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Protein

Lamin-B receptor

Gene

Lbr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Anchors the lamina and the heterochromatin to the inner nuclear membrane.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-191273. Cholesterol biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B receptor
Alternative name(s):
Integral nuclear envelope inner membrane protein
Gene namesi
Name:Lbr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2138281. Lbr.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 221NuclearSequence analysisAdd BLAST221
Transmembranei222 – 242HelicalSequence analysisAdd BLAST21
Transmembranei269 – 289HelicalSequence analysisAdd BLAST21
Transmembranei310 – 330HelicalSequence analysisAdd BLAST21
Transmembranei337 – 357HelicalSequence analysisAdd BLAST21
Transmembranei427 – 447HelicalSequence analysisAdd BLAST21
Transmembranei458 – 478HelicalSequence analysisAdd BLAST21
Transmembranei492 – 512HelicalSequence analysisAdd BLAST21
Transmembranei572 – 592HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • integral component of membrane Source: MGI
  • integral component of nuclear inner membrane Source: GO_Central
  • membrane Source: MGI
  • nuclear envelope Source: MGI
  • nuclear inner membrane Source: MGI
  • nuclear lamina Source: MGI
  • nuclear membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002279091 – 626Lamin-B receptorAdd BLAST626

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei55N6-acetyllysineBy similarity1
Modified residuei59PhosphoserineBy similarity1
Modified residuei67PhosphoserineCombined sources1
Modified residuei71PhosphoserineCombined sources1
Modified residuei86Phosphoserine; by CDK1By similarity1
Modified residuei90PhosphoserineBy similarity1
Glycosylationi98O-linked (GlcNAc)By similarity1
Modified residuei101PhosphoserineBy similarity1
Modified residuei103PhosphoserineCombined sources1
Modified residuei128PhosphothreonineCombined sources1
Modified residuei138PhosphoserineBy similarity1
Modified residuei211PhosphothreonineBy similarity1
Modified residuei605N6-acetyllysineBy similarity1
Modified residuei612N6-acetyllysineBy similarity1

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ3U9G9.
MaxQBiQ3U9G9.
PaxDbiQ3U9G9.
PeptideAtlasiQ3U9G9.
PRIDEiQ3U9G9.

PTM databases

iPTMnetiQ3U9G9.
PhosphoSitePlusiQ3U9G9.
SwissPalmiQ3U9G9.

Expressioni

Gene expression databases

BgeeiENSMUSG00000004880.
CleanExiMM_LBR.
ExpressionAtlasiQ3U9G9. baseline and differential.
GenevisibleiQ3U9G9. MM.

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi221046. 7 interactors.
IntActiQ3U9G9. 2 interactors.
MINTiMINT-4112231.
STRINGi10090.ENSMUSP00000005003.

Structurei

3D structure databases

ProteinModelPortaliQ3U9G9.
SMRiQ3U9G9.
ModBaseiSearch...
MobiDBiSearch...

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
Contains 1 Tudor domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1435. Eukaryota.
ENOG410XP67. LUCA.
GeneTreeiENSGT00390000000417.
HOVERGENiHBG007825.
InParanoidiQ3U9G9.
KOiK19532.
OMAiAWEKYCQ.
OrthoDBiEOG091G0F22.
PhylomeDBiQ3U9G9.
TreeFamiTF101179.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR019023. Lamin-B_rcpt_of_tudor.
IPR018083. Sterol_reductase_CS.
IPR002999. Tudor.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
PF09465. LBR_tudor. 1 hit.
[Graphical view]
SMARTiSM00333. TUDOR. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3U9G9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSRKFVEGE VVRGRWPGSS LYYEVEILSH DNKSQLYTVK YKDGTELELK
60 70 80 90 100
ESDIKPLKSF KQRKSGSISS SPSRRRGSRS RSRSRSRSRS PGRAPKGSRR
110 120 130 140 150
SVSASHEGDV KEKKEKEMRR EILQVKLTPL VLKPFGNSVS VYNGEPEHME
160 170 180 190 200
KNATPYKDKQ ERIILSTEDR YIVTQYSLRP RREEVKAKEI ESEEQNLVTK
210 220 230 240 250
GPAPLGTFQV TTPQRKDLEF GGVPGAVLIM LGLPACVLLL LLQCRQKDPG
260 270 280 290 300
LLHFPPPLPA LHELWEPRVC GVYLLWFFVQ ALFHLLPVGK VAEGTPLVDG
310 320 330 340 350
RRLQYRLNGL YAFILTSAAL GAAVFWGVEL CYLYTHFLQL ALAATGFSVL
360 370 380 390 400
LSAYLYVRSL RAPREELSPA SSGNAVYDFF IGRELNPRLG AFDLKFFCEL
410 420 430 440 450
RPGLIGWVVI NLVMLLMEMK IQERAAPSLA MILVNSFQLL YVVDALWNEE
460 470 480 490 500
ALLTSMDIMH DGFGFMLAFG DLVWVPFTYS LQAFYLVSHP HDLSWPLASV
510 520 530 540 550
IIALKLCGYV IFRCANSQKN AFRKNPTDPK LAHLKTIHTS TGKSLLVSGW
560 570 580 590 600
WGFVRHPNYL GDLIMALAWS LPCGFNHLLP YFYIIYFTAL LIHREARDEH
610 620
QCRRKYGLAW EKYCQRVPYR IFPYIY
Length:626
Mass (Da):71,440
Last modified:March 21, 2006 - v2
Checksum:i559CAAFFF73836F4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti174T → A in AAH42522 (PubMed:15489334).Curated1
Sequence conflicti174T → A in AAH21516 (PubMed:15489334).Curated1
Sequence conflicti263E → G in BAE30698 (PubMed:16141072).Curated1
Sequence conflicti525N → S in BAE30698 (PubMed:16141072).Curated1
Sequence conflicti585I → T in AAH14835 (PubMed:15489334).Curated1
Sequence conflicti600H → N in BAE36563 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK030606 mRNA. Translation: BAC27042.1.
AK028426 mRNA. Translation: BAE20442.1.
AK033459 mRNA. Translation: BAE20487.1.
AK151798 mRNA. Translation: BAE30698.1.
AK161762 mRNA. Translation: BAE36563.1.
AK166850 mRNA. Translation: BAE39069.1.
AK167157 mRNA. Translation: BAE39298.1.
BC010261 mRNA. Translation: AAH10261.1.
BC014835 mRNA. Translation: AAH14835.1.
BC021516 mRNA. Translation: AAH21516.1.
BC029171 mRNA. Translation: AAH29171.1.
BC042522 mRNA. Translation: AAH42522.1.
AY148158 Genomic DNA. Translation: AAN76314.1.
AY148158 Genomic DNA. Translation: AAN76315.1.
CCDSiCCDS15584.1.
RefSeqiNP_598576.2. NM_133815.2.
XP_006497133.1. XM_006497070.3.
XP_006497134.1. XM_006497071.3.
XP_017168530.1. XM_017313041.1.
UniGeneiMm.4538.

Genome annotation databases

EnsembliENSMUST00000005003; ENSMUSP00000005003; ENSMUSG00000004880.
GeneIDi98386.
KEGGimmu:98386.
UCSCiuc007dxo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK030606 mRNA. Translation: BAC27042.1.
AK028426 mRNA. Translation: BAE20442.1.
AK033459 mRNA. Translation: BAE20487.1.
AK151798 mRNA. Translation: BAE30698.1.
AK161762 mRNA. Translation: BAE36563.1.
AK166850 mRNA. Translation: BAE39069.1.
AK167157 mRNA. Translation: BAE39298.1.
BC010261 mRNA. Translation: AAH10261.1.
BC014835 mRNA. Translation: AAH14835.1.
BC021516 mRNA. Translation: AAH21516.1.
BC029171 mRNA. Translation: AAH29171.1.
BC042522 mRNA. Translation: AAH42522.1.
AY148158 Genomic DNA. Translation: AAN76314.1.
AY148158 Genomic DNA. Translation: AAN76315.1.
CCDSiCCDS15584.1.
RefSeqiNP_598576.2. NM_133815.2.
XP_006497133.1. XM_006497070.3.
XP_006497134.1. XM_006497071.3.
XP_017168530.1. XM_017313041.1.
UniGeneiMm.4538.

3D structure databases

ProteinModelPortaliQ3U9G9.
SMRiQ3U9G9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221046. 7 interactors.
IntActiQ3U9G9. 2 interactors.
MINTiMINT-4112231.
STRINGi10090.ENSMUSP00000005003.

PTM databases

iPTMnetiQ3U9G9.
PhosphoSitePlusiQ3U9G9.
SwissPalmiQ3U9G9.

Proteomic databases

EPDiQ3U9G9.
MaxQBiQ3U9G9.
PaxDbiQ3U9G9.
PeptideAtlasiQ3U9G9.
PRIDEiQ3U9G9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005003; ENSMUSP00000005003; ENSMUSG00000004880.
GeneIDi98386.
KEGGimmu:98386.
UCSCiuc007dxo.2. mouse.

Organism-specific databases

CTDi3930.
MGIiMGI:2138281. Lbr.

Phylogenomic databases

eggNOGiKOG1435. Eukaryota.
ENOG410XP67. LUCA.
GeneTreeiENSGT00390000000417.
HOVERGENiHBG007825.
InParanoidiQ3U9G9.
KOiK19532.
OMAiAWEKYCQ.
OrthoDBiEOG091G0F22.
PhylomeDBiQ3U9G9.
TreeFamiTF101179.

Enzyme and pathway databases

ReactomeiR-MMU-191273. Cholesterol biosynthesis.

Miscellaneous databases

PROiQ3U9G9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000004880.
CleanExiMM_LBR.
ExpressionAtlasiQ3U9G9. baseline and differential.
GenevisibleiQ3U9G9. MM.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR019023. Lamin-B_rcpt_of_tudor.
IPR018083. Sterol_reductase_CS.
IPR002999. Tudor.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
PF09465. LBR_tudor. 1 hit.
[Graphical view]
SMARTiSM00333. TUDOR. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLBR_MOUSE
AccessioniPrimary (citable) accession number: Q3U9G9
Secondary accession number(s): Q3TSW2
, Q811V8, Q811V9, Q8BST3, Q8K2Y8, Q8VDM0, Q91YS5, Q91Z27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: November 2, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.