CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036053
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Prelamin-A/C 
Protein Synonyms/Alias
  
Gene Name
 LMNA 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36IAAQARLKDLEALLNubiquitination[1, 2, 3]
45LEALLNSKEAALSTAubiquitination[1, 2, 3]
56LSTALSEKRTLEGELubiquitination[2, 3]
72DLRGQVAKLEAALGEubiquitination[1, 2, 3, 4]
81EAALGEAKKQLQDEMubiquitination[2, 3, 4]
82AALGEAKKQLQDEMLubiquitination[1, 2, 3]
102ENRLQTMKEELDFQKacetylation[5, 6]
102ENRLQTMKEELDFQKubiquitination[1, 2, 3]
109KEELDFQKNIYSEELubiquitination[1, 2, 3]
120SEELRETKRRHETRLubiquitination[3]
134LVEIDNGKQREFESRubiquitination[2, 3, 4]
161EDQVEQYKKELEKTYubiquitination[2, 3, 4]
162DQVEQYKKELEKTYSubiquitination[2, 3, 4]
166QYKKELEKTYSAKLDubiquitination[1, 2, 3]
171LEKTYSAKLDNARQSacetylation[5, 6]
171LEKTYSAKLDNARQSubiquitination[1, 2, 3, 4]
212AQLSQLQKQLAAKEAacetylation[5, 6]
212AQLSQLQKQLAAKEAubiquitination[1, 2, 3, 4]
220QLAAKEAKLRDLEDSubiquitination[3]
279MEIHAYRKLLEGEEEacetylation[5]
279MEIHAYRKLLEGEEEubiquitination[2, 3, 7, 8, 9]
318QGGGSVTKKRKLESTubiquitination[2, 3]
321GSVTKKRKLESTESRubiquitination[2]
351EEVDEEGKFVRLRNKacetylation[5, 6]
351EEVDEEGKFVRLRNKubiquitination[2]
358KFVRLRNKSNEDQSMubiquitination[2, 3]
371SMGNWQIKRQNGDDPacetylation[5, 6]
371SMGNWQIKRQNGDDPubiquitination[1, 2, 3]
387LTYRFPPKFTLKAGQubiquitination[1]
498TCGQPADKASASGSGubiquitination[2, 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] 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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Coiled coil; Complete proteome; Intermediate filament; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 565 AA 
Protein Sequence
MDLEAWDPHL EPDAEAMVDG NTKKEGDLIA AQARLKDLEA LLNSKEAALS TALSEKRTLE 60
GELHDLRGQV AKLEAALGEA KKQLQDEMLR RVDAENRLQT MKEELDFQKN IYSEELRETK 120
RRHETRLVEI DNGKQREFES RLADALQELR AQHEDQVEQY KKELEKTYSA KLDNARQSAE 180
RNSNLVGAAH EELQQSRIRI DSLSAQLSQL QKQLAAKEAK LRDLEDSLAR ERDTSRRLLA 240
EKEREMAEMR ARMQQQLDEY QELLDIKLAL DMEIHAYRKL LEGEEERLRL SPSPTSQRSR 300
GRASSHSSQT QGGGSVTKKR KLESTESRSS FSQHARTSGR VAVEEVDEEG KFVRLRNKSN 360
EDQSMGNWQI KRQNGDDPLL TYRFPPKFTL KAGQVVTIWA AGAGATHSPP TDLVWKAQNT 420
WGCGNSLRTA LINSTGEEVA MRKLVRSVTV VEDDEDEDGD DLLHHHHGSH CSSSGDPAEY 480
NLRSRTVLCG TCGQPADKAS ASGSGAQVGG PISSGSSASS VTVTRSYRSV GGSGGGSFGD 540
NLVTRSYLLG NSSPRTQSPQ NCSIM 565 
Gene Ontology
 GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
 GO:0005198; F:structural molecule activity; IEA:InterPro. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR018039; Intermediate_filament_CS.
 IPR001322; Lamin_tail_dom. 
Pfam
 PF00038; Filament
 PF00932; LTD 
SMART
  
PROSITE
 PS00226; IF 
PRINTS