MOUSE:LMNA

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Species (Taxon ID)	Mus musculus (Mouse). (taxon:10090)
Gene Name(s)	Lmna ( synonyms: Lmn1 )
Protein Name(s)	Prelamin-A/C Lamin-A/C
External Links
UniProt Identifier	LMNA_MOUSE
UniProt Accessions	P48678, P11516, P97859, Q3TIH0, Q3TTS8, Q3UCA0, Q3UCJ8, Q91WF2, Q9DC21,
EMBL	D49733, D49733, D49733, X14170, D14850, AK004619, AK147150, AK149998, AK150501, AK150624, AK152539, AK161221, AK167858, BC015302, BC094020, D13181,
PIR	I53414, S04333, S18324, S28182,
RefSeq	NP_001002011.2, NP_001104572.1, NP_062263.1,
PDB	1UFG,
IntAct	P48678,
Ensembl	ENSMUST00000029699, ENSMUST00000036252, ENSMUST00000120377,
Pfam	PF00038, PF00932,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0005638	lamin filament		IDA: Inferred from Direct Assay		C	Source: MGI
	GO:0005635	nuclear envelope		IDA: Inferred from Direct Assay		C	Source: UniProtKB
	GO:0005515	protein binding		IPI: Inferred from Physical Interaction		F	Source: MGI
	GO:0005198	structural molecule activity		IEA: Inferred from Electronic Annotation		F	Source: InterPro
	GO:0006998	nuclear envelope organization		IGI: Inferred from Genetic Interaction		P	Source: MGI
	GO:0090343	positive regulation of cell aging		ISS: Inferred from Sequence or Structural Similarity		P	Source: UniProtKB
	GO:0035105	sterol regulatory element binding protein n...		IMP: Inferred from Mutant Phenotype		P	Source: MGI
	GO:0055015	ventricular cardiac muscle cell development		IMP: Inferred from Mutant Phenotype		P	Source: MGI
	GO:0005783	endoplasmic reticulum	PMID 10021336	IDA: Inferred from Direct Assay		C	Immunohistochemical staining shows location of lamin alpha to follow distribution of ER - figure 6c	complete
	GO:0005198	structural molecule activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001664	F
	GO:0005515	protein binding	PMID:11739632^[1]	IPI: Inferred from Physical Interaction	UniProtKB:O08810	F
	GO:0005515	protein binding	PMID:11739632^[1]	IPI: Inferred from Physical Interaction	UniProtKB:Q62093	F
	GO:0005515	protein binding	PMID:16380439^[2]	IPI: Inferred from Physical Interaction	UniProtKB:Q8BJS4	F
	GO:0005515	protein binding	PMID:16380439^[2]	IPI: Inferred from Physical Interaction	UniProtKB:Q9D666	F
	GO:0005515	protein binding	PMID:21498514^[3]	IPI: Inferred from Physical Interaction	UniProtKB:Q5FW52	F
	GO:0005626	insoluble fraction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000026705	C
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C
	GO:0005634	nucleus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000357283	C
	GO:0005634	nucleus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000026705	C
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C
	GO:0005634	nucleus	PMID:11739632^[1]	IDA: Inferred from Direct Assay		C
	GO:0005635	nuclear envelope	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0178	C
	GO:0005635	nuclear envelope	PMID:18606848^[4]	IDA: Inferred from Direct Assay		C
	GO:0005635	nuclear envelope	Reactome:REACT_75839	TAS: Traceable Author Statement		C
	GO:0005638	lamin filament	PMID:8032679^[5]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000357283	C
	GO:0005882	intermediate filament	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0403	C
	GO:0006997	nucleus organization	PMID:14755333^[6]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2177930	P
	GO:0006998	nuclear envelope organization	PMID:15608054^[7]	IGI: Inferred from Genetic Interaction	MGI:MGI:1890508	P
	GO:0007283	spermatogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000026705	P
	GO:0007517	muscle organ development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000357283	P
	GO:0007517	muscle organ development	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P02545-1	P
	GO:0007517	muscle organ development	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P02545-2	P
	GO:0016363	nuclear matrix	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000026705	C
	GO:0030010	establishment of cell polarity	PMID:17631533^[8]	NAS: Non-traceable Author Statement		P
	GO:0030334	regulation of cell migration	PMID:17631533^[8]	IMP: Inferred from Mutant Phenotype		P
	GO:0030951	establishment or maintenance of microtubule cytoskeleton polarity	PMID:17631533^[8]	IMP: Inferred from Mutant Phenotype		P
	GO:0034504	protein localization to nucleus	PMID:21498514^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0035105	sterol regulatory element binding protein import into nucleus	PMID:14755333^[6]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2177930	P
	GO:0042981	regulation of apoptosis	PMID:21151901^[9]	IDA: Inferred from Direct Assay		P
	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000357283	C
	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P02545-1	C
	GO:0055015	ventricular cardiac muscle cell development	PMID:14755333^[6]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2177930	P
	GO:0071456	cellular response to hypoxia	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000357283	P
	GO:0071456	cellular response to hypoxia	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P02545	P
	GO:0090343	positive regulation of cell aging	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000357283	P
	GO:0090343	positive regulation of cell aging	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P02545	P
	GO:0090343	positive regulation of cell aging	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P02545	P
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Muralikrishna B et al. (2001) Distinct changes in intranuclear lamin A/C organization during myoblast differentiation. J Cell Sci 114: 4001-11 PubMed GONUTS page
↑ ^2.0 ^2.1 Crisp M et al. (2006) Coupling of the nucleus and cytoplasm: role of the LINC complex. J Cell Biol 172: 41-53 PubMed GONUTS page
↑ ^3.0 ^3.1 Ahmady E et al. (2011) Identification of a novel muscle A-type lamin-interacting protein (MLIP). J Biol Chem 286: 19702-13 PubMed GONUTS page
↑ Zhang YQ & Sarge KD (2008) Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies. J Cell Biol 182: 35-9 PubMed GONUTS page
↑ Furukawa K et al. (1994) cDNA cloning and functional characterization of a meiosis-specific protein (MNS1) with apparent nuclear association. Chromosome Res 2: 99-113 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Nikolova V et al. (2004) Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C-deficient mice. J Clin Invest 113: 357-69 PubMed GONUTS page
↑ Fong LG et al. (2004) Heterozygosity for Lmna deficiency eliminates the progeria-like phenotypes in Zmpste24-deficient mice. Proc Natl Acad Sci U S A 101: 18111-6 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Lee JS et al. (2007) Nuclear lamin A/C deficiency induces defects in cell mechanics, polarization, and migration. Biophys J 93: 2542-52 PubMed GONUTS page
↑ Lu D et al. (2010) LMNA E82K mutation activates FAS and mitochondrial pathways of apoptosis in heart tissue specific transgenic mice. PLoS One 5: e15167 PubMed GONUTS page

[PMID:11739632-0] 1.0 ^1.1 ^1.2 Muralikrishna B et al. (2001) Distinct changes in intranuclear lamin A/C organization during myoblast differentiation. J Cell Sci 114: 4001-11 PubMed GONUTS page

[PMID:16380439-1] 2.0 ^2.1 Crisp M et al. (2006) Coupling of the nucleus and cytoplasm: role of the LINC complex. J Cell Biol 172: 41-53 PubMed GONUTS page

[PMID:21498514-2] 3.0 ^3.1 Ahmady E et al. (2011) Identification of a novel muscle A-type lamin-interacting protein (MLIP). J Biol Chem 286: 19702-13 PubMed GONUTS page

[PMID:18606848-3] Zhang YQ & Sarge KD (2008) Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies. J Cell Biol 182: 35-9 PubMed GONUTS page

[PMID:8032679-4] Furukawa K et al. (1994) cDNA cloning and functional characterization of a meiosis-specific protein (MNS1) with apparent nuclear association. Chromosome Res 2: 99-113 PubMed GONUTS page

[PMID:14755333-5] 6.0 ^6.1 ^6.2 Nikolova V et al. (2004) Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C-deficient mice. J Clin Invest 113: 357-69 PubMed GONUTS page

[PMID:15608054-6] Fong LG et al. (2004) Heterozygosity for Lmna deficiency eliminates the progeria-like phenotypes in Zmpste24-deficient mice. Proc Natl Acad Sci U S A 101: 18111-6 PubMed GONUTS page

[PMID:17631533-7] 8.0 ^8.1 ^8.2 Lee JS et al. (2007) Nuclear lamin A/C deficiency induces defects in cell mechanics, polarization, and migration. Biophys J 93: 2542-52 PubMed GONUTS page

[PMID:21151901-8] Lu D et al. (2010) LMNA E82K mutation activates FAS and mitochondrial pathways of apoptosis in heart tissue specific transgenic mice. PLoS One 5: e15167 PubMed GONUTS page

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MOUSE:LMNA

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