DCC-interacting protein 13-alpha

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• beta-tubulin binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.26

    "APPL proteins promote TGFbeta-induced nuclear transport of the TGFbeta type I receptor intracellular domain."
    Song J., Mu Y., Li C., Bergh A., Miaczynska M., Heldin C.H., Landstroem M.
    Oncotarget 7:279-292(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH TGFBR1 AND PRKCZ, SUBCELLULAR LOCATION, FUNCTION.
• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Crystal structures of the BAR-PH and PTB domains of human APPL1."
    Li J., Mao X., Dong L.Q., Liu F., Tong L.
    Structure 15:525-533(2007) [PubMed] [Europe PMC] [Abstract]
  • "Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5."
    Zhu G., Chen J., Liu J., Brunzelle J.S., Huang B., Wakeham N., Terzyan S., Li X., Rao Z., Li G., Zhang X.C.
    EMBO J 26:3484-3493(2007) [PubMed] [Europe PMC] [Abstract]
  • Ref.11

    "Membrane targeting by APPL1 and APPL2: dynamic scaffolds that oligomerize and bind phosphoinositides."
    Chial H.J., Wu R., Ustach C.V., McPhail L.C., Mobley W.C., Chen Y.Q.
    Traffic 9:215-229(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, INTERACTION WITH APPL2, DOMAIN, SUBCELLULAR LOCATION.
  • "A proteome-scale map of the human interactome network."
    Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M.

    , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
    Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
  • "Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations."
    Fragoza R., Das J., Wierbowski S.D., Liang J., Tran T.N., Liang S., Beltran J.F., Rivera-Erick C.A., Ye K., Wang T.Y., Yao L., Mort M., Stenson P.D., Cooper D.N., Wei X., Keinan A., Schimenti J.C., Clark A.G., Yu H.
    Nat Commun 10:4141-4141(2019) [PubMed] [Europe PMC] [Abstract]
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• phosphatidylinositol binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Membrane targeting by APPL1 and APPL2: dynamic scaffolds that oligomerize and bind phosphoinositides."
    Chial H.J., Wu R., Ustach C.V., McPhail L.C., Mobley W.C., Chen Y.Q.
    Traffic 9:215-229(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, INTERACTION WITH APPL2, DOMAIN, SUBCELLULAR LOCATION.
• phosphatidylserine binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Membrane targeting by APPL1 and APPL2: dynamic scaffolds that oligomerize and bind phosphoinositides."
    Chial H.J., Wu R., Ustach C.V., McPhail L.C., Mobley W.C., Chen Y.Q.
    Traffic 9:215-229(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, INTERACTION WITH APPL2, DOMAIN, SUBCELLULAR LOCATION.
• protein-containing complex binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.6

    "APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment."
    Miaczynska M., Christoforidis S., Giner A., Shevchenko A., Uttenweiler-Joseph S., Habermann B., Wilm M., Parton R.G., Zerial M.
    Cell 116:445-456(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A AND NURD/MECP1 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Membrane targeting by APPL1 and APPL2: dynamic scaffolds that oligomerize and bind phosphoinositides."
    Chial H.J., Wu R., Ustach C.V., McPhail L.C., Mobley W.C., Chen Y.Q.
    Traffic 9:215-229(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, INTERACTION WITH APPL2, DOMAIN, SUBCELLULAR LOCATION.
• protein kinase B binding Source: BHF-UCLInferred from physical interactionⁱ
  • "The interaction of Akt with APPL1 is required for insulin-stimulated Glut4 translocation."
    Saito T., Jones C.C., Huang S., Czech M.P., Pilch P.F.
    J Biol Chem 282:32280-32287(2007) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• adiponectin-activated signaling pathway Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.12

    "Yin-Yang regulation of adiponectin signaling by APPL isoforms in muscle cells."
    Wang C., Xin X., Xiang R., Ramos F.J., Liu M., Lee H.J., Chen H., Mao X., Kikani C.K., Liu F., Dong L.Q.
    J. Biol. Chem. 284:31608-31615(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH APPL2.
• cell cycle Source: UniProtKB-KW
• cellular response to hepatocyte growth factor stimulus Source: UniProtKB
• insulin receptor signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.25

    "Loss-of-function mutations in APPL1 in familial diabetes mellitus."
    Prudente S., Jungtrakoon P., Marucci A., Ludovico O., Buranasupkajorn P., Mazza T., Hastings T., Milano T., Morini E., Mercuri L., Bailetti D., Mendonca C., Alberico F., Basile G., Romani M., Miccinilli E., Pizzuti A., Carella M.

    , Barbetti F., Pascarella S., Marchetti P., Trischitta V., Di Paola R., Doria A.
    Am. J. Hum. Genet. 97:177-185(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INVOLVEMENT IN MODY14, VARIANT MODY14 ASN-94, CHARACTERIZATION OF VARIANT MODY14 ASN-94.
• negative regulation of Fc-gamma receptor signaling pathway involved in phagocytosis Source: UniProtKB
• positive regulation of cytokine production involved in inflammatory response Source: UniProtKB
• positive regulation of glucose import Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.23

    "The adaptor protein APPL2 inhibits insulin-stimulated glucose uptake by interacting with TBC1D1 in skeletal muscle."
    Cheng K.K., Zhu W., Chen B., Wang Y., Wu D., Sweeney G., Wang B., Lam K.S., Xu A.
    Diabetes 63:3748-3758(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• positive regulation of macropinocytosis Source: UniProtKB
• positive regulation of melanin biosynthetic process Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Interactions between GIPC-APPL and GIPC-TRP1 regulate melanosomal protein trafficking and melanogenesis in human melanocytes."
    Kedlaya R., Kandala G., Liu T.F., Maddodi N., Devi S., Setaluri V.
    Arch Biochem Biophys 508:227-233(2011) [PubMed] [Europe PMC] [Abstract]
• protein import into nucleus Source: UniProtKBInferred from direct assayⁱ
  • Ref.26

    "APPL proteins promote TGFbeta-induced nuclear transport of the TGFbeta type I receptor intracellular domain."
    Song J., Mu Y., Li C., Bergh A., Miaczynska M., Heldin C.H., Landstroem M.
    Oncotarget 7:279-292(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH TGFBR1 AND PRKCZ, SUBCELLULAR LOCATION, FUNCTION.
• regulation of fibroblast migration Source: UniProtKB
• regulation of G1/S transition of mitotic cell cycle Source: UniProtKBInferred from direct assayⁱ
  • Ref.6

    "APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment."
    Miaczynska M., Christoforidis S., Giner A., Shevchenko A., Uttenweiler-Joseph S., Habermann B., Wilm M., Parton R.G., Zerial M.
    Cell 116:445-456(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A AND NURD/MECP1 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
• regulation of glucose import Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "The interaction of Akt with APPL1 is required for insulin-stimulated Glut4 translocation."
    Saito T., Jones C.C., Huang S., Czech M.P., Pilch P.F.
    J Biol Chem 282:32280-32287(2007) [PubMed] [Europe PMC] [Abstract]
• regulation of innate immune response Source: UniProtKB
• regulation of protein localization to plasma membrane Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "The interaction of Akt with APPL1 is required for insulin-stimulated Glut4 translocation."
    Saito T., Jones C.C., Huang S., Czech M.P., Pilch P.F.
    J Biol Chem 282:32280-32287(2007) [PubMed] [Europe PMC] [Abstract]
• regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
• signaling Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• signal transduction Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.1

    "Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2."
    Mitsuuchi Y., Johnson S.W., Sonoda G., Tanno S., Golemis E.A., Testa J.R.
    Oncogene 18:4891-4898(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH AKT2 AND PIK3CA.
• transforming growth factor beta receptor signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.26

    "APPL proteins promote TGFbeta-induced nuclear transport of the TGFbeta type I receptor intracellular domain."
    Song J., Mu Y., Li C., Bergh A., Miaczynska M., Heldin C.H., Landstroem M.
    Oncotarget 7:279-292(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH TGFBR1 AND PRKCZ, SUBCELLULAR LOCATION, FUNCTION.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Mutagenesis

Keywords - Diseaseⁱ

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• beta-tubulin binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.26

    "APPL proteins promote TGFbeta-induced nuclear transport of the TGFbeta type I receptor intracellular domain."
    Song J., Mu Y., Li C., Bergh A., Miaczynska M., Heldin C.H., Landstroem M.
    Oncotarget 7:279-292(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH TGFBR1 AND PRKCZ, SUBCELLULAR LOCATION, FUNCTION.
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Crystal structures of the BAR-PH and PTB domains of human APPL1."
    Li J., Mao X., Dong L.Q., Liu F., Tong L.
    Structure 15:525-533(2007) [PubMed] [Europe PMC] [Abstract]
  • "Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5."
    Zhu G., Chen J., Liu J., Brunzelle J.S., Huang B., Wakeham N., Terzyan S., Li X., Rao Z., Li G., Zhang X.C.
    EMBO J 26:3484-3493(2007) [PubMed] [Europe PMC] [Abstract]
  • Ref.11

    "Membrane targeting by APPL1 and APPL2: dynamic scaffolds that oligomerize and bind phosphoinositides."
    Chial H.J., Wu R., Ustach C.V., McPhail L.C., Mobley W.C., Chen Y.Q.
    Traffic 9:215-229(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, INTERACTION WITH APPL2, DOMAIN, SUBCELLULAR LOCATION.
  • "A proteome-scale map of the human interactome network."
    Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M.

    , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
    Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
  • "Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations."
    Fragoza R., Das J., Wierbowski S.D., Liang J., Tran T.N., Liang S., Beltran J.F., Rivera-Erick C.A., Ye K., Wang T.Y., Yao L., Mort M., Stenson P.D., Cooper D.N., Wei X., Keinan A., Schimenti J.C., Clark A.G., Yu H.
    Nat Commun 10:4141-4141(2019) [PubMed] [Europe PMC] [Abstract]
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Membrane targeting by APPL1 and APPL2: dynamic scaffolds that oligomerize and bind phosphoinositides."
    Chial H.J., Wu R., Ustach C.V., McPhail L.C., Mobley W.C., Chen Y.Q.
    Traffic 9:215-229(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBUNIT, INTERACTION WITH APPL2, DOMAIN, SUBCELLULAR LOCATION.
• protein kinase B binding Source: BHF-UCLInferred from physical interactionⁱ
  • "The interaction of Akt with APPL1 is required for insulin-stimulated Glut4 translocation."
    Saito T., Jones C.C., Huang S., Czech M.P., Pilch P.F.
    J Biol Chem 282:32280-32287(2007) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Coiled coil

Motif

Compositional bias

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MPGIDKLPIE ETLEDSPQTR SLLGVFEEDA TAISNYMNQL YQAMHRIYDA 
        60         70         80         90        100
QNELSAATHL TSKLLKEYEK QRFPLGGDDE VMSSTLQQFS KVIDELSSCH 
       110        120        130        140        150
AVLSTQLADA MMFPITQFKE RDLKEILTLK EVFQIASNDH DAAINRYSRL 
       160        170        180        190        200
SKKRENDKVK YEVTEDVYTS RKKQHQTMMH YFCALNTLQY KKKIALLEPL 
       210        220        230        240        250
LGYMQAQISF FKMGSENLNE QLEEFLANIG TSVQNVRREM DSDIETMQQT 
       260        270        280        290        300
IEDLEVASDP LYVPDPDPTK FPVNRNLTRK AGYLNARNKT GLVSSTWDRQ 
       310        320        330        340        350
FYFTQGGNLM SQARGDVAGG LAMDIDNCSV MAVDCEDRRY CFQITSFDGK 
       360        370        380        390        400
KSSILQAESK KDHEEWICTI NNISKQIYLS ENPEETAARV NQSALEAVTP 
       410        420        430        440        450
SPSFQQRHES LRPAAGQSRP PTARTSSSGS LGSESTNLAA LSLDSLVAPD 
       460        470        480        490        500
TPIQFDIISP VCEDQPGQAK AFGQGGRRTN PFGESGGSTK SETEDSILHQ 
       510        520        530        540        550
LFIVRFLGSM EVKSDDHPDV VYETMRQILA ARAIHNIFRM TESHLLVTCD 
       560        570        580        590        600
CLKLIDPQTQ VTRLTFPLPC VVLYATHQEN KRLFGFVLRT SSGRSESNLS 
       610        620        630        640        650
SVCYIFESNN EGEKICDSVG LAKQIALHAE LDRRASEKQK EIERVKEKQQ 
       660        670        680        690        700
KELNKQKQIE KDLEEQSRLI AASSRPNQAS SEGQFVVLSS SQSEESDLGE 

GGKKRESEA                                              

Natural variant

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Human chromosome 3
   Human chromosome 3: entries, gene names and cross-references to MIM
2. Human entries with genetic variants
   List of human entries with genetic variants
3. Human variants curated from literature reports
   Index of human variants curated from literature reports
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