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Entry version 138 (08 May 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Lamin-B1

Gene

Lmnb1

Organism
Rattus norvegicus (Rat)
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.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.By similarity

<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-RNO-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)
R-RNO-2980766 Nuclear Envelope Breakdown
R-RNO-2995383 Initiation of Nuclear Envelope Reformation
R-RNO-352238 Breakdown of the nuclear lamina
R-RNO-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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
620522 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_00000638182 – 584Lamin-B1Add BLAST583
<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_0000403468585 – 587Removed 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 residuei14Omega-N-methylarginineBy similarity1
Modified residuei16PhosphoserineBy similarity1
Modified residuei20PhosphothreonineBy similarity1
Modified residuei23PhosphoserineBy similarity1
Modified residuei25PhosphothreonineBy similarity1
Modified residuei28PhosphoserineBy 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-linki102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei111N6-acetyllysineBy similarity1
Cross-linki123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei126PhosphoserineCombined sources1
Cross-linki145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei157N6-acetyllysine; alternateBy similarity1
Cross-linki157Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei158PhosphoserineCombined sources1
Cross-linki181Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei200PhosphoserineBy similarity1
Modified residuei232PhosphoserineBy similarity1
Cross-linki241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei271N6-acetyllysine; alternateBy similarity1
Cross-linki271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei278PhosphoserineBy similarity1
Modified residuei302PhosphoserineBy similarity1
Cross-linki312Glycyl 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 bondi317InterchainBy similarity
Modified residuei330N6-acetyllysine; alternateBy similarity1
Cross-linki330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei375PhosphoserineBy similarity1
Modified residuei413Omega-N-methylarginineBy similarity1
Modified residuei483N6-acetyllysineBy similarity1
Cross-linki532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei534PhosphoserineBy similarity1
Cross-linki547Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei576PhosphothreonineCombined sources1
Modified residuei584Cysteine 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>Lipidationi584S-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 (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P70615

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

More...
PaxDbi
P70615

PRoteomics IDEntifications database

More...
PRIDEi
P70615

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0004:P70615

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P70615

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P70615

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

More...
PhosphoSitePlusi
P70615

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
250568, 13 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000019351

<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
P70615

Database of comparative protein structure models

More...
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>Domaini32 – 388IF rodPROSITE-ProRule annotationAdd BLAST357
Domaini430 – 546LTDPROSITE-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 – 34HeadAdd BLAST33
Regioni35 – 69Coil 1AAdd BLAST35
Regioni70 – 81Linker 1Add BLAST12
Regioni82 – 215Coil 1BAdd BLAST134
Regioni216 – 243Linker 2Add BLAST28
Regioni244 – 386Coil 2Add BLAST143
Regioni387 – 587TailAdd 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>Motifi415 – 420Nuclear 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 biasi552 – 560Glu-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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007711

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P70615

KEGG Orthology (KO)

More...
KOi
K07611

Database of Orthologous Groups

More...
OrthoDBi
701388at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P70615

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
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
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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P70615-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATATPVQQR AGSRASAPAT PFSPTRLSRL QEKEELRELN DRLAVYIDKV
60 70 80 90 100
RSLETENSAL QLQVTEREEV RGRELTGLKA LYETELADAR RALDDTARER
110 120 130 140 150
AKLQIELGKF KAEHDQLLLN YAKKESDLSG AQIKLREYEA ALNSKDAALA
160 170 180 190 200
TALGDKKSLE GDLEDLKDQI AQLEASLSAA KKQLADETLL KVDLENRCQS
210 220 230 240 250
LTEDLEFRKN MYEEEINETR RKHETRLVEV DSGRQIEYEY KLAQALHEMR
260 270 280 290 300
EQHDAQVRLY KEELEQTYHA KLENARLSSE MNTSTVNSAR GGMMESRMRI
310 320 330 340 350
ESLSSQLSNL QKDSRACLER IQELEDMLAK ERDNSRRMLS DKEREMAEIR
360 370 380 390 400
DQMQQQLNDY EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSSRVTV
410 420 430 440 450
SRASSSRSVR TTRGKRKRVD VEESEASSSV SISHSASATG NVCIEEIDVD
460 470 480 490 500
GKFIRLKNTS EQDQPMGGWE MIRKIGDTSV SYKYTSRYVL KAGQTVTVWA
510 520 530 540 550
ANAGVTASPP TDLIWKNQNS WGTGEDVKVV LKNSQGEEVA QRSTVFKTTI
560 570 580
PEEEEEEEEE PIGVPLEEER FHQQGTPRAS NKSCAIM
Length:587
Mass (Da):66,606
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:i8187CA32728CC012
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
G3V7U4G3V7U4_RAT
Lamin-B1
Lmnb1 rCG_46767
587Annotation score:

Annotation score:2 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>

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
U72353 mRNA Translation: AAB09600.1

NCBI Reference Sequences

More...
RefSeqi
NP_446357.1, NM_053905.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
116685

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:116685

UCSC genome browser

More...
UCSCi
RGD:620522 rat

<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
U72353 mRNA Translation: AAB09600.1
RefSeqiNP_446357.1, NM_053905.1

3D structure databases

SMRiP70615
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250568, 13 interactors
STRINGi10116.ENSRNOP00000019351

PTM databases

CarbonylDBiP70615
iPTMnetiP70615
PhosphoSitePlusiP70615

2D gel databases

World-2DPAGEi0004:P70615

Proteomic databases

jPOSTiP70615
PaxDbiP70615
PRIDEiP70615

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi116685
KEGGirno:116685
UCSCiRGD:620522 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4001
RGDi620522 Lmnb1

Phylogenomic databases

eggNOGiKOG0977 Eukaryota
ENOG410Y2H6 LUCA
HOGENOMiHOG000007711
InParanoidiP70615
KOiK07611
OrthoDBi701388at2759
PhylomeDBiP70615

Enzyme and pathway databases

ReactomeiR-RNO-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)
R-RNO-2980766 Nuclear Envelope Breakdown
R-RNO-2995383 Initiation of Nuclear Envelope Reformation
R-RNO-352238 Breakdown of the nuclear lamina
R-RNO-4419969 Depolymerisation of the Nuclear Lamina

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P70615

Family and domain databases

Gene3Di2.60.40.1260, 1 hit
InterProiView protein in InterPro
IPR018039 IF_conserved
IPR039008 IF_rod_dom
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...

<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_RAT
<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: P70615
<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: December 13, 2001
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 138 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
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