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UniProtKB - Q14739 (LBR_HUMAN)

Protein

Lamin-B receptor

Gene

LBR

Organism
Homo sapiens (Human)
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

Anchors the lamina and the heterochromatin to the inner nuclear membrane.1 Publication

<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

  • chromo shadow domain binding Source: BHF-UCL
  • delta14-sterol reductase activity Source: Reactome
  • DNA binding Source: ProtInc
  • lamin binding Source: ProtInc
  • RNA binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cholesterol biosynthetic process Source: Reactome
  • sterol biosynthetic process Source: GO_Central
View the complete GO annotation on QuickGO ...

<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>Keywordsi

Molecular functionDNA-binding, Receptor

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS07110-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.3.1.70 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-191273 Cholesterol biosynthesis
R-HSA-9022692 Regulation of MECP2 expression and activity

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q14739

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001239

<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-B receptor
Alternative name(s):
Integral nuclear envelope inner membrane protein
LMN2R
<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:LBR
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000143815.14

Human Gene Nomenclature Database

More...HGNCi		HGNC:6518 LBR

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600024 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q14739

<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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 211NuclearSequence analysisAdd BLAST211
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei212 – 232HelicalSequence analysisAdd BLAST21
Transmembranei258 – 278HelicalSequence analysisAdd BLAST21
Transmembranei299 – 319HelicalSequence analysisAdd BLAST21
Transmembranei326 – 346HelicalSequence analysisAdd BLAST21
Transmembranei386 – 406HelicalSequence analysisAdd BLAST21
Transmembranei447 – 467HelicalSequence analysisAdd BLAST21
Transmembranei481 – 501HelicalSequence analysisAdd BLAST21
Transmembranei561 – 581HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Membrane, 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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Pelger-Huet anomaly (PHA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant inherited abnormality of granulocytes, characterized by abnormal ovoid shape, reduced nuclear segmentation and an apparently looser chromatin structure.
See also OMIM:169400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_017841119P → L in PHA. 1 PublicationCorresponds to variant dbSNP:rs137852605EnsemblClinVar.1
Natural variantiVAR_017842569P → R in PHA. 1 PublicationCorresponds to variant dbSNP:rs137852606EnsemblClinVar.1
Greenberg dysplasia (GRBGD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal recessive chondrodystrophy characterized by early in utero lethality. Affected fetuses typically present with fetal hydrops, short-limbed dwarfism, and a marked disorganization of chondro-osseous calcification, and ectopic ossification centers.
See also OMIM:215140
Reynolds syndrome (REYNS)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome specifically associating limited cutaneous systemic sclerosis and primary biliary cirrhosis. It is characterized by liver disease, telangiectasia, abrupt onset of digital paleness or cyanosis in response to cold exposure or stress (Raynaud phenomenon), and variable features of scleroderma. The liver disease is characterized by pruritis, jaundice, hepatomegaly, increased serum alkaline phosphatase and positive serum mitochondrial autoantibodies, all consistent with primary biliary cirrhosis.
See also OMIM:613471
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063811372R → C in REYNS. 1 PublicationCorresponds to variant dbSNP:rs200180113EnsemblClinVar.1
Pelger-Huet anomaly with mild skeletal anomalies (PHASK)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by abnormal nuclear shape and chromatin organization in blood granulocytes, short stature, and mild skeletal anomalies. Initial skeletal features may improve with age.
See also OMIM:618019
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08100576 – 615Missing in PHASK. 1 PublicationCorresponds to variant dbSNP:rs869312905Add BLAST540
Natural variantiVAR_081006547N → S in PHASK; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs374343844EnsemblClinVar.1
Natural variantiVAR_081007586R → H in PHASK; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs573510559EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNET

More...DisGeNETi		3930

MalaCards human disease database

More...MalaCardsi		LBR
MIMi169400 phenotype
215140 phenotype
613471 phenotype
618019 phenotype

Open Targets

More...OpenTargetsi		ENSG00000143815

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		1426 Greenberg dysplasia
448267 Regressive spondylometaphyseal dysplasia
779 Reynolds syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30304

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		LBR

Domain mapping of disease mutations (DMDM)

More...DMDMi		20141468

<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_00002075101 – 615Lamin-B receptorAdd BLAST615

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 residuei55N6-acetyllysineCombined sources1
Modified residuei58PhosphothreonineCombined sources1
Modified residuei59PhosphoserineCombined sources1
Modified residuei67PhosphoserineBy similarity1
Modified residuei71Phosphoserine; by CDK11 Publication1
Modified residuei86Phosphoserine; by CDK11 Publication1
Modified residuei97PhosphoserineCombined sources1
Modified residuei99PhosphoserineCombined sources1
Modified residuei118PhosphothreonineCombined sources1
Modified residuei128PhosphoserineCombined sources1
Modified residuei200PhosphothreonineCombined sources1
Modified residuei594N6-acetyllysineCombined sources1
Modified residuei601N6-acetyllysineCombined 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

Phosphorylated by CDK1 in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin. It is phosphorylated by different protein kinases in interphase when the membrane is associated with these structures. Phosphorylation of LBR and HP1 proteins may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle. Phosphorylated by SRPK1. In late anaphase LBR is dephosphorylated, probably by PP1 and/or PP2A, allowing reassociation with chromatin.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q14739

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q14739

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q14739

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

More...PaxDbi		Q14739

PeptideAtlas

More...PeptideAtlasi		Q14739

PRoteomics IDEntifications database

More...PRIDEi		Q14739

ProteomicsDB human proteome resource

More...ProteomicsDBi		60152

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q14739

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q14739

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

More...PhosphoSitePlusi		Q14739

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q14739

<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

More...Bgeei		ENSG00000143815 Expressed in 238 organ(s), highest expression level in bone marrow

CleanEx database of gene expression profiles

More...CleanExi		HS_LBR

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q14739 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q14739 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA049840
HPA062236

<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

Interacts directly with CBX5. Can interact with chromodomain proteins. Interacts directly with DNA. Interaction with DNA is sequence independent with higher affinity for supercoiled and relaxed circular DNA than linear DNA.3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110122, 62 interactors

Database of interacting proteins

More...DIPi		DIP-5987N

Protein interaction database and analysis system

More...IntActi		Q14739, 32 interactors

Molecular INTeraction database

More...MINTi		Q14739

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000272163

<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

1615
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
2DIGNMR-A1-55[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q14739

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

More...SMRi		Q14739

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q14739

<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>Domaini1 – 62TudorAdd BLAST62

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The Tudor domain may not recognize methylation marks, but rather bind unassembled free histone H3.By similarity

<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 ERG4/ERG24 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1435 Eukaryota
ENOG410XP67 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000000417

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000193296

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG007825

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q14739

KEGG Orthology (KO)

More...KOi		K19532

Identification of Orthologs from Complete Genome Data

More...OMAi		PCGFNHI

Database of Orthologous Groups

More...OrthoDBi		532774at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q14739

TreeFam database of animal gene trees

More...TreeFami		TF101179

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001171 Ergosterol_biosynth_ERG4_ERG24
IPR019023 Lamin-B_rcpt_of_tudor
IPR018083 Sterol_reductase_CS
IPR002999 Tudor

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01222 ERG4_ERG24, 1 hit
PF09465 LBR_tudor, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00333 TUDOR, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01017 STEROL_REDUCT_1, 1 hit
PS01018 STEROL_REDUCT_2, 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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q14739-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPSRKFADGE VVRGRWPGSS LYYEVEILSH DSTSQLYTVK YKDGTELELK 
        60         70         80         90        100
ENDIKPLTSF RQRKGGSTSS SPSRRRGSRS RSRSRSPGRP PKSARRSASA 
       110        120        130        140        150
SHQADIKEAR REVEVKLTPL ILKPFGNSIS RYNGEPEHIE RNDAPHKNTQ 
       160        170        180        190        200
EKFSLSQESS YIATQYSLRP RREEVKLKEI DSKEEKYVAK ELAVRTFEVT 
       210        220        230        240        250
PIRAKDLEFG GVPGVFLIMF GLPVFLFLLL LMCKQKDPSL LNFPPPLPAL 
       260        270        280        290        300
YELWETRVFG VYLLWFLIQV LFYLLPIGKV VEGTPLIDGR RLKYRLNGFY 
       310        320        330        340        350
AFILTSAVIG TSLFQGVEFH YVYSHFLQFA LAATVFCVVL SVYLYMRSLK 
       360        370        380        390        400
APRNDLSPAS SGNAVYDFFI GRELNPRIGT FDLKYFCELR PGLIGWVVIN 
       410        420        430        440        450
LVMLLAEMKI QDRAVPSLAM ILVNSFQLLY VVDALWNEEA LLTTMDIIHD 
       460        470        480        490        500
GFGFMLAFGD LVWVPFIYSF QAFYLVSHPN EVSWPMASLI IVLKLCGYVI 
       510        520        530        540        550
FRGANSQKNA FRKNPSDPKL AHLKTIHTST GKNLLVSGWW GFVRHPNYLG 
       560        570        580        590        600
DLIMALAWSL PCGFNHILPY FYIIYFTMLL VHREARDEYH CKKKYGVAWE 
       610 
KYCQRVPYRI FPYIY
Length:615
Mass (Da):70,703
Last modified:January 31, 2002 - 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:i5A7388776F43C66D
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JXK0C9JXK0_HUMAN
Lamin-B receptor
LBR
213Annotation 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>
C9JES9C9JES9_HUMAN
Lamin-B receptor
LBR
51Annotation 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 BAD92751 differs from that shown. Reason: Erroneous initiation.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 conflicti301A → P in AAA59494 (PubMed:8157662).Curated1
Sequence conflicti452F → L in BAD96554 (Ref. 5) Curated1
Sequence conflicti530T → S in AAA59494 (PubMed:8157662).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08100576 – 615Missing in PHASK. 1 PublicationCorresponds to variant dbSNP:rs869312905Add BLAST540
Natural variantiVAR_017841119P → L in PHA. 1 PublicationCorresponds to variant dbSNP:rs137852605EnsemblClinVar.1
Natural variantiVAR_024318154S → N5 PublicationsCorresponds to variant dbSNP:rs2230419EnsemblClinVar.1
Natural variantiVAR_052155169R → C. Corresponds to variant dbSNP:rs2230420Ensembl.1
Natural variantiVAR_020209311T → A. Corresponds to variant dbSNP:rs2275601Ensembl.1
Natural variantiVAR_063811372R → C in REYNS. 1 PublicationCorresponds to variant dbSNP:rs200180113EnsemblClinVar.1
Natural variantiVAR_081006547N → S in PHASK; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs374343844EnsemblClinVar.1
Natural variantiVAR_017842569P → R in PHA. 1 PublicationCorresponds to variant dbSNP:rs137852606EnsemblClinVar.1
Natural variantiVAR_081007586R → H in PHASK; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs573510559EnsemblClinVar.1

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
L25931 mRNA Translation: AAA59494.1
L25941
, L25932, L25933, L25934, L25935, L25936, L25937, L25938, L25939, L25940 Genomic DNA Translation: AAA59495.1
AB209514 mRNA Translation: BAD92751.1 Different initiation.
AK222834 mRNA Translation: BAD96554.1
AK312258 mRNA Translation: BAG35190.1
CH471098 Genomic DNA Translation: EAW69741.1
BC020079 mRNA Translation: AAH20079.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS1545.1

Protein sequence database of the Protein Information Resource

More...PIRi		A53616

NCBI Reference Sequences

More...RefSeqi		NP_002287.2, NM_002296.3
NP_919424.1, NM_194442.2
XP_011542487.1, XM_011544185.2

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.435166
Hs.735694

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000272163; ENSP00000272163; ENSG00000143815
ENST00000338179; ENSP00000339883; ENSG00000143815

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3930

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3930

UCSC genome browser

More...UCSCi		uc001hoy.4 human

Keywords - Coding sequence diversityi

Polymorphism

<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
L25931 mRNA Translation: AAA59494.1
L25941
, L25932, L25933, L25934, L25935, L25936, L25937, L25938, L25939, L25940 Genomic DNA Translation: AAA59495.1
AB209514 mRNA Translation: BAD92751.1 Different initiation.
AK222834 mRNA Translation: BAD96554.1
AK312258 mRNA Translation: BAG35190.1
CH471098 Genomic DNA Translation: EAW69741.1
BC020079 mRNA Translation: AAH20079.1
CCDSiCCDS1545.1
PIRiA53616
RefSeqiNP_002287.2, NM_002296.3
NP_919424.1, NM_194442.2
XP_011542487.1, XM_011544185.2
UniGeneiHs.435166
Hs.735694

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DIGNMR-A1-55[»]
ProteinModelPortaliQ14739
SMRiQ14739
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110122, 62 interactors
DIPiDIP-5987N
IntActiQ14739, 32 interactors
MINTiQ14739
STRINGi9606.ENSP00000272163

Chemistry databases

SwissLipidsiSLP:000001239

PTM databases

iPTMnetiQ14739
PhosphoSitePlusiQ14739
SwissPalmiQ14739

Polymorphism and mutation databases

BioMutaiLBR
DMDMi20141468

Proteomic databases

EPDiQ14739
jPOSTiQ14739
MaxQBiQ14739
PaxDbiQ14739
PeptideAtlasiQ14739
PRIDEiQ14739
ProteomicsDBi60152
TopDownProteomicsiQ14739

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		3930
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272163; ENSP00000272163; ENSG00000143815
ENST00000338179; ENSP00000339883; ENSG00000143815
GeneIDi3930
KEGGihsa:3930
UCSCiuc001hoy.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3930
DisGeNETi3930
EuPathDBiHostDB:ENSG00000143815.14

GeneCards: human genes, protein and diseases

More...GeneCardsi		LBR
HGNCiHGNC:6518 LBR
HPAiHPA049840
HPA062236
MalaCardsiLBR
MIMi169400 phenotype
215140 phenotype
600024 gene
613471 phenotype
618019 phenotype
neXtProtiNX_Q14739
OpenTargetsiENSG00000143815
Orphaneti1426 Greenberg dysplasia
448267 Regressive spondylometaphyseal dysplasia
779 Reynolds syndrome
PharmGKBiPA30304

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1435 Eukaryota
ENOG410XP67 LUCA
GeneTreeiENSGT00390000000417
HOGENOMiHOG000193296
HOVERGENiHBG007825
InParanoidiQ14739
KOiK19532
OMAiPCGFNHI
OrthoDBi532774at2759
PhylomeDBiQ14739
TreeFamiTF101179

Enzyme and pathway databases

BioCyciMetaCyc:HS07110-MONOMER
BRENDAi1.3.1.70 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
R-HSA-9022692 Regulation of MECP2 expression and activity
SIGNORiQ14739

Miscellaneous databases

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

More...ChiTaRSi		LBR human
EvolutionaryTraceiQ14739

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Lamin_B_receptor

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		3930

Protein Ontology

More...PROi		PR:Q14739

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000143815 Expressed in 238 organ(s), highest expression level in bone marrow
CleanExiHS_LBR
ExpressionAtlasiQ14739 baseline and differential
GenevisibleiQ14739 HS

Family and domain databases

InterProiView protein in InterPro
IPR001171 Ergosterol_biosynth_ERG4_ERG24
IPR019023 Lamin-B_rcpt_of_tudor
IPR018083 Sterol_reductase_CS
IPR002999 Tudor
PfamiView protein in Pfam
PF01222 ERG4_ERG24, 1 hit
PF09465 LBR_tudor, 1 hit
SMARTiView protein in SMART
SM00333 TUDOR, 1 hit
PROSITEiView protein in PROSITE
PS01017 STEROL_REDUCT_1, 1 hit
PS01018 STEROL_REDUCT_2, 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 nameiLBR_HUMAN
<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: Q14739
Secondary accession number(s): B2R5P3
, Q14740, Q53GU7, Q59FE6
<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: November 1, 1997
Last sequence update: January 31, 2002
Last modified: January 16, 2019
This is version 187 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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