Lbr
entrez
98386
canonical
uniprot
Q3U9G9
canonical
ensembl
ENSMUSG00000004880
resolver
ensp
ENSMUSP00000005003
resolver
ensp
ENSMUSP00000228231
resolver
ensp
ENSMUSP00000228232
resolver
ensp
ENSMUSP00000330729
resolver
ensp
ENSMUSP00000330734
resolver
ensp
ENSMUSP00000330735
resolver
enst
ENSMUST00000005003
resolver
genesymbol
Lbr
resolver
uniprot
Q3TSW2
resolver
uniprot
Q811V8
resolver
uniprot
Q811V9
resolver
uniprot
Q8BST3
resolver
uniprot
Q8K2Y8
resolver
uniprot
Q8VDM0
resolver
uniprot
Q91YS5
resolver
uniprot
Q91Z27
resolver
uniprot_entry
LBR_MOUSE
resolver
uniprot_sec
Q3TSW2
resolver
uniprot_sec
Q811V8
resolver
uniprot_sec
Q811V9
resolver
uniprot_sec
Q8BST3
resolver
uniprot_sec
Q8K2Y8
resolver
uniprot_sec
Q8VDM0
resolver
uniprot_sec
Q91YS5
resolver
uniprot_sec
Q91Z27
resolver
amino_acid_sequence
MPSRKFVEGEVVRGRWPGSSLYYEVEILSHDNKSQLYTVKYKDGTELELKESDIKPLKSFKQRKSGSISSSPSRRRGSRSRSRSRSRSRSPGRAPKGSRRSVSASHEGDVKEKKEKEMRREILQVKLTPLVLKPFGNSVSVYNGEPEHMEKNATPYKDKQERIILSTEDRYIVTQYSLRPRREEVKAKEIESEEQNLVTKGPAPLGTFQVTTPQRKDLEFGGVPGAVLIMLGLPACVLLLLLQCRQKDPGLLHFPPPLPALHELWEPRVCGVYLLWFFVQALFHLLPVGKVAEGTPLVDGRRLQYRLNGLYAFILTSAALGAAVFWGVELCYLYTHFLQLALAATGFSVLLSAYLYVRSLRAPREELSPASSGNAVYDFFIGRELNPRLGAFDLKFFCELRPGLIGWVVINLVMLLMEMKIQERAAPSLAMILVNSFQLLYVVDALWNEEALLTSMDIMHDGFGFMLAFGDLVWVPFTYSLQAFYLVSHPHDLSWPLASVIIALKLCGYVIFRCANSQKNAFRKNPTDPKLAHLKTIHTSTGKSLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHLLPYFYIIYFTALLIHREARDEHQCRRKYGLAWEKYCQRVPYRIFPYIY
uniprot
proteins
ec_number
1.3.1.70
uniprot
proteins
function
FUNCTION: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:18785926). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (PubMed:22140257). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (PubMed:22140257). Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity). {ECO:0000250|UniProtKB:Q14739, ECO:0000269|PubMed:18785926, ECO:0000269|PubMed:22140257}.
uniprot
proteins
mass_dalton
71440
uniprot
proteins
pathway_participation
PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CDK1 in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin (By similarity). It is phosphorylated by different protein kinases in interphase when the membrane is associated with these structures (By similarity). 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 (By similarity). Phosphorylated by SRPK1 (By similarity). In late anaphase LBR is dephosphorylated, probably by PP1 and/or PP2A, allowing reassociation with chromatin (By similarity). {ECO:0000250|UniProtKB:Q14739}.
uniprot
proteins
protein_family
ERG4/ERG24 family
uniprot
proteins
pubmed
12490533
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18785926
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21327084
uniprot
proteins
pubmed
22140257
uniprot
proteins
pubmed
26009488
uniprot
proteins
sequence_length
626
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:18785926}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q14739}.
uniprot
proteins
transmembrane_region
TRANSMEM 222..242; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 269..289; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 310..330; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 337..357; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 427..447; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 458..478; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 492..512; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 572..592; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins