Q9Y6Q6 · TNR11_HUMAN
- ProteinTumor necrosis factor receptor superfamily member 11A
- GeneTNFRSF11A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids616 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Its interaction with EEIG1 promotes osteoclastogenesis via facilitating the transcription of NFATC1 and activation of PLCG2 (By similarity).
Involved in the regulation of interactions between T-cells and dendritic cells (By similarity).
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTumor necrosis factor receptor superfamily member 11A
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y6Q6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Isoform RANK-e5a
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 30-212 | Extracellular | ||||
Sequence: IAPPCTSEKHYEHLGRCCNKCEPGKYMSSKCTTTSDSVCLPCGPDEYLDSWNEEDKCLLHKVCDTGKALVAVVAGNSTTPRRCACTAGYHWSQDCECCRRNTECAPGLGAQHPLQLNKDTVCKPCLAGYFSDAFSSTDKCRPWTNCTFLGKRVEHHGTEKSDAVCSSSLPARKPPNEPHVYLP | ||||||
Transmembrane | 213-233 | Helical | ||||
Sequence: GLIILLLFASVALVAAIIFGV | ||||||
Topological domain | 234-616 | Cytoplasmic | ||||
Sequence: CYRKKGKALTANLWHWINEACGRLSGDKESSGDSCVSTHTANFGQQGACEGVLLLTLEEKTFPEDMCYPDQGGVCQGTCVGGGPYAQGEDARMLSLVSKTEIEEDSFRQMPTEDEYMDRPSQPTDQLLFLTEPGSKSTPPFSEPLEVGENDSLSQCFTGTQSTVGSESCNCTEPLCRTDWTPMSSENYLQKEVDSGHCPHWAASPSPNWADVCTGCRNPPGEDCEPLVGSPKRGPLPQCAYGMGLPPEEEASRTEARDQPEDGADGRLPSSARAGAGSGSSPGGQSPASGNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGAAAAAEPMGRPVQEETLARRDSFAGNGPRFPDPCGGPEGLREPEKASRPVQEQGGAKA |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Familial expansile osteolysis (FEO)
- Note
- DescriptionRare autosomal dominant bone disorder characterized by focal areas of increased bone remodeling. The osteolytic lesions develop usually in the long bones during early adulthood. FEO is often associated with early-onset deafness and loss of dentition.
- See alsoMIM:174810
Natural variants in FEO
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_011517 | 21 | L>LLLCALL | in FEO |
Paget disease of bone 2, early-onset (PDB2)
- Note
- DescriptionA 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.
- See alsoMIM:602080
Natural variants in PDB2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_011516 | 21 | L>LALLLLCALL | in PDB2 |
Osteopetrosis, autosomal recessive 7 (OPTB7)
- Note
- DescriptionA rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB7 is characterized by paucity of osteoclasts, suggesting a molecular defect in osteoclast development. OPTB7 is associated with hypogammaglobulinemia.
- See alsoMIM:612301
Natural variants in OPTB7
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_046788 | 53 | G>R | in OPTB7; two patients with osteoclast-poor osteopetrosis; dbSNP:rs121908659 | |
VAR_046789 | 129 | R>C | in OPTB7; a patient with osteoclast-poor osteopetrosis; dbSNP:rs121908657 | |
VAR_046791 | 170 | R>G | in OPTB7; two siblings with osteoclast-poor osteopetrosis; dbSNP:rs121908655 | |
VAR_046792 | 175 | C>R | in OPTB7; two patients with osteoclast-poor osteopetrosis; dbSNP:rs121908656 | |
VAR_046793 | 244 | A>S | in OPTB7; one patient with osteoclast-poor osteopetrosis; dbSNP:rs121908658 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_011516 | 21 | in PDB2 | |||
Sequence: L → LALLLLCALL | ||||||
Natural variant | VAR_011517 | 21 | in FEO | |||
Sequence: L → LLLCALL | ||||||
Natural variant | VAR_046788 | 53 | in OPTB7; two patients with osteoclast-poor osteopetrosis; dbSNP:rs121908659 | |||
Sequence: G → R | ||||||
Natural variant | VAR_046789 | 129 | in OPTB7; a patient with osteoclast-poor osteopetrosis; dbSNP:rs121908657 | |||
Sequence: R → C | ||||||
Natural variant | VAR_046790 | 141 | in dbSNP:rs35211496 | |||
Sequence: H → Y | ||||||
Natural variant | VAR_046791 | 170 | in OPTB7; two siblings with osteoclast-poor osteopetrosis; dbSNP:rs121908655 | |||
Sequence: R → G | ||||||
Natural variant | VAR_046792 | 175 | in OPTB7; two patients with osteoclast-poor osteopetrosis; dbSNP:rs121908656 | |||
Sequence: C → R | ||||||
Natural variant | VAR_011518 | 192 | in dbSNP:rs1805034 | |||
Sequence: A → V | ||||||
Natural variant | VAR_046793 | 244 | in OPTB7; one patient with osteoclast-poor osteopetrosis; dbSNP:rs121908658 | |||
Sequence: A → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 742 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-29 | UniProt | |||||
Sequence: MAPRARRRRPLFALLLLCALLARLQVALQ | |||||||
Chain | PRO_0000034585 | 30-616 | UniProt | Tumor necrosis factor receptor superfamily member 11A | |||
Sequence: IAPPCTSEKHYEHLGRCCNKCEPGKYMSSKCTTTSDSVCLPCGPDEYLDSWNEEDKCLLHKVCDTGKALVAVVAGNSTTPRRCACTAGYHWSQDCECCRRNTECAPGLGAQHPLQLNKDTVCKPCLAGYFSDAFSSTDKCRPWTNCTFLGKRVEHHGTEKSDAVCSSSLPARKPPNEPHVYLPGLIILLLFASVALVAAIIFGVCYRKKGKALTANLWHWINEACGRLSGDKESSGDSCVSTHTANFGQQGACEGVLLLTLEEKTFPEDMCYPDQGGVCQGTCVGGGPYAQGEDARMLSLVSKTEIEEDSFRQMPTEDEYMDRPSQPTDQLLFLTEPGSKSTPPFSEPLEVGENDSLSQCFTGTQSTVGSESCNCTEPLCRTDWTPMSSENYLQKEVDSGHCPHWAASPSPNWADVCTGCRNPPGEDCEPLVGSPKRGPLPQCAYGMGLPPEEEASRTEARDQPEDGADGRLPSSARAGAGSGSSPGGQSPASGNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGAAAAAEPMGRPVQEETLARRDSFAGNGPRFPDPCGGPEGLREPEKASRPVQEQGGAKA | |||||||
Disulfide bond | 34↔46 | UniProt | |||||
Sequence: CTSEKHYEHLGRC | |||||||
Disulfide bond | 47↔60 | UniProt | |||||
Sequence: CNKCEPGKYMSSKC | |||||||
Disulfide bond | 50↔68 | UniProt | |||||
Sequence: CEPGKYMSSKCTTTSDSVC | |||||||
Disulfide bond | 71↔86 | UniProt | |||||
Sequence: CGPDEYLDSWNEEDKC | |||||||
Disulfide bond | 92↔112 | UniProt | |||||
Sequence: CDTGKALVAVVAGNSTTPRRC | |||||||
Glycosylation | 105 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 114↔127 | UniProt | |||||
Sequence: CTAGYHWSQDCECC | |||||||
Disulfide bond | 124↔126 | UniProt | |||||
Sequence: CEC | |||||||
Disulfide bond | 133↔151 | UniProt | |||||
Sequence: CAPGLGAQHPLQLNKDTVC | |||||||
Disulfide bond | 154↔169 | UniProt | |||||
Sequence: CLAGYFSDAFSSTDKC | |||||||
Glycosylation | 174 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 175↔194 | UniProt | |||||
Sequence: CTFLGKRVEHHGTEKSDAVC | |||||||
Modified residue (large scale data) | 463 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 580 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 580 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Part of a complex composed of EEIG1, TNFRSF11A/RANK, PLCG2, GAB2, TEC and BTK; complex formation increases in the presence of TNFSF11/RANKL (PubMed:23478294).
Interacts with TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6 (PubMed:9774460).
Interacts (via cytoplasmic domain) with GAB2 (PubMed:15750601).
Interacts (via cytoplasmic domain); with EEIG1 (via N-terminus); when in the presence of TNFSF11/RANKL (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y6Q6 | TNFSF11 PRO_0000034515 O14788 | 9 | EBI-525675, EBI-15488409 | |
BINARY | Q9Y6Q6 | TRAF2 Q12933 | 2 | EBI-525675, EBI-355744 | |
BINARY | Q9Y6Q6-2 | EGFR P00533 | 3 | EBI-20899422, EBI-297353 | |
BINARY | Q9Y6Q6-2 | TRAF2 Q12933 | 5 | EBI-20899422, EBI-355744 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 34-68 | TNFR-Cys 1 | ||||
Sequence: CTSEKHYEHLGRCCNKCEPGKYMSSKCTTTSDSVC | ||||||
Repeat | 71-112 | TNFR-Cys 2 | ||||
Sequence: CGPDEYLDSWNEEDKCLLHKVCDTGKALVAVVAGNSTTPRRC | ||||||
Repeat | 114-151 | TNFR-Cys 3 | ||||
Sequence: CTAGYHWSQDCECCRRNTECAPGLGAQHPLQLNKDTVC | ||||||
Repeat | 154-194 | TNFR-Cys 4 | ||||
Sequence: CLAGYFSDAFSSTDKCRPWTNCTFLGKRVEHHGTEKSDAVC | ||||||
Region | 468-536 | Disordered | ||||
Sequence: PLPQCAYGMGLPPEEEASRTEARDQPEDGADGRLPSSARAGAGSGSSPGGQSPASGNVTGNSNSTFISS | ||||||
Compositional bias | 483-497 | Basic and acidic residues | ||||
Sequence: EASRTEARDQPEDGA | ||||||
Compositional bias | 507-536 | Polar residues | ||||
Sequence: AGAGSGSSPGGQSPASGNVTGNSNSTFISS | ||||||
Region | 544-549 | Required for interaction with EEIG1 and osteoclast differentiation | ||||
Sequence: GDIIVV | ||||||
Region | 556-616 | Disordered | ||||
Sequence: QEGAAAAAEPMGRPVQEETLARRDSFAGNGPRFPDPCGGPEGLREPEKASRPVQEQGGAKA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 6 isoforms produced by Alternative splicing.
Q9Y6Q6-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length616
- Mass (Da)66,034
- Last updated1999-11-01 v1
- ChecksumE3DE9A7A08196F81
Q9Y6Q6-2
- Name2
- Synonymsdelta7,8,9
- Differences from canonical
- 206-522: Missing
Q9Y6Q6-3
- Name3
- Synonymsdelta8,9
- Differences from canonical
- 244-522: Missing
Q9Y6Q6-4
- Name4
- Synonymsdelta9
Q9Y6Q6-5
- Name5
- Synonymsexon9a
- NoteReduced ability to bind RANKL and to activate NF-kappaB as compared to isoform 1.
- Differences from canonical
- 523-616: GNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGAAAAAEPMGRPVQEETLARRDSFAGNGPRFPDPCGGPEGLREPEKASRPVQEQGGAKA → D
Q9Y6Q6-6
- NameRANK-e5a
- NoteReduced ability to bind RANKL and to activate NF-kappaB as compared to isoform 1.
- Differences from canonical
- 143-157: LQLNKDTVCKPCLAG → C
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_054179 | 143-157 | in isoform RANK-e5a | |||
Sequence: LQLNKDTVCKPCLAG → C | ||||||
Alternative sequence | VSP_046901 | 206-522 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_054180 | 244-522 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_054181 | 263 | in isoform 4 | |||
Sequence: S → M | ||||||
Alternative sequence | VSP_054182 | 264-616 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 483-497 | Basic and acidic residues | ||||
Sequence: EASRTEARDQPEDGA | ||||||
Compositional bias | 507-536 | Polar residues | ||||
Sequence: AGAGSGSSPGGQSPASGNVTGNSNSTFISS | ||||||
Alternative sequence | VSP_054183 | 523-616 | in isoform 5 | |||
Sequence: GNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGAAAAAEPMGRPVQEETLARRDSFAGNGPRFPDPCGGPEGLREPEKASRPVQEQGGAKA → D |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF018253 EMBL· GenBank· DDBJ | AAB86809.1 EMBL· GenBank· DDBJ | mRNA | ||
HF584702 EMBL· GenBank· DDBJ | CCQ44072.1 EMBL· GenBank· DDBJ | mRNA | ||
HE647782 EMBL· GenBank· DDBJ | CCF23032.1 EMBL· GenBank· DDBJ | mRNA | ||
HE649916 EMBL· GenBank· DDBJ | CCF55033.1 EMBL· GenBank· DDBJ | mRNA | ||
HE649917 EMBL· GenBank· DDBJ | CCF55034.1 EMBL· GenBank· DDBJ | mRNA | ||
HE659518 EMBL· GenBank· DDBJ | CCF77738.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209762 EMBL· GenBank· DDBJ | BAD92999.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |