CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036957
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Ezrin 
Protein Synonyms/Alias
  
Gene Name
 EZR 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MPKPINVRVTubiquitination[1, 2, 3]
27IQPNTTGKQLFDQVSubiquitination[4]
40VSAQEVRKENPLQFKacetylation[5]
40VSAQEVRKENPLQFKubiquitination[2]
47KENPLQFKFRAKFYPacetylation[6]
47KENPLQFKFRAKFYPubiquitination[1, 2, 3, 4, 7, 8, 9]
51LQFKFRAKFYPEDVAubiquitination[2, 4, 7]
107AKFGDYNKEVHKSGYacetylation[5]
107AKFGDYNKEVHKSGYubiquitination[2, 3, 4, 7]
111DYNKEVHKSGYLSSEubiquitination[2, 4, 7]
130QRVMDQHKLTRDQWEubiquitination[2, 4, 7, 8]
152AEHRGMLKDNAMLEYubiquitination[2, 4, 7]
177GINYFEIKNKKGTDLubiquitination[4, 7, 8, 10]
179NYFEIKNKKGTDLWLubiquitination[4]
180YFEIKNKKGTDLWLGubiquitination[4]
198LGLNIYEKDDKLTPKubiquitination[4]
201NIYEKDDKLTPKIGFubiquitination[7]
205KDDKLTPKIGFPWSEubiquitination[1, 2, 3, 4, 7, 9]
221RNISFNDKKFVIKPIacetylation[3, 5]
221RNISFNDKKFVIKPIubiquitination[1, 2, 3, 4, 7]
222NISFNDKKFVIKPIDubiquitination[2, 3]
226NDKKFVIKPIDKKAPacetylation[3, 5, 6]
226NDKKFVIKPIDKKAPubiquitination[2]
230FVIKPIDKKAPDFVFacetylation[3]
230FVIKPIDKKAPDFVFubiquitination[4, 7]
231VIKPIDKKAPDFVFYubiquitination[2, 3, 4, 7]
264ELYMRRRKPDTIEVQubiquitination[2, 3, 4, 7]
274TIEVQQMKAQAREEKubiquitination[4, 7]
305RETVEREKEQMMREKubiquitination[7]
312KEQMMREKEELMLRLubiquitination[1, 2, 4, 7]
325RLQDYEEKTKKAEREubiquitination[4, 7]
327QDYEEKTKKAERELSubiquitination[2]
380RQAVDQIKSQEQLAAubiquitination[4, 7]
395ELAEYTAKIALLEEAubiquitination[4, 7]
406LEEARRRKEDEVEEWubiquitination[4, 7]
418EEWQHRAKEAQDDLVubiquitination[2, 3, 4, 7]
426EAQDDLVKTKEELHLubiquitination[2, 3, 4, 7]
491KRITEAEKNERVQRQubiquitination[4, 7]
514SQARDENKRTHNDIIubiquitination[4]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 554 AA 
Protein Sequence
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVSAQEVRK ENPLQFKFRA KFYPEDVAEE 60
LIQDITQKLF FLQVKEGILS DEIYCPPETA VLLGSYAVQA KFGDYNKEVH KSGYLSSERL 120
IPQRVMDQHK LTRDQWEDRI QVWHAEHRGM LKDNAMLEYL KIAQDLEMYG INYFEIKNKK 180
GTDLWLGVDA LGLNIYEKDD KLTPKIGFPW SEIRNISFND KKFVIKPIDK KAPDFVFYAP 240
RLRINKRILQ LCMGNHELYM RRRKPDTIEV QQMKAQAREE KHQKQLERQQ LETEKKRRET 300
VEREKEQMMR EKEELMLRLQ DYEEKTKKAE RELSEQIQRA LQLEEERKRA QEEAERLEAD 360
RMAALRAKEE LERQAVDQIK SQEQLAAELA EYTAKIALLE EARRRKEDEV EEWQHRAKEA 420
QDDLVKTKEE LHLVMTAPPP PPPPVYEPVS YHVQESLQDE GAEPTGYSAE LSSEGIRDDR 480
NEEKRITEAE KNERVQRQLL TLSSELSQAR DENKRTHNDI IHNENMRQGR DKYKTLRQIR 540
QGNTKQRIDE FEAL 554 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0005856; C:cytoskeleton; IEA:InterPro.
 GO:0019898; C:extrinsic to membrane; IEA:InterPro.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA. 
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.
 IPR018980; FERM_PH-like_C.
 IPR008954; Moesin.
 IPR011993; PH_like_dom. 
Pfam
 PF00769; ERM
 PF09380; FERM_C
 PF00373; FERM_M 
SMART
 SM00295; B41 
PROSITE
 PS00661; FERM_2
 PS50057; FERM_3 
PRINTS
 PR00935; BAND41.
 PR00661; ERMFAMILY.