O14763 · TR10B_HUMAN
- ProteinTumor necrosis factor receptor superfamily member 10B
- GeneTNFRSF10B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids440 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis
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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Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | plasma membrane | |
Molecular Function | signaling receptor activity | |
Molecular Function | TRAIL binding | |
Molecular Function | TRAIL receptor activity | |
Biological Process | activation of NF-kappaB-inducing kinase activity | |
Biological Process | apoptotic process | |
Biological Process | cell surface receptor signaling pathway | |
Biological Process | cellular response to mechanical stimulus | |
Biological Process | defense response to tumor cell | |
Biological Process | extrinsic apoptotic signaling pathway via death domain receptors | |
Biological Process | intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress | |
Biological Process | positive regulation of apoptotic process | |
Biological Process | positive regulation of canonical NF-kappaB signal transduction | |
Biological Process | regulation of apoptotic process | |
Biological Process | response to endoplasmic reticulum stress | |
Biological Process | TRAIL-activated apoptotic signaling pathway |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTumor necrosis factor receptor superfamily member 10B
- 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 accessionO14763
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 56-210 | Extracellular | ||||
Sequence: ITQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCDSGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVHKESGTKHSGEVPAVEETVTSSPGTPASPCS | ||||||
Transmembrane | 211-231 | Helical | ||||
Sequence: LSGIIIGVTVAAVVLIVAVFV | ||||||
Topological domain | 232-440 | Cytoplasmic | ||||
Sequence: CKSLLWKKVLPYLKGICSGGGGDPERVDRSSQRPGAEDNVLNEIVSILQPTQVPEQEMEVQEPAEPTGVNMLSPGESEHLLEPAEAERSQRRRLLVPANEGDPTETLRQCFDDFADLVPFDSWEPLMRKLGLMDNEIKVAKAEAAGHRDTLYTMLIKWVNKTGRDASVHTLLDALETLGERLAKQKIEDHLLSSGKFMYLEGNADSAMS |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Squamous cell carcinoma of the head and neck (HNSCC)
- Note
- DescriptionA non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes.
- See alsoMIM:275355
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_016153 | 32 | in dbSNP:rs1129424 | |||
Sequence: P → L | ||||||
Natural variant | VAR_016154 | 67 | in dbSNP:rs1047266 | |||
Sequence: A → V | ||||||
Natural variant | VAR_059831 | 191 | in dbSNP:rs13265018 | |||
Sequence: V → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 576 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-55 | |||||
Sequence: MEQRGQNAPAASGARKRHGPGPREARGARPGPRVPKTLVLVVAAVLLLVSAESAL | ||||||
Chain | PRO_0000034580 | 56-440 | Tumor necrosis factor receptor superfamily member 10B | |||
Sequence: ITQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCDSGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVHKESGTKHSGEVPAVEETVTSSPGTPASPCSLSGIIIGVTVAAVVLIVAVFVCKSLLWKKVLPYLKGICSGGGGDPERVDRSSQRPGAEDNVLNEIVSILQPTQVPEQEMEVQEPAEPTGVNMLSPGESEHLLEPAEAERSQRRRLLVPANEGDPTETLRQCFDDFADLVPFDSWEPLMRKLGLMDNEIKVAKAEAAGHRDTLYTMLIKWVNKTGRDASVHTLLDALETLGERLAKQKIEDHLLSSGKFMYLEGNADSAMS | ||||||
Disulfide bond | 81↔94 | |||||
Sequence: CPPGHHISEDGRDC | ||||||
Disulfide bond | 97↔113 | |||||
Sequence: CKYGQDYSTHWNDLLFC | ||||||
Disulfide bond | 116↔129 | |||||
Sequence: CTRCDSGEVELSPC | ||||||
Disulfide bond | 119↔137 | |||||
Sequence: CDSGEVELSPCTTTRNTVC | ||||||
Disulfide bond | 139↔153 | |||||
Sequence: CEEGTFREEDSPEMC | ||||||
Disulfide bond | 156↔170 | |||||
Sequence: CRTGCPRGMVKVGDC | ||||||
Disulfide bond | 160↔178 | |||||
Sequence: CPRGMVKVGDCTPWSDIEC |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
Can interact with TRADD and RIPK1. Interacts with HCMV protein UL141; this interaction prevents TNFRSF10B cell surface expression. Two TNFRSF10B monomers interact with a UL141 homodimer. Three TNFRSF10B molecules interact with TNFSF10 homotrimer (PubMed:10549288).
In the absence of stimulation, interacts with BIRC2, DDX3X and GSK3B. The interaction with BIRC2 and DDX3X is further enhanced upon receptor stimulation and accompanied by DDX3X and BIRC2 cleavage (PubMed:18846110).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O14763 | ASPH Q12797-6 | 3 | EBI-518882, EBI-12092171 | |
BINARY | O14763 | MUC1 P15941-11 | 3 | EBI-518882, EBI-17263240 | |
BINARY | O14763 | TNFSF10 P50591 | 21 | EBI-518882, EBI-495373 | |
BINARY | O14763 | ZDHHC15 Q96MV8 | 6 | EBI-518882, EBI-12837904 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MEQRGQNAPAASGARKRHGPGPREARGARPGP | ||||||
Repeat | 57-94 | TNFR-Cys 1 | ||||
Sequence: TQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDC | ||||||
Compositional bias | 60-77 | Polar residues | ||||
Sequence: DLAPQQRAAPQQKRSSPS | ||||||
Region | 60-84 | Disordered | ||||
Sequence: DLAPQQRAAPQQKRSSPSEGLCPPG | ||||||
Repeat | 97-137 | TNFR-Cys 2 | ||||
Sequence: CKYGQDYSTHWNDLLFCLRCTRCDSGEVELSPCTTTRNTVC | ||||||
Repeat | 138-178 | TNFR-Cys 3 | ||||
Sequence: QCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIEC | ||||||
Repeat | 192-206 | TAPE | ||||
Sequence: PAVEETVTSSPGTPA | ||||||
Domain | 339-422 | Death | ||||
Sequence: RQCFDDFADLVPFDSWEPLMRKLGLMDNEIKVAKAEAAGHRDTLYTMLIKWVNKTGRDASVHTLLDALETLGERLAKQKIEDHL |
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 3 isoforms produced by Alternative splicing.
O14763-1
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.
- NameLong
- SynonymsTRICK2B
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
- Length440
- Mass (Da)47,878
- Last updated2010-11-30 v2
- Checksum60358EAF2A835870
O14763-3
- Name3
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
- Differences from canonical
- 119-440: Missing
O14763-2
- NameShort
- SynonymsTRICK2A
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
- Differences from canonical
- 185-213: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PBT3 | E9PBT3_HUMAN | TNFRSF10B | 90 |
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 60-77 | Polar residues | ||||
Sequence: DLAPQQRAAPQQKRSSPS | ||||||
Alternative sequence | VSP_039125 | 119-440 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_006490 | 185-213 | in isoform Short | |||
Sequence: Missing | ||||||
Sequence conflict | 439 | in Ref. 8; AAB67103 and 12; AAQ88644 | ||||
Sequence: M → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF018657 EMBL· GenBank· DDBJ | AAB70577.1 EMBL· GenBank· DDBJ | mRNA | ||
AF018658 EMBL· GenBank· DDBJ | AAB70578.1 EMBL· GenBank· DDBJ | mRNA | ||
AF016849 EMBL· GenBank· DDBJ | AAC51778.1 EMBL· GenBank· DDBJ | mRNA | ||
AF016266 EMBL· GenBank· DDBJ | AAB81180.1 EMBL· GenBank· DDBJ | mRNA | ||
AF016268 EMBL· GenBank· DDBJ | AAC01565.1 EMBL· GenBank· DDBJ | mRNA | ||
AF020501 EMBL· GenBank· DDBJ | AAB71412.1 EMBL· GenBank· DDBJ | mRNA | ||
AF022386 EMBL· GenBank· DDBJ | AAB71949.1 EMBL· GenBank· DDBJ | mRNA | ||
AF012628 EMBL· GenBank· DDBJ | AAB67109.1 EMBL· GenBank· DDBJ | mRNA | ||
AF012535 EMBL· GenBank· DDBJ | AAB67103.1 EMBL· GenBank· DDBJ | mRNA | ||
AB014718 EMBL· GenBank· DDBJ | BAA33723.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF153687 EMBL· GenBank· DDBJ | AAF75587.1 EMBL· GenBank· DDBJ | mRNA | ||
AF192548 EMBL· GenBank· DDBJ | AAF07175.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358277 EMBL· GenBank· DDBJ | AAQ88644.1 EMBL· GenBank· DDBJ | mRNA | ||
BX538104 EMBL· GenBank· DDBJ | CAD98017.1 EMBL· GenBank· DDBJ | mRNA | ||
AC107959 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC001281 EMBL· GenBank· DDBJ | AAH01281.1 EMBL· GenBank· DDBJ | mRNA |