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P15311 (EZRI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ezrin
Alternative name(s):
Cytovillin
Villin-2
p81
Gene names
Name:EZR
Synonyms:VIL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Ref.17 Ref.19 Ref.20

Enzyme regulation

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.

Subunit structure

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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21

Subcellular location

Apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Cell projectionmicrovillus membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcell cortex. Cytoplasmcytoskeleton. 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). Ref.18

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. Ref.15

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. Ref.15

Post-translational modification

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. Ref.9 Ref.10 Ref.18 Ref.19

Sequence similarities

Contains 1 FERM domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processCell shape
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityPolymorphism
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament bundle assembly

Inferred from direct assay PubMed 10793131. Source: UniProtKB

axon guidance

Traceable author statement. Source: Reactome

cytoskeletal anchoring at plasma membrane

Non-traceable author statement PubMed 10793131. Source: UniProtKB

establishment of endothelial barrier

Inferred from genetic interaction PubMed 23264465. Source: UniProt

establishment or maintenance of apical/basal cell polarity

Inferred from electronic annotation. Source: Ensembl

filopodium assembly

Inferred from electronic annotation. Source: Ensembl

leukocyte cell-cell adhesion

Inferred from expression pattern PubMed 12082081. Source: BHF-UCL

membrane to membrane docking

Inferred from expression pattern PubMed 12082081. Source: BHF-UCL

positive regulation of gene expression

Inferred from genetic interaction PubMed 23264465. Source: UniProt

receptor internalization

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSchwann cell microvillus

Inferred from electronic annotation. Source: Ensembl

T-tubule

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Inferred from direct assay PubMed 10793131. Source: UniProtKB

actin filament

Inferred from direct assay PubMed 11598191. Source: HGNC

apical part of cell

Inferred from direct assay PubMed 12082081. Source: BHF-UCL

apical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

astrocyte projection

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cell body

Inferred from electronic annotation. Source: Ensembl

cell tip

Inferred from electronic annotation. Source: Ensembl

cortical cytoskeleton

Traceable author statement PubMed 11598191. Source: HGNC

cytosol

Inferred from direct assay PubMed 9852149. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

extrinsic component of membrane

Inferred from direct assay PubMed 7844168. Source: UniProtKB

filopodium

Inferred from direct assay PubMed 12082081. Source: BHF-UCL

membrane raft

Inferred from electronic annotation. Source: Ensembl

microspike

Inferred from electronic annotation. Source: Ensembl

microvillus

Inferred from direct assay PubMed 12082081. Source: BHF-UCL

microvillus membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

ruffle

Inferred from direct assay PubMed 9852149. Source: UniProtKB

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

uropod

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactin filament binding

Inferred from direct assay PubMed 10793131. Source: UniProtKB

cell adhesion molecule binding

Inferred from physical interaction PubMed 12082081Ref.14. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 586585Ezrin
PRO_0000219408

Regions

Domain2 – 295294FERM
Region244 – 586343Interaction with SCYL3

Amino acid modifications

Modified residue601N6-acetyllysine Ref.22
Modified residue1461Phosphotyrosine; by PDGFR Ref.18
Modified residue3541Phosphotyrosine; by PDGFR
Modified residue4781Phosphotyrosine Ref.18
Modified residue5351Phosphoserine Ref.24
Modified residue5671Phosphothreonine; by ROCK2 and PKC/PRKCI Probable

Natural variations

Natural variant1801R → C.
Corresponds to variant rs3103004 [ dbSNP | Ensembl ].
VAR_030572
Natural variant4941A → P.
Corresponds to variant rs2230143 [ dbSNP | Ensembl ].
VAR_030573
Natural variant5321L → V. Ref.1 Ref.2
VAR_015112

Secondary structure

..................................................... 586
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15311 [UniParc].

Last modified February 6, 2007. Version 4.
Checksum: F1B592CF49A7CC46

FASTA58669,413
        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 

« Hide

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA34400.
RefSeqNP_001104547.1. NM_001111077.1.
NP_003370.2. NM_003379.4.
UniGeneHs.487027.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NI2X-ray2.30A/B2-297[»]
ProteinModelPortalP15311.
SMRP15311. Positions 1-586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113271. 91 interactions.
DIPDIP-38868N.
IntActP15311. 25 interactions.
MINTMINT-195721.
STRING9606.ENSP00000338934.

Chemistry

ChEMBLCHEMBL1932896.

PTM databases

PhosphoSiteP15311.

Polymorphism databases

DMDM125987826.

2D gel databases

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

Proteomic databases

PaxDbP15311.
PRIDEP15311.

Protocols and materials databases

DNASU7430.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337147; ENSP00000338934; ENSG00000092820.
ENST00000367075; ENSP00000356042; ENSG00000092820.
GeneID7430.
KEGGhsa:7430.
UCSCuc003qrt.4. human.

Organism-specific databases

CTD7430.
GeneCardsGC06M159186.
HGNCHGNC:12691. EZR.
HPACAB004035.
CAB047324.
HPA021616.
MIM123900. gene.
neXtProtNX_P15311.
PharmGKBPA162385512.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236035.
HOGENOMHOG000007113.
HOVERGENHBG002185.
KOK08007.
OMALQDEGTE.
OrthoDBEOG7BGHK6.
PhylomeDBP15311.
TreeFamTF313935.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressP15311.
BgeeP15311.
CleanExHS_EZR.
GenevestigatorP15311.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR019749. 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.
[Graphical view]
PfamPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFPIRSF002305. ERM. 1 hit.
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEZR. human.
EvolutionaryTraceP15311.
GeneWikiEzrin.
GenomeRNAi7430.
NextBio29100.
PROP15311.
SOURCESearch...

Entry information

Entry nameEZRI_HUMAN
AccessionPrimary (citable) accession number: P15311
Secondary accession number(s): E1P5A8 expand/collapse secondary AC list , P23714, Q4VX75, Q96CU8, Q9NSJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

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Human chromosome 6

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