UniProt Accession

 LMNA_HUMAN; P02545; B4DI32; D3DVB0; E7EUI9; P02546; Q5TCJ2; Q5TCJ3; Q969I8; Q96JA2 

Genbank Protein ID

 X03444; X03445; M13451; M13452; AK295390; AL135927; AL135927; AL355388; AL356734; CH471121; CH471121; BC000511; BC003162; BC014507; AF381029 

Genbank Nucleotide ID

 CAA27173.1; CAA27174.1; AAA36164.1; AAA36160.1; BAG58344.1; CAI15521.1; CAI15522.1; EAW52997.1; EAW52999.1; AAH00511.1; AAH03162.1; AAH14507.1; AAK59326.1 

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
32	RITRLQEKEDLQELN	acetylation	[1]
32	RITRLQEKEDLQELN	ubiquitination	[2, 3]
78	SREVSGIKAAYEAEL	ubiquitination	[2, 3, 4, 5]
90	AELGDARKTLDSVAK	ubiquitination	[2, 5]
97	KTLDSVAKERARLQL	acetylation	[1, 6, 7]
97	KTLDSVAKERARLQL	ubiquitination	[2, 3]
108	RLQLELSKVREEFKE	acetylation	[1, 6, 7]
108	RLQLELSKVREEFKE	ubiquitination	[2, 4, 5]
114	SKVREEFKELKARNT	acetylation	[1, 6, 7]
114	SKVREEFKELKARNT	ubiquitination	[5]
135	IAAQARLKDLEALLN	ubiquitination	[2, 4, 5, 8]
144	LEALLNSKEAALSTA	ubiquitination	[2, 4, 5]
155	LSTALSEKRTLEGEL	ubiquitination	[2]
171	DLRGQVAKLEAALGE	ubiquitination	[2, 4, 5]
180	EAALGEAKKQLQDEM	ubiquitination	[2]
181	AALGEAKKQLQDEML	acetylation	[9]
181	AALGEAKKQLQDEML	ubiquitination	[2, 4, 5]
201	ENRLQTMKEELDFQK	sumoylation	[10, 11]
201	ENRLQTMKEELDFQK	ubiquitination	[2, 4, 5]
208	KEELDFQKNIYSEEL	ubiquitination	[2, 4, 5]
233	LVEIDNGKQREFESR	ubiquitination	[2, 5]
260	EDQVEQYKKELEKTY	ubiquitination	[2]
261	DQVEQYKKELEKTYS	ubiquitination	[2]
265	QYKKELEKTYSAKLD	ubiquitination	[2, 4]
270	LEKTYSAKLDNARQS	acetylation	[6]
270	LEKTYSAKLDNARQS	ubiquitination	[2, 4, 5]
311	AQLSQLQKQLAAKEA	acetylation	[6]
311	AQLSQLQKQLAAKEA	ubiquitination	[2, 4, 5, 8]
378	MEIHAYRKLLEGEEE	acetylation	[6]
378	MEIHAYRKLLEGEEE	sumoylation	[12]
378	MEIHAYRKLLEGEEE	ubiquitination	[2, 5]
417	QGGGSVTKKRKLEST	acetylation	[13]
417	QGGGSVTKKRKLEST	ubiquitination	[2]
420	GSVTKKRKLESTESR	sumoylation	[14]
420	GSVTKKRKLESTESR	ubiquitination	[2]
450	EEVDEEGKFVRLRNK	acetylation	[6]
450	EEVDEEGKFVRLRNK	ubiquitination	[2, 5]
457	KFVRLRNKSNEDQSM	ubiquitination	[2]
470	SMGNWQIKRQNGDDP	ubiquitination	[2, 4, 5]
486	LTYRFPPKFTLKAGQ	ubiquitination	[4, 5]
597	TCGQPADKASASGSG	ubiquitination	[2]

Reference

 [1] 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]
 [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] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [10] 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]
 [11] SUMO and its role in human diseases.
 Sarge KD, Park-Sarge OK.
 Int Rev Cell Mol Biol. 2011;288:167-83. [PMID: 21482412]
 [12] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [13] 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]
 [14] A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells.
 Galisson F, Mahrouche L, Courcelles M, Bonneil E, Meloche S, Chelbi-Alix MK, Thibault P.
 Mol Cell Proteomics. 2011 Feb;10(2):M110.004796. [PMID: 21098080] 

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

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