CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008070
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prelamin-A/C 
Protein Synonyms/Alias
 Lamin-A/C 
Gene Name
 Lmna 
Gene Synonyms/Alias
 Lmn1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
123LKARNTKKEGDLLAAacetylation[1, 2]
135LAAQARLKDLEALLNacetylation[2]
135LAAQARLKDLEALLNubiquitination[3]
144LEALLNSKEAALSTAacetylation[2, 4]
144LEALLNSKEAALSTAsuccinylation[2]
144LEALLNSKEAALSTAubiquitination[3]
155LSTALSEKRTLEGELacetylation[2, 4]
155LSTALSEKRTLEGELubiquitination[3]
171DLRGQVAKLEAALGEacetylation[1, 2, 4]
171DLRGQVAKLEAALGEsuccinylation[2]
171DLRGQVAKLEAALGEubiquitination[3]
180EAALGEAKKQLQDEMubiquitination[3]
181AALGEAKKQLQDEMLubiquitination[3]
201ENRLQTLKEELDFQKacetylation[1, 2, 4]
201ENRLQTLKEELDFQKsuccinylation[2]
201ENRLQTLKEELDFQKsumoylation[5]
201ENRLQTLKEELDFQKubiquitination[3]
208KEELDFQKNIYSEELubiquitination[3]
219SEELRETKRRHETRLubiquitination[3]
233LVEIDNGKQREFESRacetylation[4]
233LVEIDNGKQREFESRubiquitination[3]
260EDQVEQYKKELEKTYacetylation[1, 2]
270LEKTYSAKLDNARQSacetylation[1, 2]
270LEKTYSAKLDNARQSsuccinylation[2]
270LEKTYSAKLDNARQSubiquitination[3]
311AQLSQLQKQLAAKEAacetylation[1, 2]
311AQLSQLQKQLAAKEAubiquitination[3]
319QLAAKEAKLRDLEDSacetylation[4]
319QLAAKEAKLRDLEDSubiquitination[3]
420GSVTKKRKLESSESRacetylation[2]
450EEVDEEGKFVRLRNKacetylation[1, 2, 4]
450EEVDEEGKFVRLRNKsuccinylation[2]
450EEVDEEGKFVRLRNKubiquitination[3]
457KFVRLRNKSNEDQSMacetylation[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] 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]
 [3] 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]
 [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]
 [5] Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies.
 Zhang YQ, Sarge KD.
 J Cell Biol. 2008 Jul 14;182(1):35-9. [PMID: 18606848] 
Functional Description
 Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (By similarity). 
Sequence Annotation
 REGION 1 130 Interaction with MLIP (By similarity).
 REGION 1 33 Head.
 REGION 34 383 Rod.
 REGION 34 70 Coil 1A.
 REGION 71 80 Linker 1.
 REGION 81 218 Coil 1B.
 REGION 219 242 Linker 2.
 REGION 243 383 Coil 2.
 REGION 384 665 Tail.
 MOTIF 417 422 Nuclear localization signal (Potential).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 3 3 Phosphothreonine (By similarity).
 MOD_RES 12 12 Phosphoserine.
 MOD_RES 18 18 Phosphoserine (By similarity).
 MOD_RES 19 19 Phosphothreonine.
 MOD_RES 22 22 Phosphoserine.
 MOD_RES 108 108 N6-acetyllysine (By similarity).
 MOD_RES 212 212 Phosphoserine (By similarity).
 MOD_RES 270 270 N6-acetyllysine (By similarity).
 MOD_RES 277 277 Phosphoserine (By similarity).
 MOD_RES 301 301 Phosphoserine.
 MOD_RES 311 311 N6-acetyllysine (By similarity).
 MOD_RES 390 390 Phosphoserine.
 MOD_RES 392 392 Phosphoserine; by CDK1.
 MOD_RES 395 395 Phosphoserine (By similarity).
 MOD_RES 398 398 Phosphoserine.
 MOD_RES 404 404 Phosphoserine (By similarity).
 MOD_RES 406 406 Phosphoserine.
 MOD_RES 407 407 Phosphoserine.
 MOD_RES 409 409 Phosphoserine.
 MOD_RES 414 414 Phosphoserine.
 MOD_RES 431 431 Phosphoserine (By similarity).
 MOD_RES 450 450 N6-acetyllysine (By similarity).
 MOD_RES 458 458 Phosphoserine (By similarity).
 MOD_RES 463 463 Phosphoserine (By similarity).
 MOD_RES 496 496 Phosphothreonine (By similarity).
 MOD_RES 500 500 Phosphoserine (By similarity).
 MOD_RES 505 505 Phosphothreonine (By similarity).
 MOD_RES 510 510 Phosphothreonine (By similarity).
 MOD_RES 573 573 Phosphoserine.
 MOD_RES 575 575 Phosphoserine.
 MOD_RES 629 629 Phosphoserine.
 MOD_RES 633 633 Phosphoserine.
 MOD_RES 637 637 Phosphoserine.
 MOD_RES 653 653 Phosphoserine (By similarity).
 MOD_RES 662 662 Cysteine methyl ester (By similarity).
 LIPID 662 662 S-farnesyl cysteine (By similarity).
 CROSSLNK 201 201 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Coiled coil; Complete proteome; Direct protein sequencing; Intermediate filament; Isopeptide bond; Lipoprotein; Methylation; Nucleus; Phosphoprotein; Prenylation; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 665 AA 
Protein Sequence
METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR 60
LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKELKARN 120
TKKEGDLLAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALGEAK 180
KQLQDEMLRR VDAENRLQTL KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR 240
LADALQELRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID 300
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA RMQQQLDEYQ 360
ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQSQ GGGSVTKKRK 420
LESSESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIR RQNGDDPLMT 480
YRFPPKFTLK AGQVVTIWAS GAGATHSPPT DLVWKAQNTW GCGSSLRTAL INSTGEEVAM 540
RKLVRSLTMV EDNEDDDEDG EELLHHHRGS HCSGSGDPAE YNLRSRTVLC GTCGQPADKA 600
AGGAGAQVGG SISSGSSASS VTVTRSFRSV GGSGGGSFGD NLVTRSYLLG NSSPRSQSSQ 660
NCSIM 665 
Gene Ontology
 GO:0005638; C:lamin filament; IDA:MGI.
 GO:0005635; C:nuclear envelope; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:BHF-UCL.
 GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0071456; P:cellular response to hypoxia; ISS:BHF-UCL.
 GO:0030010; P:establishment of cell polarity; NAS:BHF-UCL.
 GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:BHF-UCL.
 GO:0007517; P:muscle organ development; ISS:BHF-UCL.
 GO:0006998; P:nuclear envelope organization; IGI:MGI.
 GO:0090343; P:positive regulation of cell aging; ISS:UniProtKB.
 GO:0030334; P:regulation of cell migration; IMP:BHF-UCL.
 GO:0035105; P:sterol regulatory element binding protein import into nucleus; IMP:MGI.
 GO:0055015; P:ventricular cardiac muscle cell development; IMP:MGI. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR018039; Intermediate_filament_CS.
 IPR001322; Lamin_tail_dom. 
Pfam
 PF00038; Filament
 PF00932; LTD 
SMART
  
PROSITE
 PS00226; IF 
PRINTS