Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00152
Entry Name
UniProt Accession
Theoretical PI
5.39
Molecular Weight
47878.31
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Tumor necrosis factor receptor superfamily member 10B
Protein Synonyms/Alias
Death receptor 5; TNF-related apoptosis-inducing ligand receptor 2; TRAIL receptor 2; TRAIL-R2; CD262;
Gene Name
TNFRSF10B
Gene Synonyms/Alias
DR5; KILLER; TRAILR2; TRICK2; ZTNFR9; UNQ160/PRO186;
Created Date
26-SEP-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
248
Canonical
LPYLKGICSGGGGDP
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
Receptor for the cytotoxic ligand TNFSF10/TRAIL. 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.
Sequence Annotation
Topological domain: 56 210 Extracellular.
Transmembrane: 211 231 Helical.
Topological domain: 232 440 Cytoplasmic.
Domain: 339 422 Death.
Protein Length
440 AA.
Protein Sequence
(Canonical)
MEQRGQNAPA ASGARKRHGP GPREARGARP GPRVPKTLVL VVAAVLLLVS AESALITQQD  60
LAPQQRAAPQ QKRSSPSEGL CPPGHHISED GRDCISCKYG QDYSTHWNDL LFCLRCTRCD  120
SGEVELSPCT TTRNTVCQCE EGTFREEDSP EMCRKCRTGC PRGMVKVGDC TPWSDIECVH  180
KESGTKHSGE VPAVEETVTS SPGTPASPCS LSGIIIGVTV AAVVLIVAVF VCKSLLWKKV  240
LPYLKGICSG GGGDPERVDR SSQRPGAEDN VLNEIVSILQ PTQVPEQEME VQEPAEPTGV  300
NMLSPGESEH LLEPAEAERS QRRRLLVPAN EGDPTETLRQ CFDDFADLVP FDSWEPLMRK  360
LGLMDNEIKV AKAEAAGHRD TLYTMLIKWV NKTGRDASVH TLLDALETLG ERLAKQKIED  420
HLLSSGKFMY LEGNADSAMS                                              440
FASTA
(Canonical)
>LipidDB-9606-00152|O14763
MEQRGQNAPAASGARKRHGPGPREARGARPGPRVPKTLVLVVAAVLLLVSAESALITQQD
LAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCD
SGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVH
KESGTKHSGEVPAVEETVTSSPGTPASPCSLSGIIIGVTVAAVVLIVAVFVCKSLLWKKV
LPYLKGICSGGGGDPERVDRSSQRPGAEDNVLNEIVSILQPTQVPEQEMEVQEPAEPTGV
NMLSPGESEHLLEPAEAERSQRRRLLVPANEGDPTETLRQCFDDFADLVPFDSWEPLMRK
LGLMDNEIKVAKAEAAGHRDTLYTMLIKWVNKTGRDASVHTLLDALETLGERLAKQKIED
HLLSSGKFMYLEGNADSAMS
Gene Ontology
GO:0016021; C:integral component of membrane; IC:UniProtKB
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0004872; F:receptor activity; NAS:UniProtKB
GO:0045569; F:TRAIL binding; NAS:UniProtKB
GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome
GO:0007250; P:activation of NF-kappaB-inducing kinase activity; NAS:UniProtKB
GO:0006915; P:apoptotic process; NAS:UniProtKB
GO:0097190; P:apoptotic signaling pathway; TAS:Reactome
GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc
GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB
GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; NAS:UniProtKB
GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB
GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB
GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB
GO:2001239; P:regulation of extrinsic apoptotic signaling pathway in absence of ligand; TAS:Reactome
GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB
Interpro
InterPro; IPR011029; DEATH-like_dom
InterPro; IPR000488; Death_domain
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg
InterPro; IPR020465; TNFR_10
Pfam
Pfam; PF00531; Death;
Pfam; PF00020; TNFR_c6;
SMART
SMART; SM00005; DEATH;
SMART; SM00208; TNFR;
PROSITE
PROSITE; PS50017; DEATH_DOMAIN;
PROSITE; PS00652; TNFR_NGFR_1;
PROSITE; PS50050; TNFR_NGFR_2;
PRINTS
PRINTS; PR01956; TNFACTORR10;