TR10B_HUMAN
ID TR10B_HUMAN Reviewed; 440 AA.
AC O14763; O14720; O15508; O15517; O15531; Q6UXM8; Q7Z360; Q9BVE0;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 10B;
DE AltName: Full=Death receptor 5;
DE AltName: Full=TNF-related apoptosis-inducing ligand receptor 2;
DE Short=TRAIL receptor 2;
DE Short=TRAIL-R2;
DE AltName: CD_antigen=CD262;
DE Flags: Precursor;
GN Name=TNFRSF10B; Synonyms=DR5, KILLER, TRAILR2, TRICK2, ZTNFR9;
GN ORFNames=UNQ160/PRO186;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), ALTERNATIVE SPLICING,
RP AND VARIANTS LEU-32; VAL-67 AND ALA-191.
RX PubMed=9285725; DOI=10.1016/s0960-9822(06)00297-1;
RA Screaton G.R., Mongkolsapaya J., Xu X.-N., Cowper A.E., McMichael A.J.,
RA Bell J.I.;
RT "TRICK2, a new alternatively spliced receptor that transduces the cytotoxic
RT signal from TRAIL.";
RL Curr. Biol. 7:693-696(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PROTEIN SEQUENCE OF N-TERMINUS,
RP AND VARIANT ALA-191.
RC TISSUE=Foreskin fibroblast;
RX PubMed=9311998; DOI=10.1093/emboj/16.17.5386;
RA Walczak H., Degli-Esposti M.A., Johnson R.S., Smolak P.J., Waugh J.Y.,
RA Boiani N., Timour M.S., Gerhart M.J., Schooley K.A., Smith C.A.,
RA Goodwin R.G., Rauch C.T.;
RT "TRAIL-R2: a novel apoptosis-mediating receptor for TRAIL.";
RL EMBO J. 16:5386-5397(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), CHARACTERIZATION, AND VARIANTS
RP LEU-32; VAL-67 AND ALA-191.
RC TISSUE=Liver, and Spleen;
RX PubMed=9373179; DOI=10.1016/s0014-5793(97)01231-3;
RA Schneider P., Bodmer J.-L., Thome M., Hofmann K., Holler N., Tschopp J.;
RT "Characterization of two receptors for TRAIL.";
RL FEBS Lett. 416:329-334(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND VARIANTS LEU-32 AND VAL-67.
RX PubMed=9430227; DOI=10.1016/s1074-7613(00)80400-8;
RA Chaudhary P.M., Eby M., Jasmin A., Bookwalter A., Murray J., Hood L.;
RT "Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-
RT dependent apoptosis and activate the NF-kappaB pathway.";
RL Immunity 7:821-830(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND VARIANTS LEU-32 AND VAL-67.
RX PubMed=9325248; DOI=10.1074/jbc.272.41.25417;
RA MacFarlane M., Ahmad M., Srinivasula S.M., Fernandes-Alnemri T.,
RA Cohen G.M., Alnemri E.S.;
RT "Identification and molecular cloning of two novel receptors for the
RT cytotoxic ligand TRAIL.";
RL J. Biol. Chem. 272:25417-25420(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC TISSUE=Ovary;
RX PubMed=9326928; DOI=10.1038/ng1097-141;
RA Wu G.S., Burns T.F., McDonald E.R. III, Jiang W., Meng R., Krantz I.D.,
RA Kao G., Gan D.D., Zhou J.Y., Muschel R., Hamilton S.R., Spinner N.B.,
RA Markowitz S., Wu G., el-Deiry W.S.;
RT "KILLER/DR5 is a DNA damage-inducible p53-regulated death receptor gene.";
RL Nat. Genet. 17:141-143(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=9242610; DOI=10.1126/science.277.5327.815;
RA Pan G., Ni J., Wei Y.-F., Yu G.-L., Gentz R., Dixit V.M.;
RT "An antagonist decoy receptor and a death domain-containing receptor for
RT TRAIL.";
RL Science 277:815-818(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND VARIANT LEU-32.
RX PubMed=9242611; DOI=10.1126/science.277.5327.818;
RA Sheridan J.P., Marsters S.A., Pitti R.M., Gurney A., Skubatch M.,
RA Baldwin D.T., Ramakrishnan L., Gray C.L., Baker K., Wood W.I.,
RA Goddard A.D., Godowski P.J., Ashkenazi A.;
RT "Control of TRAIL-induced apoptosis by a family of signaling and decoy
RT receptors.";
RL Science 277:818-821(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANTS
RP LEU-32; VAL-67 AND ALA-191.
RX PubMed=10072170; DOI=10.1016/s0304-3835(98)00230-4;
RA Arai T., Akiyama Y., Okabe S., Saito K., Iwai T., Yuasa Y.;
RT "Genomic organization and mutation analyses of the DR5/TRAIL receptor 2
RT gene in colorectal carcinomas.";
RL Cancer Lett. 133:197-204(1998).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RA Cao X., Zhang W., Wan T.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND VARIANTS LEU-32 AND VAL-67.
RA Farrah T., Vu T., Gilbert T., Gross J., O'Hara P.;
RT "Homo sapiens homolog of tumor necrosis factor receptor.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT), AND VARIANT LEU-32.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LEU-32.
RC TISSUE=Colon endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANTS LEU-32
RP AND ALA-191.
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [16]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [17]
RP FUNCTION, AND INDUCTION.
RX PubMed=15322075; DOI=10.1074/jbc.m406933200;
RA Yamaguchi H., Wang H.G.;
RT "CHOP is involved in endoplasmic reticulum stress-induced apoptosis by
RT enhancing DR5 expression in human carcinoma cells.";
RL J. Biol. Chem. 279:45495-45502(2004).
RN [18]
RP INTERACTION WITH DDX3X; GSK3B AND BIRC2.
RX PubMed=18846110; DOI=10.1038/cdd.2008.124;
RA Sun M., Song L., Li Y., Zhou T., Jope R.S.;
RT "Identification of an antiapoptotic protein complex at death receptors.";
RL Cell Death Differ. 15:1887-1900(2008).
RN [19]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL141.
RX PubMed=23498957; DOI=10.1016/j.chom.2013.02.003;
RA Smith W., Tomasec P., Aicheler R., Loewendorf A., Nemcovicova I.,
RA Wang E.C., Stanton R.J., Macauley M., Norris P., Willen L., Ruckova E.,
RA Nomoto A., Schneider P., Hahn G., Zajonc D.M., Ware C.F., Wilkinson G.W.,
RA Benedict C.A.;
RT "Human cytomegalovirus glycoprotein UL141 targets the TRAIL death receptors
RT to thwart host innate antiviral defenses.";
RL Cell Host Microbe 13:324-335(2013).
RN [20]
RP GLYCOSYLATION (MICROBIAL INFECTION).
RX PubMed=30902834; DOI=10.1074/mcp.ra118.001093;
RA Newson J.P.M., Scott N.E., Yeuk Wah Chung I., Wong Fok Lung T., Giogha C.,
RA Gan J., Wang N., Strugnell R.A., Brown N.F., Cygler M., Pearson J.S.,
RA Hartland E.L.;
RT "Salmonella effectors SseK1 and SseK3 target death domain proteins in the
RT TNF and TRAIL signaling pathways.";
RL Mol. Cell. Proteomics 18:1138-1156(2019).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 54-183 IN COMPLEX WITH TNFSF10,
RP DISULFIDE BOND, AND SUBUNIT.
RX PubMed=10549288; DOI=10.1016/s1097-2765(00)80207-5;
RA Hymowitz S.G., Christinger H.W., Fuh G., Ultsch M., O'Connell M.,
RA Kelley R.F., Ashkenazi A., de Vos A.M.;
RT "Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex
RT with death receptor 5.";
RL Mol. Cell 4:563-571(1999).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 69-184 IN COMPLEX WITH TNFSF10,
RP AND DISULFIDE BOND.
RX PubMed=10542098; DOI=10.1038/14935;
RA Mongkolsapaya J., Grimes J.M., Chen N., Xu X.-N., Stuart D.I., Jones E.Y.,
RA Screaton G.R.;
RT "Structure of the TRAIL-DR5 complex reveals mechanisms conferring
RT specificity in apoptotic initiation.";
RL Nat. Struct. Biol. 6:1048-1053(1999).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 58-184, INTERACTION WITH HUMAN
RP CYTOMEGALOVIRUS PROTEIN UL141, AND DISULFIDE BOND.
RX PubMed=23555243; DOI=10.1371/journal.ppat.1003224;
RA Nemcovicova I., Benedict C.A., Zajonc D.M.;
RT "Structure of human cytomegalovirus UL141 binding to TRAIL-R2 reveals
RT novel, non-canonical death receptor interactions.";
RL PLoS Pathog. 9:E1003224-E1003224(2013).
CC -!- FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL
CC (PubMed:10549288). The adapter molecule FADD recruits caspase-8 to the
CC activated receptor. The resulting death-inducing signaling complex
CC (DISC) performs caspase-8 proteolytic activation which initiates the
CC subsequent cascade of caspases (aspartate-specific cysteine proteases)
CC mediating apoptosis. Promotes the activation of NF-kappa-B. Essential
CC for ER stress-induced apoptosis. {ECO:0000269|PubMed:10542098,
CC ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:15322075}.
CC -!- SUBUNIT: Monomer (PubMed:10549288). Can interact with TRADD and RIPK1.
CC Interacts with HCMV protein UL141; this interaction prevents TNFRSF10B
CC cell surface expression. Two TNFRSF10B monomers interact with a UL141
CC homodimer. Three TNFRSF10B molecules interact with TNFSF10 homotrimer
CC (PubMed:10549288). In the absence of stimulation, interacts with BIRC2,
CC DDX3X and GSK3B. The interaction with BIRC2 and DDX3X is further
CC enhanced upon receptor stimulation and accompanied by DDX3X and BIRC2
CC cleavage (PubMed:18846110). {ECO:0000269|PubMed:10549288,
CC ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:23498957,
CC ECO:0000269|PubMed:23555243}.
CC -!- INTERACTION:
CC O14763; Q12797-6: ASPH; NbExp=3; IntAct=EBI-518882, EBI-12092171;
CC O14763; P15941-11: MUC1; NbExp=3; IntAct=EBI-518882, EBI-17263240;
CC O14763; P50591: TNFSF10; NbExp=21; IntAct=EBI-518882, EBI-495373;
CC O14763; Q96MV8: ZDHHC15; NbExp=6; IntAct=EBI-518882, EBI-12837904;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Long; Synonyms=TRICK2B;
CC IsoId=O14763-1; Sequence=Displayed;
CC Name=3;
CC IsoId=O14763-3; Sequence=VSP_039125;
CC Name=Short; Synonyms=TRICK2A;
CC IsoId=O14763-2; Sequence=VSP_006490;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues; very
CC highly expressed in tumor cell lines such as HeLaS3, K-562, HL-60,
CC SW480, A-549 and G-361; highly expressed in heart, peripheral blood
CC lymphocytes, liver, pancreas, spleen, thymus, prostate, ovary, uterus,
CC placenta, testis, esophagus, stomach and throughout the intestinal
CC tract; not detectable in brain.
CC -!- INDUCTION: By ER stress. Regulated by p53/TP53.
CC {ECO:0000269|PubMed:15322075}.
CC -!- PTM: (Microbial infection) Glycosylated on Arg residue by S.typhimurium
CC protein Ssek3. {ECO:0000269|PubMed:30902834}.
CC -!- DISEASE: Squamous cell carcinoma of the head and neck (HNSCC)
CC [MIM:275355]: A non-melanoma skin cancer affecting the head and neck.
CC The hallmark of cutaneous SCC is malignant transformation of normal
CC epidermal keratinocytes. Note=The disease may be caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform Long]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Short]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
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DR EMBL; AF018657; AAB70577.1; -; mRNA.
DR EMBL; AF018658; AAB70578.1; -; mRNA.
DR EMBL; AF016849; AAC51778.1; -; mRNA.
DR EMBL; AF016266; AAB81180.1; -; mRNA.
DR EMBL; AF016268; AAC01565.1; -; mRNA.
DR EMBL; AF020501; AAB71412.1; -; mRNA.
DR EMBL; AF022386; AAB71949.1; -; mRNA.
DR EMBL; AF012628; AAB67109.1; -; mRNA.
DR EMBL; AF012535; AAB67103.1; -; mRNA.
DR EMBL; AB014718; BAA33723.1; -; Genomic_DNA.
DR EMBL; AF153687; AAF75587.1; -; mRNA.
DR EMBL; AF192548; AAF07175.1; -; mRNA.
DR EMBL; AY358277; AAQ88644.1; -; mRNA.
DR EMBL; BX538104; CAD98017.1; -; mRNA.
DR EMBL; AC107959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001281; AAH01281.1; -; mRNA.
DR CCDS; CCDS6035.1; -. [O14763-1]
DR CCDS; CCDS6036.1; -. [O14763-2]
DR RefSeq; NP_003833.4; NM_003842.4. [O14763-1]
DR RefSeq; NP_671716.2; NM_147187.2. [O14763-2]
DR PDB; 1D0G; X-ray; 2.40 A; R/S/T=54-183.
DR PDB; 1D4V; X-ray; 2.20 A; A=69-184.
DR PDB; 1DU3; X-ray; 2.20 A; A/B/C/G/H/I=54-183.
DR PDB; 1ZA3; X-ray; 3.35 A; R/S=54-183.
DR PDB; 2H9G; X-ray; 2.32 A; R/S=54-183.
DR PDB; 3X3F; X-ray; 2.10 A; A=54-184.
DR PDB; 4I9X; X-ray; 2.10 A; C/D=58-184.
DR PDB; 4N90; X-ray; 3.30 A; R/S/T=57-182.
DR PDB; 4OD2; X-ray; 3.20 A; S=73-183.
DR PDB; 6NHW; NMR; -; A/B/C/D/E/F=208-242.
DR PDB; 6NHY; NMR; -; A/B/C=208-242.
DR PDB; 6T3J; X-ray; 3.05 A; E/J=58-184.
DR PDBsum; 1D0G; -.
DR PDBsum; 1D4V; -.
DR PDBsum; 1DU3; -.
DR PDBsum; 1ZA3; -.
DR PDBsum; 2H9G; -.
DR PDBsum; 3X3F; -.
DR PDBsum; 4I9X; -.
DR PDBsum; 4N90; -.
DR PDBsum; 4OD2; -.
DR PDBsum; 6NHW; -.
DR PDBsum; 6NHY; -.
DR PDBsum; 6T3J; -.
DR AlphaFoldDB; O14763; -.
DR SMR; O14763; -.
DR BioGRID; 114323; 164.
DR CORUM; O14763; -.
DR DIP; DIP-33566N; -.
DR IntAct; O14763; 55.
DR MINT; O14763; -.
DR STRING; 9606.ENSP00000276431; -.
DR BindingDB; O14763; -.
DR ChEMBL; CHEMBL1075153; -.
DR DrugBank; DB05895; HGS-TR2J.
DR DrugBank; DB06599; Lexatumumab.
DR GuidetoPHARMACOLOGY; 1880; -.
DR GlyGen; O14763; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14763; -.
DR PhosphoSitePlus; O14763; -.
DR SwissPalm; O14763; -.
DR BioMuta; TNFRSF10B; -.
DR EPD; O14763; -.
DR jPOST; O14763; -.
DR MassIVE; O14763; -.
DR MaxQB; O14763; -.
DR PaxDb; O14763; -.
DR PeptideAtlas; O14763; -.
DR PRIDE; O14763; -.
DR ProteomicsDB; 48210; -. [O14763-1]
DR ProteomicsDB; 48211; -. [O14763-2]
DR ProteomicsDB; 48212; -. [O14763-3]
DR ABCD; O14763; 52 sequenced antibodies.
DR Antibodypedia; 9665; 1282 antibodies from 48 providers.
DR DNASU; 8795; -.
DR Ensembl; ENST00000276431.9; ENSP00000276431.4; ENSG00000120889.13. [O14763-1]
DR Ensembl; ENST00000347739.3; ENSP00000317859.3; ENSG00000120889.13. [O14763-2]
DR GeneID; 8795; -.
DR KEGG; hsa:8795; -.
DR MANE-Select; ENST00000276431.9; ENSP00000276431.4; NM_003842.5; NP_003833.4.
DR UCSC; uc003xct.4; human. [O14763-1]
DR CTD; 8795; -.
DR DisGeNET; 8795; -.
DR GeneCards; TNFRSF10B; -.
DR HGNC; HGNC:11905; TNFRSF10B.
DR HPA; ENSG00000120889; Low tissue specificity.
DR MalaCards; TNFRSF10B; -.
DR MIM; 275355; phenotype.
DR MIM; 603612; gene.
DR neXtProt; NX_O14763; -.
DR OpenTargets; ENSG00000120889; -.
DR Orphanet; 500481; Squamous cell carcinoma of salivary glands.
DR Orphanet; 494547; Squamous cell carcinoma of the hypopharynx.
DR Orphanet; 494550; Squamous cell carcinoma of the larynx.
DR Orphanet; 502366; Squamous cell carcinoma of the lip.
DR Orphanet; 500464; Squamous cell carcinoma of the nasal cavity and paranasal sinuses.
DR Orphanet; 502363; Squamous cell carcinoma of the oral cavity.
DR Orphanet; 500478; Squamous cell carcinoma of the oropharynx.
DR PharmGKB; PA36598; -.
DR VEuPathDB; HostDB:ENSG00000120889; -.
DR eggNOG; ENOG502RBEC; Eukaryota.
DR GeneTree; ENSGT00940000164765; -.
DR HOGENOM; CLU_038161_1_0_1; -.
DR InParanoid; O14763; -.
DR OMA; CQNGQDY; -.
DR PhylomeDB; O14763; -.
DR TreeFam; TF333916; -.
DR PathwayCommons; O14763; -.
DR Reactome; R-HSA-140534; Caspase activation via Death Receptors in the presence of ligand.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-3371378; Regulation by c-FLIP.
DR Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-HSA-5218900; CASP8 activity is inhibited.
DR Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands.
DR Reactome; R-HSA-69416; Dimerization of procaspase-8.
DR Reactome; R-HSA-75158; TRAIL signaling.
DR SignaLink; O14763; -.
DR SIGNOR; O14763; -.
DR BioGRID-ORCS; 8795; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; TNFRSF10B; human.
DR EvolutionaryTrace; O14763; -.
DR GeneWiki; TNFRSF10B; -.
DR GenomeRNAi; 8795; -.
DR Pharos; O14763; Tbio.
DR PRO; PR:O14763; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O14763; protein.
DR Bgee; ENSG00000120889; Expressed in cartilage tissue and 196 other tissues.
DR ExpressionAtlas; O14763; baseline and differential.
DR Genevisible; O14763; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0045569; F:TRAIL binding; NAS:UniProtKB.
DR GO; GO:0036463; F:TRAIL receptor activity; IDA:ARUK-UCL.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; NAS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0002357; P:defense response to tumor cell; IDA:ARUK-UCL.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; NAS:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IBA:GO_Central.
DR CDD; cd08315; Death_TRAILR_DR4_DR5; 1.
DR CDD; cd10580; TNFRSF10; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020465; TNFR_10.
DR InterPro; IPR034024; TNFRSF10_N.
DR InterPro; IPR034029; TNFRSF10A/B_death.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00020; TNFR_c6; 2.
DR PIRSF; PIRSF037867; CD261_antigen; 1.
DR PRINTS; PR01956; TNFACTORR10.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00208; TNFR; 2.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00652; TNFR_NGFR_1; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..55
FT /evidence="ECO:0000269|PubMed:9311998"
FT CHAIN 56..440
FT /note="Tumor necrosis factor receptor superfamily member
FT 10B"
FT /id="PRO_0000034580"
FT TOPO_DOM 56..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 57..94
FT /note="TNFR-Cys 1"
FT REPEAT 97..137
FT /note="TNFR-Cys 2"
FT REPEAT 138..178
FT /note="TNFR-Cys 3"
FT REPEAT 192..206
FT /note="TAPE"
FT DOMAIN 339..422
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 81..94
FT /evidence="ECO:0000269|PubMed:10542098,
FT ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:23555243,
FT ECO:0007744|PDB:1D0G, ECO:0007744|PDB:1D4V,
FT ECO:0007744|PDB:4I9X"
FT DISULFID 97..113
FT /evidence="ECO:0000269|PubMed:10542098,
FT ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:23555243,
FT ECO:0007744|PDB:1D0G, ECO:0007744|PDB:1D4V,
FT ECO:0007744|PDB:4I9X"
FT DISULFID 116..129
FT /evidence="ECO:0000269|PubMed:10542098,
FT ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:23555243,
FT ECO:0007744|PDB:1D0G, ECO:0007744|PDB:1D4V,
FT ECO:0007744|PDB:4I9X"
FT DISULFID 119..137
FT /evidence="ECO:0000269|PubMed:10542098,
FT ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:23555243,
FT ECO:0007744|PDB:1D0G, ECO:0007744|PDB:1D4V,
FT ECO:0007744|PDB:4I9X"
FT DISULFID 139..153
FT /evidence="ECO:0000269|PubMed:10542098,
FT ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:23555243,
FT ECO:0007744|PDB:1D0G, ECO:0007744|PDB:1D4V,
FT ECO:0007744|PDB:4I9X, ECO:0007744|PDB:4N90"
FT DISULFID 156..170
FT /evidence="ECO:0000269|PubMed:10542098,
FT ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:23555243,
FT ECO:0007744|PDB:1D0G, ECO:0007744|PDB:1D4V,
FT ECO:0007744|PDB:4I9X"
FT DISULFID 160..178
FT /evidence="ECO:0000269|PubMed:10542098,
FT ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:23555243,
FT ECO:0007744|PDB:1D0G, ECO:0007744|PDB:1D4V,
FT ECO:0007744|PDB:4I9X"
FT VAR_SEQ 119..440
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039125"
FT VAR_SEQ 185..213
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:9242610, ECO:0000303|PubMed:9242611,
FT ECO:0000303|PubMed:9285725, ECO:0000303|PubMed:9325248,
FT ECO:0000303|PubMed:9326928, ECO:0000303|PubMed:9430227,
FT ECO:0000303|Ref.10, ECO:0000303|Ref.11"
FT /id="VSP_006490"
FT VARIANT 32
FT /note="P -> L (in dbSNP:rs1129424)"
FT /evidence="ECO:0000269|PubMed:10072170,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:9242611,
FT ECO:0000269|PubMed:9285725, ECO:0000269|PubMed:9325248,
FT ECO:0000269|PubMed:9373179, ECO:0000269|PubMed:9430227,
FT ECO:0000269|Ref.11"
FT /id="VAR_016153"
FT VARIANT 67
FT /note="A -> V (in dbSNP:rs1047266)"
FT /evidence="ECO:0000269|PubMed:10072170,
FT ECO:0000269|PubMed:9285725, ECO:0000269|PubMed:9325248,
FT ECO:0000269|PubMed:9373179, ECO:0000269|PubMed:9430227,
FT ECO:0000269|Ref.11"
FT /id="VAR_016154"
FT VARIANT 191
FT /note="V -> A (in dbSNP:rs13265018)"
FT /evidence="ECO:0000269|PubMed:10072170,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9285725,
FT ECO:0000269|PubMed:9311998, ECO:0000269|PubMed:9373179"
FT /id="VAR_059831"
FT CONFLICT 439
FT /note="M -> L (in Ref. 8; AAB67103 and 12; AAQ88644)"
FT /evidence="ECO:0000305"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1D4V"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3X3F"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1D4V"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3X3F"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3X3F"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:3X3F"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3X3F"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:3X3F"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1D4V"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:3X3F"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4I9X"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4I9X"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4I9X"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1DU3"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4I9X"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:6NHW"
FT HELIX 214..236
FT /evidence="ECO:0007829|PDB:6NHW"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:6NHY"
SQ SEQUENCE 440 AA; 47878 MW; 60358EAF2A835870 CRC64;
MEQRGQNAPA ASGARKRHGP GPREARGARP GPRVPKTLVL VVAAVLLLVS AESALITQQD
LAPQQRAAPQ QKRSSPSEGL CPPGHHISED GRDCISCKYG QDYSTHWNDL LFCLRCTRCD
SGEVELSPCT TTRNTVCQCE EGTFREEDSP EMCRKCRTGC PRGMVKVGDC TPWSDIECVH
KESGTKHSGE VPAVEETVTS SPGTPASPCS LSGIIIGVTV AAVVLIVAVF VCKSLLWKKV
LPYLKGICSG GGGDPERVDR SSQRPGAEDN VLNEIVSILQ PTQVPEQEME VQEPAEPTGV
NMLSPGESEH LLEPAEAERS QRRRLLVPAN EGDPTETLRQ CFDDFADLVP FDSWEPLMRK
LGLMDNEIKV AKAEAAGHRD TLYTMLIKWV NKTGRDASVH TLLDALETLG ERLAKQKIED
HLLSSGKFMY LEGNADSAMS
