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Protein

Tumor necrosis factor receptor superfamily member 10B

Gene

TNFRSF10B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.1 Publication

GO - Molecular functioni

  1. receptor activity Source: UniProtKB
  2. TRAIL binding Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  2. activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  3. apoptotic process Source: UniProtKB
  4. apoptotic signaling pathway Source: Reactome
  5. cell surface receptor signaling pathway Source: ProtInc
  6. cellular response to mechanical stimulus Source: UniProtKB
  7. extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
  8. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  9. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  10. regulation of apoptotic process Source: UniProtKB
  11. regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome
  12. response to endoplasmic reticulum stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_1503. Caspase-8 activation by cleavage.
REACT_164011. Regulation by c-FLIP.
REACT_402. TRAIL signaling.
REACT_832. Dimerization of procaspase-8.
SignaLinkiO14763.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor receptor superfamily member 10B
Alternative name(s):
Death receptor 5
TNF-related apoptosis-inducing ligand receptor 2
Short name:
TRAIL receptor 2
Short name:
TRAIL-R2
CD_antigen: CD262
Gene namesi
Name:TNFRSF10B
Synonyms:DR5, KILLER, TRAILR2, TRICK2, ZTNFR9
ORF Names:UNQ160/PRO186
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:11905. TNFRSF10B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini56 – 210155ExtracellularSequence AnalysisAdd
BLAST
Transmembranei211 – 23121HelicalSequence AnalysisAdd
BLAST
Topological domaini232 – 440209CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Squamous cell carcinoma of the head and neck (HNSCC)

The disease may be caused by mutations affecting the gene represented in this entry.

Disease descriptionA non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes.

See also OMIM:275355

Organism-specific databases

MIMi275355. phenotype.
Orphaneti67037. Squamous cell carcinoma of head and neck.
PharmGKBiPA36598.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 55551 PublicationAdd
BLAST
Chaini56 – 440385Tumor necrosis factor receptor superfamily member 10BPRO_0000034580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi81 ↔ 94
Disulfide bondi97 ↔ 113
Disulfide bondi116 ↔ 129
Disulfide bondi119 ↔ 137
Disulfide bondi139 ↔ 153
Disulfide bondi156 ↔ 170
Disulfide bondi160 ↔ 178

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiO14763.
PaxDbiO14763.
PRIDEiO14763.

PTM databases

PhosphoSiteiO14763.

Expressioni

Tissue specificityi

Widely expressed in adult and fetal tissues; very highly expressed in tumor cell lines such as HeLaS3, K-562, HL-60, SW480, A-549 and G-361; highly expressed in heart, peripheral blood lymphocytes, liver, pancreas, spleen, thymus, prostate, ovary, uterus, placenta, testis, esophagus, stomach and throughout the intestinal tract; not detectable in brain.

Inductioni

By ER stress. Regulated by p53/TP53.1 Publication

Gene expression databases

BgeeiO14763.
CleanExiHS_TNFRSF10B.
ExpressionAtlasiO14763. baseline and differential.
GenevestigatoriO14763.

Organism-specific databases

HPAiHPA023625.

Interactioni

Subunit structurei

Homotrimer. 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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TNFSF10P5059121EBI-518882,EBI-495373

Protein-protein interaction databases

BioGridi114323. 49 interactions.
DIPiDIP-33566N.
IntActiO14763. 7 interactions.
MINTiMINT-109111.
STRINGi9606.ENSP00000276431.

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi77 – 793Combined sources
Beta strandi85 – 873Combined sources
Beta strandi89 – 913Combined sources
Beta strandi94 – 963Combined sources
Turni99 – 1013Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi123 – 1275Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi178 – 1803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D0GX-ray2.40R/S/T54-183[»]
1D4VX-ray2.20A69-184[»]
1DU3X-ray2.20A/B/C/G/H/I54-183[»]
1ZA3X-ray3.35R/S54-183[»]
2H9GX-ray2.32R/S54-183[»]
4I9XX-ray2.10C/D58-184[»]
4N90X-ray3.30R/S/T57-182[»]
4OD2X-ray3.20S73-183[»]
ProteinModelPortaliO14763.
SMRiO14763. Positions 75-182.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14763.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati57 – 9438TNFR-Cys 1Add
BLAST
Repeati97 – 13741TNFR-Cys 2Add
BLAST
Repeati138 – 17841TNFR-Cys 3Add
BLAST
Repeati192 – 20615TAPEAdd
BLAST
Domaini339 – 42284DeathPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi250 – 2534Poly-Gly

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

eggNOGiNOG131298.
GeneTreeiENSGT00730000110985.
HOVERGENiHBG061626.
InParanoidiO14763.
KOiK04722.
OMAiPEQEMEV.
OrthoDBiEOG71VSSN.
PhylomeDBiO14763.
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. 1 hit.
[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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: O14763-1) [UniParc]FASTAAdd to basket

Also known as: TRICK2B

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.

« Hide

        10         20         30         40         50
MEQRGQNAPA ASGARKRHGP GPREARGARP GPRVPKTLVL VVAAVLLLVS
60 70 80 90 100
AESALITQQD LAPQQRAAPQ QKRSSPSEGL CPPGHHISED GRDCISCKYG
110 120 130 140 150
QDYSTHWNDL LFCLRCTRCD SGEVELSPCT TTRNTVCQCE EGTFREEDSP
160 170 180 190 200
EMCRKCRTGC PRGMVKVGDC TPWSDIECVH KESGTKHSGE VPAVEETVTS
210 220 230 240 250
SPGTPASPCS LSGIIIGVTV AAVVLIVAVF VCKSLLWKKV LPYLKGICSG
260 270 280 290 300
GGGDPERVDR SSQRPGAEDN VLNEIVSILQ PTQVPEQEME VQEPAEPTGV
310 320 330 340 350
NMLSPGESEH LLEPAEAERS QRRRLLVPAN EGDPTETLRQ CFDDFADLVP
360 370 380 390 400
FDSWEPLMRK LGLMDNEIKV AKAEAAGHRD TLYTMLIKWV NKTGRDASVH
410 420 430 440
TLLDALETLG ERLAKQKIED HLLSSGKFMY LEGNADSAMS

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Length:440
Mass (Da):47,878
Last modified:November 30, 2010 - v2
Checksum:i60358EAF2A835870
GO
Isoform 3 (identifier: O14763-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     119-440: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:118
Mass (Da):12,793
Checksum:i6ED1332A3DF0FD39
GO
Isoform Short (identifier: O14763-2) [UniParc]FASTAAdd to basket

Also known as: TRICK2A

The sequence of this isoform differs from the canonical sequence as follows:
     185-213: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:411
Mass (Da):45,083
Checksum:i57D50020E72CC954
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti439 – 4391M → L in AAB67103 (PubMed:9242611).Curated
Sequence conflicti439 – 4391M → L in AAQ88644 (PubMed:12975309).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321P → L.10 Publications
Corresponds to variant rs1129424 [ dbSNP | Ensembl ].
VAR_016153
Natural varianti67 – 671A → V.6 Publications
Corresponds to variant rs1047266 [ dbSNP | Ensembl ].
VAR_016154
Natural varianti191 – 1911V → A.5 Publications
Corresponds to variant rs13265018 [ dbSNP | Ensembl ].
VAR_059831

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei119 – 440322Missing in isoform 3. 1 PublicationVSP_039125Add
BLAST
Alternative sequencei185 – 21329Missing in isoform Short. 9 PublicationsVSP_006490Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018657 mRNA. Translation: AAB70577.1.
AF018658 mRNA. Translation: AAB70578.1.
AF016849 mRNA. Translation: AAC51778.1.
AF016266 mRNA. Translation: AAB81180.1.
AF016268 mRNA. Translation: AAC01565.1.
AF020501 mRNA. Translation: AAB71412.1.
AF022386 mRNA. Translation: AAB71949.1.
AF012628 mRNA. Translation: AAB67109.1.
AF012535 mRNA. Translation: AAB67103.1.
AB014718 Genomic DNA. Translation: BAA33723.1.
AF153687 mRNA. Translation: AAF75587.1.
AF192548 mRNA. Translation: AAF07175.1.
AY358277 mRNA. Translation: AAQ88644.1.
BX538104 mRNA. Translation: CAD98017.1.
AC107959 Genomic DNA. No translation available.
BC001281 mRNA. Translation: AAH01281.1.
CCDSiCCDS6035.1. [O14763-1]
CCDS6036.1. [O14763-2]
RefSeqiNP_003833.4. NM_003842.4. [O14763-1]
NP_671716.2. NM_147187.2. [O14763-2]
UniGeneiHs.521456.

Genome annotation databases

EnsembliENST00000276431; ENSP00000276431; ENSG00000120889. [O14763-1]
ENST00000347739; ENSP00000317859; ENSG00000120889. [O14763-2]
GeneIDi8795.
KEGGihsa:8795.
UCSCiuc003xct.2. human. [O14763-2]
uc003xcu.2. human. [O14763-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018657 mRNA. Translation: AAB70577.1.
AF018658 mRNA. Translation: AAB70578.1.
AF016849 mRNA. Translation: AAC51778.1.
AF016266 mRNA. Translation: AAB81180.1.
AF016268 mRNA. Translation: AAC01565.1.
AF020501 mRNA. Translation: AAB71412.1.
AF022386 mRNA. Translation: AAB71949.1.
AF012628 mRNA. Translation: AAB67109.1.
AF012535 mRNA. Translation: AAB67103.1.
AB014718 Genomic DNA. Translation: BAA33723.1.
AF153687 mRNA. Translation: AAF75587.1.
AF192548 mRNA. Translation: AAF07175.1.
AY358277 mRNA. Translation: AAQ88644.1.
BX538104 mRNA. Translation: CAD98017.1.
AC107959 Genomic DNA. No translation available.
BC001281 mRNA. Translation: AAH01281.1.
CCDSiCCDS6035.1. [O14763-1]
CCDS6036.1. [O14763-2]
RefSeqiNP_003833.4. NM_003842.4. [O14763-1]
NP_671716.2. NM_147187.2. [O14763-2]
UniGeneiHs.521456.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D0GX-ray2.40R/S/T54-183[»]
1D4VX-ray2.20A69-184[»]
1DU3X-ray2.20A/B/C/G/H/I54-183[»]
1ZA3X-ray3.35R/S54-183[»]
2H9GX-ray2.32R/S54-183[»]
4I9XX-ray2.10C/D58-184[»]
4N90X-ray3.30R/S/T57-182[»]
4OD2X-ray3.20S73-183[»]
ProteinModelPortaliO14763.
SMRiO14763. Positions 75-182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114323. 49 interactions.
DIPiDIP-33566N.
IntActiO14763. 7 interactions.
MINTiMINT-109111.
STRINGi9606.ENSP00000276431.

Chemistry

ChEMBLiCHEMBL1075153.
GuidetoPHARMACOLOGYi1880.

PTM databases

PhosphoSiteiO14763.

Proteomic databases

MaxQBiO14763.
PaxDbiO14763.
PRIDEiO14763.

Protocols and materials databases

DNASUi8795.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276431; ENSP00000276431; ENSG00000120889. [O14763-1]
ENST00000347739; ENSP00000317859; ENSG00000120889. [O14763-2]
GeneIDi8795.
KEGGihsa:8795.
UCSCiuc003xct.2. human. [O14763-2]
uc003xcu.2. human. [O14763-1]

Organism-specific databases

CTDi8795.
GeneCardsiGC08M022877.
HGNCiHGNC:11905. TNFRSF10B.
HPAiHPA023625.
MIMi275355. phenotype.
603612. gene.
neXtProtiNX_O14763.
Orphaneti67037. Squamous cell carcinoma of head and neck.
PharmGKBiPA36598.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG131298.
GeneTreeiENSGT00730000110985.
HOVERGENiHBG061626.
InParanoidiO14763.
KOiK04722.
OMAiPEQEMEV.
OrthoDBiEOG71VSSN.
PhylomeDBiO14763.
TreeFamiTF333916.

Enzyme and pathway databases

ReactomeiREACT_1503. Caspase-8 activation by cleavage.
REACT_164011. Regulation by c-FLIP.
REACT_402. TRAIL signaling.
REACT_832. Dimerization of procaspase-8.
SignaLinkiO14763.

Miscellaneous databases

EvolutionaryTraceiO14763.
GeneWikiiTNFRSF10B.
GenomeRNAii8795.
NextBioi32984.
PROiO14763.
SOURCEiSearch...

Gene expression databases

BgeeiO14763.
CleanExiHS_TNFRSF10B.
ExpressionAtlasiO14763. baseline and differential.
GenevestigatoriO14763.

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. 1 hit.
[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. "TRICK2, a new alternatively spliced receptor that transduces the cytotoxic signal from TRAIL."
    Screaton G.R., Mongkolsapaya J., Xu X.-N., Cowper A.E., McMichael A.J., Bell J.I.
    Curr. Biol. 7:693-696(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), ALTERNATIVE SPLICING, VARIANTS LEU-32; VAL-67 AND ALA-191.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PROTEIN SEQUENCE OF N-TERMINUS, VARIANT ALA-191.
    Tissue: Foreskin fibroblast.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), CHARACTERIZATION, VARIANTS LEU-32; VAL-67 AND ALA-191.
    Tissue: Liver and Spleen.
  4. "Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappaB pathway."
    Chaudhary P.M., Eby M., Jasmin A., Bookwalter A., Murray J., Hood L.
    Immunity 7:821-830(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), VARIANTS LEU-32 AND VAL-67.
  5. "Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL."
    MacFarlane M., Ahmad M., Srinivasula S.M., Fernandes-Alnemri T., Cohen G.M., Alnemri E.S.
    J. Biol. Chem. 272:25417-25420(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), VARIANTS LEU-32 AND VAL-67.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    Tissue: Ovary.
  7. "An antagonist decoy receptor and a death domain-containing receptor for TRAIL."
    Pan G., Ni J., Wei Y.-F., Yu G.-L., Gentz R., Dixit V.M.
    Science 277:815-818(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), VARIANT LEU-32.
  9. "Genomic organization and mutation analyses of the DR5/TRAIL receptor 2 gene in colorectal carcinomas."
    Arai T., Akiyama Y., Okabe S., Saito K., Iwai T., Yuasa Y.
    Cancer Lett. 133:197-204(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANTS LEU-32; VAL-67 AND ALA-191.
  10. Cao X., Zhang W., Wan T.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
  11. "Homo sapiens homolog of tumor necrosis factor receptor."
    Farrah T., Vu T., Gilbert T., Gross J., O'Hara P.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), VARIANTS LEU-32 AND VAL-67.
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT), VARIANT LEU-32.
  13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT LEU-32.
    Tissue: Colon endothelium.
  14. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  15. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANTS LEU-32 AND ALA-191.
    Tissue: Cervix.
  16. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  17. "CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells."
    Yamaguchi H., Wang H.G.
    J. Biol. Chem. 279:45495-45502(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  18. Cited for: INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL141.
  19. "Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5."
    Hymowitz S.G., Christinger H.W., Fuh G., Ultsch M., O'Connell M., Kelley R.F., Ashkenazi A., de Vos A.M.
    Mol. Cell 4:563-571(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 54-183.
  20. "Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation."
    Mongkolsapaya J., Grimes J.M., Chen N., Xu X.-N., Stuart D.I., Jones E.Y., Screaton G.R.
    Nat. Struct. Biol. 6:1048-1053(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 69-184.
  21. "Structure of human cytomegalovirus UL141 binding to TRAIL-R2 reveals novel, non-canonical death receptor interactions."
    Nemcovicova I., Benedict C.A., Zajonc D.M.
    PLoS Pathog. 9:E1003224-E1003224(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 58-184, INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL141.

Entry informationi

Entry nameiTR10B_HUMAN
AccessioniPrimary (citable) accession number: O14763
Secondary accession number(s): O14720
, O15508, O15517, O15531, Q6UXM8, Q7Z360, Q9BVE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 30, 2010
Last modified: January 7, 2015
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.