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Protein

Lamin-B receptor

Gene

LBR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • chromo shadow domain binding Source: BHF-UCL
  • delta14-sterol reductase activity Source: Reactome
  • DNA binding Source: ProtInc
  • lamin binding Source: ProtInc
  • oxidoreductase activity, acting on the CH-CH group of donors Source: GO_Central
  • RNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Receptor

Enzyme and pathway databases

BioCyciMetaCyc:HS07110-MONOMER
BRENDAi1.3.1.70 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
SIGNORiQ14739

Chemistry databases

SwissLipidsiSLP:000001239

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B receptor
Alternative name(s):
Integral nuclear envelope inner membrane protein
LMN2R
Gene namesi
Name:LBR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000143815.14
HGNCiHGNC:6518 LBR
MIMi600024 gene
neXtProtiNX_Q14739

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
Topological domaini1 – 211NuclearSequence analysisAdd BLAST211
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

Pathology & Biotechi

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. Some individuals occasionally have skeletal anomalies, developmental delay, and seizures.
See also OMIM:169400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3930
MalaCardsiLBR
MIMi169400 phenotype
215140 phenotype
613471 phenotype
OpenTargetsiENSG00000143815
Orphaneti1426 Greenberg dysplasia
779 Reynolds syndrome
PharmGKBiPA30304

Polymorphism and mutation databases

BioMutaiLBR
DMDMi20141468

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002075101 – 615Lamin-B receptorAdd BLAST615

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

EPDiQ14739
MaxQBiQ14739
PaxDbiQ14739
PeptideAtlasiQ14739
PRIDEiQ14739
TopDownProteomicsiQ14739

PTM databases

iPTMnetiQ14739
PhosphoSitePlusiQ14739
SwissPalmiQ14739

Expressioni

Gene expression databases

BgeeiENSG00000143815
CleanExiHS_LBR
ExpressionAtlasiQ14739 baseline and differential
GenevisibleiQ14739 HS

Organism-specific databases

HPAiHPA049840
HPA062236

Interactioni

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

Binary interactionsi

Show more details

GO - Molecular functioni

  • chromo shadow domain binding Source: BHF-UCL
  • lamin binding Source: ProtInc

Protein-protein interaction databases

BioGridi110122, 56 interactors
DIPiDIP-5987N
IntActiQ14739, 29 interactors
MINTiQ14739
STRINGi9606.ENSP00000272163

Structurei

Secondary structure

1615
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 15Combined sources5
Turni17 – 19Combined sources3
Beta strandi22 – 31Combined sources10
Turni32 – 35Combined sources4
Beta strandi36 – 40Combined sources5
Beta strandi46 – 50Combined sources5
Turni51 – 53Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ14739

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 62TudorAdd BLAST62

Domaini

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

Sequence similaritiesi

Belongs to the ERG4/ERG24 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1435 Eukaryota
ENOG410XP67 LUCA
GeneTreeiENSGT00390000000417
HOGENOMiHOG000193296
HOVERGENiHBG007825
InParanoidiQ14739
KOiK19532
OMAiMPSRKFA
OrthoDBiEOG091G0F22
PhylomeDBiQ14739
TreeFamiTF101179

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

Sequencei

Sequence statusi: Complete.

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
Checksum:i5A7388776F43C66D
GO

Sequence cautioni

The sequence BAD92751 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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_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_017842569P → R in PHA. 1 PublicationCorresponds to variant dbSNP:rs137852606EnsemblClinVar.1

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiLBR_HUMAN
AccessioniPrimary (citable) accession number: Q14739
Secondary accession number(s): B2R5P3
, Q14740, Q53GU7, Q59FE6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 31, 2002
Last modified: May 23, 2018
This is version 180 of the entry and version 2 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health