CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005481
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Moesin 
Protein Synonyms/Alias
 Membrane-organizing extension spike protein 
Gene Name
 Msn 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
60KAFSTWLKLNKKVTAacetylation[1]
60KAFSTWLKLNKKVTAubiquitination[2]
63STWLKLNKKVTAQDVacetylation[1]
64TWLKLNKKVTAQDVRacetylation[3]
64TWLKLNKKVTAQDVRsuccinylation[3]
72VTAQDVRKESPLLFKacetylation[1, 3]
72VTAQDVRKESPLLFKsuccinylation[3]
72VTAQDVRKESPLLFKubiquitination[2]
79KESPLLFKFRAKFYPacetylation[1, 3, 4]
79KESPLLFKFRAKFYPsuccinylation[3]
79KESPLLFKFRAKFYPubiquitination[2]
83LLFKFRAKFYPEDVSubiquitination[2]
139SKYGDFNKEVHKSGYacetylation[1]
139SKYGDFNKEVHKSGYubiquitination[2]
143DFNKEVHKSGYLAGDubiquitination[2]
151SGYLAGDKLLPQRVLacetylation[3, 4]
151SGYLAGDKLLPQRVLsuccinylation[3]
162QRVLEQHKLNKDQWEacetylation[3]
162QRVLEQHKLNKDQWEubiquitination[2]
165LEQHKLNKDQWEERIacetylation[1, 3]
165LEQHKLNKDQWEERIubiquitination[2]
209GVNYFSIKNKKGSELubiquitination[2]
350EKEELMEKLKQIEEQubiquitination[2]
352EELMEKLKQIEEQTKubiquitination[2]
360QIEEQTKKAQQELEEubiquitination[2]
400RQEAEEAKEALLQASacetylation[4]
412QASRDQKKTQEQLASacetylation[3]
438LEMARKKKESEAVEWacetylation[1]
448EAVEWQQKAQMVQEDubiquitination[2]
458MVQEDLEKTRAELKTacetylation[1]
458MVQEDLEKTRAELKTubiquitination[2]
464EKTRAELKTAMSTPHubiquitination[2]
523ERVQKHLKALTSELAubiquitination[2]
537ANARDESKKTANDMIubiquitination[2]
538NARDESKKTANDMIHubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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
Functional Description
 Probably involved in connections of major cytoskeletal structures to the plasma membrane. 
Sequence Annotation
 DOMAIN 2 295 FERM.
 MOD_RES 79 79 N6-acetyllysine (By similarity).
 MOD_RES 116 116 Phosphotyrosine.
 MOD_RES 139 139 N6-acetyllysine (By similarity).
 MOD_RES 558 558 Phosphothreonine; by ROCK2 and STK10.
 MOD_RES 576 576 Phosphoserine.  
Keyword
 Acetylation; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 577 AA 
Protein Sequence
MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKAFSTWLK 60
LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE 120
TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR 180
GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF 240
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI 300
EVQQMKAQAR EEKHQKQMER ALLENEKKKR ELAEKEKEKI EREKEELMEK LKQIEEQTKK 360
AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLASE 420
MAELTARISQ LEMARKKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEH 480
DEQDENGAEA SAELRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA 540
NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM 577 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IDA:MGI.
 GO:0016323; C:basolateral plasma membrane; IDA:MGI.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 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:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0001931; C:uropod; IDA:MGI.
 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.