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Protein

Lamin-B receptor

Gene

Lbr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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

  • mitotic nuclear division Source: RGD
  • sterol biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B receptor
Alternative name(s):
Integral nuclear envelope inner membrane protein
NBP60
Gene namesi
Name:Lbr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620813. Lbr.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 215215NuclearSequence analysisAdd
BLAST
Transmembranei216 – 23621HelicalSequence analysisAdd
BLAST
Transmembranei263 – 28321HelicalSequence analysisAdd
BLAST
Transmembranei304 – 32421HelicalSequence analysisAdd
BLAST
Transmembranei331 – 35121HelicalSequence analysisAdd
BLAST
Transmembranei452 – 47221HelicalSequence analysisAdd
BLAST
Transmembranei486 – 50621HelicalSequence analysisAdd
BLAST
Transmembranei525 – 54723HelicalSequence analysisAdd
BLAST
Transmembranei566 – 58621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: RGD
  • integral component of nuclear inner membrane Source: GO_Central
  • nuclear envelope Source: RGD
  • nuclear pore Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Lamin-B receptorPRO_0000227911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysineBy similarity
Modified residuei59 – 591PhosphoserineBy similarity
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei71 – 711Phosphoserine; by CDK1By similarity
Modified residuei86 – 861Phosphoserine; by CDK1By similarity
Modified residuei88 – 881PhosphoserineBy similarity
Glycosylationi96 – 961O-linked (GlcNAc)1 Publication
Modified residuei99 – 991PhosphoserineBy similarity
Modified residuei101 – 1011PhosphoserineBy similarity
Modified residuei123 – 1231PhosphothreonineBy similarity
Modified residuei133 – 1331PhosphoserineBy similarity
Modified residuei205 – 2051PhosphothreonineBy similarity
Modified residuei599 – 5991N6-acetyllysineBy similarity
Modified residuei606 – 6061N6-acetyllysineBy similarity

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

PRIDEiO08984.

PTM databases

iPTMnetiO08984.
PhosphoSiteiO08984.

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

  • chaperone binding Source: RGD

Protein-protein interaction databases

BioGridi250124. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliO08984.
SMRiO08984. Positions 1-55.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6262TudorAdd
BLAST

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

HOGENOMiHOG000193296.
HOVERGENiHBG007825.
InParanoidiO08984.
KOiK19532.
PhylomeDBiO08984.

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.

O08984-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGRKFADGE VVRGRWPGSS LYYEVEILSH DSTSQLYTVK YKDGTELELK
60 70 80 90 100
ESDIKPLKSF KQRKSGSTSS SPSRRRSSRS RSRSRSRSPG RAPKGSRRSV
110 120 130 140 150
SASYQADAKE KEMRREILQV KLTPLVLKPF ANSVSVYNGE PEHMEKSATP
160 170 180 190 200
PKNKQERVIL STEDSYIATQ YSLRPRREEV KPKHRVRGTN LVTRGPVPLG
210 220 230 240 250
TFQVTTPQRR DLEFGGVPGA LLIMLGLPAC VFLLLLQCAQ KDPGLLQFPP
260 270 280 290 300
PLPALRELWE ARVCGVYLLW FFLQALFSLL PVGKVVEGTP LVDGRRLKYR
310 320 330 340 350
LNGLYAFILT SAAVGTAVFW DIELYYLYTH FLQFALAAIV FSVVLSVYLY
360 370 380 390 400
ARSLKVPRDE LSPASSGNAV YDFFIGRELN PRIGAFDLKF FCELRPGLIG
410 420 430 440 450
WVVINLVMLL AEMKVQERSA PSLAMTLVNS FQLLYVVDAL WFEEALLTTM
460 470 480 490 500
DIIHDGFGFM LAFGDLVWVP FTYSLQAFYL VNHPQDLSWP LTSVIIALKL
510 520 530 540 550
CGYVIFRCAN SQKNAFRKNP TDPKLAHLKT IPTSTWKSLL VSGWWGFVRH
560 570 580 590 600
PNYLGDLIMA LAWSLPCGFN HILPYFYVIY FTALLIHREA RDEHQCRRKY
610 620
GLAWEKYCQR VPYRIFPYIY
Length:620
Mass (Da):70,724
Last modified:July 1, 1997 - v1
Checksum:i04BD9FDDCC61ED5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002466 mRNA. Translation: BAA20471.1.
PIRiJC5567.
RefSeqiNP_604448.1. NM_134453.1.
UniGeneiRn.6499.

Genome annotation databases

GeneIDi89789.
KEGGirno:89789.
UCSCiRGD:620813. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002466 mRNA. Translation: BAA20471.1.
PIRiJC5567.
RefSeqiNP_604448.1. NM_134453.1.
UniGeneiRn.6499.

3D structure databases

ProteinModelPortaliO08984.
SMRiO08984. Positions 1-55.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250124. 3 interactions.

PTM databases

iPTMnetiO08984.
PhosphoSiteiO08984.

Proteomic databases

PRIDEiO08984.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi89789.
KEGGirno:89789.
UCSCiRGD:620813. rat.

Organism-specific databases

CTDi3930.
RGDi620813. Lbr.

Phylogenomic databases

HOGENOMiHOG000193296.
HOVERGENiHBG007825.
InParanoidiO08984.
KOiK19532.
PhylomeDBiO08984.

Miscellaneous databases

PROiO08984.

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_RAT
AccessioniPrimary (citable) accession number: O08984
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 1, 1997
Last modified: July 6, 2016
This is version 104 of the entry and version 1 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. 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.