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O75970

- MPDZ_HUMAN

UniProt

O75970 - MPDZ_HUMAN

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Protein

Multiple PDZ domain protein

Gene
MPDZ, MUPP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein C-terminus binding Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: Ensembl
  2. myelination Source: Ensembl
  3. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Names & Taxonomyi

Protein namesi
Recommended name:
Multiple PDZ domain protein
Alternative name(s):
Multi-PDZ domain protein 1
Gene namesi
Name:MPDZ
Synonyms:MUPP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:7208. MPDZ.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB-SubCell
  2. apicolateral plasma membrane Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. cytoplasmic vesicle Source: Ensembl
  5. dendrite Source: UniProtKB-SubCell
  6. postsynaptic density Source: UniProtKB-SubCell
  7. postsynaptic membrane Source: UniProtKB-KW
  8. Schmidt-Lanterman incisure Source: Ensembl
  9. tight junction Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome, Tight junction

Pathology & Biotechi

Involvement in diseasei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi147 – 1504GLGF → PSES: Loss of interaction with CAMK2A. 1 Publication

Organism-specific databases

MIMi615219. phenotype.
Orphaneti269505. Congenital communicating hydrocephalus.
PharmGKBiPA30914.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20702070Multiple PDZ domain proteinPRO_0000094594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei230 – 2301Phosphoserine1 Publication
Modified residuei483 – 4831Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75970.
PaxDbiO75970.
PRIDEiO75970.

PTM databases

PhosphoSiteiO75970.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

ArrayExpressiO75970.
BgeeiO75970.
GenevestigatoriO75970.

Organism-specific databases

HPAiCAB013512.
HPA020255.
HPA026686.

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OR2AG1Q9H2058EBI-821405,EBI-7590304
PLEKHA1Q9HB216EBI-821405,EBI-2652984
Plekha2Q9ERS55EBI-821405,EBI-8079166From a different organism.
SSTR3P327455EBI-821405,EBI-6266935
TP53P046373EBI-821405,EBI-366083

Protein-protein interaction databases

BioGridi114307. 14 interactions.
IntActiO75970. 25 interactions.
MINTiMINT-275229.

Structurei

Secondary structure

1
2070
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi120 – 13011
Beta strandi135 – 1417
Beta strandi144 – 1463
Beta strandi152 – 1565
Beta strandi163 – 1675
Helixi175 – 1795
Beta strandi187 – 1915
Helixi202 – 21110
Beta strandi214 – 22310
Beta strandi373 – 3819
Beta strandi389 – 3924
Beta strandi406 – 4105
Helixi415 – 4195
Beta strandi427 – 4315
Helixi441 – 4499
Beta strandi453 – 46311
Beta strandi1150 – 11545
Beta strandi1164 – 11674
Beta strandi1185 – 11906
Beta strandi1192 – 11943
Helixi1195 – 11995
Beta strandi1207 – 12115
Helixi1221 – 12299
Beta strandi1233 – 12408
Beta strandi1626 – 16338
Beta strandi1641 – 16455
Beta strandi1653 – 16597
Helixi1664 – 16685
Beta strandi1676 – 16805
Helixi1690 – 16989
Beta strandi1702 – 17109
Beta strandi1723 – 17297
Beta strandi1737 – 17415
Beta strandi1744 – 17463
Beta strandi1750 – 17545
Helixi1759 – 17635
Beta strandi1771 – 17755
Helixi1785 – 179410
Beta strandi1797 – 18048
Beta strandi1861 – 18666
Beta strandi1875 – 18839
Beta strandi1886 – 189510
Helixi1900 – 19045
Beta strandi1912 – 19165
Helixi1926 – 193510
Beta strandi1938 – 19458
Beta strandi1984 – 19907
Beta strandi1998 – 200710
Beta strandi2010 – 201910
Helixi2024 – 20285
Beta strandi2036 – 20405
Helixi2050 – 205910
Beta strandi2062 – 20709

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO75970.
SMRiO75970. Positions 119-227, 373-463, 1148-1244, 1331-1446, 1625-1716, 1722-1806, 1859-1951, 1983-2070.

Miscellaneous databases

EvolutionaryTraceiO75970.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6363L27Add
BLAST
Domaini137 – 22488PDZ 1Add
BLAST
Domaini257 – 33781PDZ 2Add
BLAST
Domaini377 – 46387PDZ 3Add
BLAST
Domaini553 – 63482PDZ 4Add
BLAST
Domaini700 – 78687PDZ 5Add
BLAST
Domaini1008 – 108982PDZ 6Add
BLAST
Domaini1151 – 124393PDZ 7Add
BLAST
Domaini1350 – 143384PDZ 8Add
BLAST
Domaini1483 – 156482PDZ 9Add
BLAST
Domaini1629 – 171284PDZ 10Add
BLAST
Domaini1725 – 180783PDZ 11Add
BLAST
Domaini1862 – 194887PDZ 12Add
BLAST
Domaini1987 – 207084PDZ 13Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1818 – 184831Ser-richAdd
BLAST

Domaini

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 SYNGAP1.3 Publications

Sequence similaritiesi

Contains 1 L27 domain.
Contains 13 PDZ (DHR) domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG252837.
HOVERGENiHBG080134.
KOiK06095.
OrthoDBiEOG72ZCD0.
PhylomeDBiO75970.
TreeFamiTF330709.

Family and domain databases

Gene3Di2.30.42.10. 13 hits.
InterProiIPR004172. L27.
IPR015132. L27_2.
IPR001478. PDZ.
[Graphical view]
PfamiPF09045. L27_2. 1 hit.
PF00595. PDZ. 13 hits.
[Graphical view]
SMARTiSM00569. L27. 1 hit.
SM00228. PDZ. 13 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 13 hits.
PROSITEiPS51022. L27. 1 hit.
PS50106. PDZ. 13 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75970-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MLEAIDKNRA LHAAERLQTK LRERGDVANE DKLSLLKSVL QSPLFSQILS     50
LQTSVQQLKD QVNIATSATS NIEYAHVPHL SPAVIPTLQN ESFLLSPNNG 100
NLEALTGPGI PHINGKPACD EFDQLIKNMA QGRHVEVFEL LKPPSGGLGF 150
SVVGLRSENR GELGIFVQEI QEGSVAHRDG RLKETDQILA INGQALDQTI 200
THQQAISILQ KAKDTVQLVI ARGSLPQLVS PIVSRSPSAA STISAHSNPV 250
HWQHMETIEL VNDGSGLGFG IIGGKATGVI VKTILPGGVA DQHGRLCSGD 300
HILKIGDTDL AGMSSEQVAQ VLRQCGNRVK LMIARGAIEE RTAPTALGIT 350
LSSSPTSTPE LRVDASTQKG EESETFDVEL TKNVQGLGIT IAGYIGDKKL 400
EPSGIFVKSI TKSSAVEHDG RIQIGDQIIA VDGTNLQGFT NQQAVEVLRH 450
TGQTVLLTLM RRGMKQEAEL MSREDVTKDA DLSPVNASII KENYEKDEDF 500
LSSTRNTNIL PTEEEGYPLL SAEIEEIEDA QKQEAALLTK WQRIMGINYE 550
IVVAHVSKFS ENSGLGISLE ATVGHHFIRS VLPEGPVGHS GKLFSGDELL 600
EVNGITLLGE NHQDVVNILK ELPIEVTMVC CRRTVPPTTQ SELDSLDLCD 650
IELTEKPHVD LGEFIGSSET EDPVLAMTDA GQSTEEVQAP LAMWEAGIQH 700
IELEKGSKGL GFSILDYQDP IDPASTVIII RSLVPGGIAE KDGRLLPGDR 750
LMFVNDVNLE NSSLEEAVEA LKGAPSGTVR IGVAKPLPLS PEEGYVSAKE 800
DSFLYPPHSC EEAGLADKPL FRADLALVGT NDADLVDEST FESPYSPEND 850
SIYSTQASIL SLHGSSCGDG LNYGSSLPSS PPKDVIENSC DPVLDLHMSL 900
EELYTQNLLQ RQDENTPSVD ISMGPASGFT INDYTPANAI EQQYECENTI 950
VWTESHLPSE VISSAELPSV LPDSAGKGSE YLLEQSSLAC NAECVMLQNV 1000
SKESFERTIN IAKGNSSLGM TVSANKDGLG MIVRSIIHGG AISRDGRIAI 1050
GDCILSINEE STISVTNAQA RAMLRRHSLI GPDIKITYVP AEHLEEFKIS 1100
LGQQSGRVMA LDIFSSYTGR DIPELPEREE GEGEESELQN TAYSNWNQPR 1150
RVELWREPSK SLGISIVGGR GMGSRLSNGE VMRGIFIKHV LEDSPAGKNG 1200
TLKPGDRIVE VDGMDLRDAS HEQAVEAIRK AGNPVVFMVQ SIINRPRKSP 1250
LPSLLHNLYP KYNFSSTNPF ADSLQINADK APSQSESEPE KAPLCSVPPP 1300
PPSAFAEMGS DHTQSSASKI SQDVDKEDEF GYSWKNIRER YGTLTGELHM 1350
IELEKGHSGL GLSLAGNKDR SRMSVFIVGI DPNGAAGKDG RLQIADELLE 1400
INGQILYGRS HQNASSIIKC APSKVKIIFI RNKDAVNQMA VCPGNAVEPL 1450
PSNSENLQNK ETEPTVTTSD AAVDLSSFKN VQHLELPKDQ GGLGIAISEE 1500
DTLSGVIIKS LTEHGVAATD GRLKVGDQIL AVDDEIVVGY PIEKFISLLK 1550
TAKMTVKLTI HAENPDSQAV PSAAGAASGE KKNSSQSLMV PQSGSPEPES 1600
IRNTSRSSTP AIFASDPATC PIIPGCETTI EISKGRTGLG LSIVGGSDTL 1650
LGAIIIHEVY EEGAACKDGR LWAGDQILEV NGIDLRKATH DEAINVLRQT 1700
PQRVRLTLYR DEAPYKEEEV CDTLTIELQK KPGKGLGLSI VGKRNDTGVF 1750
VSDIVKGGIA DADGRLMQGD QILMVNGEDV RNATQEAVAA LLKCSLGTVT 1800
LEVGRIKAGP FHSERRPSQS SQVSEGSLSS FTFPLSGSST SESLESSSKK 1850
NALASEIQGL RTVEMKKGPT DSLGISIAGG VGSPLGDVPI FIAMMHPTGV 1900
AAQTQKLRVG DRIVTICGTS TEGMTHTQAV NLLKNASGSI EMQVVAGGDV 1950
SVVTGHQQEP ASSSLSFTGL TSSSIFQDDL GPPQCKSITL ERGPDGLGFS 2000
IVGGYGSPHG DLPIYVKTVF AKGAASEDGR LKRGDQIIAV NGQSLEGVTH 2050
EEAVAILKRT KGTVTLMVLS 2070
Length:2,070
Mass (Da):221,618
Last modified:January 11, 2011 - v2
Checksum:iA4D304C20401FD45
GO
Isoform 2 (identifier: O75970-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,041
Mass (Da):218,507
Checksum:i03736D2490F3E2C7
GO
Isoform 3 (identifier: O75970-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,037
Mass (Da):217,915
Checksum:i99D1557E87DECAE9
GO
Isoform 4 (identifier: O75970-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,008
Mass (Da):214,804
Checksum:iC0EBEA38A7020807
GO

Sequence cautioni

The sequence AAC61870.1 differs from that shown. Reason: Aberrant splicing.
The sequence CAI56786.1 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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921S → L.
Corresponds to variant rs17273542 [ dbSNP | Ensembl ].
VAR_056115
Natural varianti351 – 3511L → F.
Corresponds to variant rs3739757 [ dbSNP | Ensembl ].
VAR_056116
Natural varianti702 – 7021E → K.
Corresponds to variant rs4741289 [ dbSNP | Ensembl ].
VAR_056117
Natural varianti702 – 7021E → V.
Corresponds to variant rs4740548 [ dbSNP | Ensembl ].
VAR_056118
Natural varianti1604 – 16041T → A.
Corresponds to variant rs16930134 [ dbSNP | Ensembl ].
VAR_056119
Natural varianti1663 – 16631G → R.
Corresponds to variant rs2274648 [ dbSNP | Ensembl ].
VAR_056120

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1248 – 128033Missing in isoform 3 and isoform 4. VSP_040450Add
BLAST
Alternative sequencei1794 – 182229Missing in isoform 2 and isoform 4. VSP_040451Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1950 – 19501V → M in CAI56786. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS47951.1. [O75970-2]
CCDS59119.1. [O75970-5]
CCDS59120.1. [O75970-3]
RefSeqiNP_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]
UniGeneiHs.169378.

Genome annotation databases

EnsembliENST00000319217; 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]
GeneIDi8777.
KEGGihsa:8777.
UCSCiuc003zlb.4. human. [O75970-2]
uc010mhz.4. human. [O75970-3]
uc010mia.1. human. [O75970-1]
uc011lmn.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS47951.1. [O75970-2 ]
CCDS59119.1. [O75970-5 ]
CCDS59120.1. [O75970-3 ]
RefSeqi NP_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 ]
UniGenei Hs.169378.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FCF X-ray 1.76 A 1148-1243 [» ]
2FNE X-ray 1.83 A/B/C 1983-2070 [» ]
2IWN X-ray 1.35 A 373-463 [» ]
2IWO X-ray 1.70 A/B 1859-1951 [» ]
2IWP X-ray 2.15 A/B 1859-1951 [» ]
2IWQ X-ray 1.80 A 1148-1243 [» ]
2O2T X-ray 2.70 A/B 117-227 [» ]
2OPG X-ray 1.50 A/B 1625-1716 [» ]
2QG1 X-ray 1.40 A 1722-1806 [» ]
ProteinModelPortali O75970.
SMRi O75970. Positions 119-227, 373-463, 1148-1244, 1331-1446, 1625-1716, 1722-1806, 1859-1951, 1983-2070.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114307. 14 interactions.
IntActi O75970. 25 interactions.
MINTi MINT-275229.

PTM databases

PhosphoSitei O75970.

Proteomic databases

MaxQBi O75970.
PaxDbi O75970.
PRIDEi O75970.

Protocols and materials databases

DNASUi 8777.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319217 ; 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 ]
GeneIDi 8777.
KEGGi hsa:8777.
UCSCi uc003zlb.4. human. [O75970-2 ]
uc010mhz.4. human. [O75970-3 ]
uc010mia.1. human. [O75970-1 ]
uc011lmn.3. human.

Organism-specific databases

CTDi 8777.
GeneCardsi GC09M013095.
H-InvDB HIX0007919.
HGNCi HGNC:7208. MPDZ.
HPAi CAB013512.
HPA020255.
HPA026686.
MIMi 603785. gene.
615219. phenotype.
neXtProti NX_O75970.
Orphaneti 269505. Congenital communicating hydrocephalus.
PharmGKBi PA30914.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG252837.
HOVERGENi HBG080134.
KOi K06095.
OrthoDBi EOG72ZCD0.
PhylomeDBi O75970.
TreeFami TF330709.

Miscellaneous databases

EvolutionaryTracei O75970.
GeneWikii MPDZ.
GenomeRNAii 8777.
NextBioi 32912.
PROi O75970.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75970.
Bgeei O75970.
Genevestigatori O75970.

Family and domain databases

Gene3Di 2.30.42.10. 13 hits.
InterProi IPR004172. L27.
IPR015132. L27_2.
IPR001478. PDZ.
[Graphical view ]
Pfami PF09045. L27_2. 1 hit.
PF00595. PDZ. 13 hits.
[Graphical view ]
SMARTi SM00569. L27. 1 hit.
SM00228. PDZ. 13 hits.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 13 hits.
PROSITEi PS51022. L27. 1 hit.
PS50106. PDZ. 13 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. 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.

Entry informationi

Entry nameiMPDZ_HUMAN
AccessioniPrimary (citable) accession number: O75970
Secondary accession number(s): A6NLC2
, B2RTS3, B7ZMI4, O43798, Q4LE30, Q5CZ80, Q5JTX3, Q5JTX6, Q5JTX7, Q5JUC3, Q5JUC4, Q5VZ62, Q8N790
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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