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Protein

Prelamin-A/C

Gene

Lmna

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Isoform C2 may have a role in determining the organization of nuclear and chromosomal structures during spermatogenesis.6 Publications
Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei266Heptad change of phase1
Sitei325StutterBy similarity1
Sitei330Heptad change of phase1

GO - Molecular functioni

GO - Biological processi

  • cellular response to hypoxia Source: BHF-UCL
  • establishment of cell polarity Source: BHF-UCL
  • establishment or maintenance of microtubule cytoskeleton polarity Source: BHF-UCL
  • muscle organ development Source: BHF-UCL
  • negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  • negative regulation of mesenchymal cell proliferation Source: MGI
  • negative regulation of release of cytochrome c from mitochondria Source: MGI
  • nuclear envelope organization Source: MGI
  • nucleus organization Source: MGI
  • positive regulation of cell aging Source: UniProtKB
  • positive regulation of gene expression Source: MGI
  • protein localization to nucleus Source: UniProtKB
  • regulation of cell migration Source: BHF-UCL
  • regulation of protein localization to nucleus Source: MGI
  • sterol regulatory element binding protein import into nucleus Source: MGI
  • ventricular cardiac muscle cell development Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2993913. Clearance of Nuclear Envelope Membranes from Chromatin.
R-MMU-2995383. Initiation of Nuclear Envelope Reformation.
R-MMU-352238. Breakdown of the nuclear lamina.
R-MMU-4419969. Depolymerisation of the Nuclear Lamina.

Names & Taxonomyi

Protein namesi
Recommended name:
Prelamin-A/C
Cleaved into the following chain:
Gene namesi
Name:Lmna
Synonyms:Lmn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:96794. Lmna.

Subcellular locationi

  • Nucleus
  • Nucleus envelope
  • Nucleus lamina By similarity
  • Nucleusnucleoplasm By similarity

  • Note: Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular matrix Source: MGI
  • lamin filament Source: MGI
  • nuclear envelope Source: UniProtKB
  • nuclear membrane Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: BHF-UCL
  • perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant mice survive postnatally for 6-8 weeks and show skeletal and cardiac myopathy, sarcopenia, osteopenia, decreased bone formation, neuropathy, abnormal neuromuscular junctions, decreased skeletal muscle growth and decreased muscle satellite cell proliferation. Within 2-3 weeks they show a reduction in their growth rate and by week 4 their growth ceases with their mean body weight being half of that of the wild-type or the heterozygous littermates. Simultaneous knockout of Lmna and Lap2 results in partial rescue of the phenotype, with a 30% increase in survival rate and a 25-50% increase in body weight.6 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi201K → L: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. 1 Publication1
Mutagenesisi203E → G or K: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003988371 – 662Prelamin-A/CAdd BLAST662
ChainiPRO_00000638111 – 647Lamin-A/CAdd BLAST647
PropeptideiPRO_0000398838648 – 662Removed in Lamin-A/C formAdd BLAST15
PropeptideiPRO_0000403443663 – 665Removed in Prelamin-A/C form and in Lamin-A/C form3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei3PhosphothreonineBy similarity1
Modified residuei12PhosphoserineCombined sources1
Modified residuei18PhosphoserineBy similarity1
Modified residuei19PhosphothreonineCombined sources1
Modified residuei22PhosphoserineCombined sources1
Modified residuei32N6-acetyllysine; alternateCombined sources1
Modified residuei32N6-succinyllysine; alternateCombined sources1
Modified residuei51PhosphoserineBy similarity1
Modified residuei66PhosphoserineBy similarity1
Modified residuei71PhosphoserineBy similarity1
Cross-linki97Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei107PhosphoserineBy similarity1
Modified residuei108N6-acetyllysineBy similarity1
Modified residuei123N6-acetyllysineCombined sources1
Modified residuei135N6-acetyllysineCombined sources1
Modified residuei155N6-acetyllysineCombined sources1
Modified residuei171N6-acetyllysine; alternateCombined sources1
Modified residuei171N6-succinyllysine; alternateCombined sources1
Modified residuei201N6-acetyllysine; alternateCombined sources1
Cross-linki201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei212PhosphoserineBy similarity1
Cross-linki233Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei260N6-acetyllysine; alternateCombined sources1
Cross-linki260Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei270N6-acetyllysine; alternateCombined sources1
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei277PhosphoserineBy similarity1
Modified residuei301PhosphoserineCombined sources1
Modified residuei307PhosphoserineBy similarity1
Modified residuei311N6-acetyllysine; alternateCombined sources1
Cross-linki311Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei390PhosphoserineCombined sources1
Modified residuei392Phosphoserine; by CDK1Combined sources1 Publication1
Modified residuei395PhosphoserineBy similarity1
Modified residuei398PhosphoserineBy similarity1
Modified residuei403PhosphoserineBy similarity1
Modified residuei404PhosphoserineBy similarity1
Modified residuei407Phosphoserine1 Publication1
Modified residuei409Phosphoserine1 Publication1
Modified residuei414PhosphoserineBy similarity1
Cross-linki417Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei429PhosphoserineBy similarity1
Modified residuei431PhosphoserineBy similarity1
Modified residuei450N6-acetyllysineCombined sources1
Modified residuei457N6-acetyllysineCombined sources1
Modified residuei458PhosphoserineCombined sources1
Modified residuei463PhosphoserineBy similarity1
Modified residuei496PhosphothreonineBy similarity1
Modified residuei500PhosphoserineBy similarity1
Modified residuei505PhosphothreonineBy similarity1
Modified residuei510PhosphothreonineBy similarity1
Modified residuei533PhosphoserineBy similarity1
Modified residuei546PhosphoserineCombined sources1
Modified residuei548PhosphothreonineCombined sources1
Modified residuei570PhosphoserineCombined sources1
Modified residuei573PhosphoserineCombined sources1
Cross-linki599Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki599Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei613PhosphoserineBy similarity1
Modified residuei614PhosphoserineBy similarity1
Modified residuei617PhosphoserineCombined sources1
Modified residuei620PhosphoserineCombined sources1
Modified residuei629PhosphoserineCombined sources1
Modified residuei633PhosphoserineCombined sources1
Modified residuei637PhosphoserineCombined sources1
Modified residuei653PhosphoserineCombined sources1
Modified residuei662Cysteine methyl esterBy similarity1
Lipidationi662S-farnesyl cysteineBy similarity1
Isoform C2 (identifier: P48678-3)
Modified residuei460PhosphoserineCombined sources1
Isoform C (identifier: P48678-2)
Modified residuei572PhosphoserineCombined sources1

Post-translational modificationi

Proteolytic cleavage of the C-terminal of 18 residues of prelamin-A/C results in the production of lamin-A/C. The prelamin-A/C maturation pathway includes farnesylation of CAAX motif, ZMPSTE24/FACE1 mediated cleavage of the last three amino acids, methylation of the C-terminal cysteine and endoproteolytic removal of the last 15 C-terminal amino acids. Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage (By similarity).By similarity
Sumoylation is necessary for the localization to the nuclear envelope.By similarity
Farnesylation of prelamin-A/C facilitates nuclear envelope targeting.By similarity
Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.
Isoform C is phosphorylated on Ser-392, Ser-407 and Ser-409 at interphase.1 Publication
The N-terminus is blocked.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei647 – 648Cleavage; by endoproteaseBy similarity2

Keywords - PTMi

Acetylation, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

EPDiP48678.
MaxQBiP48678.
PaxDbiP48678.
PeptideAtlasiP48678.
PRIDEiP48678.
TopDownProteomicsiP48678-2. [P48678-2]

2D gel databases

REPRODUCTION-2DPAGEIPI00400300.
IPI00620256.

PTM databases

iPTMnetiP48678.
PhosphoSitePlusiP48678.
SwissPalmiP48678.

Expressioni

Tissue specificityi

Expressed in liver and in bone marrow (at protein level). Isoform C2 is specifically expressed in germ cells.2 Publications

Gene expression databases

BgeeiENSMUSG00000028063.
CleanExiMM_LMNA.
ExpressionAtlasiP48678. baseline and differential.
GenevisibleiP48678. MM.

Interactioni

Subunit structurei

Homodimer of lamin A and lamin C. Interacts with lamin-associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin. Proteolytically processed isoform A interacts with NARF (By similarity). Interacts with SREBF1, SREBF2, SUN1, SUN2 and TMEM43. Prelamin-A/C interacts with EMD. Interacts with DMPK; may regulate nuclear envelope stability (By similarity). Interacts with MLIP; may regulate MLIP localization to the nucleus envelope. Interacts with SUV39H1; the interaction increases stability of SUV39H1.By similarity8 Publications

Protein-protein interaction databases

BioGridi201176. 68 interactors.
DIPiDIP-31384N.
IntActiP48678. 17 interactors.
MINTiMINT-1868521.
STRINGi10090.ENSMUSP00000029699.

Structurei

Secondary structure

1665
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi417 – 420Combined sources4
Beta strandi433 – 436Combined sources4
Beta strandi438 – 445Combined sources8
Beta strandi449 – 456Combined sources8
Beta strandi458 – 460Combined sources3
Beta strandi468 – 473Combined sources6
Beta strandi479 – 482Combined sources4
Beta strandi494 – 503Combined sources10
Turni508 – 510Combined sources3
Beta strandi511 – 514Combined sources4
Beta strandi516 – 518Combined sources3
Beta strandi523 – 531Combined sources9
Beta strandi533 – 535Combined sources3
Beta strandi537 – 544Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UFGNMR-A408-545[»]
ProteinModelPortaliP48678.
SMRiP48678.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48678.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini432 – 544LTDAdd BLAST113

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 130Interaction with MLIPBy similarityAdd BLAST130
Regioni1 – 33HeadAdd BLAST33
Regioni34 – 383RodAdd BLAST350
Regioni34 – 70Coil 1AAdd BLAST37
Regioni71 – 80Linker 110
Regioni81 – 218Coil 1BAdd BLAST138
Regioni219 – 242Linker 2Add BLAST24
Regioni243 – 383Coil 2Add BLAST141
Regioni384 – 665TailAdd BLAST282

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi417 – 422Nuclear localization signalSequence analysis6

Sequence similaritiesi

Belongs to the intermediate filament family.Curated
Contains 1 LTD domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00830000128282.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP48678.
KOiK12641.
OMAiSHVSRHR.
OrthoDBiEOG091G063B.
PhylomeDBiP48678.
TreeFamiTF101181.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Isoform A and isoform C are present in equal amounts in the lamina of mammals.
Isoform A (identifier: P48678-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR
60 70 80 90 100
SLETENAGLR LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA
110 120 130 140 150
RLQLELSKVR EEFKELKARN TKKEGDLLAA QARLKDLEAL LNSKEAALST
160 170 180 190 200
ALSEKRTLEG ELHDLRGQVA KLEAALGEAK KQLQDEMLRR VDAENRLQTL
210 220 230 240 250
KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR LADALQELRA
260 270 280 290 300
QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID
310 320 330 340 350
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA
360 370 380 390 400
RMQQQLDEYQ ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG
410 420 430 440 450
RASSHSSQSQ GGGSVTKKRK LESSESRSSF SQHARTSGRV AVEEVDEEGK
460 470 480 490 500
FVRLRNKSNE DQSMGNWQIR RQNGDDPLMT YRFPPKFTLK AGQVVTIWAS
510 520 530 540 550
GAGATHSPPT DLVWKAQNTW GCGSSLRTAL INSTGEEVAM RKLVRSLTMV
560 570 580 590 600
EDNEDDDEDG EELLHHHRGS HCSGSGDPAE YNLRSRTVLC GTCGQPADKA
610 620 630 640 650
AGGAGAQVGG SISSGSSASS VTVTRSFRSV GGSGGGSFGD NLVTRSYLLG
660
NSSPRSQSSQ NCSIM
Length:665
Mass (Da):74,238
Last modified:January 24, 2006 - v2
Checksum:i5434F574803FCB15
GO
Isoform C (identifier: P48678-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     569-574: GSHCSG → VSGSRR
     575-665: Missing.

Show »
Length:574
Mass (Da):65,446
Checksum:iA736DF1CCEDB65BE
GO
Isoform C2 (identifier: P48678-3) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: Missing.
     113-118: FKELKA → MGNAEG
     569-574: GSHCSG → VSGSRR
     575-665: Missing.

Show »
Length:462
Mass (Da):52,652
Checksum:i4A12573CECAA93AA
GO

Sequence cautioni

The sequence BAE31539 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4P → S in BAE31384 (PubMed:16141072).Curated1
Sequence conflicti4P → S in BAE29519 (PubMed:16141072).Curated1
Sequence conflicti118 – 119AR → VC in CAA32372 (PubMed:2719959).Curated2
Sequence conflicti118A → D in BAE39876 (PubMed:16141072).Curated1
Sequence conflicti340E → G in BAE29614 (PubMed:16141072).Curated1
Sequence conflicti401R → P in CAA32372 (PubMed:2719959).Curated1
Sequence conflicti439 – 440RV → WL in CAA32372 (PubMed:2719959).Curated2
Sequence conflicti450K → E in BAE31384 (PubMed:16141072).Curated1
Sequence conflicti453R → L in BAE36246 (PubMed:16141072).Curated1
Sequence conflicti612I → V in BAB23415 (PubMed:16141072).Curated1
Sequence conflicti617S → Y in BAB23415 (PubMed:16141072).Curated1
Sequence conflicti623V → A in BAA02476 (PubMed:7916626).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0024711 – 112Missing in isoform C2. 1 PublicationAdd BLAST112
Alternative sequenceiVSP_002472113 – 118FKELKA → MGNAEG in isoform C2. 1 Publication6
Alternative sequenceiVSP_017064569 – 574GSHCSG → VSGSRR in isoform C and isoform C2. 4 Publications6
Alternative sequenceiVSP_017065575 – 665Missing in isoform C and isoform C2. 4 PublicationsAdd BLAST91

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49733 Genomic DNA. Translation: BAA08569.1.
D49733 Genomic DNA. Translation: BAA08570.1.
D49733 Genomic DNA. Translation: BAA08571.1.
X14170 mRNA. Translation: CAA32372.1.
D14850 mRNA. Translation: BAA03578.1.
DQ832702 mRNA. Translation: ABI16251.1.
DQ832703 mRNA. Translation: ABI16252.1.
AK004619 mRNA. Translation: BAB23415.1.
AK147150 mRNA. Translation: BAE27717.1.
AK149998 mRNA. Translation: BAE29226.1.
AK150391 mRNA. Translation: BAE29519.1.
AK150501 mRNA. Translation: BAE29614.1.
AK150624 mRNA. Translation: BAE29714.1.
AK152539 mRNA. Translation: BAE31294.1.
AK152646 mRNA. Translation: BAE31384.1.
AK152846 mRNA. Translation: BAE31539.1. Different initiation.
AK161221 mRNA. Translation: BAE36246.1.
AK167858 mRNA. Translation: BAE39876.1.
CH466547 Genomic DNA. Translation: EDL15275.1.
BC015302 mRNA. Translation: AAH15302.1.
BC094020 mRNA. Translation: AAH94020.1.
D13181 mRNA. Translation: BAA02476.1.
CCDSiCCDS38482.1. [P48678-1]
CCDS38483.1. [P48678-3]
CCDS50951.1. [P48678-2]
PIRiI53414.
S04333.
S18324.
S28182.
RefSeqiNP_001002011.2. NM_001002011.3. [P48678-1]
NP_001104572.1. NM_001111102.2. [P48678-2]
NP_062263.1. NM_019390.3. [P48678-3]
XP_006501136.1. XM_006501073.1. [P48678-1]
UniGeneiMm.243014.
Mm.471227.

Genome annotation databases

EnsembliENSMUST00000029699; ENSMUSP00000029699; ENSMUSG00000028063. [P48678-1]
ENSMUST00000036252; ENSMUSP00000040265; ENSMUSG00000028063. [P48678-3]
ENSMUST00000120377; ENSMUSP00000113093; ENSMUSG00000028063. [P48678-2]
GeneIDi16905.
KEGGimmu:16905.
UCSCiuc008pvj.3. mouse. [P48678-1]
uc008pvk.3. mouse. [P48678-3]
uc008pvl.3. mouse. [P48678-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49733 Genomic DNA. Translation: BAA08569.1.
D49733 Genomic DNA. Translation: BAA08570.1.
D49733 Genomic DNA. Translation: BAA08571.1.
X14170 mRNA. Translation: CAA32372.1.
D14850 mRNA. Translation: BAA03578.1.
DQ832702 mRNA. Translation: ABI16251.1.
DQ832703 mRNA. Translation: ABI16252.1.
AK004619 mRNA. Translation: BAB23415.1.
AK147150 mRNA. Translation: BAE27717.1.
AK149998 mRNA. Translation: BAE29226.1.
AK150391 mRNA. Translation: BAE29519.1.
AK150501 mRNA. Translation: BAE29614.1.
AK150624 mRNA. Translation: BAE29714.1.
AK152539 mRNA. Translation: BAE31294.1.
AK152646 mRNA. Translation: BAE31384.1.
AK152846 mRNA. Translation: BAE31539.1. Different initiation.
AK161221 mRNA. Translation: BAE36246.1.
AK167858 mRNA. Translation: BAE39876.1.
CH466547 Genomic DNA. Translation: EDL15275.1.
BC015302 mRNA. Translation: AAH15302.1.
BC094020 mRNA. Translation: AAH94020.1.
D13181 mRNA. Translation: BAA02476.1.
CCDSiCCDS38482.1. [P48678-1]
CCDS38483.1. [P48678-3]
CCDS50951.1. [P48678-2]
PIRiI53414.
S04333.
S18324.
S28182.
RefSeqiNP_001002011.2. NM_001002011.3. [P48678-1]
NP_001104572.1. NM_001111102.2. [P48678-2]
NP_062263.1. NM_019390.3. [P48678-3]
XP_006501136.1. XM_006501073.1. [P48678-1]
UniGeneiMm.243014.
Mm.471227.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UFGNMR-A408-545[»]
ProteinModelPortaliP48678.
SMRiP48678.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201176. 68 interactors.
DIPiDIP-31384N.
IntActiP48678. 17 interactors.
MINTiMINT-1868521.
STRINGi10090.ENSMUSP00000029699.

PTM databases

iPTMnetiP48678.
PhosphoSitePlusiP48678.
SwissPalmiP48678.

2D gel databases

REPRODUCTION-2DPAGEIPI00400300.
IPI00620256.

Proteomic databases

EPDiP48678.
MaxQBiP48678.
PaxDbiP48678.
PeptideAtlasiP48678.
PRIDEiP48678.
TopDownProteomicsiP48678-2. [P48678-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029699; ENSMUSP00000029699; ENSMUSG00000028063. [P48678-1]
ENSMUST00000036252; ENSMUSP00000040265; ENSMUSG00000028063. [P48678-3]
ENSMUST00000120377; ENSMUSP00000113093; ENSMUSG00000028063. [P48678-2]
GeneIDi16905.
KEGGimmu:16905.
UCSCiuc008pvj.3. mouse. [P48678-1]
uc008pvk.3. mouse. [P48678-3]
uc008pvl.3. mouse. [P48678-2]

Organism-specific databases

CTDi4000.
MGIiMGI:96794. Lmna.

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00830000128282.
HOGENOMiHOG000007711.
HOVERGENiHBG013015.
InParanoidiP48678.
KOiK12641.
OMAiSHVSRHR.
OrthoDBiEOG091G063B.
PhylomeDBiP48678.
TreeFamiTF101181.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2993913. Clearance of Nuclear Envelope Membranes from Chromatin.
R-MMU-2995383. Initiation of Nuclear Envelope Reformation.
R-MMU-352238. Breakdown of the nuclear lamina.
R-MMU-4419969. Depolymerisation of the Nuclear Lamina.

Miscellaneous databases

ChiTaRSiLmna. mouse.
EvolutionaryTraceiP48678.
PROiP48678.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028063.
CleanExiMM_LMNA.
ExpressionAtlasiP48678. baseline and differential.
GenevisibleiP48678. MM.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLMNA_MOUSE
AccessioniPrimary (citable) accession number: P48678
Secondary accession number(s): B3RH23
, B3RH24, P11516, P97859, Q3TIH0, Q3TTS8, Q3U733, Q3U7I5, Q3UCA0, Q3UCJ8, Q3UCU3, Q91WF2, Q9DC21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 24, 2006
Last modified: November 30, 2016
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.