HUMAN:EZRI

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	EZR (synonyms: VIL2)
Protein Name(s)	Ezrin Cytovillin Villin-2 p81
External Links
UniProt	P15311
EMBL	X51521 J05021 AL162086 AL589931 CH471051 BC013903
CCDS	CCDS5258.1
PIR	A34400
RefSeq	NP_001104547.1 NP_003370.2
UniGene	Hs.487027
PDB	1NI2
PDBsum	1NI2
ProteinModelPortal	P15311
SMR	P15311
BioGrid	113271
DIP	DIP-38868N
IntAct	P15311
MINT	MINT-195721
STRING	9606.ENSP00000338934
BindingDB	P15311
ChEMBL	CHEMBL1932896
PhosphoSite	P15311
DMDM	125987826
DOSAC-COBS-2DPAGE	P15311
REPRODUCTION-2DPAGE	IPI00843975
SWISS-2DPAGE	P15311
MaxQB	P15311
PaxDb	P15311
PRIDE	P15311
DNASU	7430
Ensembl	ENST00000337147 ENST00000367075
GeneID	7430
KEGG	hsa:7430
UCSC	uc003qrt.4
CTD	7430
GeneCards	GC06M159186
HGNC	HGNC:12691
HPA	CAB004035 CAB047324 HPA021616
MIM	123900
neXtProt	NX_P15311
PharmGKB	PA162385512
eggNOG	NOG236035
GeneTree	ENSGT00760000119078
HOGENOM	HOG000007113
HOVERGEN	HBG002185
InParanoid	P15311
KO	K08007
OMA	SEVEEWQ
OrthoDB	EOG7BGHK6
PhylomeDB	P15311
TreeFam	TF313935
Reactome	REACT_22237 REACT_22365
ChiTaRS	EZR
EvolutionaryTrace	P15311
GeneWiki	Ezrin
GenomeRNAi	7430
NextBio	29100
PRO	PR:P15311
Proteomes	UP000005640
Bgee	P15311
CleanEx	HS_EZR
ExpressionAtlas	P15311
Genevestigator	P15311
GO	GO:0015629 GO:0005884 GO:0045177 GO:0016324 GO:0097449 GO:0016323 GO:0044297 GO:0051286 GO:0036064 GO:0030863 GO:0005829 GO:0005615 GO:0070062 GO:0019898 GO:0030175 GO:0005925 GO:0016020 GO:0045121 GO:0044393 GO:0005902 GO:0031528 GO:0005730 GO:0005886 GO:0001726 GO:0032587 GO:0097454 GO:0030315 GO:0001931 GO:0031982 GO:0051015 GO:0050839 GO:0044822 GO:0051017 GO:0007411 GO:0007016 GO:0061028 GO:0035088 GO:0046847 GO:0007159 GO:0022614 GO:0010628 GO:0031623 GO:0008360
Gene3D	1.20.80.10 2.30.29.30
InterPro	IPR019749 IPR011174 IPR011259 IPR000798 IPR014352 IPR019748 IPR019747 IPR000299 IPR018979 IPR018980 IPR008954 IPR011993 IPR029071
Pfam	PF00769 PF09380 PF00373 PF09379
PIRSF	PIRSF002305
PRINTS	PR00935 PR00661
SMART	SM00295
SUPFAM	SSF47031 SSF48678 SSF54236
PROSITE	PS00660 PS00661 PS50057

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005515	protein binding	PMID:25618778^[1]	ECO:0000315			F		The study analyzes expression and sub-cellular distribution allowing for the necessary information	complete CACAO 10611
part_of	GO:0071437	invadopodium	PMID:25486435^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0051018	protein kinase A binding	PMID:25097019^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P10644	F		Seeded From UniProt	complete
enables	GO:0051018	protein kinase A binding	PMID:25097019^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P13861	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:25097019^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0045296	cadherin binding	PMID:25468996^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0034237	protein kinase A regulatory subunit binding	PMID:17911601^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P10644	F		Seeded From UniProt	complete
NOT\|involved_in	GO:0032956	regulation of actin cytoskeleton organization	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008360	regulation of cell shape	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:0034629	cellular protein-containing complex localization	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(GO:0036398) occurs_in:(GO:0001772) occurs_in:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:0072659	protein localization to plasma membrane	PMID:17825285^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q92887) occurs_in:(CL:0002563) occurs_at:(GO:0016324)	Seeded From UniProt	complete
NOT\|involved_in	GO:0008361	regulation of cell size	PMID:22467863^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050860	negative regulation of T cell receptor signaling pathway	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(GO:0001772)	Seeded From UniProt	complete
involved_in	GO:0010737	protein kinase A signaling	PMID:17911601^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:0071320	cellular response to cAMP	PMID:17911601^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:1900041	negative regulation of interleukin-2 secretion	PMID:17911601^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084) happens_during:(GO:0010737) happens_during:(GO:0071320)	Seeded From UniProt	complete
involved_in	GO:0072659	protein localization to plasma membrane	PMID:17911601^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084) occurs_at:(GO:0044853) has_direct_input:(UniProtKB:P10644)	Seeded From UniProt	complete
enables	GO:0034236	protein kinase A catalytic subunit binding	PMID:17911601^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P17612	F		Seeded From UniProt	complete
colocalizes_with	GO:0001772	immunological synapse	PMID:17911601^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000084)	Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	PMID:23857773^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0051117	ATPase binding	PMID:17825285^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q92887	F		Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:17825285^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	PMID:17825285^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002563)	Seeded From UniProt	complete
involved_in	GO:0070373	negative regulation of ERK1 and ERK2 cascade	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0050860)	Seeded From UniProt	complete
involved_in	GO:0030953	astral microtubule organization	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:0043622	cortical microtubule organization	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084) occurs_in:(GO:0001772)	Seeded From UniProt	complete
involved_in	GO:0072697	protein localization to cell cortex	PMID:25554515^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P46940) occurs_in:(CL:0000066)	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:25554515^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P46940	F		Seeded From UniProt	complete
enables	GO:0044548	S100 protein binding	PMID:25554515^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P25815	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:25554515^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0001726	ruffle	PMID:25554515^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0034237	protein kinase A regulatory subunit binding	PMID:17911601^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P13861	F		Seeded From UniProt	complete
part_of	GO:0044853	plasma membrane raft	PMID:17911601^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084) has_input:(InterPro:IPR008366)	Seeded From UniProt	complete
involved_in	GO:1903753	negative regulation of p38MAPK cascade	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084) happens_during:(GO:0050852)	Seeded From UniProt	complete
involved_in	GO:0051660	establishment of centrosome localization	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084)	Seeded From UniProt	complete
part_of	GO:0001772	immunological synapse	PMID:20551903^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000084)	Seeded From UniProt	complete
NOT\|involved_in	GO:1901222	regulation of NIK/NF-kappaB signaling	PMID:20551903^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|involved_in	GO:0045198	establishment of epithelial cell apical/basal polarity	PMID:24862762^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|involved_in	GO:0022612	gland morphogenesis	PMID:24862762^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:24862762^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002563)	Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	PMID:24862762^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002563) part_of:(UBERON:0000317)	Seeded From UniProt	complete
part_of	GO:0042995	cell projection	PMID:25889165^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000038)	Seeded From UniProt	complete
involved_in	GO:1902966	positive regulation of protein localization to early endosome	PMID:21148287^[13]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P26038 UniProtKB:P35241	P	has_regulation_target:(UniProtKB:P51149)	Seeded From UniProt	complete
involved_in	GO:1902115	regulation of organelle assembly	PMID:21148287^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	results_in_maturation_of:(GO:0005770)	Seeded From UniProt	complete
involved_in	GO:1902115	regulation of organelle assembly	PMID:21148287^[13]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P26038 UniProtKB:P35241	P	results_in_maturation_of:(GO:0005770)	Seeded From UniProt	complete
involved_in	GO:2000643	positive regulation of early endosome to late endosome transport	PMID:21148287^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P00533)	Seeded From UniProt	complete
involved_in	GO:2000643	positive regulation of early endosome to late endosome transport	PMID:21148287^[13]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P26038 UniProtKB:P35241	P	has_input:(UniProtKB:P00533)	Seeded From UniProt	complete
involved_in	GO:1903364	positive regulation of cellular protein catabolic process	PMID:21148287^[13]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P26038 UniProtKB:P35241	P	has_regulation_target:(UniProtKB:P00533)	Seeded From UniProt	complete
part_of	GO:0005768	endosome	PMID:21148287^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0046847	filopodium assembly	PMID:23106337^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0003376)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:23106337^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031532	actin cytoskeleton reorganization	PMID:23106337^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0003376)	Seeded From UniProt	complete
involved_in	GO:0003376	sphingosine-1-phosphate receptor signaling pathway	PMID:23106337^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:23106337^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0003376)	Seeded From UniProt	complete
part_of	GO:0030175	filopodium	PMID:23106337^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0003376)	Seeded From UniProt	complete
involved_in	GO:0050714	positive regulation of protein secretion	PMID:25591774^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0002368) has_regulation_target:(UniProtKB:P98088)	Seeded From UniProt	complete
involved_in	GO:0048015	phosphatidylinositol-mediated signaling	PMID:25591774^[15]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0002368)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:25591774^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000483) part_of:(UBERON:0000344) part_of:(UBERON:0002185)	Seeded From UniProt	complete
part_of	GO:0098592	cytoplasmic side of apical plasma membrane	PMID:25591774^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000483) part_of:(UBERON:0000344) part_of:(UBERON:0002185)	Seeded From UniProt	complete
part_of	GO:0005903	brush border	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P26040	C	part_of:(CL:0000584)	Seeded From UniProt	complete
part_of	GO:0071944	cell periphery	PMID:22291017^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	PMID:22797597^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002563)	Seeded From UniProt	complete
involved_in	GO:0030033	microvillus assembly	PMID:22797597^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0002563)	Seeded From UniProt	complete
NOT\|involved_in	GO:0045198	establishment of epithelial cell apical/basal polarity	PMID:22797597^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[18]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031982	vesicle	PMID:19190083^[19]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002202)	Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[20]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[21]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[22]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[22]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
involved_in	GO:0061028	establishment of endothelial barrier	PMID:23264465^[23]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P26038 UniProtKB:P35241	P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:23264465^[23]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q96S97	P	has_regulation_target:(UniProtKB:P05362) occurs_in:(UBERON:0001986)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:16502470^[24]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001914)	Seeded From UniProt	complete
enables	GO:0050839	cell adhesion molecule binding	PMID:15498789^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P16278	F		Seeded From UniProt	complete
enables	GO:0050839	cell adhesion molecule binding	PMID:12082081^[26]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P32942	F		Seeded From UniProt	complete
enables	GO:0050839	cell adhesion molecule binding	PMID:12082081^[26]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19320	F		Seeded From UniProt	complete
part_of	GO:0045177	apical part of cell	PMID:12082081^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030175	filopodium	PMID:12082081^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0022614	membrane to membrane docking	PMID:12082081^[26]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007159	leukocyte cell-cell adhesion	PMID:12082081^[26]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0005925	focal adhesion	PMID:21282464^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005902	microvillus	PMID:12082081^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005884	actin filament	PMID:11598191^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051017	actin filament bundle assembly	PMID:10793131^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	PMID:10793131^[29]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[30]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[31]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0019898	extrinsic component of membrane	PMID:7844168^[32]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P31977	C		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	PMID:10793131^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007016	cytoskeletal anchoring at plasma membrane	PMID:10793131^[29]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:9852149^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0001726	ruffle	PMID:9852149^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:29568061^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15311	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21988832^[35]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15311	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0001650	fibrillar center	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903078	positive regulation of protein localization to plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	P		Seeded From UniProt	complete
involved_in	GO:1902896	terminal web assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	P		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	F		Seeded From UniProt	complete
part_of	GO:0045177	apical part of cell	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	C		Seeded From UniProt	complete
involved_in	GO:0040018	positive regulation of multicellular organism growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	P		Seeded From UniProt	complete
part_of	GO:0036064	ciliary basal body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	C		Seeded From UniProt	complete
involved_in	GO:0035088	establishment or maintenance of apical/basal cell polarity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	P		Seeded From UniProt	complete
involved_in	GO:0032532	regulation of microvillus length	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	P		Seeded From UniProt	complete
involved_in	GO:0031623	receptor internalization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	P		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	C		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	F		Seeded From UniProt	complete
part_of	GO:0005903	brush border	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	C		Seeded From UniProt	complete
part_of	GO:0005902	microvillus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	C		Seeded From UniProt	complete
involved_in	GO:0001951	intestinal D-glucose absorption	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	P		Seeded From UniProt	complete
part_of	GO:0001931	uropod	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P26040 ensembl:ENSMUSP00000063734	C		Seeded From UniProt	complete
part_of	GO:0097454	Schwann cell microvillus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
part_of	GO:0097449	astrocyte projection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
part_of	GO:0051286	cell tip	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
involved_in	GO:0046847	filopodium assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	P		Seeded From UniProt	complete
part_of	GO:0045121	membrane raft	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	F		Seeded From UniProt	complete
part_of	GO:0044393	microspike	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
part_of	GO:0044297	cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
part_of	GO:0031528	microvillus membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
involved_in	GO:0030855	epithelial cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	P		Seeded From UniProt	complete
part_of	GO:0030315	T-tubule	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
part_of	GO:0030175	filopodium	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	F		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P31977 ensembl:ENSRNOP00000046593	C		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008954 InterPro:IPR011174	F		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000299	C		Seeded From UniProt	complete
enables	GO:0008092	cytoskeletal protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000798	F		Seeded From UniProt	complete
part_of	GO:0030863	cortical cytoskeleton	PMID:11598191^[28]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007411	axon guidance	Reactome:R-HSA-422475	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-NUL-443049 Reactome:R-HSA-445089 Reactome:R-HSA-443779 Reactome:R-HSA-374680 Reactome:R-HSA-374664 Reactome:R-HSA-374663 Reactome:R-HSA-374662	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966 UniProtKB-SubCell:SL-0280	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003	C		Seeded From UniProt	complete
involved_in	GO:0008360	regulation of cell shape	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0133	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0031528	microvillus membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0294	C		Seeded From UniProt	complete
part_of	GO:0005938	cell cortex	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0138	C		Seeded From UniProt	complete
part_of	GO:0005902	microvillus	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0293	C		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0015	C		Seeded From UniProt	complete
part_of	GO:0032587	ruffle membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0301	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Lo Vasco, VR et al. (2015) Ezrin-related Phosphoinositide pathway modifies RhoA and Rac1 in human osteosarcoma cell lines. J Cell Commun Signal 9 55-62 PubMed GONUTS page
↑ Martín-Villar, E et al. (2015) Podoplanin mediates ECM degradation by squamous carcinoma cells through control of invadopodia stability. Oncogene 34 4531-44 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Burgers, PP et al. (2015) A systematic evaluation of protein kinase A-A-kinase anchoring protein interaction motifs. Biochemistry 54 11-21 PubMed GONUTS page
↑ Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 ^5.8 Ruppelt, A et al. (2007) Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin. J. Immunol. 179 5159-68 PubMed GONUTS page
↑ ^6.00 ^6.01 ^6.02 ^6.03 ^6.04 ^6.05 ^6.06 ^6.07 ^6.08 ^6.09 ^6.10 ^6.11 Lasserre, R et al. (2010) Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse. EMBO J. 29 2301-14 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Yang, Q et al. (2007) Ezrin and radixin both regulate the apical membrane localization of ABCC2 (MRP2) in human intestinal epithelial Caco-2 cells. Exp. Cell Res. 313 3517-25 PubMed GONUTS page
↑ Valderrama, F et al. (2012) Radixin regulates cell migration and cell-cell adhesion through Rac1. J. Cell. Sci. 125 3310-9 PubMed GONUTS page
↑ Solinet, S et al. (2013) The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex. J. Cell Biol. 202 251-60 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 Nammalwar, RC et al. (2015) Ezrin interacts with the scaffold protein IQGAP1 and affects its cortical localization. Biochim. Biophys. Acta 1853 2086-94 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Georgescu, MM et al. (2014) NHERF1/EBP50 controls morphogenesis of 3D colonic glands by stabilizing PTEN and ezrin-radixin-moesin proteins at the apical membrane. Neoplasia 16 365-74.e1-2 PubMed GONUTS page
↑ Panichakul, T et al. (2015) Plasmodium vivax inhibits erythroid cell growth through altered phosphorylation of the cytoskeletal protein ezrin. Malar. J. 14 138 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 ^13.6 Chirivino, D et al. (2011) The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes. Mol. Biol. Cell 22 375-85 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 Gandy, KA et al. (2013) Sphingosine 1-phosphate induces filopodia formation through S1PR2 activation of ERM proteins. Biochem. J. 449 661-72 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 Li, Q et al. (2015) Ezrin/Exocyst complex regulates mucin 5AC secretion induced by neutrophil elastase in human airway epithelial cells. Cell. Physiol. Biochem. 35 326-38 PubMed GONUTS page
↑ Fidalgo, M et al. (2012) Adaptor protein cerebral cavernous malformation 3 (CCM3) mediates phosphorylation of the cytoskeletal proteins ezrin/radixin/moesin by mammalian Ste20-4 to protect cells from oxidative stress. J. Biol. Chem. 287 11556-65 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 Gloerich, M et al. (2012) Rap2A links intestinal cell polarity to brush border formation. Nat. Cell Biol. 14 793-801 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ ^22.0 ^22.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^23.0 ^23.1 Aranda, JF et al. (2013) MYADM controls endothelial barrier function through ERM-dependent regulation of ICAM-1 expression. Mol. Biol. Cell 24 483-94 PubMed GONUTS page
↑ Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page
↑ Ma, J et al. (2005) Role of a novel EGF-like domain-containing gene NGX6 in cell adhesion modulation in nasopharyngeal carcinoma cells. Carcinogenesis 26 281-91 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 ^26.6 Barreiro, O et al. (2002) Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes. J. Cell Biol. 157 1233-45 PubMed GONUTS page
↑ Coene, ED et al. (2011) A novel role for BRCA1 in regulating breast cancer cell spreading and motility. J. Cell Biol. 192 497-512 PubMed GONUTS page
↑ ^28.0 ^28.1 Mykkänen, OM et al. (2001) Characterization of human palladin, a microfilament-associated protein. Mol. Biol. Cell 12 3060-73 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 Berryman, M & Bretscher, A (2000) Identification of a novel member of the chloride intracellular channel gene family (CLIC5) that associates with the actin cytoskeleton of placental microvilli. Mol. Biol. Cell 11 1509-21 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ Andréoli, C et al. (1994) Ezrin has properties to self-associate at the plasma membrane. J. Cell. Sci. 107 ( Pt 9) 2509-21 PubMed GONUTS page
↑ ^33.0 ^33.1 Buss, F et al. (1998) The localization of myosin VI at the golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation. J. Cell Biol. 143 1535-45 PubMed GONUTS page
↑ Liu, X et al. (2018) An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations. Nat Commun 9 1188 PubMed GONUTS page
↑ Wang, J et al. (2011) Toward an understanding of the protein interaction network of the human liver. Mol. Syst. Biol. 7 536 PubMed GONUTS page

[PMID:25618778-1] Lo Vasco, VR et al. (2015) Ezrin-related Phosphoinositide pathway modifies RhoA and Rac1 in human osteosarcoma cell lines. J Cell Commun Signal 9 55-62 PubMed GONUTS page

[PMID:25486435-2] Martín-Villar, E et al. (2015) Podoplanin mediates ECM degradation by squamous carcinoma cells through control of invadopodia stability. Oncogene 34 4531-44 PubMed GONUTS page

[PMID:25097019-3] 3.0 ^3.1 ^3.2 Burgers, PP et al. (2015) A systematic evaluation of protein kinase A-A-kinase anchoring protein interaction motifs. Biochemistry 54 11-21 PubMed GONUTS page

[PMID:25468996-4] Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page

[PMID:17911601-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 ^5.8 Ruppelt, A et al. (2007) Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin. J. Immunol. 179 5159-68 PubMed GONUTS page

[PMID:20551903-6] 6.00 ^6.01 ^6.02 ^6.03 ^6.04 ^6.05 ^6.06 ^6.07 ^6.08 ^6.09 ^6.10 ^6.11 Lasserre, R et al. (2010) Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse. EMBO J. 29 2301-14 PubMed GONUTS page

[PMID:17825285-7] 7.0 ^7.1 ^7.2 ^7.3 Yang, Q et al. (2007) Ezrin and radixin both regulate the apical membrane localization of ABCC2 (MRP2) in human intestinal epithelial Caco-2 cells. Exp. Cell Res. 313 3517-25 PubMed GONUTS page

[PMID:22467863-8] Valderrama, F et al. (2012) Radixin regulates cell migration and cell-cell adhesion through Rac1. J. Cell. Sci. 125 3310-9 PubMed GONUTS page

[PMID:23857773-9] Solinet, S et al. (2013) The actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex. J. Cell Biol. 202 251-60 PubMed GONUTS page

[PMID:25554515-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 Nammalwar, RC et al. (2015) Ezrin interacts with the scaffold protein IQGAP1 and affects its cortical localization. Biochim. Biophys. Acta 1853 2086-94 PubMed GONUTS page

[PMID:24862762-11] 11.0 ^11.1 ^11.2 ^11.3 Georgescu, MM et al. (2014) NHERF1/EBP50 controls morphogenesis of 3D colonic glands by stabilizing PTEN and ezrin-radixin-moesin proteins at the apical membrane. Neoplasia 16 365-74.e1-2 PubMed GONUTS page

[PMID:25889165-12] Panichakul, T et al. (2015) Plasmodium vivax inhibits erythroid cell growth through altered phosphorylation of the cytoskeletal protein ezrin. Malar. J. 14 138 PubMed GONUTS page

[PMID:21148287-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 ^13.6 Chirivino, D et al. (2011) The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes. Mol. Biol. Cell 22 375-85 PubMed GONUTS page

[PMID:23106337-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 Gandy, KA et al. (2013) Sphingosine 1-phosphate induces filopodia formation through S1PR2 activation of ERM proteins. Biochem. J. 449 661-72 PubMed GONUTS page

[PMID:25591774-15] 15.0 ^15.1 ^15.2 ^15.3 Li, Q et al. (2015) Ezrin/Exocyst complex regulates mucin 5AC secretion induced by neutrophil elastase in human airway epithelial cells. Cell. Physiol. Biochem. 35 326-38 PubMed GONUTS page

[PMID:22291017-16] Fidalgo, M et al. (2012) Adaptor protein cerebral cavernous malformation 3 (CCM3) mediates phosphorylation of the cytoskeletal proteins ezrin/radixin/moesin by mammalian Ste20-4 to protect cells from oxidative stress. J. Biol. Chem. 287 11556-65 PubMed GONUTS page

[PMID:22797597-17] 17.0 ^17.1 ^17.2 Gloerich, M et al. (2012) Rap2A links intestinal cell polarity to brush border formation. Nat. Cell Biol. 14 793-801 PubMed GONUTS page

[PMID:23533145-18] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19190083-19] Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page

[PMID:21423176-20] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:19946888-21] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:20458337-22] 22.0 ^22.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:23264465-23] 23.0 ^23.1 Aranda, JF et al. (2013) MYADM controls endothelial barrier function through ERM-dependent regulation of ICAM-1 expression. Mol. Biol. Cell 24 483-94 PubMed GONUTS page

[PMID:16502470-24] Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page

[PMID:15498789-25] Ma, J et al. (2005) Role of a novel EGF-like domain-containing gene NGX6 in cell adhesion modulation in nasopharyngeal carcinoma cells. Carcinogenesis 26 281-91 PubMed GONUTS page

[PMID:12082081-26] 26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 ^26.6 Barreiro, O et al. (2002) Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes. J. Cell Biol. 157 1233-45 PubMed GONUTS page

[PMID:21282464-27] Coene, ED et al. (2011) A novel role for BRCA1 in regulating breast cancer cell spreading and motility. J. Cell Biol. 192 497-512 PubMed GONUTS page

[PMID:11598191-28] 28.0 ^28.1 Mykkänen, OM et al. (2001) Characterization of human palladin, a microfilament-associated protein. Mol. Biol. Cell 12 3060-73 PubMed GONUTS page

[PMID:10793131-29] 29.0 ^29.1 ^29.2 ^29.3 Berryman, M & Bretscher, A (2000) Identification of a novel member of the chloride intracellular channel gene family (CLIC5) that associates with the actin cytoskeleton of placental microvilli. Mol. Biol. Cell 11 1509-21 PubMed GONUTS page

[PMID:22658674-30] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:22681889-31] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:7844168-32] Andréoli, C et al. (1994) Ezrin has properties to self-associate at the plasma membrane. J. Cell. Sci. 107 ( Pt 9) 2509-21 PubMed GONUTS page

[PMID:9852149-33] 33.0 ^33.1 Buss, F et al. (1998) The localization of myosin VI at the golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation. J. Cell Biol. 143 1535-45 PubMed GONUTS page

[PMID:29568061-34] Liu, X et al. (2018) An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations. Nat Commun 9 1188 PubMed GONUTS page

[PMID:21988832-35] Wang, J et al. (2011) Toward an understanding of the protein interaction network of the human liver. Mol. Syst. Biol. 7 536 PubMed GONUTS page

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