CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008281
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Emerin 
Protein Synonyms/Alias
  
Gene Name
 EMD 
Gene Synonyms/Alias
 EDMD; STA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
79DMYDLPKKEDALLYQubiquitination[1, 2, 3, 4, 5]
88DALLYQSKGYNDDYYubiquitination[2, 3, 4, 5, 6, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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
Functional Description
 Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta- catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C. 
Sequence Annotation
 DOMAIN 1 45 LEM.
 REGION 46 222 Interaction with F-actin (Probable).
 REGION 168 186 Interaction with CTNNB1.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 8 8 Phosphoserine.
 MOD_RES 49 49 Phosphoserine; by PKA.
 MOD_RES 54 54 Phosphoserine.
 MOD_RES 60 60 Phosphoserine.
 MOD_RES 87 87 Phosphoserine.
 MOD_RES 161 161 Phosphotyrosine (By similarity).
 MOD_RES 171 171 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Actin-binding; Cardiomyopathy; Complete proteome; Direct protein sequencing; Disease mutation; Emery-Dreifuss muscular dystrophy; Membrane; Microtubule; Nucleus; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 254 AA 
Protein Sequence
MDNYADLSDT ELTTLLRRYN IPHGPVVGST RRLYEKKIFE YETQRRRLSP PSSSAASSYS 60
FSDLNSTRGD ADMYDLPKKE DALLYQSKGY NDDYYEESYF TTRTYGEPES AGPSRAVRQS 120
VTSFPDADAF HHQVHDDDLL SSSEEECKDR ERPMYGRDSA YQSITHYRPV SASRSSLDLS 180
YYPTSSSTSF MSSSSSSSSW LTRRAIRPEN RAPGAGLGQD RQVPLWGQLL LFLVFVIVLF 240
FIYHFMQAEE GNPF 254 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:HPA.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005637; C:nuclear inner membrane; NAS:BHF-UCL.
 GO:0005640; C:nuclear outer membrane; IDA:UniProtKB.
 GO:0003779; F:actin binding; IDA:UniProtKB.
 GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
 GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
 GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
 GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome.
 GO:0006936; P:muscle contraction; TAS:ProtInc.
 GO:0007517; P:muscle organ development; TAS:ProtInc.
 GO:0035414; P:negative regulation of catenin import into nucleus; IMP:BHF-UCL.
 GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL.
 GO:0046827; P:positive regulation of protein export from nucleus; IMP:BHF-UCL.
 GO:0060828; P:regulation of canonical Wnt receptor signaling pathway; IMP:BHF-UCL.
 GO:0035914; P:skeletal muscle cell differentiation; IEA:Compara. 
Interpro
 IPR011015; LEM/LEM-like_dom.
 IPR003887; LEM_dom. 
Pfam
 PF03020; LEM 
SMART
 SM00540; LEM 
PROSITE
 PS50954; LEM 
PRINTS