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P15311

- EZRI_HUMAN

UniProt

P15311 - EZRI_HUMAN

Protein

Ezrin

Gene

EZR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 4 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis.3 Publications

    Enzyme regulationi

    A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding.By similarity

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. cell adhesion molecule binding Source: BHF-UCL
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin filament bundle assembly Source: UniProtKB
    2. axon guidance Source: Reactome
    3. cytoskeletal anchoring at plasma membrane Source: UniProtKB
    4. establishment of endothelial barrier Source: UniProt
    5. establishment or maintenance of apical/basal cell polarity Source: Ensembl
    6. filopodium assembly Source: Ensembl
    7. leukocyte cell-cell adhesion Source: BHF-UCL
    8. membrane to membrane docking Source: BHF-UCL
    9. positive regulation of gene expression Source: UniProt
    10. receptor internalization Source: Ensembl
    11. regulation of cell shape Source: UniProtKB-KW

    Keywords - Biological processi

    Cell shape

    Enzyme and pathway databases

    ReactomeiREACT_22237. Netrin-1 signaling.
    REACT_22365. Recycling pathway of L1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ezrin
    Alternative name(s):
    Cytovillin
    Villin-2
    p81
    Gene namesi
    Name:EZR
    Synonyms:VIL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:12691. EZR.

    Subcellular locationi

    Apical cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell projection 1 Publication. Cell projectionmicrovillus membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell projectionruffle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmcell cortex 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Localizes to cell extensions and peripheral processes of astrocytes By similarity. Microvillar peripheral membrane protein (cytoplasmic side).By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. actin filament Source: HGNC
    3. apical part of cell Source: BHF-UCL
    4. apical plasma membrane Source: UniProtKB-SubCell
    5. astrocyte projection Source: Ensembl
    6. basolateral plasma membrane Source: UniProtKB
    7. cell body Source: Ensembl
    8. cell tip Source: Ensembl
    9. cortical cytoskeleton Source: HGNC
    10. cytosol Source: UniProtKB
    11. extracellular space Source: UniProt
    12. extracellular vesicular exosome Source: UniProt
    13. extrinsic component of membrane Source: UniProtKB
    14. filopodium Source: BHF-UCL
    15. membrane Source: UniProtKB
    16. membrane raft Source: Ensembl
    17. microspike Source: Ensembl
    18. microvillus Source: BHF-UCL
    19. microvillus membrane Source: UniProtKB-SubCell
    20. nucleolus Source: HPA
    21. plasma membrane Source: HPA
    22. ruffle Source: UniProtKB
    23. ruffle membrane Source: UniProtKB-SubCell
    24. Schwann cell microvillus Source: Ensembl
    25. T-tubule Source: Ensembl
    26. uropod Source: Ensembl
    27. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162385512.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 586585EzrinPRO_0000219408Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei60 – 601N6-acetyllysine1 Publication
    Modified residuei146 – 1461Phosphotyrosine; by PDGFR3 Publications
    Modified residuei354 – 3541Phosphotyrosine; by PDGFR2 Publications
    Modified residuei478 – 4781Phosphotyrosine2 Publications
    Modified residuei535 – 5351Phosphoserine2 Publications
    Modified residuei567 – 5671Phosphothreonine; by ROCK2 and PKC/PRKCI2 Publications

    Post-translational modificationi

    Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP15311.
    PaxDbiP15311.
    PRIDEiP15311.

    2D gel databases

    DOSAC-COBS-2DPAGEP15311.
    REPRODUCTION-2DPAGEIPI00843975.
    SWISS-2DPAGEP15311.

    PTM databases

    PhosphoSiteiP15311.

    Expressioni

    Tissue specificityi

    Expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. Weakly expressed in brain stem and diencephalon. Stronger expression was detected in gray matter of frontal lobe compared to white matter (at protein level). Component of the microvilli of intestinal epithelial cells. Preferentially expressed in astrocytes of hippocampus, frontal cortex, thalamus, parahippocampal cortex, amygdala, insula, and corpus callosum. Not detected in neurons in most tissues studied.1 Publication

    Developmental stagei

    Very strong staining is detected in the Purkinje cell layer and in part of the molecular layer of the infant brain compared to adult brain.1 Publication

    Gene expression databases

    ArrayExpressiP15311.
    BgeeiP15311.
    CleanExiHS_EZR.
    GenevestigatoriP15311.

    Organism-specific databases

    HPAiCAB004035.
    CAB047324.
    HPA021616.

    Interactioni

    Subunit structurei

    Interacts with MPP5 and SLC9A3R2. Found in a complex with EZR, PODXL and SLC9A3R2 By similarity. Interacts with MCC, PLEKHG6, PODXL, SCYL3/PACE1, SLC9A3R1 and TMEM8B. Interacts (when phosphorylated) with FES/FPS. Interacts with dimeric S100P, the interaction may be activating through unmasking of F-actin binding sites.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAPN1P073842EBI-1056902,EBI-1542113
    FESP073328EBI-1056902,EBI-1055635
    MDM2Q009873EBI-1056902,EBI-389668
    SCYL3Q8IZE34EBI-1056902,EBI-1380680

    Protein-protein interaction databases

    BioGridi113271. 91 interactions.
    DIPiDIP-38868N.
    IntActiP15311. 27 interactions.
    MINTiMINT-195721.
    STRINGi9606.ENSP00000338934.

    Structurei

    Secondary structure

    1
    586
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Beta strandi14 – 207
    Helixi26 – 3712
    Helixi42 – 443
    Beta strandi45 – 517
    Beta strandi56 – 583
    Beta strandi61 – 644
    Helixi65 – 673
    Beta strandi74 – 8411
    Helixi89 – 924
    Helixi96 – 11116
    Helixi119 – 13416
    Turni139 – 1413
    Beta strandi146 – 1494
    Helixi155 – 1606
    Helixi165 – 17814
    Helixi184 – 19512
    Turni199 – 2024
    Beta strandi204 – 2107
    Beta strandi215 – 2206
    Beta strandi222 – 2298
    Beta strandi232 – 2354
    Beta strandi237 – 2426
    Beta strandi245 – 2539
    Beta strandi255 – 2628
    Beta strandi268 – 2703
    Helixi274 – 29320

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NI2X-ray2.30A/B2-297[»]
    ProteinModelPortaliP15311.
    SMRiP15311. Positions 1-586.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15311.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 295294FERMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni244 – 586343Interaction with SCYL3Add
    BLAST

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG236035.
    HOGENOMiHOG000007113.
    HOVERGENiHBG002185.
    KOiK08007.
    OMAiLQDEGTE.
    OrthoDBiEOG7BGHK6.
    PhylomeDBiP15311.
    TreeFamiTF313935.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    IPR011174. ERM.
    IPR011259. ERM_C_dom.
    IPR000798. Ez/rad/moesin_like.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR019747. FERM_CS.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR018980. FERM_PH-like_C.
    IPR008954. Moesin_tail.
    IPR011993. PH_like_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00769. ERM. 1 hit.
    PF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002305. ERM. 1 hit.
    PRINTSiPR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTiSM00295. B41. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF48678. SSF48678. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15311-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLHYV    50
    DNKGFPTWLK LDKKVSAQEV RKENPLQFKF RAKFYPEDVA EELIQDITQK 100
    LFFLQVKEGI LSDEIYCPPE TAVLLGSYAV QAKFGDYNKE VHKSGYLSSE 150
    RLIPQRVMDQ HKLTRDQWED RIQVWHAEHR GMLKDNAMLE YLKIAQDLEM 200
    YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF PWSEIRNISF 250
    NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI 300
    EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM MREKEELMLR 350
    LQDYEEKTKK AERELSEQIQ RALQLEEERK RAQEEAERLE ADRMAALRAK 400
    EELERQAVDQ IKSQEQLAAE LAEYTAKIAL LEEARRRKED EVEEWQHRAK 450
    EAQDDLVKTK EELHLVMTAP PPPPPPVYEP VSYHVQESLQ DEGAEPTGYS 500
    AELSSEGIRD DRNEEKRITE AEKNERVQRQ LLTLSSELSQ ARDENKRTHN 550
    DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAL 586
    Length:586
    Mass (Da):69,413
    Last modified:February 6, 2007 - v4
    Checksum:iF1B592CF49A7CC46
    GO

    Sequence cautioni

    The sequence AAA61278.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB82418.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti180 – 1801R → C.
    Corresponds to variant rs3103004 [ dbSNP | Ensembl ].
    VAR_030572
    Natural varianti494 – 4941A → P.
    Corresponds to variant rs2230143 [ dbSNP | Ensembl ].
    VAR_030573
    Natural varianti532 – 5321L → V.2 Publications
    VAR_015112

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51521 mRNA. Translation: CAA35893.1.
    J05021 mRNA. Translation: AAA61278.1. Different initiation.
    AL162086 mRNA. Translation: CAB82418.1. Different initiation.
    AL589931 Genomic DNA. Translation: CAI95307.1.
    CH471051 Genomic DNA. Translation: EAW47647.1.
    BC013903 mRNA. Translation: AAH13903.1.
    CCDSiCCDS5258.1.
    PIRiA34400.
    RefSeqiNP_001104547.1. NM_001111077.1.
    NP_003370.2. NM_003379.4.
    UniGeneiHs.487027.

    Genome annotation databases

    EnsembliENST00000337147; ENSP00000338934; ENSG00000092820.
    ENST00000367075; ENSP00000356042; ENSG00000092820.
    GeneIDi7430.
    KEGGihsa:7430.
    UCSCiuc003qrt.4. human.

    Polymorphism databases

    DMDMi125987826.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51521 mRNA. Translation: CAA35893.1 .
    J05021 mRNA. Translation: AAA61278.1 . Different initiation.
    AL162086 mRNA. Translation: CAB82418.1 . Different initiation.
    AL589931 Genomic DNA. Translation: CAI95307.1 .
    CH471051 Genomic DNA. Translation: EAW47647.1 .
    BC013903 mRNA. Translation: AAH13903.1 .
    CCDSi CCDS5258.1.
    PIRi A34400.
    RefSeqi NP_001104547.1. NM_001111077.1.
    NP_003370.2. NM_003379.4.
    UniGenei Hs.487027.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NI2 X-ray 2.30 A/B 2-297 [» ]
    ProteinModelPortali P15311.
    SMRi P15311. Positions 1-586.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113271. 91 interactions.
    DIPi DIP-38868N.
    IntActi P15311. 27 interactions.
    MINTi MINT-195721.
    STRINGi 9606.ENSP00000338934.

    Chemistry

    ChEMBLi CHEMBL1932896.

    PTM databases

    PhosphoSitei P15311.

    Polymorphism databases

    DMDMi 125987826.

    2D gel databases

    DOSAC-COBS-2DPAGE P15311.
    REPRODUCTION-2DPAGE IPI00843975.
    SWISS-2DPAGE P15311.

    Proteomic databases

    MaxQBi P15311.
    PaxDbi P15311.
    PRIDEi P15311.

    Protocols and materials databases

    DNASUi 7430.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337147 ; ENSP00000338934 ; ENSG00000092820 .
    ENST00000367075 ; ENSP00000356042 ; ENSG00000092820 .
    GeneIDi 7430.
    KEGGi hsa:7430.
    UCSCi uc003qrt.4. human.

    Organism-specific databases

    CTDi 7430.
    GeneCardsi GC06M159186.
    HGNCi HGNC:12691. EZR.
    HPAi CAB004035.
    CAB047324.
    HPA021616.
    MIMi 123900. gene.
    neXtProti NX_P15311.
    PharmGKBi PA162385512.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236035.
    HOGENOMi HOG000007113.
    HOVERGENi HBG002185.
    KOi K08007.
    OMAi LQDEGTE.
    OrthoDBi EOG7BGHK6.
    PhylomeDBi P15311.
    TreeFami TF313935.

    Enzyme and pathway databases

    Reactomei REACT_22237. Netrin-1 signaling.
    REACT_22365. Recycling pathway of L1.

    Miscellaneous databases

    ChiTaRSi EZR. human.
    EvolutionaryTracei P15311.
    GeneWikii Ezrin.
    GenomeRNAii 7430.
    NextBioi 29100.
    PROi P15311.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15311.
    Bgeei P15311.
    CleanExi HS_EZR.
    Genevestigatori P15311.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    IPR011174. ERM.
    IPR011259. ERM_C_dom.
    IPR000798. Ez/rad/moesin_like.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR019747. FERM_CS.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR018980. FERM_PH-like_C.
    IPR008954. Moesin_tail.
    IPR011993. PH_like_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00769. ERM. 1 hit.
    PF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002305. ERM. 1 hit.
    PRINTSi PR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTi SM00295. B41. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF48678. SSF48678. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1."
      Gould K.L., Bretscher A., Esch F.S., Hunter T.
      EMBO J. 8:4133-4142(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT VAL-532.
    2. "Cytovillin, a microvillar Mr 75,000 protein. cDNA sequence, prokaryotic expression, and chromosomal localization."
      Turunen O., Winqvist R., Pakkanen R., Grzeschik K.-H., Wahlstroem T., Vaheri A.
      J. Biol. Chem. 264:16727-16732(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-532.
      Tissue: Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Melanoma.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Colon.
    7. "Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes."
      Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.
      Biochem. Biophys. Res. Commun. 224:666-674(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 172-180 AND 343-350.
    8. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 264-273; 428-435 AND 530-542, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    9. "Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin."
      Krieg J., Hunter T.
      J. Biol. Chem. 267:19258-19265(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-146 AND TYR-354 BY PDGFR.
    10. "Identification of ezrin as an 81-kDa tyrosine-phosphorylated protein in T cells."
      Egerton M., Burgess W.H., Chen D., Druker B.J., Bretscher A., Samelson L.E.
      J. Immunol. 149:1847-1852(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    11. "Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family."
      Reczek D., Berryman M., Bretscher A.
      J. Cell Biol. 139:169-179(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC9A3R1.
    12. "PACE-1, a novel protein that interacts with the C-terminal domain of ezrin."
      Sullivan A., Uff C.R., Isacke C.M., Thorne R.F.
      Exp. Cell Res. 284:224-238(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCYL3.
      Tissue: Kidney.
    13. "Ca2+-dependent binding and activation of dormant ezrin by dimeric S100P."
      Koltzscher M., Neumann C., Konig S., Gerke V.
      Mol. Biol. Cell 14:2372-2384(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH S100P.
    14. "Role of a novel EGF-like domain-containing gene NGX6 in cell adhesion modulation in nasopharyngeal carcinoma cells."
      Ma J., Zhou J., Fan S., Wang L.-L., Li X.-L., Yan Q., Zhou M., Liu H.-Y., Zhang Q., Zhou H., Gan K., Li Z., Peng C., Xiong W., Tan C., Shen S.-R., Yang J., Li J., Li G.-Y.
      Carcinogenesis 26:281-291(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMEM8B.
    15. "Characterization of the NF2 protein merlin and the ERM protein ezrin in human, rat, and mouse central nervous system."
      Groenholm M., Teesalu T., Tyynelaa J., Piltti K., Boehling T., Wartiovaara K., Vaheri A., Carpen O.
      Mol. Cell. Neurosci. 28:683-693(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    16. "Podocalyxin increases the aggressive phenotype of breast and prostate cancer cells in vitro through its interaction with ezrin."
      Sizemore S., Cicek M., Sizemore N., Ng K.P., Casey G.
      Cancer Res. 67:6183-6191(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PODXL.
    17. "Interaction of ezrin with the novel guanine nucleotide exchange factor PLEKHG6 promotes RhoG-dependent apical cytoskeleton rearrangements in epithelial cells."
      D'Angelo R., Aresta S., Blangy A., Del Maestro L., Louvard D., Arpin M.
      Mol. Biol. Cell 18:4780-4793(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PLEKHG6.
    18. "Spatial recruitment and activation of the Fes kinase by ezrin promotes HGF-induced cell scattering."
      Naba A., Reverdy C., Louvard D., Arpin M.
      EMBO J. 27:38-50(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FES/FPS, PHOSPHORYLATION AT TYR-146 AND TYR-478, SUBCELLULAR LOCATION.
    19. "Atypical protein kinase C (iota) activates ezrin in the apical domain of intestinal epithelial cells."
      Wald F.A., Oriolo A.S., Mashukova A., Fregien N.L., Langshaw A.H., Salas P.J.
      J. Cell Sci. 121:644-654(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-567.
    20. "Generation and characterization of a novel, permanently active S100P mutant."
      Austermann J., Nazmi A.R., Heil A., Fritz G., Kolinski M., Filipek S., Gerke V.
      Biochim. Biophys. Acta 1793:1078-1085(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH S100P.
    21. "MCC, a new interacting protein for Scrib, is required for cell migration in epithelial cells."
      Arnaud C., Sebbagh M., Nola S., Audebert S., Bidaut G., Hermant A., Gayet O., Dusetti N.J., Ollendorff V., Santoni M.J., Borg J.P., Lecine P.
      FEBS Lett. 583:2326-2332(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCC.
    22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions."
      Smith W.J., Nassar N., Bretscher A., Cerione R.A., Karplus P.A.
      J. Biol. Chem. 278:4949-4956(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-297.

    Entry informationi

    Entry nameiEZRI_HUMAN
    AccessioniPrimary (citable) accession number: P15311
    Secondary accession number(s): E1P5A8
    , P23714, Q4VX75, Q96CU8, Q9NSJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 168 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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