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UniProtKB/Swiss-Prot entry P15311


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

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Entry information
Entry name EZRI_HUMAN
Primary accession number P15311
Secondary accession numbers P23714 Q4VX75 Q96CU8 Q9NSJ4
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on February 6, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 102)
Name and origin of the protein
Protein name Ezrin
Synonyms p81
Cytovillin
Villin-2
Gene name
Name: EZR
Synonyms: VIL2
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], PARTIAL PROTEIN SEQUENCE, AND VARIANT VAL-532.
PubMed=2591371 [NCBI, ExPASy, EBI, Israel, Japan]
Gould K.L., Bretscher A., Esch F.S., Hunter T.;
"cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1.";
EMBO J. 8:4133-4142(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-532.
TISSUE=Placenta;
PubMed=2674140 [NCBI, ExPASy, EBI, Israel, Japan]
Turunen O., Winqvist R., Pakkanen R., Grzeschik K.-H., Wahlstroem T., Vaheri A.;
"Cytovillin, a microvillar Mr 75,000 protein. cDNA sequence, prokaryotic expression, and chromosomal localization.";
J. Biol. Chem. 264:16727-16732(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Melanoma;
The German cDNA consortium;
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
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]
PROTEIN SEQUENCE OF 172-180 AND 343-350.
DOI=10.1006/bbrc.1996.1082; PubMed=8713105 [NCBI, ExPASy, EBI, Israel, Japan]
Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.;
"Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes.";
Biochem. Biophys. Res. Commun. 224:666-674(1996).
[7]
PHOSPHORYLATION BY PDGFR.
PubMed=1382070 [NCBI, ExPASy, EBI, Israel, Japan]
Krieg J., Hunter T.;
"Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin.";
J. Biol. Chem. 267:19258-19265(1992).
[8]
PHOSPHORYLATION.
PubMed=1381389 [NCBI, ExPASy, EBI, Israel, Japan]
Egerton M., Burgess W.H., Chen D., Druker B.J., Bretscher A., Samelson L.E.;
"Identification of ezrin as an 81-kDa tyrosine-phosphorylated protein in T cells.";
J. Immunol. 149:1847-1852(1992).
[9]
INTERACTION WITH SLC9A3R1.
DOI=10.1083/jcb.139.1.169; PubMed=9314537 [NCBI, ExPASy, EBI, Israel, Japan]
Reczek D., Berryman M., Bretscher A.;
"Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family.";
J. Cell Biol. 139:169-179(1997).
[10]
INTERACTION WITH SCYL3.
TISSUE=Kidney;
DOI=10.1016/S0014-4827(02)00054-X; PubMed=12651155 [NCBI, ExPASy, EBI, Israel, Japan]
Sullivan A., Uff C.R., Isacke C.M., Thorne R.F.;
"PACE-1, a novel protein that interacts with the C-terminal domain of ezrin.";
Exp. Cell Res. 284:224-238(2003).
[11]
INTERACTION WITH NGX6.
DOI=10.1093/carcin/bgh312; PubMed=15498789 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Role of a novel EGF-like domain-containing gene NGX6 in cell adhesion modulation in nasopharyngeal carcinoma cells.";
Carcinogenesis 26:281-291(2005).
[12]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
DOI=10.1016/j.mcn.2004.11.014; PubMed=15797715 [NCBI, ExPASy, EBI, Israel, Japan]
Groenholm M., Teesalu T., Tyynelaa J., Piltti K., Boehling T., Wartiovaara K., Vaheri A., Carpen O.;
"Characterization of the NF2 protein merlin and the ERM protein ezrin in human, rat, and mouse central nervous system.";
Mol. Cell. Neurosci. 28:683-693(2005).
[13]
FUNCTION, AND INTERACTION WITH PLEKHG6.
DOI=10.1091/mbc.E06-12-1144; PubMed=17881735 [NCBI, ExPASy, EBI, Israel, Japan]
D'Angelo R., Aresta S., Blangy A., Del Maestro L., Louvard D., Arpin M.;
"Interaction of ezrin with the novel guanine nucleotide exchange factor PLEKHG6 promotes RhoG-dependent apical cytoskeleton rearrangements in epithelial cells.";
Mol. Biol. Cell 18:4780-4793(2007).
[14]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-297.
DOI=10.1074/jbc.M210601200; PubMed=12429733 [NCBI, ExPASy, EBI, Israel, Japan]
Smith W.J., Nassar N., Bretscher A., Cerione R.A., Karplus P.A.;
"Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions.";
J. Biol. Chem. 278:4949-4956(2003).
Comments
  • FUNCTION: 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.
  • SUBUNIT: Interacts with MPP5 (By similarity). Interacts with SLC9A3R1 and SCYL3/PACE1. Interacts with PLEKHG6. Interacts with NGX6.
  • INTERACTION:
    P60520:GABARAPL2; NbExp=1; IntAct=EBI-1056902, EBI-720116;
    P30480:HLA-B; NbExp=1; IntAct=EBI-1056902, EBI-1054175;
    P23508:MCC; NbExp=1; IntAct=EBI-1056902, EBI-307531;
    Q9Y478:PRKAB1; NbExp=1; IntAct=EBI-1056902, EBI-719769;
    Q8IZE3:SCYL3; NbExp=2; IntAct=EBI-1056902, EBI-1380680;
  • SUBCELLULAR LOCATION: Apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Cell projection, microvillus membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. 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).
  • TISSUE SPECIFICITY: 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.
  • DEVELOPMENTAL STAGE: 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.
  • PTM: Phosphorylated by tyrosine-protein kinases.
  • SIMILARITY: Contains 1 FERM domain.
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
X51521; CAA35893.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J05021; AAA61278.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL162086; CAB82418.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL589931; CAI95307.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013903; AAH13903.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A34400; A34400.
RefSeq NP_001104547.1; -.
NP_003370.2; -.
UniGene Hs.487027
3D structure databases
PDB
1NI2; X-ray; 2.30 A; A/B=2-297.[ExPASy / RCSB / EBI]
PDBsum 1NI2; -.
ModBase P15311.
Protein-protein interaction databases
IntAct P15311; -.
PTM databases
PhosphoSite P15311; -.
2D gel databases
SWISS-2DPAGE P15311; -.
DOSAC-COBS-2DPAGE P15311; -.
REPRODUCTION-2DPAGE IPI00843975; -.
Organism-specific databases
HGNC HGNC:12691; EZR.
GenAtlas EZR.
HPA CAB004035; -.
MIM 123900; gene. [NCBI / EBI]
PharmGKB PA37310; -.
GeneCards P15311.
Gene expression databases
ArrayExpress P15311; -.
CleanEx HS_EZR; -.
GermOnline ENSG00000092820; Homo sapiens.
Ontologies
GO
GO:0005884; Cellular component: actin filament (inferred from direct assay from HGNC).
GO:0045177; Cellular component: apical part of cell (inferred from direct assay from UniProtKB).
GO:0030863; Cellular component: cortical cytoskeleton (traceable author statement from HGNC).
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0019898; Cellular component: extrinsic to membrane (inferred from direct assay from UniProtKB).
GO:0030175; Cellular component: filopodium (inferred from direct assay from UniProtKB).
GO:0005902; Cellular component: microvillus (non-traceable author statement from UniProtKB).
GO:0001726; Cellular component: ruffle (inferred from direct assay from UniProtKB).
GO:0051015; Molecular function: actin filament binding (inferred from direct assay from UniProtKB).
GO:0050839; Molecular function: cell adhesion molecule binding (inferred from physical interaction from UniProtKB).
GO:0043621; Molecular function: protein self-association (inferred from physical interaction from UniProtKB).
GO:0051017; Biological process: actin filament bundle formation (inferred from direct assay from UniProtKB).
GO:0007016; Biological process: cytoskeletal anchoring at plasma membrane (non-traceable author statement from UniProtKB).
GO:0007159; Biological process: leukocyte adhesion (inferred from expression pattern from UniProtKB).
GO:0022614; Biological process: membrane to membrane docking (inferred from expression pattern from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000299; Band_4.1_N.
IPR011174; ERM.
IPR011259; ERM_C.
IPR000798; Ez/rad/moesin.
IPR014352; FERM/acyl-CoA_bd_prot_3-hlx.
IPR011993; PH_type.
Graphical view of domain structure.
Gene3D G3DSA:1.20.80.10; ACBP; 1.
G3DSA:2.30.29.30; PH_type; 1.
Pfam PF00373; Band_41; 1.
PF00769; ERM; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF002305; ERM; 1.
PRINTS PR00935; BAND41.
PR00661; ERMFAMILY.
SMART SM00295; B41; 1.
SMART graphical view of domain structure.
PROSITE PS00660; FERM_1; 1.
PS00661; FERM_2; 1.
PS50057; FERM_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P15311.
Genome annotation databases
Ensembl ENSG00000092820; Homo sapiens. [Contig view]
GeneID 7430; -.
KEGG hsa:7430; -.
Phylogenomic databases
HOVERGEN P15311; -.
Other
SOURCE EZR; Homo sapiens.
ProtoNet P15311.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Cell projection; Cell shape; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism; Structural protein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   586  585     Ezrin. PRO_0000219408
DOMAIN   2   295  294     FERM. 
REGION   244   586  343     Interaction with SCYL3. 
MOD_RES   146   146        Phosphotyrosine; by PDGFR. 
MOD_RES   354   354        Phosphotyrosine; by PDGFR. 
VARIANT   180   180  1     R -> C (in dbSNP:rs3103004 [NCBI]). VAR_030572 [3D]
VARIANT   494   494  1     A -> P (in dbSNP:rs2230143 [NCBI]). VAR_030573 
VARIANT   532   532  1     L -> V. VAR_015112 
STRAND   5    11  7      
STRAND   14    20  7      
HELIX   26    37  12      
HELIX   42    44  3      
STRAND   45    51  7      
STRAND   56    58  3      
STRAND   61    64  4      
HELIX   65    67  3      
STRAND   74    84  11      
HELIX   89    92  4      
HELIX   96   111  16      
HELIX   119   134  16      
TURN   139   141  3      
STRAND   146   149  4      
HELIX   155   160  6      
HELIX   165   178  14      
HELIX   184   195  12      
TURN   199   202  4      
STRAND   204   210  7      
STRAND   215   220  6      
STRAND   222   229  8      
STRAND   232   235  4      
STRAND   237   242  6      
STRAND   245   253  9      
STRAND   255   262  8      
STRAND   268   270  3      
HELIX   274   293  20      
Sequence information
Length: 586 AA [This is the length of the unprocessed precursor] Molecular weight: 69413 Da [This is the MW of the unprocessed precursor] CRC64: F1B592CF49A7CC46 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLHYV DNKGFPTWLK 

        70         80         90        100        110        120 
LDKKVSAQEV RKENPLQFKF RAKFYPEDVA EELIQDITQK LFFLQVKEGI LSDEIYCPPE 

       130        140        150        160        170        180 
TAVLLGSYAV QAKFGDYNKE VHKSGYLSSE RLIPQRVMDQ HKLTRDQWED RIQVWHAEHR 

       190        200        210        220        230        240 
GMLKDNAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF 

       250        260        270        280        290        300 
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI 

       310        320        330        340        350        360 
EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM MREKEELMLR LQDYEEKTKK 

       370        380        390        400        410        420 
AERELSEQIQ RALQLEEERK RAQEEAERLE ADRMAALRAK EELERQAVDQ IKSQEQLAAE 

       430        440        450        460        470        480 
LAEYTAKIAL LEEARRRKED EVEEWQHRAK EAQDDLVKTK EELHLVMTAP PPPPPPVYEP 

       490        500        510        520        530        540 
VSYHVQESLQ DEGAEPTGYS AELSSEGIRD DRNEEKRITE AEKNERVQRQ LLTLSSELSQ 

       550        560        570        580 
ARDENKRTHN DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAL 

P15311 in FASTA format

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