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Protein

Tumor necrosis factor receptor superfamily member 10B

Gene

Tnfrsf10b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiR-MMU-3371378. Regulation by c-FLIP.
R-MMU-5213460. RIPK1-mediated regulated necrosis.
R-MMU-5218900. CASP8 activity is inhibited.
R-MMU-69416. Dimerization of procaspase-8.
R-MMU-75158. TRAIL signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor receptor superfamily member 10B
Alternative name(s):
Death receptor 5
MK
CD_antigen: CD262
Gene namesi
Name:Tnfrsf10b
Synonyms:Dr5, Killer
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1341090. Tnfrsf10b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini53 – 180128ExtracellularSequence analysisAdd
BLAST
Transmembranei181 – 20121HelicalSequence analysisAdd
BLAST
Topological domaini202 – 381180CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5252Sequence analysisAdd
BLAST
Chaini53 – 381329Tumor necrosis factor receptor superfamily member 10BPRO_0000034581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi74 ↔ 85PROSITE-ProRule annotation
Disulfide bondi88 ↔ 105PROSITE-ProRule annotation
Disulfide bondi108 ↔ 121PROSITE-ProRule annotation
Disulfide bondi111 ↔ 129PROSITE-ProRule annotation
Disulfide bondi131 ↔ 145PROSITE-ProRule annotation
Disulfide bondi148 ↔ 161PROSITE-ProRule annotation
Disulfide bondi151 ↔ 169PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiQ9QZM4.
MaxQBiQ9QZM4.
PaxDbiQ9QZM4.
PRIDEiQ9QZM4.

PTM databases

PhosphoSiteiQ9QZM4.

Expressioni

Tissue specificityi

Highly expressed in heart, lung and kidney.

Inductioni

TNFRSF10B is regulated by the tumor suppressor p53.

Gene expression databases

BgeeiQ9QZM4.
GenevisibleiQ9QZM4. MM.

Interactioni

Subunit structurei

Homotrimer. Can interact with TRADD and RIPK1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9QZM4. 1 interaction.
STRINGi10090.ENSMUSP00000022663.

Structurei

3D structure databases

ProteinModelPortaliQ9QZM4.
SMRiQ9QZM4. Positions 68-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati26 – 8661TNFR-Cys 1Add
BLAST
Repeati87 – 12943TNFR-Cys 2Add
BLAST
Repeati130 – 16940TNFR-Cys 3Add
BLAST
Domaini273 – 35684DeathPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation
Contains 3 TNFR-Cys repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IZX0. Eukaryota.
ENOG4111ZZM. LUCA.
GeneTreeiENSGT00730000110985.
HOGENOMiHOG000142423.
HOVERGENiHBG061626.
InParanoidiQ9QZM4.
KOiK04722.
OMAiSGNGHNV.
OrthoDBiEOG71VSSN.
TreeFamiTF333916.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020465. TNFR_10.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00020. TNFR_c6. 2 hits.
[Graphical view]
PIRSFiPIRSF037867. CD261_antigen. 1 hit.
PRINTSiPR01956. TNFACTORR10.
SMARTiSM00005. DEATH. 1 hit.
SM00208. TNFR. 2 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QZM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPPGPSTPT ASAAARADHY TPGLRPLPKR RLLYSFALLL AVLQAVFVPV
60 70 80 90 100
TANPAHNRPA GLQRPEESPS RGPCLAGQYL SEGNCKPCRE GIDYTSHSNH
110 120 130 140 150
SLDSCILCTV CKEDKVVETR CNITTNTVCR CKPGTFEDKD SPEICQSCSN
160 170 180 190 200
CTDGEEELTS CTPRENRKCV SKTAWASWHK LGLWIGLLVP VVLLIGALLV
210 220 230 240 250
WKTGAWRQWL LCIKRGCERD PESANSVHSS LLDRQTSSTT NDSNHNTEPG
260 270 280 290 300
KTQKTGKKLL VPVNGNDSAD DLKFIFEYCS DIVPFDSWNR LMRQLGLTDN
310 320 330 340 350
QIQMVKAETL VTREALYQML LKWRHQTGRS ASINHLLDAL EAVEERDAME
360 370 380
KIEDYAVKSG RFTYQNAAAQ PETGPGGSQC V
Length:381
Mass (Da):42,165
Last modified:July 27, 2011 - v3
Checksum:i222531758F4ADE0A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421V → M in BAA96462 (Ref. 2) Curated
Sequence conflicti42 – 421V → M in BAA96463 (Ref. 2) Curated
Sequence conflicti97 – 971H → R in BAA96463 (Ref. 2) Curated
Sequence conflicti128 – 1281V → E in BAA96463 (Ref. 2) Curated
Sequence conflicti180 – 1801K → N in BAA96463 (Ref. 2) Curated
Sequence conflicti187 – 1871L → AT in BAA96463 (Ref. 2) Curated
Sequence conflicti215 – 2151R → RAYP in BAA96463 (Ref. 2) Curated
Sequence conflicti229 – 2291S → L in BAA96462 (Ref. 2) Curated
Sequence conflicti229 – 2291S → L in BAA96463 (Ref. 2) Curated
Sequence conflicti306 – 3061K → R in BAA96463 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176833 mRNA. Translation: AAD52656.1.
AB031081 mRNA. Translation: BAA96462.1.
AB031082 Genomic DNA. Translation: BAA96463.1.
AK050753 mRNA. Translation: BAC34404.1.
AK080069 mRNA. Translation: BAC37821.1.
AK154993 mRNA. Translation: BAE32980.1.
BC065141 mRNA. Translation: AAH65141.1.
CCDSiCCDS27243.1.
RefSeqiNP_064671.2. NM_020275.4.
UniGeneiMm.193430.

Genome annotation databases

EnsembliENSMUST00000022663; ENSMUSP00000022663; ENSMUSG00000022074.
GeneIDi21933.
KEGGimmu:21933.
UCSCiuc007umu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176833 mRNA. Translation: AAD52656.1.
AB031081 mRNA. Translation: BAA96462.1.
AB031082 Genomic DNA. Translation: BAA96463.1.
AK050753 mRNA. Translation: BAC34404.1.
AK080069 mRNA. Translation: BAC37821.1.
AK154993 mRNA. Translation: BAE32980.1.
BC065141 mRNA. Translation: AAH65141.1.
CCDSiCCDS27243.1.
RefSeqiNP_064671.2. NM_020275.4.
UniGeneiMm.193430.

3D structure databases

ProteinModelPortaliQ9QZM4.
SMRiQ9QZM4. Positions 68-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QZM4. 1 interaction.
STRINGi10090.ENSMUSP00000022663.

PTM databases

PhosphoSiteiQ9QZM4.

Proteomic databases

EPDiQ9QZM4.
MaxQBiQ9QZM4.
PaxDbiQ9QZM4.
PRIDEiQ9QZM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022663; ENSMUSP00000022663; ENSMUSG00000022074.
GeneIDi21933.
KEGGimmu:21933.
UCSCiuc007umu.2. mouse.

Organism-specific databases

CTDi8795.
MGIiMGI:1341090. Tnfrsf10b.

Phylogenomic databases

eggNOGiENOG410IZX0. Eukaryota.
ENOG4111ZZM. LUCA.
GeneTreeiENSGT00730000110985.
HOGENOMiHOG000142423.
HOVERGENiHBG061626.
InParanoidiQ9QZM4.
KOiK04722.
OMAiSGNGHNV.
OrthoDBiEOG71VSSN.
TreeFamiTF333916.

Enzyme and pathway databases

ReactomeiR-MMU-3371378. Regulation by c-FLIP.
R-MMU-5213460. RIPK1-mediated regulated necrosis.
R-MMU-5218900. CASP8 activity is inhibited.
R-MMU-69416. Dimerization of procaspase-8.
R-MMU-75158. TRAIL signaling.

Miscellaneous databases

NextBioi301528.
PROiQ9QZM4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZM4.
GenevisibleiQ9QZM4. MM.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020465. TNFR_10.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00020. TNFR_c6. 2 hits.
[Graphical view]
PIRSFiPIRSF037867. CD261_antigen. 1 hit.
PRINTSiPR01956. TNFACTORR10.
SMARTiSM00005. DEATH. 1 hit.
SM00208. TNFR. 2 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional analysis of the mouse homologue of the KILLER/DR5 tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) death receptor."
    Wu G.S., Burns T.F., Zhan Y., Alnemri E.S., El-Deiry W.S.
    Cancer Res. 59:2770-2775(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Mouse TRAIL receptor."
    Nakamura Y., Tamari M., Watanabe O.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Spleen.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Aorta, Embryo and Vein.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye.

Entry informationi

Entry nameiTR10B_MOUSE
AccessioniPrimary (citable) accession number: Q9QZM4
Secondary accession number(s): Q6GSD9, Q9JJL5, Q9JJL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.