O08984
uniprot
O08984
canonical
amino_acid_sequence
MPGRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKESDIKPLKSFKQRKSGSTSSSPSRRRSSRSRSRSRSRSPGRAPKGSRRSVSASYQADAKEKEMRREILQVKLTPLVLKPFANSVSVYNGEPEHMEKSATPPKNKQERVILSTEDSYIATQYSLRPRREEVKPKHRVRGTNLVTRGPVPLGTFQVTTPQRRDLEFGGVPGALLIMLGLPACVFLLLLQCAQKDPGLLQFPPPLPALRELWEARVCGVYLLWFFLQALFSLLPVGKVVEGTPLVDGRRLKYRLNGLYAFILTSAAVGTAVFWDIELYYLYTHFLQFALAAIVFSVVLSVYLYARSLKVPRDELSPASSGNAVYDFFIGRELNPRIGAFDLKFFCELRPGLIGWVVINLVMLLAEMKVQERSAPSLAMTLVNSFQLLYVVDALWFEEALLTTMDIIHDGFGFMLAFGDLVWVPFTYSLQAFYLVNHPQDLSWPLTSVIIALKLCGYVIFRCANSQKNAFRKNPTDPKLAHLKTIPTSTWKSLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHILPYFYVIYFTALLIHREARDEHQCRRKYGLAWEKYCQRVPYRIFPYIY
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 (By similarity). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity). {ECO:0000250|UniProtKB:Q14739, ECO:0000250|UniProtKB:Q3U9G9}.
uniprot
proteins
mass_dalton
70724
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
12438562
uniprot
proteins
pubmed
16784888
uniprot
proteins
pubmed
9192729
uniprot
proteins
sequence_length
620
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q14739}; 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 216..236; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 263..283; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 304..324; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 331..351; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 452..472; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 486..506; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 525..547; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 566..586; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins