Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P48678

- LMNA_MOUSE

UniProt

P48678 - LMNA_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Prelamin-A/C

Gene

Lmna

Organism
Mus musculus (Mouse)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei266 – 2661Heptad change of phase
Sitei325 – 3251StutterBy similarity
Sitei330 – 3301Heptad change of phase
Sitei647 – 6482Cleavage; by endoproteaseBy similarity

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. cellular response to hypoxia Source: BHF-UCL
  2. establishment of cell polarity Source: BHF-UCL
  3. establishment or maintenance of microtubule cytoskeleton polarity Source: BHF-UCL
  4. muscle organ development Source: BHF-UCL
  5. negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  6. negative regulation of release of cytochrome c from mitochondria Source: MGI
  7. nuclear envelope organization Source: MGI
  8. nucleus organization Source: MGI
  9. positive regulation of cell aging Source: UniProtKB
  10. protein localization to nucleus Source: UniProtKB
  11. regulation of cell migration Source: BHF-UCL
  12. regulation of protein localization to nucleus Source: MGI
  13. sterol regulatory element binding protein import into nucleus Source: MGI
  14. ventricular cardiac muscle cell development Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_106572. XBP1(S) activates chaperone genes.
REACT_198626. Meiotic synapsis.
REACT_208718. Depolymerisation of the Nuclear Lamina.
REACT_209025. Breakdown of the nuclear lamina.
REACT_210180. Initiation of Nuclear Envelope Reformation.
REACT_221677. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_75800. Meiotic Synapsis.

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
ProteomesiUP000000589: 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

  1. lamin filament Source: MGI
  2. nuclear envelope Source: UniProtKB
  3. nucleus Source: BHF-UCL
  4. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi201 – 2011K → L: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. 1 Publication
Mutagenesisi203 – 2031E → G or K: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 662662Prelamin-A/CPRO_0000398837Add
BLAST
Chaini1 – 647647Lamin-A/CPRO_0000063811Add
BLAST
Propeptidei648 – 66215Removed in Lamin-A/C formPRO_0000398838Add
BLAST
Propeptidei663 – 6653Removed in Prelamin-A/C form and in Lamin-A/C formPRO_0000403443

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei3 – 31PhosphothreonineBy similarity
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei18 – 181PhosphoserineBy similarity
Modified residuei19 – 191Phosphothreonine1 Publication
Modified residuei22 – 221Phosphoserine2 Publications
Modified residuei32 – 321N6-acetyllysine; alternate1 Publication
Modified residuei32 – 321N6-succinyllysine; alternate1 Publication
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei123 – 1231N6-acetyllysine1 Publication
Modified residuei135 – 1351N6-acetyllysine1 Publication
Modified residuei155 – 1551N6-acetyllysine1 Publication
Modified residuei171 – 1711N6-acetyllysine; alternate1 Publication
Modified residuei171 – 1711N6-succinyllysine; alternate1 Publication
Modified residuei201 – 2011N6-acetyllysine; alternate1 Publication
Cross-linki201 – 201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Modified residuei212 – 2121PhosphoserineBy similarity
Modified residuei260 – 2601N6-acetyllysine1 Publication
Modified residuei270 – 2701N6-acetyllysine1 Publication
Modified residuei277 – 2771PhosphoserineBy similarity
Modified residuei301 – 3011PhosphoserineBy similarity
Modified residuei311 – 3111N6-acetyllysine1 Publication
Modified residuei390 – 3901Phosphoserine1 Publication
Modified residuei392 – 3921Phosphoserine; by CDK12 Publications
Modified residuei395 – 3951PhosphoserineBy similarity
Modified residuei404 – 4041PhosphoserineBy similarity
Modified residuei407 – 4071Phosphoserine1 Publication
Modified residuei409 – 4091Phosphoserine1 Publication
Modified residuei414 – 4141PhosphoserineBy similarity
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei450 – 4501N6-acetyllysine1 Publication
Modified residuei457 – 4571N6-acetyllysine1 Publication
Modified residuei458 – 4581PhosphoserineBy similarity
Modified residuei463 – 4631PhosphoserineBy similarity
Modified residuei496 – 4961PhosphothreonineBy similarity
Modified residuei500 – 5001PhosphoserineBy similarity
Modified residuei505 – 5051PhosphothreonineBy similarity
Modified residuei510 – 5101PhosphothreonineBy similarity
Modified residuei546 – 5461Phosphoserine1 Publication
Modified residuei629 – 6291PhosphoserineBy similarity
Modified residuei633 – 6331PhosphoserineBy similarity
Modified residuei637 – 6371PhosphoserineBy similarity
Modified residuei653 – 6531Phosphoserine1 Publication
Modified residuei662 – 6621Cysteine methyl esterBy similarity
Lipidationi662 – 6621S-farnesyl cysteineBy similarity

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.2 Publications
The N-terminus is blocked.

Keywords - PTMi

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

Proteomic databases

MaxQBiP48678.
PaxDbiP48678.
PRIDEiP48678.

2D gel databases

REPRODUCTION-2DPAGEIPI00400300.
IPI00620256.

PTM databases

PhosphoSiteiP48678.

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

BgeeiP48678.
CleanExiMM_LMNA.
ExpressionAtlasiP48678. baseline and differential.
GenevestigatoriP48678.

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. 60 interactions.
IntActiP48678. 8 interactions.
MINTiMINT-1868521.
STRINGi10090.ENSMUSP00000029699.

Structurei

Secondary structure

1
665
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi417 – 4204Combined sources
Beta strandi433 – 4364Combined sources
Beta strandi438 – 4458Combined sources
Beta strandi449 – 4568Combined sources
Beta strandi458 – 4603Combined sources
Beta strandi468 – 4736Combined sources
Beta strandi479 – 4824Combined sources
Beta strandi494 – 50310Combined sources
Turni508 – 5103Combined sources
Beta strandi511 – 5144Combined sources
Beta strandi516 – 5183Combined sources
Beta strandi523 – 5319Combined sources
Beta strandi533 – 5353Combined sources
Beta strandi537 – 5448Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UFGNMR-A408-545[»]
ProteinModelPortaliP48678.
SMRiP48678. Positions 313-386, 415-546.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48678.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini432 – 544113LTDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 130130Interaction with MLIPBy similarityAdd
BLAST
Regioni1 – 3333HeadAdd
BLAST
Regioni34 – 383350RodAdd
BLAST
Regioni34 – 7037Coil 1AAdd
BLAST
Regioni71 – 8010Linker 1
Regioni81 – 218138Coil 1BAdd
BLAST
Regioni219 – 24224Linker 2Add
BLAST
Regioni243 – 383141Coil 2Add
BLAST
Regioni384 – 665282TailAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi417 – 4226Nuclear localization signalSequence Analysis

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG325506.
GeneTreeiENSGT00760000118905.
HOVERGENiHBG013015.
InParanoidiP48678.
KOiK12641.
OMAiHCSGSGD.
OrthoDBiEOG7MD4PW.
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]
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. Align

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 BAE31539.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41P → S in BAE31384. (PubMed:16141072)Curated
Sequence conflicti4 – 41P → S in BAE29519. (PubMed:16141072)Curated
Sequence conflicti118 – 1192AR → VC in CAA32372. (PubMed:2719959)Curated
Sequence conflicti118 – 1181A → D in BAE39876. (PubMed:16141072)Curated
Sequence conflicti340 – 3401E → G in BAE29614. (PubMed:16141072)Curated
Sequence conflicti401 – 4011R → P in CAA32372. (PubMed:2719959)Curated
Sequence conflicti439 – 4402RV → WL in CAA32372. (PubMed:2719959)Curated
Sequence conflicti450 – 4501K → E in BAE31384. (PubMed:16141072)Curated
Sequence conflicti453 – 4531R → L in BAE36246. (PubMed:16141072)Curated
Sequence conflicti612 – 6121I → V in BAB23415. (PubMed:16141072)Curated
Sequence conflicti617 – 6171S → Y in BAB23415. (PubMed:16141072)Curated
Sequence conflicti623 – 6231V → A in BAA02476. (PubMed:7916626)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 112112Missing in isoform C2. 1 PublicationVSP_002471Add
BLAST
Alternative sequencei113 – 1186FKELKA → MGNAEG in isoform C2. 1 PublicationVSP_002472
Alternative sequencei569 – 5746GSHCSG → VSGSRR in isoform C and isoform C2. 4 PublicationsVSP_017064
Alternative sequencei575 – 66591Missing in isoform C and isoform C2. 4 PublicationsVSP_017065Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.2. mouse. [P48678-1]
uc008pvk.2. mouse. [P48678-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS38482.1. [P48678-1 ]
CCDS38483.1. [P48678-3 ]
CCDS50951.1. [P48678-2 ]
PIRi I53414.
S04333.
S18324.
S28182.
RefSeqi NP_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 ]
UniGenei Mm.243014.
Mm.471227.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UFG NMR - A 408-545 [» ]
ProteinModelPortali P48678.
SMRi P48678. Positions 313-386, 415-546.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201176. 60 interactions.
IntActi P48678. 8 interactions.
MINTi MINT-1868521.
STRINGi 10090.ENSMUSP00000029699.

PTM databases

PhosphoSitei P48678.

2D gel databases

REPRODUCTION-2DPAGE IPI00400300.
IPI00620256.

Proteomic databases

MaxQBi P48678.
PaxDbi P48678.
PRIDEi P48678.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029699 ; ENSMUSP00000029699 ; ENSMUSG00000028063 . [P48678-1 ]
ENSMUST00000036252 ; ENSMUSP00000040265 ; ENSMUSG00000028063 . [P48678-3 ]
ENSMUST00000120377 ; ENSMUSP00000113093 ; ENSMUSG00000028063 . [P48678-2 ]
GeneIDi 16905.
KEGGi mmu:16905.
UCSCi uc008pvj.2. mouse. [P48678-1 ]
uc008pvk.2. mouse. [P48678-3 ]

Organism-specific databases

CTDi 4000.
MGIi MGI:96794. Lmna.

Phylogenomic databases

eggNOGi NOG325506.
GeneTreei ENSGT00760000118905.
HOVERGENi HBG013015.
InParanoidi P48678.
KOi K12641.
OMAi HCSGSGD.
OrthoDBi EOG7MD4PW.
PhylomeDBi P48678.
TreeFami TF101181.

Enzyme and pathway databases

Reactomei REACT_106572. XBP1(S) activates chaperone genes.
REACT_198626. Meiotic synapsis.
REACT_208718. Depolymerisation of the Nuclear Lamina.
REACT_209025. Breakdown of the nuclear lamina.
REACT_210180. Initiation of Nuclear Envelope Reformation.
REACT_221677. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

EvolutionaryTracei P48678.
NextBioi 290934.
PROi P48678.
SOURCEi Search...

Gene expression databases

Bgeei P48678.
CleanExi MM_LMNA.
ExpressionAtlasi P48678. baseline and differential.
Genevestigatori P48678.

Family and domain databases

Gene3Di 2.60.40.1260. 1 hit.
InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR001322. Lamin_tail_dom.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
Pfami PF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view ]
SUPFAMi SSF74853. SSF74853. 1 hit.
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic structure of the mouse A-type lamin gene locus encoding somatic and germ cell-specific lamins."
    Nakajima N., Abe K.
    FEBS Lett. 365:108-114(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence of the full-length mouse lamin C cDNA and its deduced amino-acid sequence."
    Riedel W., Werner D.
    Biochim. Biophys. Acta 1008:119-122(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
  3. "Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice."
    Furukawa K., Inagaki H., Hotta Y.
    Exp. Cell Res. 212:426-430(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C2).
    Strain: ddY.
    Tissue: Testis.
  4. "Lamin A binds to Runx2."
    Fujita T.
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C).
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
    Strain: BALB/c and C57BL/6J.
    Tissue: Amnion, Bone marrow, Head and Lung.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney and Salivary gland.
  8. "Nucleotide sequence of a mouse lamin A cDNA and its deduced amino acid sequence."
    Nakajima N., Sado T.
    Biochim. Biophys. Acta 1171:311-314(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 235-665 (ISOFORM A).
  9. "Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina."
    Weber K., Plessmann U., Traub P.
    FEBS Lett. 257:411-414(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 521-574, C-TERMINAL PROCESSING OF ISOFORM A.
  10. "Identification of phosphorylation sites on murine nuclear lamin C by RP-HPLC and microsequencing."
    Eggert M., Radomski N., Tripier D., Traub P., Jost E.
    FEBS Lett. 292:205-209(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-392; SER-407 AND SER-409.
  11. "Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy."
    Sullivan T., Escalante-Alcalde D., Bhatt H., Anver M., Bhat N., Nagashima K., Stewart C.L., Burke B.
    J. Cell Biol. 147:913-920(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  12. "Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse."
    De Sandre-Giovannoli A., Chaouch M., Kozlov S., Vallat J.-M., Tazir M., Kassouri N., Szepetowski P., Hammadouche T., Vandenberghe A., Stewart C.L., Grid D., Levy N.
    Am. J. Hum. Genet. 70:726-736(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  13. "A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies."
    Lloyd D.J., Trembath R.C., Shackleton S.
    Hum. Mol. Genet. 11:769-777(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SREBF1 AND SREBF2.
  14. "Coupling of the nucleus and cytoplasm: role of the LINC complex."
    Crisp M., Liu Q., Roux K., Rattner J.B., Shanahan C., Burke B., Stahl P.D., Hodzic D.
    J. Cell Biol. 172:41-53(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUN1.
  15. "SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton."
    Haque F., Lloyd D.J., Smallwood D.T., Dent C.L., Shanahan C.M., Fry A.M., Trembath R.C., Shackleton S.
    Mol. Cell. Biol. 26:3738-3751(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUN1.
  16. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-22 AND SER-653, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies."
    Zhang Y.Q., Sarge K.D.
    J. Cell Biol. 182:35-39(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUMOYLATION AT LYS-201, MUTAGENESIS OF LYS-201 AND GLU-203.
  19. "LUMA interacts with emerin and influences its distribution at the inner nuclear membrane."
    Bengtsson L., Otto H.
    J. Cell Sci. 121:536-548(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM43.
  20. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Lamin A/C-mediated neuromuscular junction defects in Emery-Dreifuss muscular dystrophy."
    Mejat A., Decostre V., Li J., Renou L., Kesari A., Hantai D., Stewart C.L., Xiao X., Hoffman E., Bonne G., Misteli T.
    J. Cell Biol. 184:31-44(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  22. "Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins."
    Ostlund C., Folker E.S., Choi J.C., Gomes E.R., Gundersen G.G., Worman H.J.
    J. Cell Sci. 122:4099-4108(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUN1 AND SUN2.
  23. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390 AND SER-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  24. "Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes."
    Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M., Shackleton S.
    J. Biol. Chem. 285:3487-3498(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUN2.
  25. "Identification of a novel muscle enriched A-type Lamin interacting protein (MLIP)."
    Ahmady E., Deeke S.A., Rabaa S., Kouri L., Kenney L., Stewart A.F., Burgon P.G.
    J. Biol. Chem. 286:19702-19713(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MLIP.
  26. "Lamin A/C deficiency is associated with fat infiltration of muscle and bone."
    Tong J., Li W., Vidal C., Yeo L.S., Fatkin D., Duque G.
    Mech. Ageing Dev. 132:552-559(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  27. "Decreased bone formation and osteopenia in lamin a/c-deficient mice."
    Li W., Yeo L.S., Vidal C., McCorquodale T., Herrmann M., Fatkin D., Duque G.
    PLoS ONE 6:E19313-E19313(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  28. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-123; LYS-135; LYS-155; LYS-171; LYS-201; LYS-260; LYS-270; LYS-311; LYS-450 AND LYS-457, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  29. "Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model."
    Liu B., Wang Z., Zhang L., Ghosh S., Zheng H., Zhou Z.
    Nat. Commun. 4:1868-1868(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUV39H1.
  30. "Defective skeletal muscle growth in lamin A/C-deficient mice is rescued by loss of Lap2alpha."
    Cohen T.V., Gnocchi V.F., Cohen J.E., Phadke A., Liu H., Ellis J.A., Foisner R., Stewart C.L., Zammit P.S., Partridge T.A.
    Hum. Mol. Genet. 22:2852-2869(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  31. "Solution structure of immunoglobulin-like domain of mouse nuclear lamin."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 406-546.

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: October 29, 2014
This is version 143 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

External Data

Dasty 3