CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005478
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MPKTISVRVTubiquitination[1, 2]
35QLFDQVVKTIGLREVubiquitination[3, 4, 5]
60KGFSTWLKLNKKVTAacetylation[6]
60KGFSTWLKLNKKVTAubiquitination[1]
64TWLKLNKKVTAQDVRacetylation[7]
72VTAQDVRKESPLLFKubiquitination[1, 2, 4, 5]
79KESPLLFKFRAKFYPacetylation[6, 8]
79KESPLLFKFRAKFYPubiquitination[1, 2, 3, 5, 9, 10, 11]
83LLFKFRAKFYPEDVSacetylation[12]
83LLFKFRAKFYPEDVSubiquitination[1, 2, 3, 4, 5, 9, 10, 11]
139SKYGDFNKEVHKSGYacetylation[2, 6, 8]
139SKYGDFNKEVHKSGYubiquitination[1, 2, 4, 5, 9, 10, 11]
143DFNKEVHKSGYLAGDubiquitination[5]
151SGYLAGDKLLPQRVLacetylation[2]
151SGYLAGDKLLPQRVLubiquitination[1, 2]
162QRVLEQHKLNKDQWEacetylation[2]
162QRVLEQHKLNKDQWEubiquitination[1, 2, 4, 5, 9, 11]
165LEQHKLNKDQWEERIacetylation[2]
165LEQHKLNKDQWEERIubiquitination[1, 2, 4, 9, 11]
209GVNYFSIKNKKGSELacetylation[8]
209GVNYFSIKNKKGSELubiquitination[3, 4, 9, 11, 13, 14]
211NYFSIKNKKGSELWLubiquitination[9]
212YFSIKNKKGSELWLGubiquitination[1]
237QNDRLTPKIGFPWSEubiquitination[3, 5, 10]
254NISFNDKKFVIKPIDubiquitination[5]
263VIKPIDKKAPDFVFYubiquitination[5]
327RAMLENEKKKREMAEacetylation[2]
344KEKIEREKEELMERLacetylation[8]
344KEKIEREKEELMERLubiquitination[2]
352EELMERLKQIEEQTKubiquitination[1, 2, 4, 5, 9, 10, 11, 15]
360QIEEQTKKAQQELEEubiquitination[1]
388RAQSEAEKLAKERQEacetylation[2, 8]
400RQEAEEAKEALLQASacetylation[2, 12]
400RQEAEEAKEALLQASubiquitination[1]
412QASRDQKKTQEQLALubiquitination[1]
448EAVEWQQKAQMVQEDubiquitination[1, 4, 11]
458MVQEDLEKTRAELKTacetylation[12]
458MVQEDLEKTRAELKTubiquitination[4]
464EKTRAELKTAMSTPHubiquitination[1, 4, 9, 10, 11]
523ERVQKHLKALTSELAubiquitination[1, 3, 4, 5, 9, 11]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [14] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [15] 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
 Probably involved in connections of major cytoskeletal structures to the plasma membrane. May inhibit herpes simplex virus 1 infection at an early stage. 
Sequence Annotation
 DOMAIN 2 295 FERM.
 MOD_RES 79 79 N6-acetyllysine.
 MOD_RES 116 116 Phosphotyrosine.
 MOD_RES 139 139 N6-acetyllysine.
 MOD_RES 558 558 Phosphothreonine; by ROCK2 and STK10.
 MOD_RES 576 576 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 577 AA 
Protein Sequence
MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKGFSTWLK 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 AMLENEKKKR EMAEKEKEKI EREKEELMER LKQIEEQTKK 360
AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLALE 420
MAELTARISQ LEMARQKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEQ 480
DEQDENGAEA SADLRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA 540
NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM 577 
Gene Ontology
 GO:0045177; C:apical part of cell; IDA:BHF-UCL.
 GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
 GO:0016323; C:basolateral plasma membrane; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005856; C:cytoskeleton; TAS:UniProtKB.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0019898; C:extrinsic to membrane; IEA:InterPro.
 GO:0030175; C:filopodium; IDA:BHF-UCL.
 GO:0005902; C:microvillus; IDA:BHF-UCL.
 GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0001931; C:uropod; IEA:Compara.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
 GO:0007159; P:leukocyte cell-cell adhesion; IEP:BHF-UCL.
 GO:0050900; P:leukocyte migration; IEP:BHF-UCL.
 GO:0022614; P:membrane to membrane docking; IEP:BHF-UCL.
 GO:2000401; P:regulation of lymphocyte migration; IMP:UniProtKB. 
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.