Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00508
Entry Name
UniProt Accession
Theoretical PI
6.57
Molecular Weight
74139.49
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Lamin-A/C
Protein Synonyms/Alias
70 kDa lamin; Renal carcinoma antigen NY-REN-32;
Gene Name
LMNA
Gene Synonyms/Alias
LMN1;
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
661
Canonical
RTQSPQNCSIM****
[1][2]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Sinensky M, Fantle K, Trujillo M, McLain T, Kupfer A, Dalton M. The processingpathway of prelamin A. J Cell Sci. 1994 Jan;107 ( Pt 1):61-7.[PMID:8175923]
[2] Kilic F, Dalton MB, Burrell SK, Mayer JP, Patterson SD, Sinensky M. In vitroassay and characterization of the farnesylation-dependent prelamin Aendoprotease. J Biol Chem. 1997 Feb 21;272(8):5298-304.[PMID:9030603]
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. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone.
Sequence Annotation
Domain: 432 545 LTD.
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.
Functional site: 266 266 Heptad change of phase.
Functional site: 325 325 Stutter.
Functional site: 330 330 Heptad change of phase.
Functional site: 646 647 Cleavage; by endoprotease.
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 3 3 Phosphothreonine.
Modified residue: 12 12 Phosphoserine.
Modified residue: 18 18 Phosphoserine.
Modified residue: 19 19 Phosphothreonine.
Modified residue: 22 22 Phosphoserine.
Modified residue: 32 32 N6-acetyllysine; alternate.
Modified residue: 32 32 N6-succinyllysine; alternate.
Modified residue: 108 108 N6-acetyllysine.
Modified residue: 123 123 N6-acetyllysine.
Modified residue: 135 135 N6-acetyllysine.
Modified residue: 155 155 N6-acetyllysine.
Modified residue: 171 171 N6-acetyllysine; alternate.
Modified residue: 171 171 N6-succinyllysine; alternate.
Modified residue: 201 201 N6-acetyllysine; alternate.
Modified residue: 212 212 Phosphoserine.
Modified residue: 260 260 N6-acetyllysine.
Modified residue: 270 270 N6-acetyllysine.
Modified residue: 277 277 Phosphoserine.
Modified residue: 301 301 Phosphoserine.
Modified residue: 311 311 N6-acetyllysine.
Modified residue: 390 390 Phosphoserine.
Modified residue: 392 392 Phosphoserine.
Modified residue: 395 395 Phosphoserine.
Modified residue: 404 404 Phosphoserine.
Modified residue: 407 407 Phosphoserine.
Modified residue: 414 414 Phosphoserine.
Modified residue: 431 431 Phosphoserine.
Modified residue: 450 450 N6-acetyllysine.
Modified residue: 457 457 N6-acetyllysine.
Modified residue: 458 458 Phosphoserine.
Modified residue: 463 463 Phosphoserine.
Modified residue: 496 496 Phosphothreonine.
Modified residue: 505 505 Phosphothreonine.
Modified residue: 510 510 Phosphothreonine.
Modified residue: 546 546 Phosphoserine.
Modified residue: 628 628 Phosphoserine.
Modified residue: 632 632 Phosphoserine.
Modified residue: 636 636 Phosphoserine.
Modified residue: 652 652 Phosphoserine.
Modified residue: 661 661 Cysteine methyl ester.
Protein Length
664 AA.
Protein Sequence
(Canonical)
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 LLHHHHGSHC SSSGDPAEYN LRSRTVLCGT CGQPADKASA  600
SGSGAQVGGP ISSGSSASSV TVTRSYRSVG GSGGGSFGDN LVTRSYLLGN SSPRTQSPQN  660
CSIM                                                               664
FASTA
(Canonical)
>LipidDB-9606-00508|P02545
METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLR
LRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARN
TKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAK
KQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESR
LADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRID
SLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQ
ELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRK
LESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLT
YRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAM
RKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASA
SGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSPQN
CSIM
Gene Ontology
GO:0005737; C:cytoplasm; IDA:HPA
GO:0005829; C:cytosol; TAS:Reactome
GO:0005882; C:intermediate filament; TAS:UniProtKB
GO:0005638; C:lamin filament; IEA:Ensembl
GO:0005635; C:nuclear envelope; IDA:UniProtKB
GO:0005652; C:nuclear lamina; TAS:UniProtKB
GO:0005654; C:nucleoplasm; TAS:Reactome
GO:0005634; C:nucleus; IDA:UniProtKB
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:0006915; P:apoptotic process; 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:0030968; P:endoplasmic reticulum unfolded protein response; TAS:Reactome
GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; ISS:BHF-UCL
GO:0000278; P:mitotic cell cycle; TAS:Reactome
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:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl
GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IEA:Ensembl
GO:0090343; P:positive regulation of cell aging; IDA:UniProtKB
GO:0034504; P:protein localization to nucleus; ISS:UniProtKB
GO:0030334; P:regulation of cell migration; ISS:BHF-UCL
GO:1900180; P:regulation of protein localization to nucleus; IEA:Ensembl
GO:0035105; P:sterol regulatory element binding protein import into nucleus; IEA:Ensembl
GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl
Interpro
InterPro; IPR001664; IF
InterPro; IPR018039; Intermediate_filament_CS
InterPro; IPR001322; Lamin_tail_dom
Pfam
Pfam; PF00038; Filament;
Pfam; PF00932; LTD;
SMART
PROSITE
PROSITE; PS00226; IF;
PRINTS