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Q8N3R9 (MPP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MAGUK p55 subfamily member 5
Gene names
Name:MPP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length675 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in tight junctions biogenesis and in the establishment of cell polarity in epithelial cells. May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter. Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton By similarity.

Subunit structure

Interacts with CRB3, LIN7C and MPDZ. Interacts with INADL, PARD6B, SC6A1 and EZR By similarity. Forms a complex with CRB1 and MPP4. Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Heterodimer with MPP1. Interacts with MPP7. Ref.7 Ref.8 Ref.11 Ref.12

Subcellular location

Cell membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Cell junctiontight junction. Note: Localized to the tight junctions of epithelial cells and a subset of intracellular vesicles. In the retina, detected at the outer limiting membrane (OLM), apical to the adherens junction (AJ), where it colocalizes with CRB1. Colocalizes with MPP1 in the retina at the outer limiting membrane (OLM). Localized to the Purkinje cell body and axon. Ref.5 Ref.12

Tissue specificity

Expressed in the retina (at protein level). Ref.5 Ref.6

Domain

The L27 domain 1 functions in targeting to the tight junctions by binding to INADL By similarity.

The PDZ domain binds to the C-terminus of SC6A1 By similarity.

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 2 L27 domains.

Contains 1 PDZ (DHR) domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAH53366.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAB14172.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Membrane
Tight junction
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH3 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell junction assembly

Traceable author statement. Source: Reactome

cell-cell junction organization

Traceable author statement. Source: Reactome

establishment of protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

myelin assembly

Inferred from electronic annotation. Source: Ensembl

peripheral nervous system myelin maintenance

Inferred from electronic annotation. Source: Ensembl

protein localization to myelin sheath abaxonal region

Inferred from electronic annotation. Source: Ensembl

tight junction assembly

Traceable author statement. Source: Reactome

   Cellular_componentSchmidt-Lanterman incisure

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: LIFEdb

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

lateral loop

Inferred from electronic annotation. Source: Ensembl

myelin sheath adaxonal region

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

protein complex

Inferred from electronic annotation. Source: Ensembl

tight junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein domain specific binding

Inferred from physical interaction Ref.8. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

INADLQ8NI354EBI-2513978,EBI-724390

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N3R9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N3R9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 675675MAGUK p55 subfamily member 5
PRO_0000094580

Regions

Domain120 – 17758L27 1
Domain179 – 23557L27 2
Domain256 – 33681PDZ
Domain345 – 41773SH3
Domain479 – 660182Guanylate kinase-like
Region21 – 140120Interaction with PARD6B By similarity
Region181 – 24363Interaction with LIN7C By similarity

Amino acid modifications

Modified residue251Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 3434Missing in isoform 2.
VSP_014002

Experimental info

Sequence conflict1001D → G in CAD38620. Ref.1
Sequence conflict1411S → Y in CAD89937. Ref.1
Sequence conflict1611N → S in BAC05295. Ref.4
Sequence conflict3241M → L in BAC05295. Ref.4
Sequence conflict4011Q → H in CAD89937. Ref.1
Sequence conflict4601N → H in CAD89937. Ref.1
Sequence conflict4901C → F in BAB14172. Ref.4
Sequence conflict6131G → V in CAD38620. Ref.1
Sequence conflict6341N → S in CAD38620. Ref.1

Secondary structure

............... 675
Helix Strand Turn

Details...

Sequences

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

Last modified October 17, 2006. Version 3.
Checksum: A3B2CB594E0908CA

FASTA67577,294
        10         20         30         40         50         60 
MTTSHMNGHV TEESDSEVKN VDLASPEEHQ KHREMAVDCP GDLGTRMMPI RRSAQLERIR 

        70         80         90        100        110        120 
QQQEDMRRRR EEEGKKQELD LNSSMRLKKL AQIPPKTGID NPMFDTEEGI VLESPHYAVK 

       130        140        150        160        170        180 
ILEIEDLFSS LKHIQHTLVD SQSQEDISLL LQLVQNKDFQ NAFKIHNAIT VHMNKASPPF 

       190        200        210        220        230        240 
PLISNAQDLA QEVQTVLKPV HHKEGQELTA LLNTPHIQAL LLAHDKVAEQ EMQLEPITDE 

       250        260        270        280        290        300 
RVYESIGQYG GETVKIVRIE KARDIPLGAT VRNEMDSVII SRIVKGGAAE KSGLLHEGDE 

       310        320        330        340        350        360 
VLEINGIEIR GKDVNEVFDL LSDMHGTLTF VLIPSQQIKP PPAKETVIHV KAHFDYDPSD 

       370        380        390        400        410        420 
DPYVPCRELG LSFQKGDILH VISQEDPNWW QAYREGDEDN QPLAGLVPGK SFQQQREAMK 

       430        440        450        460        470        480 
QTIEEDKEPE KSGKLWCAKK NKKKRKKVLY NANKNDDYDN EEILTYEEMS LYHQPANRKR 

       490        500        510        520        530        540 
PIILIGPQNC GQNELRQRLM NKEKDRFASA VPHTTRSRRD QEVAGRDYHF VSRQAFEADI 

       550        560        570        580        590        600 
AAGKFIEHGE FEKNLYGTSI DSVRQVINSG KICLLSLRTQ SLKTLRNSDL KPYIIFIAPP 

       610        620        630        640        650        660 
SQERLRALLA KEGKNPKPEE LREIIEKTRE MEQNNGHYFD TAIVNSDLDK AYQELLRLIN 

       670 
KLDTEPQWVP STWLR 

« Hide

Isoform 2 [UniParc].

Checksum: AD604D26B3580FDB
Show »

FASTA64173,421

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Skeletal muscle and Spinal cord.
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-441 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-675.
Tissue: Brain.
[5]"MPP5 recruits MPP4 to the CRB1 complex in photoreceptors."
Kantardzhieva A., Gosens I., Alexeeva S., Punte I.M., Versteeg I., Krieger E., Neefjes-Mol C.A., den Hollander A.I., Letteboer S.J.F., Klooster J., Cremers F.P.M., Roepman R., Wijnholds J.
Invest. Ophthalmol. Vis. Sci. 46:2192-2201(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPLEX FORMATION WITH CRB1 AND MPP4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"Membrane-associated guanylate kinase proteins MPP4 and MPP5 associate with Veli3 at distinct intercellular junctions of the neurosensory retina."
Stoehr H., Molday L.L., Molday R.S., Weber B.H.F., Biedermann B., Reichenbach A., Kraemer F.
J. Comp. Neurol. 481:31-41(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ARHGAP17; AMOT; INADL AND PARD3, INTERACTION WITH MPP7.
[8]"The MAGUK protein MPP7 binds to the polarity protein hDlg1 and facilitates epithelial tight junction formation."
Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A.
Mol. Biol. Cell 18:1744-1755(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPP7.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins."
Feng W., Long J.-F., Zhang M.
Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 118-177, INTERACTION WITH MPDZ.
[12]"MPP1 links the Usher protein network and the Crumbs protein complex in the retina."
Gosens I., van Wijk E., Kersten F.F., Krieger E., van der Zwaag B., Maerker T., Letteboer S.J., Dusseljee S., Peters T., Spierenburg H.A., Punte I.M., Wolfrum U., Cremers F.P.M., Kremer H., Roepman R.
Hum. Mol. Genet. 16:1993-2003(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPP1, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL832326 mRNA. Translation: CAD38620.1.
AL832578 mRNA. Translation: CAD89937.1.
CH471061 Genomic DNA. Translation: EAW80930.1.
BC053366 mRNA. Translation: AAH53366.1. Sequence problems.
BC129933 mRNA. Translation: AAI29934.1.
AK022677 mRNA. Translation: BAB14172.1. Different initiation.
AK098373 mRNA. Translation: BAC05295.1.
RefSeqNP_001243479.1. NM_001256550.1.
NP_071919.2. NM_022474.3.
XP_005268060.1. XM_005268003.1.
UniGeneHs.652312.
Hs.740524.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y76NMR-B/D118-177[»]
3UITX-ray2.05A/B/C/D119-232[»]
ProteinModelPortalQ8N3R9.
SMRQ8N3R9. Positions 61-337, 349-671.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122155. 14 interactions.
IntActQ8N3R9. 18 interactions.
MINTMINT-1772982.
STRING9606.ENSP00000261681.

PTM databases

PhosphoSiteQ8N3R9.

Polymorphism databases

DMDM116242632.

Proteomic databases

PaxDbQ8N3R9.
PRIDEQ8N3R9.

Protocols and materials databases

DNASU64398.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261681; ENSP00000261681; ENSG00000072415. [Q8N3R9-1]
ENST00000555925; ENSP00000451488; ENSG00000072415. [Q8N3R9-2]
GeneID64398.
KEGGhsa:64398.
UCSCuc001xjc.4. human. [Q8N3R9-1]

Organism-specific databases

CTD64398.
GeneCardsGC14P067708.
HGNCHGNC:18669. MPP5.
HPAHPA000993.
MIM606958. gene.
neXtProtNX_Q8N3R9.
PharmGKBPA38631.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0194.
HOGENOMHOG000233034.
HOVERGENHBG001858.
InParanoidQ8N3R9.
KOK06091.
OMAVHQKEGQ.
OrthoDBEOG79CXZ5.
PhylomeDBQ8N3R9.
TreeFamTF314263.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressQ8N3R9.
BgeeQ8N3R9.
CleanExHS_MPP5.
GenevestigatorQ8N3R9.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR004172. L27.
IPR014775. L27_C.
IPR015145. L27_N.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
PF02828. L27. 1 hit.
PF09060. L27_N. 1 hit.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS51022. L27. 2 hits.
PS50106. PDZ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8N3R9.
GeneWikiMPP5.
GenomeRNAi64398.
NextBio66338.
PROQ8N3R9.
SOURCESearch...

Entry information

Entry nameMPP5_HUMAN
AccessionPrimary (citable) accession number: Q8N3R9
Secondary accession number(s): A1L380 expand/collapse secondary AC list , Q7Z631, Q86T98, Q8N7I5, Q9H9Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM