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ezrin (human)

Overview ezrin a member of the ERM family which includes radixin and moesin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons. Plays a key role in cell surface structure adhesion, migration, and organization. Note: This description may include information from UniProtKB. Protein type: Cytoskeletal protein; Motility/polarity/chemotaxis Cellular Component: cortical cytoskeleton; microvillus; focal adhesion; basolateral plasma membrane; actin filament; cytosol; actin cytoskeleton; basal body; ruffle; extrinsic to membrane; apical part of cell; microvillus membrane; apical plasma membrane; nucleolus; plasma membrane; uropod; filopodium Molecular Function: actin filament binding; protein binding; cell adhesion molecule binding Biological Process: actin filament bundle formation; axon guidance; regulation of cell shape; leukocyte adhesion; epithelial cell differentiation; cytoskeletal anchoring; membrane to membrane docking; establishment and/or maintenance of apical/basal cell polarity Reference #:  P15311 (UniProtKB) Alt. Names/Synonyms: CVIL; CVL; Cytovillin; cytovillin 2; DKFZp762H157; EZR; EZRI; Ezrin; FLJ26216; MGC1584; p81; VIL2; villin 2 (ezrin); Villin-2 Gene Symbols: EZR Molecular weight: 69,413 Da Basal Isoelectric point: 5.94  Predict pI for various phosphorylation states CST Pathways:  B Cell Receptor Signaling Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below ezrin 1NI2 - A/B=2-297 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
cell adhesion, altered: Y146‑p, T567‑p cell differentiation, altered: T567‑p cell growth, altered: Y146‑p cell motility, altered: Y146‑p, Y354‑p, Y478‑p, T567‑p cytoskeletal reorganization: S66‑p, Y146‑p, Y354‑p, Y478‑p, T567‑p activation: Y354‑p, T567‑p intracellular localization: S66‑p, T567‑p molecular association, regulation: Y146‑p, Y191‑p, Y354‑p, Y478‑p, T567‑p phosphorylation: Y146‑p, Y191‑p, T567‑p protein conformation: T567‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	2		K3-u	_____MPkPINVRVT
0	4		K35-u	QLFDQVVkTIGLREV
0	1		T57-p	VDNKGFPtWLkLDKK
0	2		K60-a	KGFPtWLkLDKKVsA
2	0		S66-p	LkLDKKVsAQEVRkE
0	2		K72-u	VsAQEVRkENPLQFk
0	4		K79-a	kENPLQFkFRAkFYP
0	39		K79-u	kENPLQFkFRAkFYP
0	18		K83-u	LQFkFRAkFYPEDVA
0	1		K107-u	KLFFLQVkEGILsDE
0	3		S112-p	QVkEGILsDEIyCPP
0	15		Y116-p	GILsDEIyCPPETAV
0	1		Y137-p	VQAKFGDyNkEVHkS
0	1		K139-a	AKFGDyNkEVHkSGy
0	11		K139-u	AKFGDyNkEVHkSGy
0	2		K143-u	DyNkEVHkSGyLSsE
9	1		Y146-p	kEVHkSGyLSsERLI
0	1		S149-p	HkSGyLSsERLIPQR
0	13		K162-u	QRVMDQHkLTRDQWE
0	2		K184-u	AEHRGMLkDNAMLEy
1	2		Y191-p	kDNAMLEyLKIAQDL
0	2		Y201-p	IAQDLEMyGINyFEI
0	2		Y205-p	LEMyGINyFEIkNkK
0	3		K209-u	GINyFEIkNkKGTDL
0	1		K211-u	NyFEIkNkKGTDLWL
0	1		K230-u	LGLNIYEkDDkLTPk
0	2		K233-u	NIYEkDDkLTPkIGF
1	0		T235	YEkDDkLTPkIGFPW
0	7		K237-u	kDDkLTPkIGFPWSE
0	27		K253-a	RNISFNDkKFVIKPI
0	3		K253-u	RNISFNDkKFVIKPI
0	1		K254	NISFNDkKFVIKPID
0	7		K263-u	VIKPIDKkAPDFVFy
0	243		Y270-p	kAPDFVFyAPRLRIN
0	8		Y291-p	CMGNHELyMRRRKPD
0	3		K306-u	TIEVQQMkAQAREEK
0	62		T332-p	TEKKRREtVEREkEQ
0	2		K337-u	REtVEREkEQMMREk
0	3		K344-u	kEQMMREkEELMLRL
8	239		Y354-p	LMLRLQDyEEkTKKA
0	1		K357-u	RLQDyEEkTKKAERE
0	6		R363	EkTKKAERELSEQIQ
0	1		R371	ELSEQIQRALQLEEE
0	3		K412-u	RQAVDQIkSQEQLAA
0	148		Y424-p	LAAELAEytAkIALL
0	10		T425-p	AAELAEytAkIALLE
0	2		K427-u	ELAEytAkIALLEEA
0	2		K438-u	LEEARRRkEDEVEEW
0	2		K450-u	EEWQHRAkEAQDDLV
0	2		K458-u	EAQDDLVkTKEELHL
0	1		T468-p	EELHLVMtAPPPPPP
5	134		Y478-p	PPPPPPVyEPVsyHV
0	27		S482-p	PPVyEPVsyHVQEsL
0	37		Y483-p	PVyEPVsyHVQEsLQ
0	5		S488-p	VsyHVQEsLQDEGAE
0	1		T497-p	QDEGAEPtGySAELS
0	35		Y499-p	EGAEPtGySAELSSE
0	2		K523-u	KRITEAEkNERVQRQ
0	6		S535-p	QRQLLTLsSELsQAR
0	6		S539-p	LTLsSELsQARDENK
0	1		K546	sQARDENKRtHNDII
0	1		T548-p	ARDENKRtHNDIIHN
37	17		T567-p	QGRDKYKtLRQIRQG
0	1		T576-p	RQIRQGNtKQRIDEF

	mouse
K3-u	_____MPkPINVRVT
K35	QLFDQVVKTIGLREV
T57-p	VDNKGFPtWLKLDKK
K60	KGFPtWLKLDKKVSA
S66	LKLDKKVSAQEVRkE
K72-u	VSAQEVRkENPVQFk
K79	kENPVQFKFRAkFYP
K79-u	kENPVQFkFRAkFYP
K83-u	VQFkFRAkFYPEDVA
K107	KLFFLQVKDGILSDE
S112	QVKDGILSDEIYCPP
Y116	GILSDEIYCPPETAV
Y137	VQAKFGDYNkEMHkS
K139	AKFGDYNKEMHkSGy
K139-u	AKFGDYNkEMHkSGy
K143-u	DYNkEMHkSGyLSSE
Y146-p	kEMHkSGyLSSERLI
S149	HkSGyLSSERLIPQR
K162-u	QRVMDQHkLSRDQWE
K184-u	AEHRGMLkDSAMLEY
Y191	kDSAMLEYLKIAQDL
Y201	IAQDLEMYGINYFEI
Y205	LEMYGINYFEIkNKK
K209-u	GINYFEIkNKKGTDL
K211	NYFEIkNKKGTDLWL
K230	LGLNIYEKDDKLtPk
K233	NIYEKDDKLtPkIGF
T235-p	YEKDDKLtPkIGFPW
K237-u	KDDKLtPkIGFPWSE
K253-a	RNISFNDkkFVIKPI
K253-u	RNISFNDkkFVIKPI
K254-a	NISFNDkkFVIKPID
K263-u	VIKPIDKkAPDFVFy
Y270-p	kAPDFVFyAPRLRIN
Y291-p	CMGNHELyMRRRKPD
K306-u	TIEVQQMkAQAREEK
T332	TEKKRRETVEREkEQ
K337-u	RETVEREkEQMLREk
K344-u	kEQMLREkEELMLRL
Y354-p	LMLRLQDyEQKTKRA
K357	RLQDyEQKTKRAEkE
K363-u	QKTKRAEkELSEQIE
K371-u	ELSEQIEkALQLEEE
K412-u	RQAQDQIkSQEQLAA
Y424	LAAELAEYTAKIALL
T425	AAELAEYTAKIALLE
K427	ELAEYTAKIALLEEA
K438-u	LEEARRRkEDEVEEW
K450-u	EEWQHRAkEAQDDLV
K458-u	EAQDDLVkTKEELHL
T468	EELHLVMTAPPPPPP
Y478-p	PPPPPPVyEPVNyHV
N482	PPVyEPVNyHVQEGL
Y483-p	PVyEPVNyHVQEGLQ
G488	VNyHVQEGLQDEGAE
M497	QDEGAEPMGYSAELS
Y499	EGAEPMGYSAELSSE
K523-u	KRITEAEkNERVQRQ
S535-p	QRQLLTLsNELSQAR
S539	LTLsNELSQARDENk
K546-u	SQARDENkRTHNDII
T548	ARDENkRTHNDIIHN
T567-p	QGRDKYKtLRQIRQG
T576	RQIRQGNTKQRIDEF

	rat
K3	_____MPKPINVRVT
K35	QLFDQVVKTIGLREV
T57	VDNKGFPTWLKLDKK
K60	KGFPTWLKLDKKVSA
S66	LKLDKKVSAQEVRKE
K72	VSAQEVRKENPVQFK
K79	KENPVQFKFRAKFYP
K79	KENPVQFKFRAKFYP
K83	VQFKFRAKFYPEDVA
K107	KLFFLQVKEGILSDE
S112	QVKEGILSDEIYCPP
Y116	GILSDEIYCPPETAV
Y137	VQAKFGDYNKEMHKS
K139	AKFGDYNKEMHKSGY
K139	AKFGDYNKEMHKSGY
K143	DYNKEMHKSGYLSSE
Y146	KEMHKSGYLSSERLI
S149	HKSGYLSSERLIPQR
K162	QRVMDQHKLSRDQWE
K184	AEHRGMLKDSAMLEY
Y191	KDSAMLEYLKIAQDL
Y201	IAQDLEMYGINYFEI
Y205	LEMYGINYFEIKNKK
K209	GINYFEIKNKKGTDL
K211	NYFEIKNKKGTDLWL
K230	LGLNIYEKDDKLTPK
K233	NIYEKDDKLTPKIGF
T235	YEKDDKLTPKIGFPW
K237	KDDKLTPKIGFPWSE
K253	RNISFNDKKFVIKPI
K253	RNISFNDKKFVIKPI
K254	NISFNDKKFVIKPID
K263	VIKPIDKKAPDFVFy
Y270-p	KAPDFVFyAPRLRIN
Y291	CMGNHELYMRRRKPD
K306	TIEVQQMKAQAREEK
T332	TEKKRRETVEREKEQ
K337	RETVEREKEQMLREK
K344	KEQMLREKEELMLRL
F354	LMLRLQDFEQKTKRA
K357	RLQDFEQKTKRAEkE
K363-u	QKTKRAEkELSEQIE
K371	ELSEQIEKALQLEEE
K412	RQAQDQIKSQEQLAA
Y424	LAAELAEYTAKIALL
T425	AAELAEYTAKIALLE
K427	ELAEYTAKIALLEEA
K438	LEEARRRKEDEVEEW
K450	EEWQHRAKEAQDDLV
K458	EAQDDLVKTKEELHL
T468	EELHLVMTAPPPPPP
Y478	PPPPPPVYEPVNYHV
N482	PPVYEPVNYHVQEGL
Y483	PVYEPVNYHVQEGLQ
G488	VNYHVQEGLQDEGAE
M497	QDEGAEPMGYSAELS
Y499	EGAEPMGYSAELSSE
K523	KRITEAEKNERVQRQ
S535	QRQLLTLSNELSQAR
S539	LTLSNELSQARDENK
K546	SQARDENKRTHNDII
T548	ARDENKRTHNDIIHN
T567-p	QGRDKYKtLRQIRQG
T576	RQIRQGNTKQRIDEF

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