P15311 (EZRI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ezrin

Alternative name(s):
Cytovillin
Villin-2
p81

Gene names

Name:	EZR
Synonyms:	VIL2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	586 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
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
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). 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 process	Cell shape
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin 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 epithelial cell differentiation Inferred from electronic annotation. Source: Compara establishment or maintenance of apical/basal cell polarity Inferred from electronic annotation. Source: Compara 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 regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	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 basolateral plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB cortical cytoskeleton Traceable author statement PubMed 11598191. Source: HGNC cytosol Inferred from direct assay PubMed 9852149. Source: UniProtKB extrinsic to membrane Inferred from direct assay PubMed 7844168. Source: UniProtKB filopodium Inferred from direct assay PubMed 12082081. Source: BHF-UCL microtubule basal body Inferred from electronic annotation. Source: Compara 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 ruffle Inferred from direct assay PubMed 9852149. Source: UniProtKB ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell uropod Inferred from electronic annotation. Source: Compara
Molecular_function	actin filament binding Inferred from direct assay PubMed 10793131. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDM2	Q00987	3	EBI-1056902,EBI-389668
SCYL3	Q8IZE3	4	EBI-1056902,EBI-1380680

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 586

585

Ezrin

PRO_0000219408

Regions

Domain

2 – 295

294

FERM

Region

244 – 586

343

Interaction with SCYL3

Amino acid modifications

Modified residue

60

1

N6-acetyllysine Ref.21

Modified residue

146

1

Phosphotyrosine; by PDGFR

Modified residue

354

1

Phosphotyrosine; by PDGFR

Modified residue

535

1

Phosphoserine Ref.23

Modified residue

567

1

Phosphothreonine; by ROCK2 and PKC/PRKCI Probable

Natural variations

Natural variant

180

1

R → C.
Corresponds to variant rs3103004 [ dbSNP | Ensembl ].

VAR_030572

Natural variant

494

1

A → P.
Corresponds to variant rs2230143 [ dbSNP | Ensembl ].

VAR_030573

Natural variant

532

1

L → V. Ref.1 Ref.2

VAR_015112

Secondary structure

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586

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Beta strand

14 – 20

7

Helix

26 – 37

12

Helix

42 – 44

3

Beta strand

45 – 51

7

Beta strand

56 – 58

3

Beta strand

61 – 64

4

Helix

65 – 67

3

Beta strand

74 – 84

11

Helix

89 – 92

4

Helix

96 – 111

16

Helix

119 – 134

16

Turn

139 – 141

3

Beta strand

146 – 149

4

Helix

155 – 160

6

Helix

165 – 178

14

Helix

184 – 195

12

Turn

199 – 202

4

Beta strand

204 – 210

7

Beta strand

215 – 220

6

Beta strand

222 – 229

8

Beta strand

232 – 235

4

Beta strand

237 – 242

6

Beta strand

245 – 253

9

Beta strand

255 – 262

8

Beta strand

268 – 270

3

Helix

274 – 293

20

Sequences

	Sequence		Length	Mass (Da)
	P15311 [UniParc]. Last modified February 6, 2007. Version 4. Checksum: F1B592CF49A7CC46	FASTA	586	69,413
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, 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]	"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.
[21]	"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, MASS SPECTROMETRY.
[22]	"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].
[23]	"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, MASS SPECTROMETRY.
[24]	"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.

IPI

IPI00843975.

PIR

A34400.

RefSeq

NP_001104547.1. NM_001111077.1.
NP_003370.2. NM_003379.4.

UniGene

Hs.487027.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NI2	X-ray	2.30	A/B	2-297	[»]

ProteinModelPortal

P15311.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38868N.

IntAct

P15311. 16 interactions.

MINT

MINT-195721.

STRING

9606.ENSP00000338934.

PTM databases

PhosphoSite

P15311.

Polymorphism databases

DMDM

125987826.

2D gel databases

DOSAC-COBS-2DPAGE

P15311.

REPRODUCTION-2DPAGE

IPI00843975.

SWISS-2DPAGE

P15311.

Proteomic databases

PaxDb

P15311.

PRIDE

P15311.

Protocols and materials databases

DNASU

7430.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337147; ENSP00000338934; ENSG00000092820.
ENST00000367075; ENSP00000356042; ENSG00000092820.

GeneID

7430.

KEGG

hsa:7430.

UCSC

uc003qrt.4. human.

Organism-specific databases

CTD

7430.

GeneCards

GC06M159186.

HGNC

HGNC:12691. EZR.

HPA

CAB004035.
CAB047324.
HPA021616.

MIM

123900. gene.

neXtProt

NX_P15311.

PharmGKB

PA162385512.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG236035.

HOGENOM

HOG000007113.

HOVERGEN

HBG002185.

KO

K08007.

OMA

EGAEPMG.

OrthoDB

EOG4C5CJJ.

PhylomeDB

P15311.

Enzyme and pathway databases

Pathway_Interaction_DB

syndecan_2_pathway. Syndecan-2-mediated signaling events.

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

P15311.

Bgee

P15311.

CleanEx

HS_EZR.

Genevestigator

P15311.

GermOnline

ENSG00000092820. Homo sapiens.

Family and domain databases

Gene3D

1.20.80.10. 1 hit.
2.30.29.30. 1 hit.

InterPro

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.
IPR011993. PH_like_dom.
[Graphical view]

Pfam

PF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]

PIRSF

PIRSF002305. ERM. 1 hit.

PRINTS

PR00935. BAND41.
PR00661. ERMFAMILY.

SMART

SM00295. B41. 1 hit.
[Graphical view]

SUPFAM

SSF47031. FERM_3-hlx. 1 hit.
SSF48678. Moesin. 1 hit.

PROSITE

PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1932896.

ChiTaRS

EZR. human.

EvolutionaryTrace

P15311.

GenomeRNAi

7430.

NextBio

29100.

SOURCE

Search...

Entry information

Entry name

EZRI_HUMAN

Accession

Primary (citable) accession number: P15311
Secondary accession number(s): E1P5A8 , P23714, Q4VX75, Q96CU8, Q9NSJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 153 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.