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Protein

Ezrin

Gene

EZR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • actin binding Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • cell adhesion molecule binding Source: BHF-UCL
  • microtubule binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein kinase A catalytic subunit binding Source: UniProtKB
  • protein kinase A regulatory subunit binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • actin filament bundle assembly Source: UniProtKB
  • astral microtubule organization Source: UniProtKB
  • axon guidance Source: Reactome
  • cellular protein complex localization Source: UniProtKB
  • cellular response to cAMP Source: UniProtKB
  • cortical microtubule organization Source: UniProtKB
  • cytoskeletal anchoring at plasma membrane Source: UniProtKB
  • establishment of centrosome localization Source: UniProtKB
  • establishment of endothelial barrier Source: UniProtKB
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • establishment or maintenance of apical/basal cell polarity Source: Ensembl
  • filopodium assembly Source: UniProtKB
  • intestinal D-glucose absorption Source: Ensembl
  • leukocyte cell-cell adhesion Source: BHF-UCL
  • membrane to membrane docking Source: BHF-UCL
  • microvillus assembly Source: UniProtKB
  • negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • negative regulation of interleukin-2 secretion Source: UniProtKB
  • negative regulation of p38MAPK cascade Source: UniProtKB
  • negative regulation of T cell receptor signaling pathway Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: UniProtKB
  • positive regulation of cellular protein catabolic process Source: UniProtKB
  • positive regulation of early endosome to late endosome transport Source: UniProtKB
  • positive regulation of establishment of protein localization to plasma membrane Source: Ensembl
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of multicellular organism growth Source: Ensembl
  • positive regulation of protein localization to early endosome Source: UniProtKB
  • positive regulation of protein secretion Source: UniProtKB
  • protein kinase A signaling Source: UniProtKB
  • protein localization to cell cortex Source: UniProtKB
  • receptor internalization Source: Ensembl
  • regulation of cell shape Source: UniProtKB
  • regulation of microvillus length Source: Ensembl
  • regulation of organelle assembly Source: UniProtKB
  • sphingosine-1-phosphate signaling pathway Source: UniProtKB
  • terminal web assembly Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell shape

Enzyme and pathway databases

BioCyciZFISH:ENSG00000092820-MONOMER.
ReactomeiR-HSA-373752. Netrin-1 signaling.
R-HSA-437239. Recycling pathway of L1.
SIGNORiP15311.

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
Proteomesi
  • UP000005640 Componenti: 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

  • actin cytoskeleton Source: UniProtKB
  • actin filament Source: HGNC
  • apical part of cell Source: BHF-UCL
  • apical plasma membrane Source: UniProtKB
  • astrocyte projection Source: Ensembl
  • basolateral plasma membrane Source: UniProtKB
  • brush border Source: UniProtKB
  • cell body Source: Ensembl
  • cell-cell adherens junction Source: BHF-UCL
  • cell periphery Source: UniProtKB
  • cell projection Source: UniProtKB
  • cell tip Source: Ensembl
  • ciliary basal body Source: Ensembl
  • cortical cytoskeleton Source: HGNC
  • cytoplasm Source: UniProtKB
  • cytoplasmic side of apical plasma membrane Source: UniProtKB
  • cytosol Source: UniProtKB
  • endosome Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • extrinsic component of membrane Source: UniProtKB
  • filopodium Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • immunological synapse Source: UniProtKB
  • membrane Source: UniProtKB
  • microspike Source: Ensembl
  • microvillus Source: BHF-UCL
  • microvillus membrane Source: UniProtKB-SubCell
  • myelin sheath Source: Ensembl
  • nucleolus Source: HPA
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • plasma membrane raft Source: UniProtKB
  • ruffle Source: UniProtKB
  • ruffle membrane Source: UniProtKB-SubCell
  • Schwann cell microvillus Source: Ensembl
  • T-tubule Source: Ensembl
  • uropod Source: Ensembl
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi7430.
OpenTargetsiENSG00000092820.
PharmGKBiPA162385512.

Chemistry databases

ChEMBLiCHEMBL1932896.

Polymorphism and mutation databases

BioMutaiEZR.
DMDMi125987826.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002194082 – 586EzrinAdd BLAST585

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei60N6-acetyllysineCombined sources1
Modified residuei146Phosphotyrosine; by PDGFR2 Publications1
Modified residuei354Phosphotyrosine; by PDGFR1 Publication1
Modified residuei366PhosphoserineCombined sources1
Modified residuei478Phosphotyrosine1 Publication1
Modified residuei535PhosphoserineBy similarity1
Modified residuei567Phosphothreonine; by ROCK2 and PKC/PRKCI1 Publication1

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
S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP15311.
MaxQBiP15311.
PaxDbiP15311.
PeptideAtlasiP15311.
PRIDEiP15311.
TopDownProteomicsiP15311.

2D gel databases

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

PTM databases

iPTMnetiP15311.
PhosphoSitePlusiP15311.
SwissPalmiP15311.

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

BgeeiENSG00000092820.
CleanExiHS_EZR.
ExpressionAtlasiP15311. baseline and differential.
GenevisibleiP15311. HS.

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 (PubMed:9314537, PubMed:12651155, PubMed:15498789, PubMed:17616675, PubMed:17881735, PubMed:19555689). Interacts (when phosphorylated) with FES/FPS (PubMed:18046454). Interacts with dimeric S100P, the interaction may be activating through unmasking of F-actin binding sites (PubMed:12808036, PubMed:19111582). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By similarity).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAPN1P073842EBI-1056902,EBI-1542113
FESP073328EBI-1056902,EBI-1055635
MDM2Q009873EBI-1056902,EBI-389668
SCYL3Q8IZE34EBI-1056902,EBI-1380680
SLC9A3R1O147452EBI-1056902,EBI-349787

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • cell adhesion molecule binding Source: BHF-UCL
  • microtubule binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein kinase A catalytic subunit binding Source: UniProtKB
  • protein kinase A regulatory subunit binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113271. 142 interactors.
DIPiDIP-38868N.
IntActiP15311. 38 interactors.
MINTiMINT-195721.
STRINGi9606.ENSP00000338934.

Chemistry databases

BindingDBiP15311.

Structurei

Secondary structure

1586
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Beta strandi15 – 20Combined sources6
Helixi26 – 37Combined sources12
Helixi42 – 44Combined sources3
Beta strandi45 – 51Combined sources7
Beta strandi56 – 58Combined sources3
Beta strandi61 – 64Combined sources4
Helixi65 – 67Combined sources3
Beta strandi74 – 84Combined sources11
Helixi89 – 92Combined sources4
Helixi96 – 111Combined sources16
Helixi119 – 134Combined sources16
Turni139 – 141Combined sources3
Turni144 – 149Combined sources6
Helixi155 – 159Combined sources5
Helixi165 – 178Combined sources14
Turni179 – 181Combined sources3
Helixi184 – 196Combined sources13
Turni199 – 202Combined sources4
Beta strandi204 – 210Combined sources7
Beta strandi215 – 221Combined sources7
Beta strandi224 – 229Combined sources6
Beta strandi233 – 235Combined sources3
Beta strandi237 – 241Combined sources5
Helixi242 – 244Combined sources3
Beta strandi245 – 251Combined sources7
Beta strandi254 – 261Combined sources8
Beta strandi267 – 270Combined sources4
Helixi274 – 295Combined sources22
Helixi520 – 523Combined sources4
Helixi525 – 539Combined sources15
Helixi544 – 546Combined sources3
Helixi549 – 559Combined sources11
Helixi564 – 571Combined sources8
Helixi576 – 585Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NI2X-ray2.30A/B2-297[»]
4RM8X-ray1.90A/B1-586[»]
4RM9X-ray2.00A1-586[»]
4RMAX-ray1.75A/B1-296[»]
ProteinModelPortaliP15311.
SMRiP15311.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15311.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 295FERMPROSITE-ProRule annotationAdd BLAST294

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni244 – 586Interaction with SCYL31 PublicationAdd BLAST343

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi115 – 120[IL]-x-C-x-x-[DE] motif1 Publication6

Domaini

The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.1 Publication

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00860000133686.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP15311.
KOiK08007.
PhylomeDBiP15311.
TreeFamiTF313935.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
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_dom-like.
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.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB82418 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030572180R → C.Corresponds to variant rs3103004dbSNPEnsembl.1
Natural variantiVAR_030573494A → P.Corresponds to variant rs2230143dbSNPEnsembl.1
Natural variantiVAR_015112532L → V.2 Publications1

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.5. human.

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.
CCDSiCCDS5258.1.
PIRiA34400.
RefSeqiNP_001104547.1. NM_001111077.1.
NP_003370.2. NM_003379.4.
UniGeneiHs.487027.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NI2X-ray2.30A/B2-297[»]
4RM8X-ray1.90A/B1-586[»]
4RM9X-ray2.00A1-586[»]
4RMAX-ray1.75A/B1-296[»]
ProteinModelPortaliP15311.
SMRiP15311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113271. 142 interactors.
DIPiDIP-38868N.
IntActiP15311. 38 interactors.
MINTiMINT-195721.
STRINGi9606.ENSP00000338934.

Chemistry databases

BindingDBiP15311.
ChEMBLiCHEMBL1932896.

PTM databases

iPTMnetiP15311.
PhosphoSitePlusiP15311.
SwissPalmiP15311.

Polymorphism and mutation databases

BioMutaiEZR.
DMDMi125987826.

2D gel databases

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

Proteomic databases

EPDiP15311.
MaxQBiP15311.
PaxDbiP15311.
PeptideAtlasiP15311.
PRIDEiP15311.
TopDownProteomicsiP15311.

Protocols and materials databases

DNASUi7430.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337147; ENSP00000338934; ENSG00000092820.
ENST00000367075; ENSP00000356042; ENSG00000092820.
GeneIDi7430.
KEGGihsa:7430.
UCSCiuc003qrt.5. human.

Organism-specific databases

CTDi7430.
DisGeNETi7430.
GeneCardsiEZR.
HGNCiHGNC:12691. EZR.
HPAiCAB004035.
CAB047324.
HPA021616.
MIMi123900. gene.
neXtProtiNX_P15311.
OpenTargetsiENSG00000092820.
PharmGKBiPA162385512.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00860000133686.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP15311.
KOiK08007.
PhylomeDBiP15311.
TreeFamiTF313935.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000092820-MONOMER.
ReactomeiR-HSA-373752. Netrin-1 signaling.
R-HSA-437239. Recycling pathway of L1.
SIGNORiP15311.

Miscellaneous databases

ChiTaRSiEZR. human.
EvolutionaryTraceiP15311.
GeneWikiiEzrin.
GenomeRNAii7430.
PROiP15311.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000092820.
CleanExiHS_EZR.
ExpressionAtlasiP15311. baseline and differential.
GenevisibleiP15311. HS.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
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_dom-like.
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.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 191 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.