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Q5T2T1 (MPP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MAGUK p55 subfamily member 7
Gene names
Name:MPP7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact. Ref.9

Subunit structure

Heterodimer; able to heterodimerize via its C-terminal L27 domain with LIN7A, LIN7B and LIN7C. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). Interacts with DLG1 via its N-terminal L27 domain. Interacts with MPP5 and INADL/PATJ. Ref.6 Ref.7 Ref.9

Subcellular location

Membrane; Peripheral membrane protein. Cell junctiontight junction. Cell junctionadherens junction Ref.7 Ref.9.

Induction

Down-regulated in patients suffering of passive Heymann nephritis (at protein level). Ref.8

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 CAI12709.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI13640.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI17344.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCell junction
Membrane
Tight junction
   Coding sequence diversityPolymorphism
   DomainRepeat
SH3 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processestablishment of cell polarity

Traceable author statement Ref.9. Source: BHF-UCL

positive regulation of protein complex assembly

Inferred from direct assay Ref.7. Source: BHF-UCL

positive regulation of signal transduction

Non-traceable author statement Ref.5. Source: GOC

protein localization to adherens junction

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

tight junction assembly

Inferred from direct assay Ref.9. Source: BHF-UCL

   Cellular_componentMPP7-DLG1-LIN7 complex

Inferred from direct assay Ref.7PubMed 20702775. Source: BHF-UCL

adherens junction

Inferred from direct assay Ref.7. Source: BHF-UCL

cell junction

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from direct assay. Source: HPA

tight junction

Inferred from direct assay Ref.9. Source: BHF-UCL

   Molecular_functionprotein binding

Inferred from physical interaction Ref.7. Source: BHF-UCL

protein complex scaffold

Inferred from direct assay Ref.7PubMed 20702775. Source: BHF-UCL

protein domain specific binding

Inferred from physical interaction Ref.9. Source: BHF-UCL

protein heterodimerization activity

Inferred from direct assay Ref.7. Source: BHF-UCL

signaling adaptor activity

Non-traceable author statement Ref.5. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 576576MAGUK p55 subfamily member 7
PRO_0000320027

Regions

Domain10 – 6556L27 1
Domain67 – 12256L27 2
Domain139 – 22082PDZ
Domain228 – 29871SH3
Domain368 – 560193Guanylate kinase-like

Amino acid modifications

Modified residue4091Phosphoserine Ref.10 Ref.11

Natural variations

Natural variant3221K → R. Ref.1 Ref.3 Ref.4
Corresponds to variant rs2997211 [ dbSNP | Ensembl ].
VAR_039110

Experimental info

Mutagenesis381L → S: Abolishes interaction with DLG1. Ref.9
Mutagenesis951L → S: Does not affect the interaction with DLG1. Ref.9

Secondary structure

................................... 576
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5T2T1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 86366E460A08C6A7

FASTA57665,524
        10         20         30         40         50         60 
MPALSTGSGS DTGLYELLAA LPAQLQPHVD SQEDLTFLWD MFGEKSLHSL VKIHEKLHYY 

        70         80         90        100        110        120 
EKQSPVPILH GAAALADDLA EELQNKPLNS EIRELLKLLS KPNVKALLSV HDTVAQKNYD 

       130        140        150        160        170        180 
PVLPPMPEDI DDEEDSVKII RLVKNREPLG ATIKKDEQTG AIIVARIMRG GAADRSGLIH 

       190        200        210        220        230        240 
VGDELREVNG IPVEDKRPEE IIQILAQSQG AITFKIIPGS KEETPSKEGK MFIKALFDYN 

       250        260        270        280        290        300 
PNEDKAIPCK EAGLSFKKGD ILQIMSQDDA TWWQAKHEAD ANPRAGLIPS KHFQERRLAL 

       310        320        330        340        350        360 
RRPEILVQPL KVSNRKSSGF RKSFRLSRKD KKTNKSMYEC KKSDQYDTAD VPTYEEVTPY 

       370        380        390        400        410        420 
RRQTNEKYRL VVLVGPVGVG LNELKRKLLI SDTQHYGVTV PHTTRARRSQ ESDGVEYIFI 

       430        440        450        460        470        480 
SKHLFETDVQ NNKFIEYGEY KNNYYGTSID SVRSVLAKNK VCLLDVQPHT VKHLRTLEFK 

       490        500        510        520        530        540 
PYVIFIKPPS IERLRETRKN AKIISSRDDQ GAAKPFTEED FQEMIKSAQI MESQYGHLFD 

       550        560        570 
KIIINDDLTV AFNELKTTFD KLETETHWVP VSWLHS 

« Hide

References

« Hide 'large scale' references
[1]"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], VARIANT ARG-322.
Tissue: Hippocampus.
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-322.
[4]"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], VARIANT ARG-322.
Tissue: Testis.
[5]"Identification and characterization of human MPP7 gene and mouse Mpp7 gene in silico."
Katoh M., Katoh M.
Int. J. Mol. Med. 13:333-338(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[6]"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: INTERACTION WITH INADL AND MPP5.
[7]"The stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 that regulates the stability and localization of DLG1 to cell junctions."
Bohl J., Brimer N., Lyons C., Vande Pol S.B.
J. Biol. Chem. 282:9392-9400(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH DLG1; LIN7A; LIN7B AND LIN7C.
[8]"Markedly increased urinary preprohaptoglobin and haptoglobin in passive Heymann nephritis: a differential proteomics approach."
Ngai H.-H., Sit W.-H., Jiang P.-P., Thongboonkerd V., Wan J.-M.
J. Proteome Res. 6:3313-3320(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DLG1 AND MPP5, MUTAGENESIS OF LEU-38 AND LEU-95.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK315046 mRNA. Translation: BAG37526.1.
AL390866, AL355501, AL391423 Genomic DNA. Translation: CAI12708.1.
AL390866, AL355501, AL391423 Genomic DNA. Translation: CAI12709.1. Sequence problems.
AL355501, AL390866, AL391423 Genomic DNA. Translation: CAI13640.1. Sequence problems.
AL355501, AL390866, AL391423 Genomic DNA. Translation: CAI13641.1.
AL391423, AL355501, AL390866 Genomic DNA. Translation: CAI17344.1. Sequence problems.
AL391423, AL355501, AL390866 Genomic DNA. Translation: CAI17345.1.
CH471072 Genomic DNA. Translation: EAW86045.1.
CH471072 Genomic DNA. Translation: EAW86047.1.
BC038105 mRNA. Translation: AAH38105.1.
CCDSCCDS7158.1.
RefSeqNP_775767.2. NM_173496.3.
XP_005252424.1. XM_005252367.1.
UniGeneHs.499159.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRAX-ray2.95A7-120[»]
3O46X-ray1.30A135-225[»]
ProteinModelPortalQ5T2T1.
SMRQ5T2T1. Positions 1-219, 232-570.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126785. 4 interactions.
IntActQ5T2T1. 2 interactions.
STRING9606.ENSP00000337907.

PTM databases

PhosphoSiteQ5T2T1.

Polymorphism databases

DMDM74762233.

Proteomic databases

MaxQBQ5T2T1.
PaxDbQ5T2T1.
PRIDEQ5T2T1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337532; ENSP00000337907; ENSG00000150054.
ENST00000375719; ENSP00000364871; ENSG00000150054.
ENST00000375732; ENSP00000364884; ENSG00000150054.
ENST00000540098; ENSP00000438693; ENSG00000150054.
GeneID143098.
KEGGhsa:143098.
UCSCuc001iua.1. human.

Organism-specific databases

CTD143098.
GeneCardsGC10M028382.
H-InvDBHIX0008732.
HGNCHGNC:26542. MPP7.
HPAHPA037598.
MIM610973. gene.
neXtProtNX_Q5T2T1.
PharmGKBPA134985345.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0194.
HOGENOMHOG000233034.
HOVERGENHBG001858.
InParanoidQ5T2T1.
OMASRDDQGA.
OrthoDBEOG79CXZ5.
PhylomeDBQ5T2T1.
TreeFamTF314263.

Gene expression databases

ArrayExpressQ5T2T1.
BgeeQ5T2T1.
CleanExHS_MPP7.
GenevestigatorQ5T2T1.

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.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
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

EvolutionaryTraceQ5T2T1.
GenomeRNAi143098.
NextBio84649.
PROQ5T2T1.
SOURCESearch...

Entry information

Entry nameMPP7_HUMAN
AccessionPrimary (citable) accession number: Q5T2T1
Secondary accession number(s): B2RCC9 expand/collapse secondary AC list , B5MDZ3, D3DRW3, Q5T2T0, Q8IY28
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM