LBR Anchors the lamina and the heterochromatin to the inner nuclear membrane. Defects in LBR are a cause of Pelger-Huet anomaly (PHA). PHA is an autosomal dominant inherited abnormality of neutrophils, characterized by reduced nuclear segmentation and an apparently looser chromatin structure. Heterozygotes show hypolobulated neutrophil nuclei with coarse chromatin. Presumed homozygous individuals have ovoid neutrophil nuclei, as well as varying degrees of developmental delay, epilepsy, and skeletal abnormalities. Defects in LBR are the cause of hydrops-ectopic calcification-moth-eaten skeletal dysplasia (HEM); also known as Greenberg skeletal dysplasia. HEM is a rare autosomal recessive chondrodystrophy characterized by early in utero lethality and, therefore, considered to be nonviable. Affected fetuses typically present with fetal hydrops, short- limbed dwarfism, and a marked disorganization of chondro-osseous calcification and may present with polydactyly and additional nonskeletal malformations. Defects in LBR may be a cause of Reynolds syndrome (REYNS). It is a syndrome specifically associating limited cutaneous systemic sclerosis and primary biliray 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. Belongs to the ERG4/ERG24 family. Note: This description may include information from UniProtKB.
Protein type: DNA-binding; Membrane protein, integral; Membrane protein, multi-pass
Chromosomal Location of Human Ortholog: 1 H5|1 84.89 cM
Cellular Component:  cytoplasm; integral component of endoplasmic reticulum membrane; integral component of membrane; membrane; nuclear envelope; nuclear inner membrane; nuclear lamina; nuclear membrane; nuclear pore; nucleus
Molecular Function:  chaperone binding; chromo shadow domain binding; DNA binding; nuclear localization sequence binding; oxidoreductase activity, acting on the CH-CH group of donors; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
Biological Process:  sterol biosynthetic process
Reference #:  Q3U9G9 (UniProtKB)
Alt. Names/Synonyms: AI505894; ic; ichthyosis; Integral nuclear envelope inner membrane protein; lamin B receptor; Lamin-B receptor; Lbr
Gene Symbols: Lbr
Molecular weight: 71,440 Da
Basal Isoelectric point: 9.43  Predict pI for various phosphorylation states
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Protein Structure Not Found.

Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene