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Q5T2T1

- MPP7_HUMAN

UniProt

Q5T2T1 - MPP7_HUMAN

Protein

MAGUK p55 subfamily member 7

Gene

MPP7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. protein binding Source: BHF-UCL
    2. protein complex scaffold Source: BHF-UCL
    3. protein domain specific binding Source: BHF-UCL
    4. protein heterodimerization activity Source: BHF-UCL
    5. signaling adaptor activity Source: BHF-UCL

    GO - Biological processi

    1. establishment of cell polarity Source: BHF-UCL
    2. positive regulation of protein complex assembly Source: BHF-UCL
    3. positive regulation of signal transduction Source: GOC
    4. protein localization to adherens junction Source: BHF-UCL
    5. tight junction assembly Source: BHF-UCL

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MAGUK p55 subfamily member 7
    Gene namesi
    Name:MPP7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:26542. MPP7.

    Subcellular locationi

    GO - Cellular componenti

    1. adherens junction Source: BHF-UCL
    2. cell junction Source: HPA
    3. mitochondrion Source: HPA
    4. MPP7-DLG1-LIN7 complex Source: BHF-UCL
    5. tight junction Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Membrane, Tight junction

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381L → S: Abolishes interaction with DLG1. 1 Publication
    Mutagenesisi95 – 951L → S: Does not affect the interaction with DLG1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134985345.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 576576MAGUK p55 subfamily member 7PRO_0000320027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei409 – 4091Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5T2T1.
    PaxDbiQ5T2T1.
    PRIDEiQ5T2T1.

    PTM databases

    PhosphoSiteiQ5T2T1.

    Expressioni

    Inductioni

    Down-regulated in patients suffering of passive Heymann nephritis (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ5T2T1.
    BgeeiQ5T2T1.
    CleanExiHS_MPP7.
    GenevestigatoriQ5T2T1.

    Organism-specific databases

    HPAiHPA037598.

    Interactioni

    Subunit structurei

    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.4 Publications

    Protein-protein interaction databases

    BioGridi126785. 4 interactions.
    IntActiQ5T2T1. 2 interactions.
    STRINGi9606.ENSP00000337907.

    Structurei

    Secondary structure

    1
    576
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 134
    Helixi14 – 196
    Helixi21 – 255
    Turni26 – 283
    Helixi34 – 418
    Helixi47 – 6115
    Helixi72 – 8413
    Helixi90 – 989
    Helixi102 – 11514
    Beta strandi138 – 14710
    Beta strandi151 – 1555
    Turni157 – 1593
    Beta strandi162 – 1676
    Helixi172 – 1765
    Beta strandi184 – 1885
    Beta strandi191 – 1933
    Helixi198 – 20710
    Beta strandi210 – 2178

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LRAX-ray2.95A7-120[»]
    3O46X-ray1.30A135-225[»]
    ProteinModelPortaliQ5T2T1.
    SMRiQ5T2T1. Positions 1-219, 232-570.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5T2T1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 6556L27 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini67 – 12256L27 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini139 – 22082PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini228 – 29871SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini368 – 560193Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MAGUK family.Curated
    Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
    Contains 2 L27 domains.PROSITE-ProRule annotation
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0194.
    HOGENOMiHOG000233034.
    HOVERGENiHBG001858.
    InParanoidiQ5T2T1.
    OMAiSRDDQGA.
    OrthoDBiEOG79CXZ5.
    PhylomeDBiQ5T2T1.
    TreeFamiTF314263.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR008145. 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]
    PfamiPF00625. Guanylate_kin. 1 hit.
    PF02828. L27. 2 hits.
    PF00595. PDZ. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00072. GuKc. 1 hit.
    SM00569. L27. 2 hits.
    SM00228. PDZ. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00856. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5T2T1-1) [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

    MPALSTGSGS DTGLYELLAA LPAQLQPHVD SQEDLTFLWD MFGEKSLHSL    50
    VKIHEKLHYY EKQSPVPILH GAAALADDLA EELQNKPLNS EIRELLKLLS 100
    KPNVKALLSV HDTVAQKNYD PVLPPMPEDI DDEEDSVKII RLVKNREPLG 150
    ATIKKDEQTG AIIVARIMRG GAADRSGLIH VGDELREVNG IPVEDKRPEE 200
    IIQILAQSQG AITFKIIPGS KEETPSKEGK MFIKALFDYN PNEDKAIPCK 250
    EAGLSFKKGD ILQIMSQDDA TWWQAKHEAD ANPRAGLIPS KHFQERRLAL 300
    RRPEILVQPL KVSNRKSSGF RKSFRLSRKD KKTNKSMYEC KKSDQYDTAD 350
    VPTYEEVTPY RRQTNEKYRL VVLVGPVGVG LNELKRKLLI SDTQHYGVTV 400
    PHTTRARRSQ ESDGVEYIFI SKHLFETDVQ NNKFIEYGEY KNNYYGTSID 450
    SVRSVLAKNK VCLLDVQPHT VKHLRTLEFK PYVIFIKPPS IERLRETRKN 500
    AKIISSRDDQ GAAKPFTEED FQEMIKSAQI MESQYGHLFD KIIINDDLTV 550
    AFNELKTTFD KLETETHWVP VSWLHS 576
    Length:576
    Mass (Da):65,524
    Last modified:December 21, 2004 - v1
    Checksum:i86366E460A08C6A7
    GO
    Isoform 2 (identifier: Q5T2T1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-125: Missing.
         470-499: TVKHLRTLEFKPYVIFIKPPSIERLRETRK → GPWFLLPLMAVPWGAKPPNARMTCGSPLDL
         500-576: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:374
    Mass (Da):42,395
    Checksum:iB38B15B10A3A1D54
    GO

    Sequence cautioni

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti322 – 3221K → R.3 Publications
    Corresponds to variant rs2997211 [ dbSNP | Ensembl ].
    VAR_039110

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 125125Missing in isoform 2. 1 PublicationVSP_056065Add
    BLAST
    Alternative sequencei470 – 49930TVKHL…RETRK → GPWFLLPLMAVPWGAKPPNA RMTCGSPLDL in isoform 2. 1 PublicationVSP_056066Add
    BLAST
    Alternative sequencei500 – 57677Missing in isoform 2. 1 PublicationVSP_056067Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK301592 mRNA. Translation: BAG63081.1.
    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.
    CCDSiCCDS7158.1.
    RefSeqiNP_775767.2. NM_173496.3.
    XP_005252424.1. XM_005252367.1.
    UniGeneiHs.499159.

    Genome annotation databases

    EnsembliENST00000337532; ENSP00000337907; ENSG00000150054.
    ENST00000375719; ENSP00000364871; ENSG00000150054.
    ENST00000375732; ENSP00000364884; ENSG00000150054.
    ENST00000445954; ENSP00000405397; ENSG00000150054.
    GeneIDi143098.
    KEGGihsa:143098.
    UCSCiuc001iua.1. human.

    Polymorphism databases

    DMDMi74762233.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK301592 mRNA. Translation: BAG63081.1 .
    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 .
    CCDSi CCDS7158.1.
    RefSeqi NP_775767.2. NM_173496.3.
    XP_005252424.1. XM_005252367.1.
    UniGenei Hs.499159.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LRA X-ray 2.95 A 7-120 [» ]
    3O46 X-ray 1.30 A 135-225 [» ]
    ProteinModelPortali Q5T2T1.
    SMRi Q5T2T1. Positions 1-219, 232-570.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 126785. 4 interactions.
    IntActi Q5T2T1. 2 interactions.
    STRINGi 9606.ENSP00000337907.

    PTM databases

    PhosphoSitei Q5T2T1.

    Polymorphism databases

    DMDMi 74762233.

    Proteomic databases

    MaxQBi Q5T2T1.
    PaxDbi Q5T2T1.
    PRIDEi Q5T2T1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337532 ; ENSP00000337907 ; ENSG00000150054 .
    ENST00000375719 ; ENSP00000364871 ; ENSG00000150054 .
    ENST00000375732 ; ENSP00000364884 ; ENSG00000150054 .
    ENST00000445954 ; ENSP00000405397 ; ENSG00000150054 .
    GeneIDi 143098.
    KEGGi hsa:143098.
    UCSCi uc001iua.1. human.

    Organism-specific databases

    CTDi 143098.
    GeneCardsi GC10M028382.
    H-InvDB HIX0008732.
    HGNCi HGNC:26542. MPP7.
    HPAi HPA037598.
    MIMi 610973. gene.
    neXtProti NX_Q5T2T1.
    PharmGKBi PA134985345.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0194.
    HOGENOMi HOG000233034.
    HOVERGENi HBG001858.
    InParanoidi Q5T2T1.
    OMAi SRDDQGA.
    OrthoDBi EOG79CXZ5.
    PhylomeDBi Q5T2T1.
    TreeFami TF314263.

    Miscellaneous databases

    EvolutionaryTracei Q5T2T1.
    GenomeRNAii 143098.
    NextBioi 84649.
    PROi Q5T2T1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5T2T1.
    Bgeei Q5T2T1.
    CleanExi HS_MPP7.
    Genevestigatori Q5T2T1.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR008145. 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 ]
    Pfami PF00625. Guanylate_kin. 1 hit.
    PF02828. L27. 2 hits.
    PF00595. PDZ. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00072. GuKc. 1 hit.
    SM00569. L27. 2 hits.
    SM00228. PDZ. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00856. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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] (ISOFORMS 1 AND 2), VARIANT ARG-322.
      Tissue: Hippocampus and Mammary gland.
    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.
      , 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. 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] (ISOFORM 1), 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. 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.
    12. "Structural basis for tandem L27 domain-mediated polymerization."
      Yang X., Xie X., Chen L., Zhou H., Wang Z., Zhao W., Tian R., Zhang R., Tian C., Long J., Shen Y.
      FASEB J. 24:4806-4815(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 7-120 IN COMPLEX WITH DLG1 AND LIN7C, SUBUNIT.
    13. "Crystal structure of the PDZ domain of mpp7."
      Structural genomics consortium (SGC)
      Submitted (AUG-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 135-225.

    Entry informationi

    Entry nameiMPP7_HUMAN
    AccessioniPrimary (citable) accession number: Q5T2T1
    Secondary accession number(s): B2RCC9
    , B4DWL9, B5MDZ3, D3DRW3, Q5T2T0, Q8IY28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 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 10
      Human chromosome 10: 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