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Entry version 191 (16 Oct 2019)
Sequence version 2 (24 Jan 2006)
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Protein

Prelamin-A/C

Gene

Lmna

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Required for cardiac homeostasis (PubMed:26436652). Isoform C2 may have a role in determining the organization of nuclear and chromosomal structures during spermatogenesis.7 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

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei266Heptad change of phase1
Sitei325StutterBy similarity1
Sitei330Heptad change of phase1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-2980766 Nuclear Envelope Breakdown
R-MMU-2995383 Initiation of Nuclear Envelope Reformation
R-MMU-352238 Breakdown of the nuclear lamina
R-MMU-4419969 Depolymerisation of the Nuclear Lamina

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Prelamin-A/C
Cleaved into the following chain:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Lmna
Synonyms:Lmn1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:96794 Lmna

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

Intermediate filament, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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. They develop ventricular dilation and cardiac dysfunction. 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. Double knockouts for MLIP and LMNA die sooner than single LMNA knockout. They develop much more severe ventricular dilation and cardiac dysfunction (PubMed:26436652).7 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003988371 – 662Prelamin-A/CAdd BLAST662
ChainiPRO_00000638111 – 647Lamin-A/CAdd BLAST647
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>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
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
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
Cross-linki171Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei201N6-acetyllysine; alternateCombined sources1
Cross-linki201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei212PhosphoserineBy similarity1
Cross-linki219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
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-linki366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By 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-acetyllysine; alternateCombined sources1
Cross-linki450Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei457N6-acetyllysineCombined sources1
Modified residuei458PhosphoserineCombined sources1
Modified residuei463PhosphoserineBy similarity1
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
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); alternateBy similarity
Cross-linki599Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy 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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi662S-farnesyl cysteineBy similarity1
Isoform C (identifier: P48678-2)
Modified residuei392PhosphoserineCombined sources1 Publication1
Modified residuei407PhosphoserineCombined sources1 Publication1
Modified residuei409PhosphoserineCombined sources1 Publication1
Modified residuei572PhosphoserineCombined sources1 Publication1
Isoform C2 (identifier: P48678-3)
Modified residuei460PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

The CPTAC Assay portal

More...
CPTACi
non-CPTAC-3719
non-CPTAC-3925

Encyclopedia of Proteome Dynamics

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EPDi
P48678

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P48678

MaxQB - The MaxQuant DataBase

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MaxQBi
P48678

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P48678

PeptideAtlas

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PeptideAtlasi
P48678

PRoteomics IDEntifications database

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PRIDEi
P48678

Consortium for Top Down Proteomics

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TopDownProteomicsi
P48678-2 [P48678-2]

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00400300
IPI00620256

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P48678

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P48678

SwissPalm database of S-palmitoylation events

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SwissPalmi
P48678

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in liver and in bone marrow (at protein level). Isoform C2 is specifically expressed in germ cells. Expressed in cardiomyocytes (PubMed:26436652).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000028063 Expressed in 291 organ(s), highest expression level in ascending aorta

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P48678 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P48678 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

Interacts with TMEM201. Prelamin-A/C interacts with EMD.

Interacts with DMPK; may regulate nuclear envelope stability (By similarity).

Interacts with MLIP (PubMed:26436652, PubMed:21498514).

Interacts with SUV39H1; the interaction increases stability of SUV39H1.

Interacts with ITSN1 isoform 2 (By similarity).

By similarity10 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
201176, 70 interactors

Database of interacting proteins

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DIPi
DIP-31384N

Protein interaction database and analysis system

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IntActi
P48678, 25 interactors

Molecular INTeraction database

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MINTi
P48678

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000029699

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1665
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P48678

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P48678

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini31 – 387IF rodPROSITE-ProRule annotationAdd BLAST357
Domaini428 – 545LTDPROSITE-ProRule annotationAdd BLAST118

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 130Interaction with MLIPBy similarityAdd BLAST130
Regioni1 – 33HeadAdd BLAST33
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
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi417 – 422Nuclear localization signalSequence analysis6

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0977 Eukaryota
ENOG410Y2H6 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157244

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000007711

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P48678

KEGG Orthology (KO)

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KOi
K12641

Identification of Orthologs from Complete Genome Data

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OMAi
ERMMSEF

Database of Orthologous Groups

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OrthoDBi
701388at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P48678

TreeFam database of animal gene trees

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TreeFami
TF101181

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.5.1160, 1 hit
2.60.40.1260, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR042180 IF_rod_dom_coil1B
IPR001322 Lamin_tail_dom
IPR036415 Lamin_tail_dom_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF00038 Filament, 1 hit
PF00932 LTD, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01391 Filament, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF74853 SSF74853, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00226 IF_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit
PS51841 LTD, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Isoform A and isoform C are present in equal amounts in the lamina of mammals.

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform A (identifier: P48678-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3YUF7D3YUF7_MOUSE
Prelamin-A/C
Lmna
117Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAE31539 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS38482.1 [P48678-1]
CCDS38483.1 [P48678-3]
CCDS50951.1 [P48678-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
I53414
S04333
S18324
S28182

NCBI Reference Sequences

More...
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]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000029699; ENSMUSP00000029699; ENSMUSG00000028063 [P48678-1]
ENSMUST00000036252; ENSMUSP00000040265; ENSMUSG00000028063 [P48678-3]
ENSMUST00000120377; ENSMUSP00000113093; ENSMUSG00000028063 [P48678-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
16905

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:16905

UCSC genome browser

More...
UCSCi
uc008pvj.3 mouse [P48678-1]
uc008pvk.3 mouse [P48678-3]
uc008pvl.3 mouse [P48678-2]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UFGNMR-A408-545[»]
SMRiP48678
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi201176, 70 interactors
DIPiDIP-31384N
IntActiP48678, 25 interactors
MINTiP48678
STRINGi10090.ENSMUSP00000029699

PTM databases

iPTMnetiP48678
PhosphoSitePlusiP48678
SwissPalmiP48678

2D gel databases

REPRODUCTION-2DPAGEiIPI00400300
IPI00620256

Proteomic databases

CPTACinon-CPTAC-3719
non-CPTAC-3925
EPDiP48678
jPOSTiP48678
MaxQBiP48678
PaxDbiP48678
PeptideAtlasiP48678
PRIDEiP48678
TopDownProteomicsiP48678-2 [P48678-2]

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

Comparative Toxicogenomics Database

More...
CTDi
4000
MGIiMGI:96794 Lmna

Phylogenomic databases

eggNOGiKOG0977 Eukaryota
ENOG410Y2H6 LUCA
GeneTreeiENSGT00940000157244
HOGENOMiHOG000007711
InParanoidiP48678
KOiK12641
OMAiERMMSEF
OrthoDBi701388at2759
PhylomeDBiP48678
TreeFamiTF101181

Enzyme and pathway databases

ReactomeiR-MMU-2980766 Nuclear Envelope Breakdown
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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Lmna mouse
EvolutionaryTraceiP48678

Protein Ontology

More...
PROi
PR:P48678

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028063 Expressed in 291 organ(s), highest expression level in ascending aorta
ExpressionAtlasiP48678 baseline and differential
GenevisibleiP48678 MM

Family and domain databases

Gene3Di1.20.5.1160, 1 hit
2.60.40.1260, 1 hit
InterProiView protein in InterPro
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR042180 IF_rod_dom_coil1B
IPR001322 Lamin_tail_dom
IPR036415 Lamin_tail_dom_sf
PfamiView protein in Pfam
PF00038 Filament, 1 hit
PF00932 LTD, 1 hit
SMARTiView protein in SMART
SM01391 Filament, 1 hit
SUPFAMiSSF74853 SSF74853, 1 hit
PROSITEiView protein in PROSITE
PS00226 IF_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit
PS51841 LTD, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLMNA_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P48678
Secondary accession number(s): B3RH23
, B3RH24, P11516, P97859, Q3TIH0, Q3TTS8, Q3U733, Q3U7I5, Q3UCA0, Q3UCJ8, Q3UCU3, Q91WF2, Q9DC21
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 24, 2006
Last modified: October 16, 2019
This is version 191 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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