Ezrin

<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>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationⁱ

<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

• actin binding Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin and radixin both regulate the apical membrane localization of ABCC2 (MRP2) in human intestinal epithelial Caco-2 cells."
    Yang Q., Onuki R., Nakai C., Sugiyama Y.
    Exp. Cell Res. 313:3517-3525(2007) [PubMed] [Europe PMC] [Abstract]
• actin filament binding Source: UniProtKB
• ATPase binding Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin and radixin both regulate the apical membrane localization of ABCC2 (MRP2) in human intestinal epithelial Caco-2 cells."
    Yang Q., Onuki R., Nakai C., Sugiyama Y.
    Exp. Cell Res. 313:3517-3525(2007) [PubMed] [Europe PMC] [Abstract]
• cell adhesion molecule binding Source: BHF-UCL
• disordered domain specific binding Source: RGDInferred from sequence orthologyⁱ
  • "Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins."
    Tyukhtenko S., Deshmukh L., Kumar V., Lary J., Cole J., Lemmon V., Vinogradova O.
    Biochemistry 47:4160-4168(2008) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: RGDInferred from sequence orthologyⁱ
  • "Toward an understanding of the protein interaction network of the human liver."
    Wang J., Huo K., Ma L., Tang L., Li D., Huang X., Yuan Y., Li C., Wang W., Guan W., Chen H., Jin C., Wei J., Zhang W., Yang Y., Liu Q., Zhou Y., Zhang C.

    , Wu Z., Xu W., Zhang Y., Liu T., Yu D., Zhang Y., Chen L., Zhu D., Zhong X., Kang L., Gan X., Yu X., Ma Q., Yan J., Zhou L., Liu Z., Zhu Y., Zhou T., He F., Yang X.
    Mol. Syst. Biol. 7:536-536(2011) [PubMed] [Europe PMC] [Abstract]
  • "An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations."
    Liu X., Salokas K., Tamene F., Jiu Y., Weldatsadik R.G., Ohman T., Varjosalo M.
    Nat Commun 9:1188-1188(2018) [PubMed] [Europe PMC] [Abstract]
• microtubule binding Source: RGDInferred from sequence orthologyⁱ
  • "The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex."
    Solinet S., Mahmud K., Stewman S.F., Ben El Kadhi K., Decelle B., Talje L., Ma A., Kwok B.H., Carreno S.
    J. Cell Biol. 202:251-260(2013) [PubMed] [Europe PMC] [Abstract]
• protein-containing complex binding Source: RGD <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
  • "Analysis of different complexes of type IIa sodium-dependent phosphate transporter in rat renal cortex using blue-native polyacrylamide gel electrophoresis."
    Tanimura A., Yamada F., Saito A., Ito M., Kimura T., Anzai N., Horie D., Yamamoto H., Miyamoto K., Taketani Y., Takeda E.
    J. Med. Invest. 58:140-147(2011) [PubMed] [Europe PMC] [Abstract]
• protein C-terminus binding Source: RGDInferred from sequence orthologyⁱ
  • "Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins."
    Tyukhtenko S., Deshmukh L., Kumar V., Lary J., Cole J., Lemmon V., Vinogradova O.
    Biochemistry 47:4160-4168(2008) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: RGDInferred from physical interactionⁱ
  • "A functional FERM domain binding motif in neurofascin."
    Gunn-Moore F.J., Hill M., Davey F., Herron L.R., Tait S., Sherman D., Brophy P.J.
    Mol. Cell. Neurosci. 33:441-446(2006) [PubMed] [Europe PMC] [Abstract]
• protein kinase A binding Source: RGDInferred from sequence orthologyⁱ
  • "A systematic evaluation of protein kinase A-A-Kinase anchoring protein interaction motifs."
    Burgers P.P., van der Heyden M.A., Kok B., Heck A.J., Scholten A.
    Biochemistry 54:11-21(2015) [PubMed] [Europe PMC] [Abstract]
• protein kinase A catalytic subunit binding Source: RGDInferred from sequence orthologyⁱ
  • "Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin."
    Ruppelt A., Mosenden R., Gronholm M., Aandahl E.M., Tobin D., Carlson C.R., Abrahamsen H., Herberg F.W., Carpen O., Tasken K.
    J. Immunol. 179:5159-5168(2007) [PubMed] [Europe PMC] [Abstract]
• protein kinase A regulatory subunit binding Source: RGDInferred from sequence orthologyⁱ
  • "Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin."
    Ruppelt A., Mosenden R., Gronholm M., Aandahl E.M., Tobin D., Carlson C.R., Abrahamsen H., Herberg F.W., Carpen O., Tasken K.
    J. Immunol. 179:5159-5168(2007) [PubMed] [Europe PMC] [Abstract]
• S100 protein binding Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin interacts with the scaffold protein IQGAP1 and affects its cortical localization."
    Nammalwar R.C., Heil A., Gerke V.
    Biochim. Biophys. Acta 1853:2086-2094(2015) [PubMed] [Europe PMC] [Abstract]
• structural molecule activity Source: RGD <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.4

    "Transcriptional regulation of the ezrin gene during rat intestinal development and epithelial differentiation."
    Barila D., Murgia C., Nobili F., Perozzi G.
    Biochim. Biophys. Acta 1263:133-140(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 427-586, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

GO - Biological processⁱ

• actin cytoskeleton reorganization Source: RGDInferred from sequence orthologyⁱ
  • "Sphingosine 1-phosphate induces filopodia formation through S1PR2 activation of ERM proteins."
    Gandy K.A., Canals D., Adada M., Wada M., Roddy P., Snider A.J., Hannun Y.A., Obeid L.M.
    Biochem. J. 449:661-672(2013) [PubMed] [Europe PMC] [Abstract]
• actin filament bundle assembly Source: UniProtKB
• astral microtubule organization Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse."
    Lasserre R., Charrin S., Cuche C., Danckaert A., Thoulouze M.I., de Chaumont F., Duong T., Perrault N., Varin-Blank N., Olivo-Marin J.C., Etienne-Manneville S., Arpin M., Di Bartolo V., Alcover A.
    EMBO J. 29:2301-2314(2010) [PubMed] [Europe PMC] [Abstract]
• cellular protein-containing complex localization Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse."
    Lasserre R., Charrin S., Cuche C., Danckaert A., Thoulouze M.I., de Chaumont F., Duong T., Perrault N., Varin-Blank N., Olivo-Marin J.C., Etienne-Manneville S., Arpin M., Di Bartolo V., Alcover A.
    EMBO J. 29:2301-2314(2010) [PubMed] [Europe PMC] [Abstract]
• cellular response to cAMP Source: RGDInferred from sequence orthologyⁱ
  • "Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin."
    Ruppelt A., Mosenden R., Gronholm M., Aandahl E.M., Tobin D., Carlson C.R., Abrahamsen H., Herberg F.W., Carpen O., Tasken K.
    J. Immunol. 179:5159-5168(2007) [PubMed] [Europe PMC] [Abstract]
• cortical microtubule organization Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse."
    Lasserre R., Charrin S., Cuche C., Danckaert A., Thoulouze M.I., de Chaumont F., Duong T., Perrault N., Varin-Blank N., Olivo-Marin J.C., Etienne-Manneville S., Arpin M., Di Bartolo V., Alcover A.
    EMBO J. 29:2301-2314(2010) [PubMed] [Europe PMC] [Abstract]
• epithelial cell differentiation Source: RGD <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • Ref.4

    "Transcriptional regulation of the ezrin gene during rat intestinal development and epithelial differentiation."
    Barila D., Murgia C., Nobili F., Perozzi G.
    Biochim. Biophys. Acta 1263:133-140(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 427-586, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
• establishment of centrosome localization Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse."
    Lasserre R., Charrin S., Cuche C., Danckaert A., Thoulouze M.I., de Chaumont F., Duong T., Perrault N., Varin-Blank N., Olivo-Marin J.C., Etienne-Manneville S., Arpin M., Di Bartolo V., Alcover A.
    EMBO J. 29:2301-2314(2010) [PubMed] [Europe PMC] [Abstract]
• establishment of endothelial barrier Source: RGDInferred from sequence orthologyⁱ
  • "MYADM controls endothelial barrier function through ERM-dependent regulation of ICAM-1 expression."
    Aranda J.F., Reglero-Real N., Marcos-Ramiro B., Ruiz-Saenz A., Fernandez-Martin L., Bernabe-Rubio M., Kremer L., Ridley A.J., Correas I., Alonso M.A., Millan J.
    Mol. Biol. Cell 24:483-494(2013) [PubMed] [Europe PMC] [Abstract]
• establishment or maintenance of apical/basal cell polarity Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin is essential for epithelial organization and villus morphogenesis in the developing intestine."
    Saotome I., Curto M., McClatchey A.I.
    Dev. Cell 6:855-864(2004) [PubMed] [Europe PMC] [Abstract]
• filopodium assembly Source: RGD <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
  • "Structural plasticity of perisynaptic astrocyte processes involves ezrin and metabotropic glutamate receptors."
    Lavialle M., Aumann G., Anlauf E., Prols F., Arpin M., Derouiche A.
    Proc. Natl. Acad. Sci. U.S.A. 108:12915-12919(2011) [PubMed] [Europe PMC] [Abstract]
• intestinal D-glucose absorption Source: RGDInferred from sequence orthologyⁱ
  • "A new role for the architecture of microvillar actin bundles in apical retention of membrane proteins."
    Revenu C., Ubelmann F., Hurbain I., El-Marjou F., Dingli F., Loew D., Delacour D., Gilet J., Brot-Laroche E., Rivero F., Louvard D., Robine S.
    Mol. Biol. Cell 23:324-336(2012) [PubMed] [Europe PMC] [Abstract]
• leukocyte cell-cell adhesion Source: RGDInferred from sequence orthologyⁱ
  • "Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes."
    Barreiro O., Yanez-Mo M., Serrador J.M., Montoya M.C., Vicente-Manzanares M., Tejedor R., Furthmayr H., Sanchez-Madrid F.
    J. Cell Biol. 157:1233-1245(2002) [PubMed] [Europe PMC] [Abstract]
• membrane to membrane docking Source: RGDInferred from sequence orthologyⁱ
  • "Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes."
    Barreiro O., Yanez-Mo M., Serrador J.M., Montoya M.C., Vicente-Manzanares M., Tejedor R., Furthmayr H., Sanchez-Madrid F.
    J. Cell Biol. 157:1233-1245(2002) [PubMed] [Europe PMC] [Abstract]
• microvillus assembly Source: RGDInferred from sequence orthologyⁱ
  • "Rap2A links intestinal cell polarity to brush border formation."
    Gloerich M., ten Klooster J.P., Vliem M.J., Koorman T., Zwartkruis F.J., Clevers H., Bos J.L.
    Nat. Cell Biol. 14:793-801(2012) [PubMed] [Europe PMC] [Abstract]
• negative regulation of ERK1 and ERK2 cascade Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse."
    Lasserre R., Charrin S., Cuche C., Danckaert A., Thoulouze M.I., de Chaumont F., Duong T., Perrault N., Varin-Blank N., Olivo-Marin J.C., Etienne-Manneville S., Arpin M., Di Bartolo V., Alcover A.
    EMBO J. 29:2301-2314(2010) [PubMed] [Europe PMC] [Abstract]
• negative regulation of interleukin-2 secretion Source: RGDInferred from sequence orthologyⁱ
  • "Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin."
    Ruppelt A., Mosenden R., Gronholm M., Aandahl E.M., Tobin D., Carlson C.R., Abrahamsen H., Herberg F.W., Carpen O., Tasken K.
    J. Immunol. 179:5159-5168(2007) [PubMed] [Europe PMC] [Abstract]
• negative regulation of p38MAPK cascade Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse."
    Lasserre R., Charrin S., Cuche C., Danckaert A., Thoulouze M.I., de Chaumont F., Duong T., Perrault N., Varin-Blank N., Olivo-Marin J.C., Etienne-Manneville S., Arpin M., Di Bartolo V., Alcover A.
    EMBO J. 29:2301-2314(2010) [PubMed] [Europe PMC] [Abstract]
• negative regulation of T cell receptor signaling pathway Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse."
    Lasserre R., Charrin S., Cuche C., Danckaert A., Thoulouze M.I., de Chaumont F., Duong T., Perrault N., Varin-Blank N., Olivo-Marin J.C., Etienne-Manneville S., Arpin M., Di Bartolo V., Alcover A.
    EMBO J. 29:2301-2314(2010) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription by RNA polymerase II Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse."
    Lasserre R., Charrin S., Cuche C., Danckaert A., Thoulouze M.I., de Chaumont F., Duong T., Perrault N., Varin-Blank N., Olivo-Marin J.C., Etienne-Manneville S., Arpin M., Di Bartolo V., Alcover A.
    EMBO J. 29:2301-2314(2010) [PubMed] [Europe PMC] [Abstract]
• phosphatidylinositol-mediated signaling Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin/Exocyst complex regulates mucin 5AC secretion induced by neutrophil elastase in human airway epithelial cells."
    Li Q., Li N., Liu C.Y., Xu R., Kolosov V.P., Perelman J.M., Zhou X.D.
    Cell. Physiol. Biochem. 35:326-338(2015) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cellular protein catabolic process Source: RGDInferred from sequence orthologyⁱ
  • "The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes."
    Chirivino D., Del Maestro L., Formstecher E., Hupe P., Raposo G., Louvard D., Arpin M.
    Mol. Biol. Cell 22:375-385(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of early endosome to late endosome transport Source: RGDInferred from sequence orthologyⁱ
  • "The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes."
    Chirivino D., Del Maestro L., Formstecher E., Hupe P., Raposo G., Louvard D., Arpin M.
    Mol. Biol. Cell 22:375-385(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of gene expression Source: RGDInferred from sequence orthologyⁱ
  • "MYADM controls endothelial barrier function through ERM-dependent regulation of ICAM-1 expression."
    Aranda J.F., Reglero-Real N., Marcos-Ramiro B., Ruiz-Saenz A., Fernandez-Martin L., Bernabe-Rubio M., Kremer L., Ridley A.J., Correas I., Alonso M.A., Millan J.
    Mol. Biol. Cell 24:483-494(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of multicellular organism growth Source: RGDInferred from sequence orthologyⁱ
  • "A new role for the architecture of microvillar actin bundles in apical retention of membrane proteins."
    Revenu C., Ubelmann F., Hurbain I., El-Marjou F., Dingli F., Loew D., Delacour D., Gilet J., Brot-Laroche E., Rivero F., Louvard D., Robine S.
    Mol. Biol. Cell 23:324-336(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein localization to early endosome Source: RGDInferred from sequence orthologyⁱ
  • "The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes."
    Chirivino D., Del Maestro L., Formstecher E., Hupe P., Raposo G., Louvard D., Arpin M.
    Mol. Biol. Cell 22:375-385(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein localization to plasma membrane Source: RGDInferred from sequence orthologyⁱ
  • "A new role for the architecture of microvillar actin bundles in apical retention of membrane proteins."
    Revenu C., Ubelmann F., Hurbain I., El-Marjou F., Dingli F., Loew D., Delacour D., Gilet J., Brot-Laroche E., Rivero F., Louvard D., Robine S.
    Mol. Biol. Cell 23:324-336(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein secretion Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin/Exocyst complex regulates mucin 5AC secretion induced by neutrophil elastase in human airway epithelial cells."
    Li Q., Li N., Liu C.Y., Xu R., Kolosov V.P., Perelman J.M., Zhou X.D.
    Cell. Physiol. Biochem. 35:326-338(2015) [PubMed] [Europe PMC] [Abstract]
• protein kinase A signaling Source: RGDInferred from sequence orthologyⁱ
  • "Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin."
    Ruppelt A., Mosenden R., Gronholm M., Aandahl E.M., Tobin D., Carlson C.R., Abrahamsen H., Herberg F.W., Carpen O., Tasken K.
    J. Immunol. 179:5159-5168(2007) [PubMed] [Europe PMC] [Abstract]
• protein localization to cell cortex Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin interacts with the scaffold protein IQGAP1 and affects its cortical localization."
    Nammalwar R.C., Heil A., Gerke V.
    Biochim. Biophys. Acta 1853:2086-2094(2015) [PubMed] [Europe PMC] [Abstract]
• protein localization to plasma membrane Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin and radixin both regulate the apical membrane localization of ABCC2 (MRP2) in human intestinal epithelial Caco-2 cells."
    Yang Q., Onuki R., Nakai C., Sugiyama Y.
    Exp. Cell Res. 313:3517-3525(2007) [PubMed] [Europe PMC] [Abstract]
  • "Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin."
    Ruppelt A., Mosenden R., Gronholm M., Aandahl E.M., Tobin D., Carlson C.R., Abrahamsen H., Herberg F.W., Carpen O., Tasken K.
    J. Immunol. 179:5159-5168(2007) [PubMed] [Europe PMC] [Abstract]
• receptor internalization Source: RGDInferred from sequence orthologyⁱ
  • "Raf-1 sets the threshold of Fas sensitivity by modulating Rok-alpha signaling."
    Piazzolla D., Meissl K., Kucerova L., Rubiolo C., Baccarini M.
    J. Cell Biol. 171:1013-1022(2005) [PubMed] [Europe PMC] [Abstract]
• regulation of cell shape Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse."
    Lasserre R., Charrin S., Cuche C., Danckaert A., Thoulouze M.I., de Chaumont F., Duong T., Perrault N., Varin-Blank N., Olivo-Marin J.C., Etienne-Manneville S., Arpin M., Di Bartolo V., Alcover A.
    EMBO J. 29:2301-2314(2010) [PubMed] [Europe PMC] [Abstract]
• regulation of microvillus length Source: RGDInferred from sequence orthologyⁱ
  • "A new role for the architecture of microvillar actin bundles in apical retention of membrane proteins."
    Revenu C., Ubelmann F., Hurbain I., El-Marjou F., Dingli F., Loew D., Delacour D., Gilet J., Brot-Laroche E., Rivero F., Louvard D., Robine S.
    Mol. Biol. Cell 23:324-336(2012) [PubMed] [Europe PMC] [Abstract]
• regulation of organelle assembly Source: RGDInferred from sequence orthologyⁱ
  • "The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes."
    Chirivino D., Del Maestro L., Formstecher E., Hupe P., Raposo G., Louvard D., Arpin M.
    Mol. Biol. Cell 22:375-385(2011) [PubMed] [Europe PMC] [Abstract]
• sphingosine-1-phosphate receptor signaling pathway Source: RGDInferred from sequence orthologyⁱ
  • "Sphingosine 1-phosphate induces filopodia formation through S1PR2 activation of ERM proteins."
    Gandy K.A., Canals D., Adada M., Wada M., Roddy P., Snider A.J., Hannun Y.A., Obeid L.M.
    Biochem. J. 449:661-672(2013) [PubMed] [Europe PMC] [Abstract]
• terminal web assembly Source: RGDInferred from sequence orthologyⁱ
  • "A new role for the architecture of microvillar actin bundles in apical retention of membrane proteins."
    Revenu C., Ubelmann F., Hurbain I., El-Marjou F., Dingli F., Loew D., Delacour D., Gilet J., Brot-Laroche E., Rivero F., Louvard D., Robine S.
    Mol. Biol. Cell 23:324-336(2012) [PubMed] [Europe PMC] [Abstract]

<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

<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

Keywords - Cellular componentⁱ

<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

2D gel 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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stageⁱ

Gene expression 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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• actin binding Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin and radixin both regulate the apical membrane localization of ABCC2 (MRP2) in human intestinal epithelial Caco-2 cells."
    Yang Q., Onuki R., Nakai C., Sugiyama Y.
    Exp. Cell Res. 313:3517-3525(2007) [PubMed] [Europe PMC] [Abstract]
• actin filament binding Source: UniProtKB
• ATPase binding Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin and radixin both regulate the apical membrane localization of ABCC2 (MRP2) in human intestinal epithelial Caco-2 cells."
    Yang Q., Onuki R., Nakai C., Sugiyama Y.
    Exp. Cell Res. 313:3517-3525(2007) [PubMed] [Europe PMC] [Abstract]
• cell adhesion molecule binding Source: BHF-UCL
• disordered domain specific binding Source: RGDInferred from sequence orthologyⁱ
  • "Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins."
    Tyukhtenko S., Deshmukh L., Kumar V., Lary J., Cole J., Lemmon V., Vinogradova O.
    Biochemistry 47:4160-4168(2008) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: RGDInferred from sequence orthologyⁱ
  • "Toward an understanding of the protein interaction network of the human liver."
    Wang J., Huo K., Ma L., Tang L., Li D., Huang X., Yuan Y., Li C., Wang W., Guan W., Chen H., Jin C., Wei J., Zhang W., Yang Y., Liu Q., Zhou Y., Zhang C.

    , Wu Z., Xu W., Zhang Y., Liu T., Yu D., Zhang Y., Chen L., Zhu D., Zhong X., Kang L., Gan X., Yu X., Ma Q., Yan J., Zhou L., Liu Z., Zhu Y., Zhou T., He F., Yang X.
    Mol. Syst. Biol. 7:536-536(2011) [PubMed] [Europe PMC] [Abstract]
  • "An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations."
    Liu X., Salokas K., Tamene F., Jiu Y., Weldatsadik R.G., Ohman T., Varjosalo M.
    Nat Commun 9:1188-1188(2018) [PubMed] [Europe PMC] [Abstract]
• microtubule binding Source: RGDInferred from sequence orthologyⁱ
  • "The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex."
    Solinet S., Mahmud K., Stewman S.F., Ben El Kadhi K., Decelle B., Talje L., Ma A., Kwok B.H., Carreno S.
    J. Cell Biol. 202:251-260(2013) [PubMed] [Europe PMC] [Abstract]
• protein C-terminus binding Source: RGDInferred from sequence orthologyⁱ
  • "Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins."
    Tyukhtenko S., Deshmukh L., Kumar V., Lary J., Cole J., Lemmon V., Vinogradova O.
    Biochemistry 47:4160-4168(2008) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: RGDInferred from physical interactionⁱ
  • "A functional FERM domain binding motif in neurofascin."
    Gunn-Moore F.J., Hill M., Davey F., Herron L.R., Tait S., Sherman D., Brophy P.J.
    Mol. Cell. Neurosci. 33:441-446(2006) [PubMed] [Europe PMC] [Abstract]
• protein kinase A binding Source: RGDInferred from sequence orthologyⁱ
  • "A systematic evaluation of protein kinase A-A-Kinase anchoring protein interaction motifs."
    Burgers P.P., van der Heyden M.A., Kok B., Heck A.J., Scholten A.
    Biochemistry 54:11-21(2015) [PubMed] [Europe PMC] [Abstract]
• protein kinase A catalytic subunit binding Source: RGDInferred from sequence orthologyⁱ
  • "Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin."
    Ruppelt A., Mosenden R., Gronholm M., Aandahl E.M., Tobin D., Carlson C.R., Abrahamsen H., Herberg F.W., Carpen O., Tasken K.
    J. Immunol. 179:5159-5168(2007) [PubMed] [Europe PMC] [Abstract]
• protein kinase A regulatory subunit binding Source: RGDInferred from sequence orthologyⁱ
  • "Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin."
    Ruppelt A., Mosenden R., Gronholm M., Aandahl E.M., Tobin D., Carlson C.R., Abrahamsen H., Herberg F.W., Carpen O., Tasken K.
    J. Immunol. 179:5159-5168(2007) [PubMed] [Europe PMC] [Abstract]
• S100 protein binding Source: RGDInferred from sequence orthologyⁱ
  • "Ezrin interacts with the scaffold protein IQGAP1 and affects its cortical localization."
    Nammalwar R.C., Heil A., Gerke V.
    Biochim. Biophys. Acta 1853:2086-2094(2015) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction 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

3D structure 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

<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 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV 
        60         70         80         90        100
DNKGFPTWLK LDKKVSAQEV RKENPVQFKF RAKFYPEDVA DELIQDITQK 
       110        120        130        140        150
LFFLQVKEGI LSDEIYCPPE TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE 
       160        170        180        190        200
RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR GMLKDSAMLE YLKIAQDLEM 
       210        220        230        240        250
YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF PWSEIRNISF 
       260        270        280        290        300
NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI 
       310        320        330        340        350
EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR 
       360        370        380        390        400
LQDFEQKTKR AEKELSEQIE KALQLEEERR RAQEEAERLE ADRMAALRAK 
       410        420        430        440        450
EELERQAQDQ IKSQEQLAAE LAEYTAKIAL LEEARRRKED EVEEWQHRAK 
       460        470        480        490        500
EAQDDLVKTK EELHLVMTAP PPPPPPVYEP VNYHVQEGLQ DEGAEPMGYS 
       510        520        530        540        550
AELSSEGILD DRNEEKRITE AEKNERVQRQ LLTLSNELSQ ARDENKRTHN 
       560        570        580 
DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM                

Experimental Info

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

• 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

PTM databases

2D gel databases

Proteomic 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