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P15311

- EZRI_HUMAN

UniProt

P15311 - EZRI_HUMAN

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Protein

Ezrin

Gene

EZR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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: Ensembl
  5. astrocyte projection Source: Ensembl
  6. basolateral plasma membrane Source: UniProtKB
  7. cell body Source: Ensembl
  8. cell tip Source: Ensembl
  9. ciliary basal body Source: Ensembl
  10. cortical cytoskeleton Source: HGNC
  11. cytosol Source: UniProtKB
  12. extracellular space Source: UniProt
  13. extracellular vesicular exosome Source: UniProtKB
  14. extrinsic component of membrane Source: UniProtKB
  15. filopodium Source: BHF-UCL
  16. focal adhesion Source: UniProtKB
  17. membrane Source: UniProtKB
  18. membrane raft Source: Ensembl
  19. microspike Source: Ensembl
  20. microvillus Source: BHF-UCL
  21. microvillus membrane Source: Ensembl
  22. nucleolus Source: HPA
  23. plasma membrane Source: HPA
  24. ruffle Source: UniProtKB
  25. Schwann cell microvillus Source: Ensembl
  26. T-tubule Source: Ensembl
  27. uropod Source: Ensembl
  28. vesicle Source: UniProtKB
Complete GO annotation...

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 PDGFR2 Publications
Modified residuei354 – 3541Phosphotyrosine; by PDGFR1 Publication
Modified residuei478 – 4781Phosphotyrosine1 Publication
Modified residuei535 – 5351Phosphoserine1 Publication
Modified residuei567 – 5671Phosphothreonine; by ROCK2 and PKC/PRKCI1 Publication

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

BgeeiP15311.
CleanExiHS_EZR.
ExpressionAtlasiP15311. baseline and differential.
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. 29 interactions.
MINTiMINT-195721.
STRINGi9606.ENSP00000338934.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119078.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP15311.
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

        10         20         30         40         50
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLHYV
60 70 80 90 100
DNKGFPTWLK LDKKVSAQEV RKENPLQFKF RAKFYPEDVA EELIQDITQK
110 120 130 140 150
LFFLQVKEGI LSDEIYCPPE TAVLLGSYAV QAKFGDYNKE VHKSGYLSSE
160 170 180 190 200
RLIPQRVMDQ HKLTRDQWED RIQVWHAEHR GMLKDNAMLE 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 MREKEELMLR
360 370 380 390 400
LQDYEEKTKK AERELSEQIQ RALQLEEERK RAQEEAERLE ADRMAALRAK
410 420 430 440 450
EELERQAVDQ IKSQEQLAAE LAEYTAKIAL LEEARRRKED EVEEWQHRAK
460 470 480 490 500
EAQDDLVKTK EELHLVMTAP PPPPPPVYEP VSYHVQESLQ DEGAEPTGYS
510 520 530 540 550
AELSSEGIRD DRNEEKRITE AEKNERVQRQ LLTLSSELSQ ARDENKRTHN
560 570 580
DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAL
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.Curated
The sequence CAB82418.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 29 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.
GeneTreei ENSGT00760000119078.
HOGENOMi HOG000007113.
HOVERGENi HBG002185.
InParanoidi P15311.
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

Bgeei P15311.
CleanExi HS_EZR.
ExpressionAtlasi P15311. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 170 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