CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005480
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ezrin 
Protein Synonyms/Alias
 Cytovillin; Villin-2; p81 
Gene Name
 Ezr 
Gene Synonyms/Alias
 Vil2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
3*****MPKPINVRVTubiquitination[1]
35QLFDQVVKTIGLREVacetylation[2]
60KGFPTWLKLDKKVSAphosphoglycerylation[3]
72VSAQEVRKENPVQFKubiquitination[1]
79KENPVQFKFRAKFYPubiquitination[1, 4]
139AKFGDYNKEMHKSGYubiquitination[1, 4]
143DYNKEMHKSGYLSSEubiquitination[1, 4]
162QRVMDQHKLSRDQWEubiquitination[1, 4]
184AEHRGMLKDSAMLEYubiquitination[1]
209GINYFEIKNKKGTDLubiquitination[1]
237KDDKLTPKIGFPWSEacetylation[2]
237KDDKLTPKIGFPWSEubiquitination[1]
253RNISFNDKKFVIKPIacetylation[5]
253RNISFNDKKFVIKPIubiquitination[1]
254NISFNDKKFVIKPIDacetylation[2]
258NDKKFVIKPIDKKAPacetylation[2]
262FVIKPIDKKAPDFVFacetylation[2]
263VIKPIDKKAPDFVFYacetylation[2]
263VIKPIDKKAPDFVFYubiquitination[1]
306TIEVQQMKAQAREEKubiquitination[1]
337RETVEREKEQMLREKubiquitination[1]
344KEQMLREKEELMLRLubiquitination[1]
363QKTKRAEKELSEQIEacetylation[6]
363QKTKRAEKELSEQIEubiquitination[1]
371ELSEQIEKALQLEEEubiquitination[1]
412RQAQDQIKSQEQLAAubiquitination[1]
438LEEARRRKEDEVEEWubiquitination[1]
450EEWQHRAKEAQDDLVubiquitination[1, 4]
458EAQDDLVKTKEELHLubiquitination[1]
523KRITEAEKNERVQRQubiquitination[1]
546SQARDENKRTHNDIIubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]
 [4] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 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 (By similarity). 
Sequence Annotation
 DOMAIN 2 295 FERM.
 REGION 244 586 Interaction with SCYL3 (By similarity).
 MOD_RES 60 60 N6-acetyllysine (By similarity).
 MOD_RES 146 146 Phosphotyrosine; by PDGFR (By
 MOD_RES 354 354 Phosphotyrosine; by PDGFR (By
 MOD_RES 535 535 Phosphoserine (By similarity).
 MOD_RES 567 567 Phosphothreonine; by ROCK2 and PKC/PRKCI  
Keyword
 Acetylation; Cell membrane; Cell projection; Cell shape; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 586 AA 
Protein Sequence
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK 60
LDKKVSAQEV RKENPVQFKF RAKFYPEDVA EELIQDITQK LFFLQVKDGI LSDEIYCPPE 120
TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR 180
GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF 240
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI 300
EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR LQDYEQKTKR 360
AEKELSEQIE KALQLEEERR RAQEEAERLE ADRMAALRAK EELERQAQDQ IKSQEQLAAE 420
LAEYTAKIAL LEEARRRKED EVEEWQHRAK EAQDDLVKTK EELHLVMTAP PPPPPPVYEP 480
VNYHVQEGLQ DEGAEPMGYS AELSSEGILD DRNEEKRITE AEKNERVQRQ LLTLSNELSQ 540
ARDENKRTHN DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM 586 
Gene Ontology
 GO:0005884; C:actin filament; ISS:UniProtKB.
 GO:0016324; C:apical plasma membrane; IDA:MGI.
 GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0019898; C:extrinsic to membrane; ISS:UniProtKB.
 GO:0030175; C:filopodium; IEA:Compara.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0005932; C:microtubule basal body; IDA:MGI.
 GO:0005902; C:microvillus; IDA:MGI.
 GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO:0001931; C:uropod; IDA:MGI.
 GO:0051015; F:actin filament binding; ISS:UniProtKB.
 GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
 GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
 GO:0030855; P:epithelial cell differentiation; IEA:Compara.
 GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:MGI.
 GO:0007159; P:leukocyte cell-cell adhesion; IEA:Compara.
 GO:0022614; P:membrane to membrane docking; IEA:Compara.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 
Interpro
 IPR019749; Band_41_domain.
 IPR019750; Band_41_fam.
 IPR011174; ERM.
 IPR011259; ERM_C_dom.
 IPR000798; Ez/rad/moesin_like.
 IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
 IPR019748; FERM_central.
 IPR019747; FERM_CS.
 IPR000299; FERM_domain.
 IPR018979; FERM_N.
 IPR018980; FERM_PH-like_C.
 IPR008954; Moesin.
 IPR011993; PH_like_dom. 
Pfam
 PF00769; ERM
 PF09380; FERM_C
 PF00373; FERM_M
 PF09379; FERM_N 
SMART
 SM00295; B41 
PROSITE
 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3 
PRINTS
 PR00935; BAND41.
 PR00661; ERMFAMILY.