TNFRSF11B
entrez
4982
canonical
uniprot
O00300
canonical
ensembl
ENSG00000164761
resolver
ensp
ENSP00000297350
resolver
enst
ENST00000297350
resolver
genesymbol
TNFRSF11B
resolver
genesymbol_syn
OCIF
resolver
genesymbol_syn
OPG
resolver
hgnc
HGNC:11909
resolver
uniprot
B2R9A8
resolver
uniprot
O60236
resolver
uniprot
Q53FX6
resolver
uniprot
Q9UHP4
resolver
uniprot_entry
TR11B_HUMAN
resolver
uniprot_sec
B2R9A8
resolver
uniprot_sec
O60236
resolver
uniprot_sec
Q53FX6
resolver
uniprot_sec
Q9UHP4
resolver
amino_acid_sequence
MNNLLCCALVFLDISIKWTTQETFPPKYLHYDEETSHQLLCDKCPPGTYLKQHCTAKWKTVCAPCPDHYYTDSWHTSDECLYCSPVCKELQYVKQECNRTHNRVCECKEGRYLEIEFCLKHRSCPPGFGVVQAGTPERNTVCKRCPDGFFSNETSSKAPCRKHTNCSVFGLLLTQKGNATHDNICSGNSESTQKCGIDVTLCEEAFFRFAVPTKFTPNWLSVLVDNLPGTKVNAESVERIKRQHSSQEQTFQLLKLWKHQNKDQDIVKKIIQDIDLCENSVQRHIGHANLTFEQLRSLMESLPGKKVGAEDIEKTIKACKPSDQILKLLSLWRIKNGDQDTLKGLMHALKHSKTYHFPKTVTQSLKKTIRFLHSFTMYKLYQKLFLEMIGNQVQSVKISCL
uniprot
proteins
disease_involvement
DISEASE: Paget disease of bone 5, juvenile-onset (PDB5) [MIM:239000]: An autosomal recessive, juvenile-onset form of Paget disease, a disorder of bone remodeling characterized by increased bone turnover affecting one or more sites throughout the skeleton, primarily the axial skeleton. Osteoclastic overactivity followed by compensatory osteoblastic activity leads to a structurally disorganized mosaic of bone (woven bone), which is mechanically weaker, larger, less compact, more vascular, and more susceptible to fracture than normal adult lamellar bone. PDB5 clinical manifestations include short stature, progressive long bone deformities, fractures, vertebral collapse, skull enlargement, and hyperostosis with progressive deafness. {ECO:0000269|PubMed:12189164}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Acts as a decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. {ECO:0000269|PubMed:22664871, ECO:0000269|PubMed:9168977}.
uniprot
proteins
mass_dalton
46026
uniprot
proteins
mutagenesis
MUTAGEN 78..79; /note="DE->AA: Decreases inhibition of osteoclast differentiation."; /evidence="ECO:0000269|PubMed:22664871"; MUTAGEN 116; /note="E->A: Reduces affinity for TNFSF11. Decreases inhibition of osteoclast differentiation."; /evidence="ECO:0000269|PubMed:22664871"; MUTAGEN 400..401; /note="Missing: Abolishes dimerization."; MUTAGEN 400; /note="C->S: Abolishes dimerization."; /evidence="ECO:0000269|PubMed:9478964
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. Contains sialic acid residues. {ECO:0000269|PubMed:22664871}.; PTM: The N-terminus is blocked.
uniprot
proteins
pubmed
11505389
uniprot
proteins
pubmed
12110935
uniprot
proteins
pubmed
12189164
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
22664871
uniprot
proteins
pubmed
9108485
uniprot
proteins
pubmed
9168977
uniprot
proteins
pubmed
9478964
uniprot
proteins
pubmed
9492069
uniprot
proteins
pubmed
9571159
uniprot
proteins
pubmed
9603945
uniprot
proteins
pubmed
9688283
uniprot
proteins
sequence_length
401
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted.
uniprot
proteins