CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001976
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prelamin-A/C 
Protein Synonyms/Alias
 Lamin-A/C; 70 kDa lamin; Renal carcinoma antigen NY-REN-32 
Gene Name
 LMNA 
Gene Synonyms/Alias
 LMN1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32RITRLQEKEDLQELNubiquitination[1]
78SREVSGIKAAYEAELubiquitination[1, 2]
90AELGDARKTLDSVAKubiquitination[2]
97KTLDSVAKERARLQLubiquitination[1]
108RLQLELSKVREEFKEubiquitination[2]
114SKVREEFKELKARNTubiquitination[2]
135IAAQARLKDLEALLNubiquitination[1, 2]
144LEALLNSKEAALSTAubiquitination[1, 2]
155LSTALSEKRTLEGELubiquitination[1]
171DLRGQVAKLEAALGEubiquitination[1, 2]
180EAALGEAKKQLQDEMubiquitination[1]
181AALGEAKKQLQDEMLubiquitination[1, 2]
201ENRLQTMKEELDFQKubiquitination[1, 2]
208KEELDFQKNIYSEELubiquitination[1, 2]
219SEELRETKRRHETRLubiquitination[1]
233LVEIDNGKQREFESRubiquitination[1, 2]
260EDQVEQYKKELEKTYubiquitination[1]
261DQVEQYKKELEKTYSubiquitination[1]
265QYKKELEKTYSAKLDubiquitination[1]
270LEKTYSAKLDNARQSubiquitination[1, 2]
311AQLSQLQKQLAAKEAubiquitination[1, 2]
319QLAAKEAKLRDLEDSubiquitination[1]
378MEIHAYRKLLEGEEEubiquitination[1, 2]
417QGGGSVTKKRKLESTubiquitination[1]
450EEVDEEGKFVRLRNKubiquitination[2]
457KFVRLRNKSNEDQSMubiquitination[1]
470SMGNWQIKRQNGDDPubiquitination[1, 2]
486LTYRFPPKFTLKAGQubiquitination[2]
Reference
 [1] 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]
 [2] 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] 
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. 
Sequence Annotation
 REGION 1 130 Interaction with MLIP.
 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 384 664 Tail.
 MOTIF 417 422 Nuclear localization signal (Potential).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 3 3 Phosphothreonine.
 MOD_RES 12 12 Phosphoserine.
 MOD_RES 18 18 Phosphoserine.
 MOD_RES 19 19 Phosphothreonine.
 MOD_RES 22 22 Phosphoserine.
 MOD_RES 108 108 N6-acetyllysine.
 MOD_RES 212 212 Phosphoserine.
 MOD_RES 270 270 N6-acetyllysine.
 MOD_RES 277 277 Phosphoserine.
 MOD_RES 301 301 Phosphoserine.
 MOD_RES 311 311 N6-acetyllysine.
 MOD_RES 390 390 Phosphoserine.
 MOD_RES 392 392 Phosphoserine.
 MOD_RES 395 395 Phosphoserine.
 MOD_RES 398 398 Phosphoserine (By similarity).
 MOD_RES 404 404 Phosphoserine.
 MOD_RES 406 406 Phosphoserine (By similarity).
 MOD_RES 407 407 Phosphoserine (By similarity).
 MOD_RES 414 414 Phosphoserine.
 MOD_RES 431 431 Phosphoserine.
 MOD_RES 450 450 N6-acetyllysine.
 MOD_RES 458 458 Phosphoserine.
 MOD_RES 463 463 Phosphoserine.
 MOD_RES 496 496 Phosphothreonine (By similarity).
 MOD_RES 505 505 Phosphothreonine.
 MOD_RES 510 510 Phosphothreonine (By similarity).
 MOD_RES 571 571 Phosphoserine (By similarity).
 MOD_RES 573 573 Phosphoserine (By similarity).
 MOD_RES 628 628 Phosphoserine.
 MOD_RES 632 632 Phosphoserine.
 MOD_RES 636 636 Phosphoserine.
 MOD_RES 652 652 Phosphoserine.
 MOD_RES 661 661 Cysteine methyl ester.
 LIPID 661 661 S-farnesyl cysteine.
 CROSSLNK 201 201 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cardiomyopathy; Charcot-Marie-Tooth disease; Coiled coil; Complete proteome; Congenital muscular dystrophy; Direct protein sequencing; Disease mutation; Emery-Dreifuss muscular dystrophy; Intermediate filament; Isopeptide bond; Limb-girdle muscular dystrophy; Lipoprotein; Methylation; Neuropathy; Nucleus; Phosphoprotein; Prenylation; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 664 AA 
Protein Sequence
METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR 60
LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKELKARN 120
TKKEGDLIAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALGEAK 180
KQLQDEMLRR VDAENRLQTM KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR 240
LADALQELRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID 300
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA RMQQQLDEYQ 360
ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQTQ GGGSVTKKRK 420
LESTESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIK RQNGDDPLLT 480
YRFPPKFTLK AGQVVTIWAA GAGATHSPPT DLVWKAQNTW GCGNSLRTAL INSTGEEVAM 540
RKLVRSVTVV EDDEDEDGDD LLHHHHVSGS RR 572 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005638; C:lamin filament; IEA:Compara.
 GO:0005635; C:nuclear envelope; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
 GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
 GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
 GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; ISS:BHF-UCL.
 GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
 GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome.
 GO:0007517; P:muscle organ development; IMP:UniProtKB.
 GO:0090343; P:positive regulation of cell aging; IDA:UniProtKB.
 GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
 GO:0042981; P:regulation of apoptotic process; IEA:Compara.
 GO:0030334; P:regulation of cell migration; ISS:BHF-UCL.
 GO:0035105; P:sterol regulatory element binding protein import into nucleus; IEA:Compara.
 GO:0055015; P:ventricular cardiac muscle cell development; IEA:Compara. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR018039; Intermediate_filament_CS.
 IPR001322; Lamin_tail_dom. 
Pfam
 PF00038; Filament
 PF00932; LTD 
SMART
  
PROSITE
 PS00226; IF 
PRINTS