RANK

TNFRSF11A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1LB5
Identifiers
Aliases	TNFRSF11A, tumor necrosis factor receptor superfamily, member 11a, NFKB activator, CD265, FEO, LOH18CR1, ODFR, OFE, OPTB7, OSTS, PDB2, RANK, TRANCER, tumor necrosis factor receptor superfamily member 11a, TNF receptor superfamily member 11a, TRANCE-R
External IDs	OMIM: 603499; MGI: 1314891; HomoloGene: 2848; GeneCards: TNFRSF11A; OMA:TNFRSF11A - orthologs
Gene location (Human) Chr. Chromosome 18 (human)[1] Band 18q21.33 Start 62,325,287 bp[1] End 62,391,288 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 E2.1 Start 105,708,443 bp[2] End 105,775,709 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in parotid gland mucosa of sigmoid colon jejunal mucosa rectum duodenum mucosa of ileum mucosa of transverse colon pancreatic ductal cell gallbladder epithelium of colon Top expressed in left colon duodenum submandibular gland ileum lumbar spinal ganglion jejunum right kidney Paneth cell stroma of bone marrow embryo More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metal ion binding protein binding tumor necrosis factor-activated receptor activity transmembrane signaling receptor activity cytokine binding signaling receptor activity Cellular component integral component of membrane membrane integral component of plasma membrane cell surface external side of plasma membrane cytosol plasma membrane Biological process regulation of apoptotic process response to cytokine response to interleukin-1 adaptive immune response ossification monocyte chemotaxis circadian temperature homeostasis positive regulation of JUN kinase activity osteoclast differentiation cell-cell signaling positive regulation of DNA-binding transcription factor activity tumor necrosis factor-mediated signaling pathway mammary gland alveolus development multicellular organism development response to tumor necrosis factor response to lipopolysaccharide positive regulation of NF-kappaB transcription factor activity positive regulation of fever generation by positive regulation of prostaglandin secretion positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling positive regulation of cell population proliferation apoptotic signaling pathway response to radiation TNFSF11-mediated signaling pathway inflammatory response lymph node development signal transduction positive regulation of bone resorption multinuclear osteoclast differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8792 21934 Ensembl ENSG00000141655 ENSMUSG00000026321 UniProt Q9Y6Q6 O35305 RefSeq (mRNA) NM_001270949 NM_001270950 NM_001270951 NM_001278268 NM_003839 NM_009399 RefSeq (protein) NP_001257878 NP_001257879 NP_001257880 NP_001265197 NP_003830 NP_033425 Location (UCSC) Chr 18: 62.33 – 62.39 Mb Chr 1: 105.71 – 105.78 Mb PubMed search [3] [4]
Wikidata
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Receptor activator of nuclear factor κ B (RANK), also known as TRANCE receptor or TNFRSF11A, is a member of the tumor necrosis factor receptor (TNFR) molecular sub-family. RANK is the receptor for RANK-Ligand (RANKL) and part of the RANK/RANKL/OPG signaling pathway that regulates osteoclast differentiation and activation. It is associated with bone remodeling and repair, immune cell function, lymph node development, thermal regulation, and mammary gland development. Osteoprotegerin (OPG) is a decoy receptor for RANKL, and regulates the stimulation of the RANK signaling pathway by competing for RANKL. The cytoplasmic domain of RANK binds TRAFs 1, 2, 3, 5, and 6 which transmit signals to downstream targets such as NF-κB and JNK.

RANK is constitutively expressed in skeletal muscle, thymus, liver, colon, small intestine, adrenal gland, osteoclast, mammary gland epithelial cells, prostate, vascular cell,^[5] and pancreas. Most commonly, activation of NF-κB is mediated by RANKL, but over-expression of RANK alone is sufficient to activate the NF-κB pathway.^[6]

RANKL (receptor activator for nuclear factor κ B ligand) is found on the surface of stromal cells, osteoblasts, and T cells.^[7][8][9] Mutations affecting RANK have been associated with infantile malignant osteopetrosis in humans, mice and cats.^[10]