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Protein

Lamin-B receptor

Gene

LBR

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Anchors the lamina and the heterochromatin to the inner nuclear membrane. Can interact with chromodomain proteins.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B receptor
Gene namesi
Name:LBR
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 205NuclearSequence analysisAdd BLAST205
Transmembranei206 – 226HelicalSequence analysisAdd BLAST21
Transmembranei250 – 270HelicalSequence analysisAdd BLAST21
Transmembranei288 – 309HelicalSequence analysisAdd BLAST22
Transmembranei317 – 338HelicalSequence analysisAdd BLAST22
Transmembranei378 – 399HelicalSequence analysisAdd BLAST22
Transmembranei403 – 425HelicalSequence analysisAdd BLAST23
Transmembranei466 – 486HelicalSequence analysisAdd BLAST21
Transmembranei554 – 574HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002075111 – 637Lamin-B receptorAdd BLAST637

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei95Phosphoserine; by PKASequence analysis1
Modified residuei96Phosphoserine; by PKASequence analysis1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP23913.
PRIDEiP23913.

PTM databases

iPTMnetiP23913.

Interactioni

Subunit structurei

Interacts directly with CBX5. 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

Protein-protein interaction databases

IntActiP23913. 1 interactor.
STRINGi9031.ENSGALP00000037953.

Structurei

Secondary structure

1637
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Beta strandi11 – 15Combined sources5
Beta strandi22 – 31Combined sources10
Turni32 – 35Combined sources4
Beta strandi36 – 41Combined sources6
Beta strandi46 – 50Combined sources5
Helixi51 – 53Combined sources3
Beta strandi57 – 59Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L8DNMR-A1-62[»]
ProteinModelPortaliP23913.
SMRiP23913.
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 H3.1 Publication

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.
HOGENOMiHOG000193296.
HOVERGENiHBG007825.
InParanoidiP23913.
KOiK19532.
PhylomeDBiP23913.

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.

P23913-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNRKYADGE VVMGRWPGSV LYYEVQVTSY DDASHLYTVK YKDGTELALK
60 70 80 90 100
ESDIRLQSSF KQRKSQSSSS SPSRRSRSRS RSRSPGRPAK GRRRSSSHSR
110 120 130 140 150
EHKEDKKKII QETSLAPPKP SENNTRRYNG EPDSTERNDT SSKLLEQQKL
160 170 180 190 200
KPDVEMERVL DQYSLRSRRE EKKKEEIYAE KKIFEAIKTP EKPSSKTKEL
210 220 230 240 250
EFGGRFGTFM LMFFLPATVL YLVLMCKQDD PSLMNFPPLP ALESLWETKV
260 270 280 290 300
FGVFLLWFFF QALFYLLPIG KVVEGLPLSN PRKLQYRING FYAFLLTAAA
310 320 330 340 350
IGTLLYFQFE LHYLYDHFVQ FAVSAAAFSM ALSIYLYIRS LKAPEEDLAP
360 370 380 390 400
GGNSGYLVYD FFTGHELNPR IGSFDLKYFC ELRPGLIGWV VINLAMLLAE
410 420 430 440 450
MKIHNQSMPS LSMILVNSFQ LLYVVDALWN EEAVLTTMDI THDGFGFMLA
460 470 480 490 500
FGDLVWVPFV YSLQAFYLVG HPIAISWPVA AAITILNCIG YYIFRSANSQ
510 520 530 540 550
KNNFRRNPAD PKLSYLKVIP TATGKGLLVT GWWGFVRHPN YLGDIIMALA
560 570 580 590 600
WSLPCGFNHI LPYFYVIYFI CLLVHREARD EHHCKKKYGL AWERYCQRVP
610 620 630
YTHISLHLLE HSTYLICKLK YTSHLCTWSV CYLGFKH
Length:637
Mass (Da):73,498
Last modified:March 1, 1992 - v1
Checksum:i69D299002DB8ECE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00822 mRNA. Translation: CAA68758.1.
PIRiA36427.
RefSeqiNP_990673.1. NM_205342.1.
UniGeneiGga.13515.
Gga.48272.

Genome annotation databases

GeneIDi396285.
KEGGigga:396285.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00822 mRNA. Translation: CAA68758.1.
PIRiA36427.
RefSeqiNP_990673.1. NM_205342.1.
UniGeneiGga.13515.
Gga.48272.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L8DNMR-A1-62[»]
ProteinModelPortaliP23913.
SMRiP23913.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP23913. 1 interactor.
STRINGi9031.ENSGALP00000037953.

PTM databases

iPTMnetiP23913.

Proteomic databases

PaxDbiP23913.
PRIDEiP23913.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396285.
KEGGigga:396285.

Organism-specific databases

CTDi3930.

Phylogenomic databases

eggNOGiKOG1435. Eukaryota.
ENOG410XP67. LUCA.
HOGENOMiHOG000193296.
HOVERGENiHBG007825.
InParanoidiP23913.
KOiK19532.
PhylomeDBiP23913.

Miscellaneous databases

PROiP23913.

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_CHICK
AccessioniPrimary (citable) accession number: P23913
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: November 2, 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.