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O75509 (TNR21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor receptor superfamily member 21
Alternative name(s):
Death receptor 6
CD_antigen=CD358
Gene names
Name:TNFRSF21
Synonyms:DR6
ORF Names:UNQ437/PRO868
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21; this triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Negatively regulates oligodendrocyte survival, maturation and myelination. Plays a role in signaling cascades triggered by stimulation of T-cell receptors, in the adaptive immune response and in the regulation of T-cell differentiation and proliferation. Negatively regulates T-cell responses and the release of cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively regulates the production of IgG, IgM and IgM in response to antigens. May inhibit the activation of JNK in response to T-cell stimulation. Ref.1 Ref.8 Ref.9

Subunit structure

Interacts with N-APP By similarity. Associates with TRADD. Interacts with NGFR. Ref.1 Ref.10

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.7.

Tissue specificity

Detected in fetal spinal cord and in brain neurons, with higher levels in brain from Alzheimer disease patients (at protein level). Highly expressed in heart, brain, placenta, pancreas, lymph node, thymus and prostate. Detected at lower levels in lung, skeletal muscle, kidney, testis, uterus, small intestine, colon, spleen, bone marrow and fetal liver. Very low levels were found in adult liver and peripheral blood leukocytes. Ref.1 Ref.8 Ref.10

Induction

Up-regulated by TNF. Ref.7 Ref.10

Sequence similarities

Contains 1 death domain.

Contains 4 TNFR-Cys repeats.

Caution

It is uncertain whether Met-1 or Met-25 is the initiator.

Sequence caution

The sequence AAH10241.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processAdaptive immunity
Apoptosis
Immunity
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

T cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

adaptive immune response

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular response to tumor necrosis factor

Inferred from direct assay Ref.7. Source: UniProtKB

humoral immune response

Inferred from sequence or structural similarity. Source: UniProtKB

myelination

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of B cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of T cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of interleukin-10 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of interleukin-13 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of interleukin-5 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of myelination

Inferred from mutant phenotype Ref.8. Source: UniProtKB

neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

oligodendrocyte apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of oligodendrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from direct assay Ref.7. Source: UniProtKB

intrinsic component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 19225519. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP050673EBI-2313231,EBI-77613

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Potential
Chain42 – 655614Tumor necrosis factor receptor superfamily member 21
PRO_0000034602

Regions

Topological domain42 – 349308Extracellular Potential
Transmembrane350 – 37021Helical; Potential
Topological domain371 – 655285Cytoplasmic Potential
Repeat50 – 8839TNFR-Cys 1
Repeat90 – 13142TNFR-Cys 2
Repeat133 – 16735TNFR-Cys 3
Repeat170 – 21142TNFR-Cys 4
Domain415 – 49884Death

Amino acid modifications

Lipidation3681S-palmitoyl cysteine Ref.7
Glycosylation821N-linked (GlcNAc...) Ref.7
Glycosylation1411N-linked (GlcNAc...) Ref.7
Glycosylation2521N-linked (GlcNAc...) Ref.7
Glycosylation2571N-linked (GlcNAc...) Ref.7
Glycosylation2781N-linked (GlcNAc...) Ref.7
Glycosylation2891N-linked (GlcNAc...) Ref.7
Disulfide bond67 ↔ 80 Ref.12 Ref.13
Disulfide bond70 ↔ 88 Ref.12 Ref.13
Disulfide bond91 ↔ 106 Ref.12 Ref.13
Disulfide bond109 ↔ 123 Ref.12 Ref.13
Disulfide bond113 ↔ 131 Ref.12 Ref.13
Disulfide bond133 ↔ 144 Ref.12 Ref.13
Disulfide bond150 ↔ 168 Ref.12 Ref.13
Disulfide bond171 ↔ 186 Ref.12 Ref.13
Disulfide bond192 ↔ 211 Ref.12 Ref.13

Experimental info

Mutagenesis821N → Q: Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-252; Q-278 and Q-289. Ref.7
Mutagenesis1411N → Q: Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-82; Q-252; Q-278 and Q-289. Ref.7
Mutagenesis2521N → Q: Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-278 and Q-289. Ref.7
Mutagenesis2571N → Q: Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-82; Q-141; Q-252; Q-278 and Q-289. Ref.7
Mutagenesis2781N → Q: Abolishes one glycosylation site and reduces total N-glycosylation. Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-82; Q-141; Q-252; Q-257 and Q-289. Ref.7
Mutagenesis2891N → Q: Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-278. Ref.7
Mutagenesis3681C → V: Abolishes palmitoylation.

Secondary structure

....................................... 655
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75509 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 48939391C4852A33

FASTA65571,845
        10         20         30         40         50         60 
MGTSPSSSTA LASCSRIARR ATATMIAGSL LLLGFLSTTT AQPEQKASNL IGTYRHVDRA 

        70         80         90        100        110        120 
TGQVLTCDKC PAGTYVSEHC TNTSLRVCSS CPVGTFTRHE NGIEKCHDCS QPCPWPMIEK 

       130        140        150        160        170        180 
LPCAALTDRE CTCPPGMFQS NATCAPHTVC PVGWGVRKKG TETEDVRCKQ CARGTFSDVP 

       190        200        210        220        230        240 
SSVMKCKAYT DCLSQNLVVI KPGTKETDNV CGTLPSFSSS TSPSPGTAIF PRPEHMETHE 

       250        260        270        280        290        300 
VPSSTYVPKG MNSTESNSSA SVRPKVLSSI QEGTVPDNTS SARGKEDVNK TLPNLQVVNH 

       310        320        330        340        350        360 
QQGPHHRHIL KLLPSMEATG GEKSSTPIKG PKRGHPRQNL HKHFDINEHL PWMIVLFLLL 

       370        380        390        400        410        420 
VLVVIVVCSI RKSSRTLKKG PRQDPSAIVE KAGLKKSMTP TQNREKWIYY CNGHGIDILK 

       430        440        450        460        470        480 
LVAAQVGSQW KDIYQFLCNA SEREVAAFSN GYTADHERAY AALQHWTIRG PEASLAQLIS 

       490        500        510        520        530        540 
ALRQHRRNDV VEKIRGLMED TTQLETDKLA LPMSPSPLSP SPIPSPNAKL ENSALLTVEP 

       550        560        570        580        590        600 
SPQDKNKGFF VDESEPLLRC DSTSSGSSAL SRNGSFITKE KKDTVLRQVR LDPCDLQPIF 

       610        620        630        640        650 
DDMLHFLNPE ELRVIEEIPQ AEDKLDRLFE IIGVKSQEAS QTLLDSVYSH LPDLL 

« Hide

References

« Hide 'large scale' references
[1]"Identification and functional characterization of DR6, a novel death domain-containing TNF receptor."
Pan G., Bauer J.H., Haridas V., Wang S., Liu D., Yu G., Vincenz C., Aggarwal B.B., Ni J., Dixit V.M.
FEBS Lett. 431:351-356(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRADD.
[2]"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].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Brain, Colon and Eye.
[7]"Functional analysis of the posttranslational modifications of the death receptor 6."
Klima M., Zajedova J., Doubravska L., Andera L.
Biochim. Biophys. Acta 1793:1579-1587(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-82; ASN-141; ASN-252; ASN-257; ASN-278 AND ASN-289, MUTAGENESIS OF ASN-82; ASN-141; ASN-252; ASN-257; ASN-278 AND ASN-289, INDUCTION BY TNF, PALMITOYLATION AT CYS-368.
[8]"Death receptor 6 negatively regulates oligodendrocyte survival, maturation and myelination."
Mi S., Lee X., Hu Y., Ji B., Shao Z., Yang W., Huang G., Walus L., Rhodes K., Gong B.J., Miller R.H., Pepinsky R.B.
Nat. Med. 17:816-821(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[9]"Death receptor 6 induces apoptosis not through type I or type II pathways, but via a unique mitochondria-dependent pathway by interacting with Bax protein."
Zeng L., Li T., Xu D.C., Liu J., Mao G., Cui M.Z., Fu X., Xu X.
J. Biol. Chem. 287:29125-29133(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"A DR6/p75(NTR) complex is responsible for beta-amyloid-induced cortical neuron death."
Hu Y., Lee X., Shao Z., Apicco D., Huang G., Gong B.J., Pepinsky R.B., Mi S.
Cell Death Dis. 4:E579-E579(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, TISSUE SPECIFICITY, INTERACTION WITH NGFR.
[11]"Solution structure of the carboxyl-terminal CARD-like domain in human TNFR-related death receptor-6."
RIKEN structural genomics initiative (RSGI)
Submitted (DEC-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 562-655.
[12]"The crystal structure of death receptor 6 (DR6): a potential receptor of the amyloid precursor protein (APP)."
Kuester M., Kemmerzehl S., Dahms S.O., Roeser D., Than M.E.
J. Mol. Biol. 409:189-201(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 42-218, DISULFIDE BOND.
[13]"S-SAD phasing study of death receptor 6 and its solution conformation revealed by SAXS."
Ru H., Zhao L., Ding W., Jiao L., Shaw N., Liang W., Zhang L., Hung L.W., Matsugaki N., Wakatsuki S., Liu Z.J.
Acta Crystallogr. D 68:521-530(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 42-349, DISULFIDE BOND, GLYCOSYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF068868 mRNA. Translation: AAC34583.1.
AY358304 mRNA. Translation: AAQ88671.1.
AK315560 mRNA. Translation: BAG37936.1.
BT007420 mRNA. Translation: AAP36088.1.
AL096801 Genomic DNA. Translation: CAB75692.1.
BC010241 mRNA. Translation: AAH10241.1. Different initiation.
BC017730 mRNA. Translation: AAH17730.1.
BC021572 mRNA. Translation: AAH21572.1.
CCDSCCDS4921.1.
RefSeqNP_055267.1. NM_014452.4.
UniGeneHs.443577.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DBHNMR-A567-655[»]
3QO4X-ray2.20A42-218[»]
3U3PX-ray2.09A42-348[»]
3U3QX-ray2.70A42-348[»]
3U3SX-ray2.70A42-348[»]
3U3TX-ray3.21A42-348[»]
3U3VX-ray2.96A42-348[»]
ProteinModelPortalO75509.
SMRO75509. Positions 51-214, 569-655.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118090. 7 interactions.
DIPDIP-53299N.
IntActO75509. 5 interactions.
MINTMINT-8247609.
STRING9606.ENSP00000296861.

PTM databases

PhosphoSiteO75509.

Proteomic databases

MaxQBO75509.
PaxDbO75509.
PRIDEO75509.

Protocols and materials databases

DNASU27242.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296861; ENSP00000296861; ENSG00000146072.
GeneID27242.
KEGGhsa:27242.
UCSCuc003oyv.3. human.

Organism-specific databases

CTD27242.
GeneCardsGC06M047246.
HGNCHGNC:13469. TNFRSF21.
HPACAB009805.
HPA006746.
MIM605732. gene.
neXtProtNX_O75509.
PharmGKBPA37775.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42658.
HOGENOMHOG000136852.
HOVERGENHBG054218.
InParanoidO75509.
KOK05157.
OMATKLENST.
OrthoDBEOG786H2Q.
PhylomeDBO75509.
TreeFamTF331157.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeO75509.
CleanExHS_TNFRSF21.
GenevestigatorO75509.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022330. TNFR_21.
[Graphical view]
PfamPF00531. Death. 1 hit.
[Graphical view]
PRINTSPR01971. TNFACTORR21.
SMARTSM00005. DEATH. 1 hit.
SM00208. TNFR. 4 hits.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNFRSF21. human.
EvolutionaryTraceO75509.
GeneWikiTNFRSF21.
GenomeRNAi27242.
NextBio50139.
PROO75509.
SOURCESearch...

Entry information

Entry nameTNR21_HUMAN
AccessionPrimary (citable) accession number: O75509
Secondary accession number(s): B2RDI9, Q0D2P5, Q96D86
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 136 of the entry and version 1 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 chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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