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O14763 (TR10B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processApoptosis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation 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

apoptotic process

Non-traceable author statement Ref.4. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement. Source: Reactome

cell surface receptor signaling pathway

Traceable author statement Ref.2. Source: ProtInc

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 signaling

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

regulation of apoptotic process

Non-traceable author statement Ref.18. Source: UniProtKB

regulation of extrinsic apoptotic signaling pathway in absence of ligand

Traceable author statement. Source: Reactome

response to endoplasmic reticulum stress

Inferred from direct assay Ref.17. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred by curator Ref.2. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionTRAIL binding

Non-traceable author statement Ref.3. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.18PubMed 19427028PubMed 20097879PubMed 20103630PubMed 21459798PubMed 21525171PubMed 21822306PubMed 22266862PubMed 23678861. Source: IntAct

receptor activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TNFSF10P5059121EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5555 Ref.2
Chain56 – 440385Tumor necrosis factor receptor superfamily member 10B
PRO_0000034580

Regions

Topological domain56 – 210155Extracellular Potential
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 440209Cytoplasmic Potential
Repeat57 – 9438TNFR-Cys 1
Repeat97 – 13741TNFR-Cys 2
Repeat138 – 17841TNFR-Cys 3
Repeat192 – 20615TAPE
Domain339 – 42284Death
Compositional bias250 – 2534Poly-Gly

Amino acid modifications

Disulfide bond81 ↔ 94
Disulfide bond97 ↔ 113
Disulfide bond116 ↔ 129
Disulfide bond119 ↔ 137
Disulfide bond139 ↔ 153
Disulfide bond156 ↔ 170
Disulfide bond160 ↔ 178

Natural variations

Alternative sequence119 – 440322Missing in isoform 3.
VSP_039125
Alternative sequence185 – 21329Missing in isoform Short.
VSP_006490
Natural variant321P → 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 variant671A → V. Ref.1 Ref.3 Ref.4 Ref.5 Ref.9 Ref.11
Corresponds to variant rs1047266 [ dbSNP | Ensembl ].
VAR_016154
Natural variant1911V → A. Ref.1 Ref.2 Ref.3 Ref.9 Ref.15
Corresponds to variant rs13265018 [ dbSNP | Ensembl ].
VAR_059831

Experimental info

Sequence conflict4391M → L in AAB67103. Ref.8
Sequence conflict4391M → L in AAQ88644. Ref.12

Secondary structure

............................... 440
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (TRICK2B) [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 60358EAF2A835870

FASTA44047,878
        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 

« Hide

Isoform 3 [UniParc].

Checksum: 6ED1332A3DF0FD39
Show »

FASTA11812,793
Isoform Short (TRICK2A) [UniParc].

Checksum: 57D50020E72CC954
Show »

FASTA41145,083

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS6035.1. [O14763-1]
CCDS6036.1. [O14763-2]
RefSeqNP_003833.4. NM_003842.4. [O14763-1]
NP_671716.2. NM_147187.2. [O14763-2]
UniGeneHs.521456.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO14763.
SMRO14763. Positions 75-182.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114323. 24 interactions.
DIPDIP-33566N.
IntActO14763. 6 interactions.
MINTMINT-109111.
STRING9606.ENSP00000276431.

Chemistry

ChEMBLCHEMBL1075153.
GuidetoPHARMACOLOGY1880.

PTM databases

PhosphoSiteO14763.

Proteomic databases

MaxQBO14763.
PaxDbO14763.
PRIDEO14763.

Protocols and materials databases

DNASU8795.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276431; ENSP00000276431; ENSG00000120889. [O14763-1]
ENST00000347739; ENSP00000317859; ENSG00000120889. [O14763-2]
GeneID8795.
KEGGhsa:8795.
UCSCuc003xct.2. human. [O14763-2]
uc003xcu.2. human. [O14763-1]

Organism-specific databases

CTD8795.
GeneCardsGC08M022877.
HGNCHGNC:11905. TNFRSF10B.
HPAHPA023625.
MIM275355. phenotype.
603612. gene.
neXtProtNX_O14763.
Orphanet67037. Squamous cell carcinoma of head and neck.
PharmGKBPA36598.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG131298.
HOVERGENHBG061626.
InParanoidO14763.
KOK04722.
OMAEMEVQEP.
OrthoDBEOG71VSSN.
PhylomeDBO14763.
TreeFamTF333916.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
SignaLinkO14763.

Gene expression databases

ArrayExpressO14763.
BgeeO14763.
CleanExHS_TNFRSF10B.
GenevestigatorO14763.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020465. TNFR_10.
[Graphical view]
PfamPF00531. Death. 1 hit.
PF00020. TNFR_c6. 1 hit.
[Graphical view]
PIRSFPIRSF037867. CD261_antigen. 1 hit.
PRINTSPR01956. TNFACTORR10.
SMARTSM00005. DEATH. 1 hit.
SM00208. TNFR. 2 hits.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO14763.
GeneWikiTNFRSF10B.
GenomeRNAi8795.
NextBio32984.
PROO14763.
SOURCESearch...

Entry information

Entry nameTR10B_HUMAN
AccessionPrimary (citable) accession number: O14763
Secondary accession number(s): O14720 expand/collapse secondary AC list , O15508, O15517, O15531, Q6UXM8, Q7Z360, Q9BVE0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries