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UniProtKB/Swiss-Prot entry Q5TCQ9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MAGI3_HUMAN
Primary accession number Q5TCQ9
Secondary accession numbers Q5TCQ8 Q5TCR0 Q9H2V6 Q9H5Y8 Q9HBC4 Q9HCD8
Integrated into Swiss-Prot on June 10, 2008
Sequence was last modified on June 10, 2008 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 7)
Name and origin of the protein
Protein name Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
Synonyms Membrane-associated guanylate kinase inverted 3
MAGI-3
Gene name
Name: MAGI3
Synonyms: KIAA1634
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH PTEN; BAI1 AND GRIN2B.
TISSUE=Mammary gland;
DOI=10.1074/jbc.M909741199; PubMed=10748157 [NCBI, ExPASy, EBI, Israel, Japan]
Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A.;
"Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase.";
J. Biol. Chem. 275:21477-21485(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
DOI=10.1016/j.yexcr.2004.10.007; PubMed=15652357 [NCBI, ExPASy, EBI, Israel, Japan]
Franklin J.L., Yoshiura K., Dempsey P.J., Bogatcheva G., Jeyakumar L., Meise K.S., Pearsall R.S., Threadgill D., Coffey R.J.;
"Identification of MAGI-3 as a transforming growth factor-alpha tail binding protein.";
Exp. Cell Res. 303:457-470(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-1506 (ISOFORM 2).
TISSUE=Brain;
DOI=10.1093/dnares/7.4.271; PubMed=10997877 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.";
DNA Res. 7:273-281(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 953-1506 (ISOFORM 1).
TISSUE=Ileal mucosa;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
SUBCELLULAR LOCATION.
DOI=10.1006/excr.2002.5475; PubMed=11969287 [NCBI, ExPASy, EBI, Israel, Japan]
Laura R.P., Ross S., Koeppen H., Lasky L.A.;
"MAGI-1: a widely expressed, alternatively spliced tight junction protein.";
Exp. Cell Res. 275:155-170(2002).
[9]
INTERACTION WITH HPV E6, AND PROBABLE UBIQUITINATION.
DOI=10.1038/sj.onc.1205668; PubMed=12140759 [NCBI, ExPASy, EBI, Israel, Japan]
Thomas M., Laura R., Hepner K., Guccione E., Sawyers C., Lasky L., Banks L.;
"Oncogenic human papillomavirus E6 proteins target the MAGI-2 and MAGI-3 proteins for degradation.";
Oncogene 21:5088-5096(2002).
[10]
INTERACTION WITH HPV E6.
DOI=10.1128/JVI.78.22.12366-12377.2004; PubMed=15507623 [NCBI, ExPASy, EBI, Israel, Japan]
Lee C., Laimins L.A.;
"Role of the PDZ domain-binding motif of the oncoprotein E6 in the pathogenesis of human papillomavirus type 31.";
J. Virol. 78:12366-12377(2004).
[11]
INTERACTION WITH HPV E6.
DOI=10.1038/sj.onc.1207977; PubMed=15378012 [NCBI, ExPASy, EBI, Israel, Japan]
Massimi P., Gammoh N., Thomas M., Banks L.;
"HPV E6 specifically targets different cellular pools of its PDZ domain-containing tumour suppressor substrates for proteasome-mediated degradation.";
Oncogene 23:8033-8039(2004).
[12]
INTERACTION WITH HTLV TAX1.
DOI=10.1016/j.virol.2003.11.014; PubMed=15003862 [NCBI, ExPASy, EBI, Israel, Japan]
Ohashi M., Sakurai M., Higuchi M., Mori N., Fukushi M., Oie M., Coffey R.J., Yoshiura K., Tanaka Y., Uchiyama M., Hatanaka M., Fujii M.;
"Human T-cell leukemia virus type 1 Tax oncoprotein induces and interacts with a multi-PDZ domain protein, MAGI-3.";
Virology 320:52-62(2004).
[13]
LIGANDS THAT BIND AND INHIBIT PDZ DOMAINS.
DOI=10.1016/j.bmcl.2006.10.006; PubMed=17055267 [NCBI, ExPASy, EBI, Israel, Japan]
Fujii N., Haresco J.J., Novak K.A., Gage R.M., Pedemonte N., Stokoe D., Kuntz I.D., Guy R.K.;
"Rational design of a nonpeptide general chemical scaffold for reversible inhibition of PDZ domain interactions.";
Bioorg. Med. Chem. Lett. 17:549-552(2007).
[14]
INTERACTION WITH LPAR2.
DOI=10.1016/j.cellsig.2006.06.008; PubMed=16904289 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang H., Wang D., Sun H., Hall R.A., Yun C.C.;
"MAGI-3 regulates LPA-induced activation of Erk and RhoA.";
Cell. Signal. 19:261-268(2007).
[15]
INTERACTION WITH HPV E6, AND PROBABLE UBIQUITINATION.
DOI=10.1038/sj.onc.1210810; PubMed=17934525 [NCBI, ExPASy, EBI, Israel, Japan]
Massimi P., Shai A., Lambert P., Banks L.;
"HPV E6 degradation of p53 and PDZ containing substrates in an E6AP null background.";
Oncogene 27:1800-1804(2008).
Comments
  • FUNCTION: Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2.
  • SUBUNIT: Interacts with ADRB1, FZD4, FZD7, PTPRB, TGFA and VANGL2. Interacts with unidentified tyrosine phosphorylated proteins (By similarity). Interacts with BAI1, LPAR2/EDG4, GRIN2B and PTEN. In case of infection, interacts with HTLV TAX1 protein, possibly affecting the transformation ability of TAX1. Does not interact with HTLV TAX2 or TAX3 proteins. In case of infection, interacts with HPV type 16 and HPV type 18 E6 protein.
  • SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell junction, tight junction. Nucleus (By similarity). Note=Concentrates in specific sites at the plasma membrane and in the nucleus. In epithelial cells, it localizes at tight junctions (By similarity).
  • ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ5TCQ9-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ5TCQ9-2
    Features which should be applied to build the isoform sequence: VSP_034286, VSP_034287.
    Name3
    Isoform IDQ5TCQ9-3
    Features which should be applied to build the isoform sequence: VSP_034285, VSP_034286, VSP_034287.
    Name4
    Isoform IDQ5TCQ9-4
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_034285.
  • TISSUE SPECIFICITY: Widely expressed.
  • PTM: Ubiquitinated following interaction with HPV E6 protein, leading to its degradation by the proteasome. Degradation is independent of E6AP ubiquitin ligase complex.
  • MISCELLANEOUS: MAGI3 PDZ domains are used to design peptide ligands that bind and inhibit PDZ domains.
  • SIMILARITY: Belongs to the MAGUK family.
  • SIMILARITY: Contains 1 guanylate kinase-like domain.
  • SIMILARITY: Contains 6 PDZ (DHR) domains.
  • SIMILARITY: Contains 2 WW domains.
  • SEQUENCE CAUTION:
    • Sequence=BAB15479.1; Type=Erroneous initiation; Note=Translation N-terminally extended
    • Sequence=BAB15479.1; Type=Frameshift; Positions=1373;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF257238; AAG24545.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF213259; AAG43837.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAH70944.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAH70944.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAH70944.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAH70944.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAH70945.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAH70945.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAH70945.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAH70945.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAH70946.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAH70946.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAH70946.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAH70946.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAH71507.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAH71507.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAH71507.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAH71507.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAH71508.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAH71508.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAH71508.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAH71508.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAH71509.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAH71509.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAH71509.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAH71509.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAH74141.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAH74141.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAH74141.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAH74141.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAH74142.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAH74142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAH74142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAH74142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAH74143.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAH74143.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAH74143.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAH74143.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAI22553.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAI22553.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAI22553.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAI22553.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAI22554.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAI22554.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAI22554.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAI22554.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133517; CAI22555.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365225; CAI22555.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389921; CAI22555.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390759; CAI22555.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471122; EAW56559.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471122; EAW56560.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471122; EAW56562.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC130409; AAI30410.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB046854; BAB13460.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK026417; BAB15479.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_690864.2; -.
3D structure databases
ModBase Q5TCQ9.
Organism-specific databases
HGNC HGNC:29647; MAGI3.
GenAtlas MAGI3.
HPA HPA007923; -.
GeneCards Q5TCQ9.
HUGE KIAA1634.
Family and domain databases
InterPro IPR001150; Form_AcTrfase_GR.
IPR008144; Guanylate_kin.
IPR008145; Guanylt/Ca.
IPR001478; PDZ.
IPR001202; WW_Rsp5_WWP.
Graphical view of domain structure.
Pfam PF00625; Guanylate_kin; 1.
PF00595; PDZ; 4.
PF00397; WW; 2.
Pfam graphical view of domain structure.
SMART SM00072; GuKc; 1.
SM00228; PDZ; 6.
SM00456; WW; 2.
SMART graphical view of domain structure.
PROSITE PS00856; GUANYLATE_KINASE_1; 1.
PS50052; GUANYLATE_KINASE_2; 1.
PS50106; PDZ; 6.
PS01159; WW_DOMAIN_1; 1.
PS50020; WW_DOMAIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q5TCQ9.
Genome annotation databases
Ensembl ENSG00000081026; Homo sapiens. [Contig view]
GeneID 260425; -.
Other
ProtoNet Q5TCQ9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Cell junction; Cell membrane; Host-virus interaction; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Repeat; Tight junction; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1506  1506     Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3. PRO_0000341407
DOMAIN   18    106  89     PDZ 1. 
DOMAIN   114    288  175     Guanylate kinase-like. 
DOMAIN   293    326  34     WW 1. 
DOMAIN   339    372  34     WW 2. 
DOMAIN   435    517  83     PDZ 2. 
DOMAIN   603    679  77     PDZ 3. 
DOMAIN   751    833  83     PDZ 4. 
DOMAIN   876    963  88     PDZ 5. 
DOMAIN   1046   1128  83     PDZ 6. 
NP_BIND   121    128  8     ATP (By similarity). 
REGION   18    106  89     Interaction with ADRB1 and TGFA (By similarity). 
REGION   435    517  83     Interaction with PTEN. 
REGION   751    833  83     Interaction with BAI1. 
REGION   876    963  88     Interaction with LPAR2 and GRIN2B. 
COMPBIAS   6      9  4     Poly-Lys. 
COMPBIAS   238    243  6     Poly-Glu. 
COMPBIAS   378    381  4     Poly-Pro. 
MOD_RES   722    722        Phosphoserine (By similarity). 
MOD_RES   724    724        Phosphoserine (By similarity). 
VAR_SEQ   360    384        Missing (in isoform 3 and isoform 4). VSP_034285
VAR_SEQ   1136   1150        DWDINNPSSSNVIYD -> LAPSGLCSYVKPEQH (in isoform 2 and isoform 3). VSP_034286
VAR_SEQ   1151   1506        Missing (in isoform 2 and isoform 3). VSP_034287
CONFLICT   9      9        K -> R (in Ref. 2; AAG43837). 
CONFLICT   59     59        V -> I (in Ref. 1; AAG24545). 
CONFLICT   66     68        SPG -> NPS (in Ref. 1; AAG24545). 
CONFLICT   246    246        E -> G (in Ref. 1; AAG24545). 
CONFLICT   257    257        R -> G (in Ref. 2; AAG43837). 
CONFLICT   491    491        L -> F (in Ref. 1; AAG24545). 
CONFLICT   573    573        L -> S (in Ref. 1; AAG24545). 
CONFLICT   641    641        G -> E (in Ref. 1; AAG24545). 
CONFLICT   685    685        P -> T (in Ref. 1; AAG24545). 
CONFLICT   801    801        I -> V (in Ref. 2; AAG43837). 
CONFLICT   823    823        R -> P (in Ref. 2; AAG43837). 
CONFLICT   942    942        D -> A (in Ref. 1; AAG24545). 
CONFLICT   1018   1018        S -> P (in Ref. 2; AAG43837). 
Sequence information
Length: 1506 AA [This is the length of the unprocessed precursor] Molecular weight: 165608 Da [This is the MW of the unprocessed precursor]