CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038908
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Moesin 
Protein Synonyms/Alias
  
Gene Name
 Msn 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
34QLFDQVVKTIGLREVacetylation[1]
59KAFSTWLKLNKKVTAacetylation[1]
78KESPLLFKFRAKFYPacetylation[1]
82LLFKFRAKFYPEDVSacetylation[1]
138SKYGDFNKEVHKSGYacetylation[1]
142DFNKEVHKSGYLAGDacetylation[1]
150SGYLAGDKLLPQRVLacetylation[1]
161QRVLEQHKLNKDQWEacetylation[1]
161QRVLEQHKLNKDQWEubiquitination[2]
164LEQHKLNKDQWEERIacetylation[1]
208GVNYFSIKNKKGSELacetylation[1]
236QNDRLTPKIGFPWSEacetylation[1]
252RNISFNDKKFVIKPIacetylation[1]
253NISFNDKKFVIKPIDacetylation[1]
257NDKKFVIKPIDKKAPacetylation[1]
261FVIKPIDKKAPDFVFacetylation[1]
326RALLENEKKKRELAEacetylation[1]
334KKRELAEKEKEKIERacetylation[1]
343KEKIEREKEELMEKLacetylation[1]
349EKEELMEKLKQIEEQacetylation[1]
351EELMEKLKQIEEQTKacetylation[1]
358KQIEEQTKKAQQELEacetylation[1]
387RAQSEAEKLAKERQEacetylation[1]
399RQEAEEAKEALLQASacetylation[1]
436QLEMARKKKESEAEEacetylation[1]
500LRADAMAKDRSEEERacetylation[1]
522ERVQKHLKALTSELAacetylation[1]
536ANARDESKKTTNDMIacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 576 AA 
Protein Sequence
PKGISVRVTT MDAELEFAIQ PNTTGKQLFD QVVKTIGLRE VWFFGLQYQD TKAFSTWLKL 60
NKKVTAQDVR KESPLLFKFR AKFYPEDVSE ELIQDITQRL FFLQVKEGIL NDDIYCPPET 120
AVLLASYAVQ SKYGDFNKEV HKSGYLAGDK LLPQRVLEQH KLNKDQWEER IQVWHEEHRG 180
MLREDAVLEY LKIAQDLEMY GVNYFSIKNK KGSELWLGVD ALGLNIYEQN DRLTPKIGFP 240
WSEIRNISFN DKKFVIKPID KKAPDFVFYA PRLRINKRIL ALCMGNHELY MRRRKPDTIE 300
VQQMKAQARE EKHQKQMERA LLENEKKKRE LAEKEKEKIE REKEELMEKL KQIEEQTKKA 360
QQELEEQTRR ALELEQERKR AQSEAEKLAK ERQEAEEAKE ALLQASRDQK KTQEQLASEM 420
AELTARISQL EMARKKKESE AEEWQQKAQM VQEDLEKTRA ELKTAMSTPH VAEPAENEHD 480
EQDENGAEAS AELRADAMAK DRSEEERTTE AEKNERVQKH LKALTSELAN ARDESKKTTN 540
DMIHAENMRL GRDKYKTLRQ IRQGNTKQRI DEFESM 576 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IEA:Compara.
 GO:0016323; C:basolateral plasma membrane; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005856; C:cytoskeleton; IEA:InterPro.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0019898; C:extrinsic to membrane; IEA:InterPro.
 GO:0030175; C:filopodium; IEA:Compara.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0005902; C:microvillus; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0001931; C:uropod; IEA:Compara.
 GO:0007159; P:leukocyte cell-cell adhesion; IEA:Compara.
 GO:0050900; P:leukocyte migration; IEA:Compara.
 GO:0022614; P:membrane to membrane docking; IEA:Compara.
 GO:2000401; P:regulation of lymphocyte migration; IEA:Compara. 
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.