LBR
entrez
3930
canonical
uniprot
Q14739
canonical
ensembl
ENSG00000143815
resolver
ensp
ENSP00000272163
resolver
ensp
ENSP00000339883
resolver
ensp
ENSP00000555854
resolver
ensp
ENSP00000555855
resolver
ensp
ENSP00000555859
resolver
ensp
ENSP00000555860
resolver
ensp
ENSP00000555862
resolver
ensp
ENSP00000603656
resolver
ensp
ENSP00000615266
resolver
ensp
ENSP00000615267
resolver
ensp
ENSP00000615268
resolver
ensp
ENSP00000662519
resolver
enst
ENST00000272163
resolver
enst
ENST00000338179
resolver
enst
ENST00000885795
resolver
enst
ENST00000885800
resolver
enst
ENST00000885801
resolver
enst
ENST00000885803
resolver
enst
ENST00000945207
resolver
enst
ENST00000945208
resolver
enst
ENST00000945209
resolver
genesymbol
LBR
resolver
hgnc
HGNC:6518
resolver
uniprot
B2R5P3
resolver
uniprot
Q14740
resolver
uniprot
Q53GU7
resolver
uniprot
Q59FE6
resolver
uniprot_entry
LBR_HUMAN
resolver
uniprot_sec
B2R5P3
resolver
uniprot_sec
Q14740
resolver
uniprot_sec
Q53GU7
resolver
uniprot_sec
Q59FE6
resolver
amino_acid_sequence
MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIKPLTSFRQRKGGSTSSSPSRRRGSRSRSRSRSPGRPPKSARRSASASHQADIKEARREVEVKLTPLILKPFGNSISRYNGEPEHIERNDAPHKNTQEKFSLSQESSYIATQYSLRPRREEVKLKEIDSKEEKYVAKELAVRTFEVTPIRAKDLEFGGVPGVFLIMFGLPVFLFLLLLMCKQKDPSLLNFPPPLPALYELWETRVFGVYLLWFLIQVLFYLLPIGKVVEGTPLIDGRRLKYRLNGFYAFILTSAVIGTSLFQGVEFHYVYSHFLQFALAATVFCVVLSVYLYMRSLKAPRNDLSPASSGNAVYDFFIGRELNPRIGTFDLKYFCELRPGLIGWVVINLVMLLAEMKIQDRAVPSLAMILVNSFQLLYVVDALWNEEALLTTMDIIHDGFGFMLAFGDLVWVPFIYSFQAFYLVSHPNEVSWPMASLIIVLKLCGYVIFRGANSQKNAFRKNPSDPKLAHLKTIHTSTGKNLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHILPYFYIIYFTMLLVHREARDEYHCKKKYGVAWEKYCQRVPYRIFPYIY
uniprot
proteins
disease_involvement
DISEASE: Pelger-Huet anomaly (PHA) [MIM:169400]: An autosomal dominant inherited abnormality of granulocytes, characterized by abnormal ovoid shape, reduced nuclear segmentation and an apparently looser chromatin structure. {ECO:0000269|PubMed:14617022}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Greenberg dysplasia (GRBGD) [MIM:215140]: A rare autosomal recessive chondrodystrophy characterized by early in utero lethality. Affected fetuses typically present with fetal hydrops, short-limbed dwarfism, and a marked disorganization of chondro-osseous calcification, and ectopic ossification centers. {ECO:0000269|PubMed:12618959, ECO:0000269|PubMed:21327084, ECO:0000269|PubMed:27336722}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Reynolds syndrome (REYNS) [MIM:613471]: A syndrome specifically associating limited cutaneous systemic sclerosis and primary biliary cirrhosis. It is characterized by liver disease, telangiectasia, abrupt onset of digital paleness or cyanosis in response to cold exposure or stress (Raynaud phenomenon), and variable features of scleroderma. The liver disease is characterized by pruritis, jaundice, hepatomegaly, increased serum alkaline phosphatase and positive serum mitochondrial autoantibodies, all consistent with primary biliary cirrhosis. {ECO:0000269|PubMed:20522425}. Note=The disease may be caused by variants affecting the gene represented in this entry.; DISEASE: Rhizomelic skeletal dysplasia with or without Pelger-Huet anomaly (SKPHA) [MIM:618019]: A disease characterized by abnormal nuclear shape and chromatin organization in blood granulocytes, short stature, and mild skeletal anomalies. Initial skeletal features may improve with age. {ECO:0000269|PubMed:23824842, ECO:0000269|PubMed:25348816}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722, PubMed:9630650). 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 (PubMed:10828963). {ECO:0000250|UniProtKB:Q3U9G9, ECO:0000269|PubMed:10828963, ECO:0000269|PubMed:12618959, ECO:0000269|PubMed:16784888, ECO:0000269|PubMed:21327084, ECO:0000269|PubMed:27336722, ECO:0000269|PubMed:9630650}.
uniprot
proteins
mass_dalton
70703
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. 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. {ECO:0000269|PubMed:10049757, ECO:0000269|PubMed:21795390}.
uniprot
proteins
protein_family
ERG4/ERG24 family
uniprot
proteins
pubmed
10049757
uniprot
proteins
pubmed
10828963
uniprot
proteins
pubmed
12118250
uniprot
proteins
pubmed
12618959
uniprot
proteins
pubmed
14617022
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15882967
uniprot
proteins
pubmed
16784888
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20522425
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21327084
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21795390
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23824842
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25348816
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26009488
uniprot
proteins
pubmed
27336722
uniprot
proteins
pubmed
32694168
uniprot
proteins
pubmed
8157662
uniprot
proteins
pubmed
8157663
uniprot
proteins
pubmed
9169472
uniprot
proteins
pubmed
9630650
uniprot
proteins
sequence_length
615
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:32694168, ECO:0000269|PubMed:8157662}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21327084}. Cytoplasm {ECO:0000269|PubMed:21327084}. Nucleus {ECO:0000269|PubMed:21327084}. Note=Nucleus; nuclear rim. {ECO:0000269|PubMed:21327084}.
uniprot
proteins
transmembrane_region
TRANSMEM 212..232; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 258..278; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 299..319; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 326..346; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 386..406; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 447..467; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 481..501; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 561..581; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins