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Entry version 190 (05 Jun 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Lamin-B1

Gene

Lmnb1

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.

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.

<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-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)
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:
Lamin-B1
<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:Lmnb1
<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 18

Organism-specific databases

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

More...
MGIi
MGI:96795 Lmnb1

<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, Membrane, Nucleus

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00000638172 – 585Lamin-B1Add BLAST584
<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_0000403467586 – 588Removed in mature formBy similarity3

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 residuei2N-acetylalanineBy similarity1
Modified residuei3PhosphothreonineBy similarity1
Modified residuei5PhosphothreonineBy similarity1
Modified residuei15Omega-N-methylarginineBy similarity1
Modified residuei17PhosphoserineCombined sources1
Modified residuei21PhosphothreonineCombined sources1
Modified residuei24PhosphoserineCombined sources1
Modified residuei26PhosphothreonineBy similarity1
Modified residuei29PhosphoserineBy similarity1
<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-linki103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei112N6-acetyllysineCombined sources1
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei127PhosphoserineBy similarity1
Cross-linki146Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei158N6-acetyllysine; alternateBy similarity1
Cross-linki158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei159PhosphoserineBy similarity1
Cross-linki182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei201PhosphoserineBy similarity1
Modified residuei233PhosphoserineBy similarity1
Cross-linki242Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei272N6-acetyllysine; alternateCombined sources1
Cross-linki272Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei279PhosphoserineBy similarity1
Modified residuei303PhosphoserineBy similarity1
Cross-linki313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi318InterchainBy similarity
Modified residuei331N6-acetyllysine; alternateCombined sources1
Cross-linki331Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei376PhosphoserineBy similarity1
Modified residuei414Omega-N-methylarginineBy similarity1
Modified residuei484N6-acetyllysineBy similarity1
Cross-linki533Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei535PhosphoserineBy similarity1
Cross-linki548Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei585Cysteine 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>Lipidationi585S-farnesyl cysteineBy similarity1

<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

B-type lamins undergo a series of modifications, such as farnesylation and phosphorylation. Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P14733

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P14733

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P14733

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

More...
PaxDbi
P14733

PeptideAtlas

More...
PeptideAtlasi
P14733

PRoteomics IDEntifications database

More...
PRIDEi
P14733

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00230394

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P14733

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P14733

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

More...
PhosphoSitePlusi
P14733

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P14733

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000024590 Expressed in 252 organ(s), highest expression level in cumulus cell

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P14733 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. Interacts with lamin-associated polypeptides IA, IB and 2. Interacts with SPAG4 and SEPT12 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
201177, 13 interactors

Protein interaction database and analysis system

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IntActi
P14733, 17 interactors

Molecular INTeraction database

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MINTi
P14733

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000025486

<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

3D structure databases

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

More...
SMRi
P14733

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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>Domaini33 – 389IF rodPROSITE-ProRule annotationAdd BLAST357
Domaini431 – 547LTDPROSITE-ProRule annotationAdd BLAST117

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>Regioni2 – 35HeadAdd BLAST34
Regioni36 – 70Coil 1AAdd BLAST35
Regioni71 – 82Linker 1Add BLAST12
Regioni83 – 216Coil 1BAdd BLAST134
Regioni217 – 244Linker 2Add BLAST28
Regioni245 – 387Coil 2Add BLAST143
Regioni388 – 588TailAdd BLAST201

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>Motifi416 – 421Nuclear localization signalSequence analysis6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi553 – 561Glu-rich (highly acidic; could be involved in chromatin binding)9

<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

More...
eggNOGi
KOG0977 Eukaryota
ENOG410Y2H6 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157199

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007711

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P14733

KEGG Orthology (KO)

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KOi
K07611

Identification of Orthologs from Complete Genome Data

More...
OMAi
ERAWLQI

Database of Orthologous Groups

More...
OrthoDBi
701388at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P14733

TreeFam database of animal gene trees

More...
TreeFami
TF101181

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.5.1160, 2 hits
2.60.40.1260, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

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

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01391 Filament, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF74853 SSF74853, 1 hit

PROSITE; a protein domain and family database

More...
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>Sequencei

<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.

P14733-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATATPVQQQ RAGSRASAPA TPLSPTRLSR LQEKEELREL NDRLAVYIDK
60 70 80 90 100
VRSLETENSA LQLQVTEREE VRGRELTGLK ALYETELADA RRALDDTARE
110 120 130 140 150
RAKLQIELGK FKAEHDQLLL NYAKKESDLS GAQIKLREYE AALNSKDAAL
160 170 180 190 200
ATALGDKKSL EGDLEDLKDQ IAQLEASLSA AKKQLADETL LKVDLENRCQ
210 220 230 240 250
SLTEDLEFRK NMYEEEINET RRKHETRLVE VDSGRQIEYE YKLAQALHEM
260 270 280 290 300
REQHDAQVRL YKEELEQTYH AKLENARLSS EMNTSTVNSA REELMESRMR
310 320 330 340 350
IESLSSQLSN LQKESRACLE RIQELEDMLA KERDNSRRML SDREREMAEI
360 370 380 390 400
RDQMQQQLSD YEQLLDVKLA LDMEISAYRK LLEGEEERLK LSPSPSSRVT
410 420 430 440 450
VSRASSSRSV RTTRGKRKRV DVEESEASSS VSISHSASAT GNVCIEEIDV
460 470 480 490 500
DGKFIRLKNT SEQDQPMGGW EMIRKIGDTS VSYKYTSRYV LKAGQTVTVW
510 520 530 540 550
AANAGVTASP PTDLIWKNQN SWGTGEDVKV ILKNSQGEEV AQRSTVFKTT
560 570 580
IPEEEEEEEE EPIGVAVEEE RFHQQGAPRA SNKSCAIM
Length:588
Mass (Da):66,786
Last modified:January 23, 2007 - v3
<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:i3602BCE63588A32D
GO

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 conflicti581S → W in CAA34677 (PubMed:3243285).Curated1
Sequence conflicti581S → W in AAC96023 (PubMed:3243285).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X16705 mRNA Translation: CAA34677.1
M35153 mRNA Translation: AAC96023.1 Sequence problems.
D50080 Genomic DNA Translation: BAA08784.1
BC052729 mRNA Translation: AAH52729.1
BC058392 mRNA Translation: AAH58392.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS29261.1

Protein sequence database of the Protein Information Resource

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PIRi
S07720

NCBI Reference Sequences

More...
RefSeqi
NP_034851.2, NM_010721.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000025486; ENSMUSP00000025486; ENSMUSG00000024590

Database of genes from NCBI RefSeq genomes

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GeneIDi
16906

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:16906

UCSC genome browser

More...
UCSCi
uc012bdd.2 mouse

<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
X16705 mRNA Translation: CAA34677.1
M35153 mRNA Translation: AAC96023.1 Sequence problems.
D50080 Genomic DNA Translation: BAA08784.1
BC052729 mRNA Translation: AAH52729.1
BC058392 mRNA Translation: AAH58392.1
CCDSiCCDS29261.1
PIRiS07720
RefSeqiNP_034851.2, NM_010721.2

3D structure databases

SMRiP14733
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201177, 13 interactors
IntActiP14733, 17 interactors
MINTiP14733
STRINGi10090.ENSMUSP00000025486

PTM databases

iPTMnetiP14733
PhosphoSitePlusiP14733
SwissPalmiP14733

2D gel databases

REPRODUCTION-2DPAGEiIPI00230394
SWISS-2DPAGEiP14733

Proteomic databases

EPDiP14733
jPOSTiP14733
MaxQBiP14733
PaxDbiP14733
PeptideAtlasiP14733
PRIDEiP14733

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025486; ENSMUSP00000025486; ENSMUSG00000024590
GeneIDi16906
KEGGimmu:16906
UCSCiuc012bdd.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4001
MGIiMGI:96795 Lmnb1

Phylogenomic databases

eggNOGiKOG0977 Eukaryota
ENOG410Y2H6 LUCA
GeneTreeiENSGT00940000157199
HOGENOMiHOG000007711
InParanoidiP14733
KOiK07611
OMAiERAWLQI
OrthoDBi701388at2759
PhylomeDBiP14733
TreeFamiTF101181

Enzyme and pathway databases

ReactomeiR-MMU-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)
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

Miscellaneous databases

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

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ChiTaRSi
Lmnb1 mouse

Protein Ontology

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PROi
PR:P14733

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000024590 Expressed in 252 organ(s), highest expression level in cumulus cell
GenevisibleiP14733 MM

Family and domain databases

Gene3Di1.20.5.1160, 2 hits
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

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ProtoNeti
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<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 nameiLMNB1_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: P14733
Secondary accession number(s): Q61791
<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: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 5, 2019
This is version 190 of the entry and version 3 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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