O14763 (TR10B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TNFRSF10B
Synonyms:	DR5, KILLER, TRAILR2, TRICK2, ZTNFR9
ORF Names:	UNQ160/PRO186

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.17
Subunit structure	Homotrimer. Can interact with TRADD and RIPK1.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	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.
Induction	By ER stress. Regulated by p53/TP53. Ref.17
Involvement in disease	Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes. Note: The disease may be caused by mutations affecting the gene represented in this entry.
Sequence similarities	Contains 1 death domain. Contains 3 TNFR-Cys repeats.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of NF-kappaB-inducing kinase activity Non-traceable author statement PubMed 11464292Ref.4. Source: UniProtKB activation of cysteine-type endopeptidase activity involved in apoptotic process Traceable author statement. Source: Reactome cellular response to mechanical stimulus Inferred from expression pattern PubMed 19593445. Source: UniProtKB extrinsic apoptotic signaling pathway via death domain receptors Non-traceable author statement Ref.2. Source: UniProtKB intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Inferred from mutant phenotype Ref.17. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from expression pattern PubMed 12761501. Source: UniProtKB
Cellular_component	integral to membrane Inferred by curator Ref.2. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome
Molecular_function	TRAIL binding Non-traceable author statement Ref.3. Source: UniProtKB receptor activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TNFSF10	P50591	23	EBI-518882,EBI-495373

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: O14763-1)

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.

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

Isoform 3 (identifier: O14763-3)

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.

Isoform Short (identifier: O14763-2)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 55

55

Ref.2

Chain

56 – 440

385

Tumor necrosis factor receptor superfamily member 10B

PRO_0000034580

Regions

Topological domain

56 – 210

155

Extracellular Potential

Transmembrane

211 – 231

21

Helical; Potential

Topological domain

232 – 440

209

Cytoplasmic Potential

Repeat

57 – 94

38

TNFR-Cys 1

Repeat

97 – 137

41

TNFR-Cys 2

Repeat

138 – 178

41

TNFR-Cys 3

Repeat

192 – 206

15

TAPE

Domain

339 – 422

84

Death

Compositional bias

250 – 253

4

Poly-Gly

Amino acid modifications

Disulfide bond

81 ↔ 94

Disulfide bond

97 ↔ 113

Disulfide bond

116 ↔ 129

Disulfide bond

119 ↔ 137

Disulfide bond

139 ↔ 153

Disulfide bond

156 ↔ 170

Disulfide bond

160 ↔ 178

Natural variations

Alternative sequence

119 – 440

322

Missing in isoform 3.

VSP_039125

Alternative sequence

185 – 213

29

Missing in isoform Short.

VSP_006490

Natural variant

32

1

P → L. Ref.1 Ref.3 Ref.4 Ref.5 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.15
Corresponds to variant rs1129424 [ dbSNP | Ensembl ].

VAR_016153

Natural variant

67

1

A → V. Ref.1 Ref.3 Ref.4 Ref.5 Ref.9 Ref.11
Corresponds to variant rs1047266 [ dbSNP | Ensembl ].

VAR_016154

Natural variant

191

1

V → A. Ref.1 Ref.2 Ref.3 Ref.9 Ref.15
Corresponds to variant rs13265018 [ dbSNP | Ensembl ].

VAR_059831

Experimental info

Sequence conflict

439

1

M → L in AAB67103. Ref.8

Sequence conflict

439

1

M → L in AAQ88644. Ref.12

Secondary structure

1

.

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.

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440

Helix Strand Turn

Details...

Beta strand

77 – 79

3

Beta strand

85 – 87

3

Beta strand

89 – 91

3

Beta strand

94 – 96

3

Turn

99 – 101

3

Beta strand

106 – 108

3

Beta strand

110 – 112

3

Beta strand

123 – 127

5

Beta strand

131 – 133

3

Beta strand

136 – 139

4

Beta strand

144 – 146

3

Beta strand

149 – 154

6

Beta strand

165 – 168

4

Beta strand

172 – 174

3

Beta strand

177 – 179

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long (TRICK2B) [UniParc]. Last modified November 30, 2010. Version 2. Checksum: 60358EAF2A835870	FASTA	440	47,878
	10 20 30 40 50 60 MEQRGQNAPA ASGARKRHGP GPREARGARP GPRVPKTLVL VVAAVLLLVS AESALITQQD 70 80 90 100 110 120 LAPQQRAAPQ QKRSSPSEGL CPPGHHISED GRDCISCKYG QDYSTHWNDL LFCLRCTRCD 130 140 150 160 170 180 SGEVELSPCT TTRNTVCQCE EGTFREEDSP EMCRKCRTGC PRGMVKVGDC TPWSDIECVH 190 200 210 220 230 240 KESGTKHSGE VPAVEETVTS SPGTPASPCS LSGIIIGVTV AAVVLIVAVF VCKSLLWKKV 250 260 270 280 290 300 LPYLKGICSG GGGDPERVDR SSQRPGAEDN VLNEIVSILQ PTQVPEQEME VQEPAEPTGV 310 320 330 340 350 360 NMLSPGESEH LLEPAEAERS QRRRLLVPAN EGDPTETLRQ CFDDFADLVP FDSWEPLMRK 370 380 390 400 410 420 LGLMDNEIKV AKAEAAGHRD TLYTMLIKWV NKTGRDASVH TLLDALETLG ERLAKQKIED 430 440 HLLSSGKFMY LEGNADSAMS
	Isoform 3 [UniParc]. Checksum: 6ED1332A3DF0FD39	FASTA	118	12,793
	10 20 30 40 50 60 MEQRGQNAPA ASGARKRHGP GPREARGARP GPRVPKTLVL VVAAVLLLVS AESALITQQD 70 80 90 100 110 LAPQQRAAPQ QKRSSPSEGL CPPGHHISED GRDCISCKYG QDYSTHWNDL LFCLRCTR
	Isoform Short (TRICK2A) [UniParc]. Checksum: 57D50020E72CC954	FASTA	411	45,083
	10 20 30 40 50 60 MEQRGQNAPA ASGARKRHGP GPREARGARP GPRVPKTLVL VVAAVLLLVS AESALITQQD 70 80 90 100 110 120 LAPQQRAAPQ QKRSSPSEGL CPPGHHISED GRDCISCKYG QDYSTHWNDL LFCLRCTRCD 130 140 150 160 170 180 SGEVELSPCT TTRNTVCQCE EGTFREEDSP EMCRKCRTGC PRGMVKVGDC TPWSDIECVH 190 200 210 220 230 240 KESGIIIGVT VAAVVLIVAV FVCKSLLWKK VLPYLKGICS GGGGDPERVD RSSQRPGAED 250 260 270 280 290 300 NVLNEIVSIL QPTQVPEQEM EVQEPAEPTG VNMLSPGESE HLLEPAEAER SQRRRLLVPA 310 320 330 340 350 360 NEGDPTETLR QCFDDFADLV PFDSWEPLMR KLGLMDNEIK VAKAEAAGHR DTLYTMLIKW 370 380 390 400 410 VNKTGRDASV HTLLDALETL GERLAKQKIE DHLLSSGKFM YLEGNADSAM S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), ALTERNATIVE SPLICING, VARIANTS LEU-32; VAL-67 AND ALA-191.
[2]	"TRAIL-R2: a novel apoptosis-mediating receptor for TRAIL." Walczak H., Degli-Esposti M.A., Johnson R.S., Smolak P.J., Waugh J.Y., Boiani N., Timour M.S., Gerhart M.J., Schooley K.A., Smith C.A., Goodwin R.G., Rauch C.T. EMBO J. 16:5386-5397(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PROTEIN SEQUENCE OF N-TERMINUS, VARIANT ALA-191. Tissue: Foreskin fibroblast.
[3]	"Characterization of two receptors for TRAIL." Schneider P., Bodmer J.-L., Thome M., Hofmann K., Holler N., Tschopp J. FEBS Lett. 416:329-334(1997) [PubMed] [Europe PMC] [Abstract] 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(1997) [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(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), VARIANTS LEU-32 AND VAL-67.
[6]	"KILLER/DR5 is a DNA damage-inducible p53-regulated death receptor gene." Wu G.S., Burns T.F., McDonald E.R. III, Jiang W., Meng R., Krantz I.D., Kao G., Gan D.D., Zhou J.Y., Muschel R., Hamilton S.R., Spinner N.B., Markowitz S., Wu G., el-Deiry W.S. Nat. Genet. 17:141-143(1997) [PubMed] [Europe PMC] [Abstract] 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(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
[8]	"Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors." Sheridan J.P., Marsters S.A., Pitti R.M., Gurney A., Skubatch M., Baldwin D.T., Ramakrishnan L., Gray C.L., Baker K., Wood W.I., Goddard A.D., Godowski P.J., Ashkenazi A. Science 277:818-821(1997) [PubMed] [Europe PMC] [Abstract] 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(1998) [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 (MAY-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 (OCT-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), VARIANTS LEU-32 AND VAL-67.
[12]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT), VARIANT LEU-32.
[13]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] 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(2006) [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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANTS LEU-32 AND ALA-191. Tissue: Cervix.
[16]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] 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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[18]	"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(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 54-183.
[19]	"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(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 69-184.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00296379.
IPI00296380.
IPI00965817.

RefSeq

NP_003833.4. NM_003842.4.
NP_671716.2. NM_147187.2.

UniGene

Hs.521456.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D0G	X-ray	2.40	R/S/T	54-183	[»]
1D4V	X-ray	2.20	A	69-184	[»]
1DU3	X-ray	2.20	A/B/C/G/H/I	54-183	[»]
1ZA3	X-ray	3.35	R/S	54-183	[»]
2H9G	X-ray	2.32	R/S	54-183	[»]
4I9X	X-ray	2.10	C/D	58-184	[»]

ProteinModelPortal

O14763.

SMR

O14763. Positions 69-184.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33566N.

IntAct

O14763. 4 interactions.

MINT

MINT-109111.

STRING

9606.ENSP00000276431.

PTM databases

PhosphoSite

O14763.

Proteomic databases

PaxDb

O14763.

PRIDE

O14763.

Protocols and materials databases

DNASU

8795.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000276431; ENSP00000276431; ENSG00000120889.
ENST00000347739; ENSP00000317859; ENSG00000120889.

GeneID

8795.

KEGG

hsa:8795.

UCSC

uc003xct.2. human.
uc003xcu.2. human.

Organism-specific databases

CTD

8795.

GeneCards

GC08M022877.

HGNC

HGNC:11905. TNFRSF10B.

HPA

HPA023625.

MIM

275355. phenotype.
603612. gene.

neXtProt

NX_O14763.

Orphanet

67037. Squamous cell carcinoma of head and neck.

PharmGKB

PA36598.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG131298.

HOVERGEN

HBG061626.

InParanoid

O14763.

KO

K04722.

OMA

EMEVQEP.

OrthoDB

EOG476K1M.

PhylomeDB

O14763.

Enzyme and pathway databases

Pathway_Interaction_DB

trail_pathway. TRAIL signaling pathway.

Reactome

REACT_578. Apoptosis.

SignaLink

O14763.

Gene expression databases

ArrayExpress

O14763.

Bgee

O14763.

CleanEx

HS_TNFRSF10B.

Genevestigator

O14763.

GermOnline

ENSG00000120889. Homo sapiens.

Family and domain databases

Gene3D

1.10.533.10. 1 hit.

InterPro

IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020465. TNFR_10.
[Graphical view]

Pfam

PF00531. Death. 1 hit.
PF00020. TNFR_c6. 1 hit.
[Graphical view]

PIRSF

PIRSF037867. CD261_antigen. 1 hit.

PRINTS

PR01956. TNFACTORR10.

SMART

SM00005. DEATH. 1 hit.
SM00208. TNFR. 2 hits.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 1 hit.

PROSITE

PS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075153.

EvolutionaryTrace

O14763.

GenomeRNAi

8795.

NextBio

32984.

SOURCE

Search...

Entry information

Entry name

TR10B_HUMAN

Accession

Primary (citable) accession number: O14763
Secondary accession number(s): O14720 , O15508, O15517, O15531, Q6UXM8, Q7Z360, Q9BVE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	November 30, 2010
Last modified:	May 29, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.