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O75970

- MPDZ_HUMAN

UniProt

O75970 - MPDZ_HUMAN

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Protein

Multiple PDZ domain protein

Gene

MPDZ

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.By similarity2 Publications

GO - Molecular functioni

  1. 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.By similarity

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. apicolateral plasma membrane Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. cytoplasmic vesicle Source: Ensembl
  5. neuron projection Source: UniProtKB-KW
  6. postsynaptic membrane Source: UniProtKB-KW
  7. Schmidt-Lanterman incisure Source: Ensembl
  8. tight junction Source: UniProtKB-KW
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

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

BgeeiO75970.
ExpressionAtlasiO75970. baseline and differential.
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.By similarity7 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. 16 interactions.
IntActiO75970. 25 interactions.
MINTiMINT-275229.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75970.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6363L27PROSITE-ProRule annotationAdd
BLAST
Domaini137 – 22488PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini257 – 33781PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini377 – 46387PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini553 – 63482PDZ 4PROSITE-ProRule annotationAdd
BLAST
Domaini700 – 78687PDZ 5PROSITE-ProRule annotationAdd
BLAST
Domaini1008 – 108982PDZ 6PROSITE-ProRule annotationAdd
BLAST
Domaini1151 – 124393PDZ 7PROSITE-ProRule annotationAdd
BLAST
Domaini1350 – 143384PDZ 8PROSITE-ProRule annotationAdd
BLAST
Domaini1483 – 156482PDZ 9PROSITE-ProRule annotationAdd
BLAST
Domaini1629 – 171284PDZ 10PROSITE-ProRule annotationAdd
BLAST
Domaini1725 – 180783PDZ 11PROSITE-ProRule annotationAdd
BLAST
Domaini1862 – 194887PDZ 12PROSITE-ProRule annotationAdd
BLAST
Domaini1987 – 207084PDZ 13PROSITE-ProRule annotationAdd
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.By similarity3 Publications

Sequence similaritiesi

Contains 1 L27 domain.PROSITE-ProRule annotation
Contains 13 PDZ (DHR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG252837.
GeneTreeiENSGT00760000119017.
HOVERGENiHBG080134.
InParanoidiO75970.
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

        10         20         30         40         50
MLEAIDKNRA LHAAERLQTK LRERGDVANE DKLSLLKSVL QSPLFSQILS
60 70 80 90 100
LQTSVQQLKD QVNIATSATS NIEYAHVPHL SPAVIPTLQN ESFLLSPNNG
110 120 130 140 150
NLEALTGPGI PHINGKPACD EFDQLIKNMA QGRHVEVFEL LKPPSGGLGF
160 170 180 190 200
SVVGLRSENR GELGIFVQEI QEGSVAHRDG RLKETDQILA INGQALDQTI
210 220 230 240 250
THQQAISILQ KAKDTVQLVI ARGSLPQLVS PIVSRSPSAA STISAHSNPV
260 270 280 290 300
HWQHMETIEL VNDGSGLGFG IIGGKATGVI VKTILPGGVA DQHGRLCSGD
310 320 330 340 350
HILKIGDTDL AGMSSEQVAQ VLRQCGNRVK LMIARGAIEE RTAPTALGIT
360 370 380 390 400
LSSSPTSTPE LRVDASTQKG EESETFDVEL TKNVQGLGIT IAGYIGDKKL
410 420 430 440 450
EPSGIFVKSI TKSSAVEHDG RIQIGDQIIA VDGTNLQGFT NQQAVEVLRH
460 470 480 490 500
TGQTVLLTLM RRGMKQEAEL MSREDVTKDA DLSPVNASII KENYEKDEDF
510 520 530 540 550
LSSTRNTNIL PTEEEGYPLL SAEIEEIEDA QKQEAALLTK WQRIMGINYE
560 570 580 590 600
IVVAHVSKFS ENSGLGISLE ATVGHHFIRS VLPEGPVGHS GKLFSGDELL
610 620 630 640 650
EVNGITLLGE NHQDVVNILK ELPIEVTMVC CRRTVPPTTQ SELDSLDLCD
660 670 680 690 700
IELTEKPHVD LGEFIGSSET EDPVLAMTDA GQSTEEVQAP LAMWEAGIQH
710 720 730 740 750
IELEKGSKGL GFSILDYQDP IDPASTVIII RSLVPGGIAE KDGRLLPGDR
760 770 780 790 800
LMFVNDVNLE NSSLEEAVEA LKGAPSGTVR IGVAKPLPLS PEEGYVSAKE
810 820 830 840 850
DSFLYPPHSC EEAGLADKPL FRADLALVGT NDADLVDEST FESPYSPEND
860 870 880 890 900
SIYSTQASIL SLHGSSCGDG LNYGSSLPSS PPKDVIENSC DPVLDLHMSL
910 920 930 940 950
EELYTQNLLQ RQDENTPSVD ISMGPASGFT INDYTPANAI EQQYECENTI
960 970 980 990 1000
VWTESHLPSE VISSAELPSV LPDSAGKGSE YLLEQSSLAC NAECVMLQNV
1010 1020 1030 1040 1050
SKESFERTIN IAKGNSSLGM TVSANKDGLG MIVRSIIHGG AISRDGRIAI
1060 1070 1080 1090 1100
GDCILSINEE STISVTNAQA RAMLRRHSLI GPDIKITYVP AEHLEEFKIS
1110 1120 1130 1140 1150
LGQQSGRVMA LDIFSSYTGR DIPELPEREE GEGEESELQN TAYSNWNQPR
1160 1170 1180 1190 1200
RVELWREPSK SLGISIVGGR GMGSRLSNGE VMRGIFIKHV LEDSPAGKNG
1210 1220 1230 1240 1250
TLKPGDRIVE VDGMDLRDAS HEQAVEAIRK AGNPVVFMVQ SIINRPRKSP
1260 1270 1280 1290 1300
LPSLLHNLYP KYNFSSTNPF ADSLQINADK APSQSESEPE KAPLCSVPPP
1310 1320 1330 1340 1350
PPSAFAEMGS DHTQSSASKI SQDVDKEDEF GYSWKNIRER YGTLTGELHM
1360 1370 1380 1390 1400
IELEKGHSGL GLSLAGNKDR SRMSVFIVGI DPNGAAGKDG RLQIADELLE
1410 1420 1430 1440 1450
INGQILYGRS HQNASSIIKC APSKVKIIFI RNKDAVNQMA VCPGNAVEPL
1460 1470 1480 1490 1500
PSNSENLQNK ETEPTVTTSD AAVDLSSFKN VQHLELPKDQ GGLGIAISEE
1510 1520 1530 1540 1550
DTLSGVIIKS LTEHGVAATD GRLKVGDQIL AVDDEIVVGY PIEKFISLLK
1560 1570 1580 1590 1600
TAKMTVKLTI HAENPDSQAV PSAAGAASGE KKNSSQSLMV PQSGSPEPES
1610 1620 1630 1640 1650
IRNTSRSSTP AIFASDPATC PIIPGCETTI EISKGRTGLG LSIVGGSDTL
1660 1670 1680 1690 1700
LGAIIIHEVY EEGAACKDGR LWAGDQILEV NGIDLRKATH DEAINVLRQT
1710 1720 1730 1740 1750
PQRVRLTLYR DEAPYKEEEV CDTLTIELQK KPGKGLGLSI VGKRNDTGVF
1760 1770 1780 1790 1800
VSDIVKGGIA DADGRLMQGD QILMVNGEDV RNATQEAVAA LLKCSLGTVT
1810 1820 1830 1840 1850
LEVGRIKAGP FHSERRPSQS SQVSEGSLSS FTFPLSGSST SESLESSSKK
1860 1870 1880 1890 1900
NALASEIQGL RTVEMKKGPT DSLGISIAGG VGSPLGDVPI FIAMMHPTGV
1910 1920 1930 1940 1950
AAQTQKLRVG DRIVTICGTS TEGMTHTQAV NLLKNASGSI EMQVVAGGDV
1960 1970 1980 1990 2000
SVVTGHQQEP ASSSLSFTGL TSSSIFQDDL GPPQCKSITL ERGPDGLGFS
2010 2020 2030 2040 2050
IVGGYGSPHG DLPIYVKTVF AKGAASEDGR LKRGDQIIAV NGQSLEGVTH
2060 2070
EEAVAILKRT KGTVTLMVLS
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.Curated
The sequence BAC05409.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE06123.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAH71900.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI40490.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI40491.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI40492.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI40494.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI40495.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI41236.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI41237.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI41238.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI41240.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI56786.1 differs from that shown. Reason: Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1950 – 19501V → M in CAI56786. (PubMed:17974005)Curated

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. 1 PublicationVSP_040450Add
BLAST
Alternative sequencei1794 – 182229Missing in isoform 2 and isoform 4. 2 PublicationsVSP_040451Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
ENST00000381022; ENSP00000370410; ENSG00000107186. [O75970-3]
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 16 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 ]
ENST00000381022 ; ENSP00000370410 ; ENSG00000107186 . [O75970-3 ]
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.
GeneTreei ENSGT00760000119017.
HOVERGENi HBG080134.
InParanoidi O75970.
KOi K06095.
OrthoDBi EOG72ZCD0.
PhylomeDBi O75970.
TreeFami TF330709.

Miscellaneous databases

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

Gene expression databases

Bgeei O75970.
ExpressionAtlasi O75970. baseline and differential.
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: November 26, 2014
This is version 126 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