYC2.
PubMed=23240096; DOI=10.1136/jmedgenet-2012-101294;
Al-Dosari M.S., Al-Owain M., Tulbah M., Kurdi W., Adly N.,
Al-Hemidan A., Masoodi T.A., Albash B., Alkuraya F.S.;
"Mutation in MPDZ causes severe congenital hydrocephalus.";
J. Med. Genet. 50:54-58(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230 AND SER-483, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; SER-790; SER-1078
AND SER-1818, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
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, AND X-RAY
CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 1983-2070.
PubMed=17384233; DOI=10.1110/ps.062657507;
Elkins J.M., Papagrigoriou E., Berridge G., Yang X., Phillips C.,
Gileadi C., Savitsky P., Doyle D.A.;
"Structure of PICK1 and other PDZ domains obtained with the help of
self-binding C-terminal extensions.";
Protein Sci. 16:683-694(2007).
-!- 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. {ECO:0000250,
ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:15312654}.
-!- SUBUNIT: 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 DLL1 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q8VBX6, ECO:0000269|PubMed:11150294,
ECO:0000269|PubMed:11802782, ECO:0000269|PubMed:15312654,
ECO:0000269|PubMed:15316081, ECO:0000269|PubMed:15364909,
ECO:0000269|PubMed:9537516}.
-!- SUBUNIT: (Microbial infection) Interacts with human adenovirus
type 9 E4-ORF1 protein. {ECO:0000269|PubMed:11000240}.
-!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus
18/HPV18 protein E6. {ECO:0000269|PubMed:11000240}.
-!- INTERACTION:
Q9H205:OR2AG1; NbExp=8; IntAct=EBI-821405, EBI-7590304;
Q9HB21:PLEKHA1; NbExp=6; IntAct=EBI-821405, EBI-2652984;
Q9ERS5:Plekha2 (xeno); NbExp=5; IntAct=EBI-821405, EBI-8079166;
P32745:SSTR3; NbExp=5; IntAct=EBI-821405, EBI-6266935;
P04637:TP53; NbExp=3; IntAct=EBI-821405, EBI-366083;
-!- 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. Cell junction, synapse. Cell
junction, synapse, synaptosome. 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.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O75970-1; Sequence=Displayed;
Name=2;
IsoId=O75970-2; Sequence=VSP_040451;
Name=3;
IsoId=O75970-3; Sequence=VSP_040450;
Name=4;
IsoId=O75970-5; Sequence=VSP_040450, VSP_040451;
-!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, liver,
skeletal muscle, kidney and pancreas.
{ECO:0000269|PubMed:9537516}.
-!- 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. {ECO:0000250, ECO:0000269|PubMed:11150294,
ECO:0000269|PubMed:11802782, ECO:0000269|PubMed:15312654}.
-!- 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. {ECO:0000269|PubMed:23240096}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAC61870.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
Sequence=BAC05409.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE06123.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAI56786.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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EMBL; AF093419; AAC61870.1; ALT_SEQ; mRNA.
EMBL; AB210041; BAE06123.1; ALT_INIT; mRNA.
EMBL; AL161449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL162386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL353639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58704.1; -; Genomic_DNA.
EMBL; BC140793; AAI40794.1; -; mRNA.
EMBL; BC144564; AAI44565.1; -; mRNA.
EMBL; CR936648; CAI56786.1; ALT_SEQ; mRNA.
EMBL; AK098775; BAC05409.1; ALT_INIT; mRNA.
EMBL; AJ001319; CAA04680.1; -; mRNA.
CCDS; CCDS47951.1; -. [O75970-2]
CCDS; CCDS59119.1; -. [O75970-5]
CCDS; CCDS59120.1; -. [O75970-3]
CCDS; CCDS83342.1; -. [O75970-1]
RefSeq; NP_001248335.1; NM_001261406.1. [O75970-3]
RefSeq; NP_001248336.1; NM_001261407.1. [O75970-5]
RefSeq; NP_001317566.1; NM_001330637.1. [O75970-1]
RefSeq; NP_003820.2; NM_003829.4. [O75970-2]
RefSeq; XP_006716948.1; XM_006716885.3. [O75970-1]
RefSeq; XP_006716949.1; XM_006716886.3. [O75970-1]
RefSeq; XP_006716950.1; XM_006716887.3. [O75970-1]
RefSeq; XP_006716951.1; XM_006716888.3. [O75970-2]
RefSeq; XP_006716952.1; XM_006716889.3. [O75970-3]
RefSeq; XP_006716954.1; XM_006716891.3. [O75970-5]
RefSeq; XP_016870742.1; XM_017015253.1. [O75970-5]
UniGene; Hs.169378; -.
PDB; 2FCF; X-ray; 1.76 A; A=1148-1243.
PDB; 2FNE; X-ray; 1.83 A; A/B/C=1983-2070.
PDB; 2IWN; X-ray; 1.35 A; A=373-463.
PDB; 2IWO; X-ray; 1.70 A; A/B=1859-1951.
PDB; 2IWP; X-ray; 2.15 A; A/B=1859-1951.
PDB; 2IWQ; X-ray; 1.80 A; A=1148-1243.
PDB; 2O2T; X-ray; 2.70 A; A/B=117-227.
PDB; 2OPG; X-ray; 1.50 A; A/B=1625-1716.
PDB; 2QG1; X-ray; 1.40 A; A=1722-1806.
PDBsum; 2FCF; -.
PDBsum; 2FNE; -.
PDBsum; 2IWN; -.
PDBsum; 2IWO; -.
PDBsum; 2IWP; -.
PDBsum; 2IWQ; -.
PDBsum; 2O2T; -.
PDBsum; 2OPG; -.
PDBsum; 2QG1; -.
ProteinModelPortal; O75970; -.
SMR; O75970; -.
BioGrid; 114307; 36.
CORUM; O75970; -.
ELM; O75970; -.
IntAct; O75970; 37.
MINT; O75970; -.
STRING; 9606.ENSP00000370410; -.
iPTMnet; O75970; -.
PhosphoSitePlus; O75970; -.
BioMuta; MPDZ; -.
EPD; O75970; -.
MaxQB; O75970; -.
PaxDb; O75970; -.
PeptideAtlas; O75970; -.
PRIDE; O75970; -.
ProteomicsDB; 50330; -.
ProteomicsDB; 50331; -. [O75970-2]
ProteomicsDB; 50332; -. [O75970-3]
DNASU; 8777; -.
Ensembl; ENST00000319217; ENSP00000320006; ENSG00000107186. [O75970-1]
Ensembl; ENST00000381022; ENSP00000370410; ENSG00000107186. [O75970-3]
Ensembl; ENST00000447879; ENSP00000415208; ENSG00000107186. [O75970-3]
Ensembl; ENST00000536827; ENSP00000444151; ENSG00000107186. [O75970-5]
Ensembl; ENST00000541718; ENSP00000439807; ENSG00000107186. [O75970-2]
GeneID; 8777; -.
KEGG; hsa:8777; -.
UCSC; uc003zlb.5; human. [O75970-1]
CTD; 8777; -.
DisGeNET; 8777; -.
EuPathDB; HostDB:ENSG00000107186.16; -.
GeneCards; MPDZ; -.
H-InvDB; HIX0007919; -.
HGNC; HGNC:7208; MPDZ.
HPA; CAB013512; -.
HPA; HPA020255; -.
HPA; HPA026686; -.
MalaCards; MPDZ; -.
MIM; 603785; gene.
MIM; 615219; phenotype.
neXtProt; NX_O75970; -.
OpenTargets; ENSG00000107186; -.
Orphanet; 269505; Congenital communicating hydrocephalus.
PharmGKB; PA30914; -.
eggNOG; KOG3528; Eukaryota.
eggNOG; ENOG4110362; LUCA.
GeneTree; ENSGT00760000119017; -.
HOVERGEN; HBG080134; -.
InParanoid; O75970; -.
KO; K06095; -.
PhylomeDB; O75970; -.
TreeFam; TF330709; -.
ChiTaRS; MPDZ; human.
EvolutionaryTrace; O75970; -.
GeneWiki; MPDZ; -.
GenomeRNAi; 8777; -.
PRO; PR:O75970; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000107186; Expressed in 224 organ(s), highest expression level in corpus callosum.
ExpressionAtlas; O75970; baseline and differential.
Genevisible; O75970; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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; 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; Host-virus interaction; Membrane;
Methylation; Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
Reference proteome; Repeat; Synapse; Synaptosome; Tight junction.
CHAIN 1 2070 Multiple PDZ domain protein.
/FTId=PRO_0000094594.
DOMAIN 1 63 L27. {ECO:0000255|PROSITE-
ProRule:PRU00365}.
DOMAIN 137 224 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 257 337 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 377 463 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 553 634 PDZ 4. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 700 786 PDZ 5. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1008 1089 PDZ 6. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1151 1243 PDZ 7. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1350 1433 PDZ 8. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1483 1564 PDZ 9. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1629 1712 PDZ 10. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1725 1807 PDZ 11. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1862 1948 PDZ 12. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1987 2070 PDZ 13. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
COMPBIAS 1818 1848 Ser-rich.
MOD_RES 230 230 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1078 1078 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1170 1170 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8VBX6}.
MOD_RES 1818 1818 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1824 1824 Phosphoserine.
{ECO:0000250|UniProtKB:O55164}.
VAR_SEQ 1248 1280 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040450.
VAR_SEQ 1794 1822 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_040451.
VARIANT 92 92 S -> L (in dbSNP:rs17273542).
/FTId=VAR_056115.
VARIANT 351 351 L -> F (in dbSNP:rs3739757).
/FTId=VAR_056116.
VARIANT 702 702 E -> K (in dbSNP:rs4741289).
/FTId=VAR_056117.
VARIANT 702 702 E -> V (in dbSNP:rs4740548).
/FTId=VAR_056118.
VARIANT 1604 1604 T -> A (in dbSNP:rs16930134).
/FTId=VAR_056119.
VARIANT 1663 1663 G -> R (in dbSNP:rs2274648).
/FTId=VAR_056120.
MUTAGEN 147 150 GLGF->PSES: Loss of interaction with
CAMK2A. {ECO:0000269|PubMed:15312654}.
CONFLICT 1950 1950 V -> M (in Ref. 6; CAI56786).
{ECO:0000305}.
HELIX 120 130 {ECO:0000244|PDB:2O2T}.
STRAND 135 141 {ECO:0000244|PDB:2O2T}.
STRAND 144 146 {ECO:0000244|PDB:2O2T}.
STRAND 152 156 {ECO:0000244|PDB:2O2T}.
STRAND 163 167 {ECO:0000244|PDB:2O2T}.
HELIX 175 179 {ECO:0000244|PDB:2O2T}.
STRAND 187 191 {ECO:0000244|PDB:2O2T}.
HELIX 202 211 {ECO:0000244|PDB:2O2T}.
STRAND 214 223 {ECO:0000244|PDB:2O2T}.
STRAND 373 381 {ECO:0000244|PDB:2IWN}.
STRAND 389 392 {ECO:0000244|PDB:2IWN}.
STRAND 406 410 {ECO:0000244|PDB:2IWN}.
HELIX 415 419 {ECO:0000244|PDB:2IWN}.
STRAND 427 431 {ECO:0000244|PDB:2IWN}.
HELIX 441 449 {ECO:0000244|PDB:2IWN}.
STRAND 453 463 {ECO:0000244|PDB:2IWN}.
STRAND 1150 1154 {ECO:0000244|PDB:2FCF}.
STRAND 1164 1167 {ECO:0000244|PDB:2FCF}.
STRAND 1185 1190 {ECO:0000244|PDB:2FCF}.
STRAND 1192 1194 {ECO:0000244|PDB:2FCF}.
HELIX 1195 1199 {ECO:0000244|PDB:2FCF}.
STRAND 1207 1211 {ECO:0000244|PDB:2FCF}.
HELIX 1221 1229 {ECO:0000244|PDB:2FCF}.
STRAND 1233 1240 {ECO:0000244|PDB:2FCF}.
STRAND 1626 1633 {ECO:0000244|PDB:2OPG}.
STRAND 1641 1645 {ECO:0000244|PDB:2OPG}.
STRAND 1653 1659 {ECO:0000244|PDB:2OPG}.
HELIX 1664 1668 {ECO:0000244|PDB:2OPG}.
STRAND 1676 1680 {ECO:0000244|PDB:2OPG}.
HELIX 1690 1698 {ECO:0000244|PDB:2OPG}.
STRAND 1702 1710 {ECO:0000244|PDB:2OPG}.
STRAND 1723 1729 {ECO:0000244|PDB:2QG1}.
STRAND 1737 1741 {ECO:0000244|PDB:2QG1}.
STRAND 1744 1746 {ECO:0000244|PDB:2QG1}.
STRAND 1750 1754 {ECO:0000244|PDB:2QG1}.
HELIX 1759 1763 {ECO:0000244|PDB:2QG1}.
STRAND 1771 1775 {ECO:0000244|PDB:2QG1}.
HELIX 1785 1794 {ECO:0000244|PDB:2QG1}.
STRAND 1797 1804 {ECO:0000244|PDB:2QG1}.
STRAND 1861 1866 {ECO:0000244|PDB:2IWO}.
TURN 1869 1871 {ECO:0000244|PDB:2IWO}.
STRAND 1875 1883 {ECO:0000244|PDB:2IWO}.
STRAND 1886 1895 {ECO:0000244|PDB:2IWO}.
HELIX 1900 1904 {ECO:0000244|PDB:2IWO}.
STRAND 1912 1916 {ECO:0000244|PDB:2IWO}.
HELIX 1926 1935 {ECO:0000244|PDB:2IWO}.
STRAND 1938 1945 {ECO:0000244|PDB:2IWO}.
STRAND 1984 1990 {ECO:0000244|PDB:2FNE}.
STRAND 1998 2007 {ECO:0000244|PDB:2FNE}.
STRAND 2010 2019 {ECO:0000244|PDB:2FNE}.
HELIX 2024 2028 {ECO:0000244|PDB:2FNE}.
STRAND 2036 2040 {ECO:0000244|PDB:2FNE}.
HELIX 2050 2059 {ECO:0000244|PDB:2FNE}.
STRAND 2062 2070 {ECO:0000244|PDB:2FNE}.
SEQUENCE 2070 AA; 221618 MW; A4D304C20401FD45 CRC64;
MLEAIDKNRA LHAAERLQTK LRERGDVANE DKLSLLKSVL QSPLFSQILS LQTSVQQLKD
QVNIATSATS NIEYAHVPHL SPAVIPTLQN ESFLLSPNNG NLEALTGPGI PHINGKPACD
EFDQLIKNMA QGRHVEVFEL LKPPSGGLGF SVVGLRSENR GELGIFVQEI QEGSVAHRDG
RLKETDQILA INGQALDQTI THQQAISILQ KAKDTVQLVI ARGSLPQLVS PIVSRSPSAA
STISAHSNPV HWQHMETIEL VNDGSGLGFG IIGGKATGVI VKTILPGGVA DQHGRLCSGD
HILKIGDTDL AGMSSEQVAQ VLRQCGNRVK LMIARGAIEE RTAPTALGIT LSSSPTSTPE
LRVDASTQKG EESETFDVEL TKNVQGLGIT IAGYIGDKKL EPSGIFVKSI TKSSAVEHDG
RIQIGDQIIA VDGTNLQGFT NQQAVEVLRH TGQTVLLTLM RRGMKQEAEL MSREDVTKDA
DLSPVNASII KENYEKDEDF LSSTRNTNIL PTEEEGYPLL SAEIEEIEDA QKQEAALLTK
WQRIMGINYE IVVAHVSKFS ENSGLGISLE ATVGHHFIRS VLPEGPVGHS GKLFSGDELL
EVNGITLLGE NHQDVVNILK ELPIEVTMVC CRRTVPPTTQ SELDSLDLCD IELTEKPHVD
LGEFIGSSET EDPVLAMTDA GQSTEEVQAP LAMWEAGIQH IELEKGSKGL GFSILDYQDP
IDPASTVIII RSLVPGGIAE KDGRLLPGDR LMFVNDVNLE NSSLEEAVEA LKGAPSGTVR
IGVAKPLPLS PEEGYVSAKE DSFLYPPHSC EEAGLADKPL FRADLALVGT NDADLVDEST
FESPYSPEND SIYSTQASIL SLHGSSCGDG LNYGSSLPSS PPKDVIENSC DPVLDLHMSL
EELYTQNLLQ RQDENTPSVD ISMGPASGFT INDYTPANAI EQQYECENTI VWTESHLPSE
VISSAELPSV LPDSAGKGSE YLLEQSSLAC NAECVMLQNV SKESFERTIN IAKGNSSLGM
TVSANKDGLG MIVRSIIHGG AISRDGRIAI GDCILSINEE STISVTNAQA RAMLRRHSLI
GPDIKITYVP AEHLEEFKIS LGQQSGRVMA LDIFSSYTGR DIPELPEREE GEGEESELQN
TAYSNWNQPR RVELWREPSK SLGISIVGGR GMGSRLSNGE VMRGIFIKHV LEDSPAGKNG
TLKPGDRIVE VDGMDLRDAS HEQAVEAIRK AGNPVVFMVQ SIINRPRKSP LPSLLHNLYP
KYNFSSTNPF ADSLQINADK APSQSESEPE KAPLCSVPPP PPSAFAEMGS DHTQSSASKI
SQDVDKEDEF GYSWKNIRER YGTLTGELHM IELEKGHSGL GLSLAGNKDR SRMSVFIVGI
DPNGAAGKDG RLQIADELLE INGQILYGRS HQNASSIIKC APSKVKIIFI RNKDAVNQMA
VCPGNAVEPL PSNSENLQNK ETEPTVTTSD AAVDLSSFKN VQHLELPKDQ GGLGIAISEE
DTLSGVIIKS LTEHGVAATD GRLKVGDQIL AVDDEIVVGY PIEKFISLLK TAKMTVKLTI
HAENPDSQAV PSAAGAASGE KKNSSQSLMV PQSGSPEPES IRNTSRSSTP AIFASDPATC
PIIPGCETTI EISKGRTGLG LSIVGGSDTL LGAIIIHEVY EEGAACKDGR LWAGDQILEV
NGIDLRKATH DEAINVLRQT PQRVRLTLYR DEAPYKEEEV CDTLTIELQK KPGKGLGLSI
VGKRNDTGVF VSDIVKGGIA DADGRLMQGD QILMVNGEDV RNATQEAVAA LLKCSLGTVT
LEVGRIKAGP FHSERRPSQS SQVSEGSLSS FTFPLSGSST SESLESSSKK NALASEIQGL
RTVEMKKGPT DSLGISIAGG VGSPLGDVPI FIAMMHPTGV AAQTQKLRVG DRIVTICGTS
TEGMTHTQAV NLLKNASGSI EMQVVAGGDV SVVTGHQQEP ASSSLSFTGL TSSSIFQDDL
GPPQCKSITL ERGPDGLGFS IVGGYGSPHG DLPIYVKTVF AKGAASEDGR LKRGDQIIAV
NGQSLEGVTH EEAVAILKRT KGTVTLMVLS


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