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O75509

- TNR21_HUMAN

UniProt

O75509 - TNR21_HUMAN

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Protein

Tumor necrosis factor receptor superfamily member 21

Gene

TNFRSF21

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

Functioni

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.3 Publications

GO - Biological processi

  1. adaptive immune response Source: UniProtKB
  2. apoptotic process Source: UniProtKB
  3. B cell apoptotic process Source: UniProtKB
  4. cellular lipid metabolic process Source: Reactome
  5. cellular response to tumor necrosis factor Source: UniProtKB
  6. humoral immune response Source: UniProtKB
  7. myelination Source: UniProtKB
  8. negative regulation of B cell proliferation Source: UniProtKB
  9. negative regulation of interleukin-10 secretion Source: UniProtKB
  10. negative regulation of interleukin-13 secretion Source: UniProtKB
  11. negative regulation of interleukin-5 secretion Source: UniProtKB
  12. negative regulation of myelination Source: UniProtKB
  13. negative regulation of T cell proliferation Source: UniProtKB
  14. neuron apoptotic process Source: UniProtKB
  15. oligodendrocyte apoptotic process Source: UniProtKB
  16. regulation of oligodendrocyte differentiation Source: UniProtKB
  17. small molecule metabolic process Source: Reactome
  18. T cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Adaptive immunity, Apoptosis, Immunity

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor receptor superfamily member 21
Alternative name(s):
Death receptor 6
CD_antigen: CD358
Gene namesi
Name:TNFRSF21
Synonyms:DR6
ORF Names:UNQ437/PRO868
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:13469. TNFRSF21.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 349308ExtracellularSequence AnalysisAdd
BLAST
Transmembranei350 – 37021HelicalSequence AnalysisAdd
BLAST
Topological domaini371 – 655285CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon Source: Ensembl
  2. integral component of plasma membrane Source: UniProtKB
  3. intrinsic component of plasma membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi82 – 821N → Q: Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-252; Q-278 and Q-289. 1 Publication
Mutagenesisi141 – 1411N → Q: Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-82; Q-252; Q-278 and Q-289. 1 Publication
Mutagenesisi252 – 2521N → Q: Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-278 and Q-289. 1 Publication
Mutagenesisi257 – 2571N → Q: Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-82; Q-141; Q-252; Q-278 and Q-289. 1 Publication
Mutagenesisi278 – 2781N → 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. 1 Publication
Mutagenesisi289 – 2891N → Q: Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-278. 1 Publication
Mutagenesisi368 – 3681C → V: Abolishes palmitoylation.

Organism-specific databases

PharmGKBiPA37775.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Sequence AnalysisAdd
BLAST
Chaini42 – 655614Tumor necrosis factor receptor superfamily member 21PRO_0000034602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi67 ↔ 80
Disulfide bondi70 ↔ 88
Glycosylationi82 – 821N-linked (GlcNAc...)1 Publication
Disulfide bondi91 ↔ 106
Disulfide bondi109 ↔ 123
Disulfide bondi113 ↔ 131
Disulfide bondi133 ↔ 144
Glycosylationi141 – 1411N-linked (GlcNAc...)1 Publication
Disulfide bondi150 ↔ 168
Disulfide bondi171 ↔ 186
Disulfide bondi192 ↔ 211
Glycosylationi252 – 2521N-linked (GlcNAc...)1 Publication
Glycosylationi257 – 2571N-linked (GlcNAc...)1 Publication
Glycosylationi278 – 2781N-linked (GlcNAc...)1 Publication
Glycosylationi289 – 2891N-linked (GlcNAc...)1 Publication
Lipidationi368 – 3681S-palmitoyl cysteine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

MaxQBiO75509.
PaxDbiO75509.
PRIDEiO75509.

PTM databases

PhosphoSiteiO75509.

Expressioni

Tissue specificityi

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.3 Publications

Inductioni

Up-regulated by TNF.2 Publications

Gene expression databases

BgeeiO75509.
CleanExiHS_TNFRSF21.
GenevestigatoriO75509.

Organism-specific databases

HPAiCAB009805.
HPA006746.

Interactioni

Subunit structurei

Interacts with N-APP (By similarity). Associates with TRADD. Interacts with NGFR.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPP050673EBI-2313231,EBI-77613

Protein-protein interaction databases

BioGridi118090. 7 interactions.
DIPiDIP-53299N.
IntActiO75509. 5 interactions.
MINTiMINT-8247609.
STRINGi9606.ENSP00000296861.

Structurei

Secondary structure

1
655
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 575Combined sources
Turni59 – 613Combined sources
Beta strandi64 – 685Combined sources
Beta strandi74 – 785Combined sources
Beta strandi82 – 843Combined sources
Beta strandi87 – 904Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi137 – 1404Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi154 – 1585Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi167 – 1704Combined sources
Beta strandi181 – 1833Combined sources
Helixi193 – 1953Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi210 – 2123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO75509.
SMRiO75509. Positions 51-214, 569-655.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75509.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati50 – 8839TNFR-Cys 1Add
BLAST
Repeati90 – 13142TNFR-Cys 2Add
BLAST
Repeati133 – 16735TNFR-Cys 3Add
BLAST
Repeati170 – 21142TNFR-Cys 4Add
BLAST
Domaini415 – 49884DeathPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation
Contains 4 TNFR-Cys repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG42658.
GeneTreeiENSGT00760000119204.
HOGENOMiHOG000136852.
HOVERGENiHBG054218.
InParanoidiO75509.
KOiK05157.
OMAiTKLENST.
OrthoDBiEOG786H2Q.
PhylomeDBiO75509.
TreeFamiTF331157.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022330. TNFR_21.
[Graphical view]
PfamiPF00531. Death. 1 hit.
[Graphical view]
PRINTSiPR01971. TNFACTORR21.
SMARTiSM00005. DEATH. 1 hit.
SM00208. TNFR. 4 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O75509-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGTSPSSSTA LASCSRIARR ATATMIAGSL LLLGFLSTTT AQPEQKASNL
60 70 80 90 100
IGTYRHVDRA TGQVLTCDKC PAGTYVSEHC TNTSLRVCSS CPVGTFTRHE
110 120 130 140 150
NGIEKCHDCS QPCPWPMIEK LPCAALTDRE CTCPPGMFQS NATCAPHTVC
160 170 180 190 200
PVGWGVRKKG TETEDVRCKQ CARGTFSDVP SSVMKCKAYT DCLSQNLVVI
210 220 230 240 250
KPGTKETDNV CGTLPSFSSS TSPSPGTAIF PRPEHMETHE VPSSTYVPKG
260 270 280 290 300
MNSTESNSSA SVRPKVLSSI QEGTVPDNTS SARGKEDVNK TLPNLQVVNH
310 320 330 340 350
QQGPHHRHIL KLLPSMEATG GEKSSTPIKG PKRGHPRQNL HKHFDINEHL
360 370 380 390 400
PWMIVLFLLL VLVVIVVCSI RKSSRTLKKG PRQDPSAIVE KAGLKKSMTP
410 420 430 440 450
TQNREKWIYY CNGHGIDILK LVAAQVGSQW KDIYQFLCNA SEREVAAFSN
460 470 480 490 500
GYTADHERAY AALQHWTIRG PEASLAQLIS ALRQHRRNDV VEKIRGLMED
510 520 530 540 550
TTQLETDKLA LPMSPSPLSP SPIPSPNAKL ENSALLTVEP SPQDKNKGFF
560 570 580 590 600
VDESEPLLRC DSTSSGSSAL SRNGSFITKE KKDTVLRQVR LDPCDLQPIF
610 620 630 640 650
DDMLHFLNPE ELRVIEEIPQ AEDKLDRLFE IIGVKSQEAS QTLLDSVYSH

LPDLL
Length:655
Mass (Da):71,845
Last modified:November 1, 1998 - v1
Checksum:i48939391C4852A33
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4921.1.
RefSeqiNP_055267.1. NM_014452.4.
UniGeneiHs.443577.

Genome annotation databases

EnsembliENST00000296861; ENSP00000296861; ENSG00000146072.
GeneIDi27242.
KEGGihsa:27242.
UCSCiuc003oyv.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS4921.1.
RefSeqi NP_055267.1. NM_014452.4.
UniGenei Hs.443577.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DBH NMR - A 567-655 [» ]
3QO4 X-ray 2.20 A 42-218 [» ]
3U3P X-ray 2.09 A 42-348 [» ]
3U3Q X-ray 2.70 A 42-348 [» ]
3U3S X-ray 2.70 A 42-348 [» ]
3U3T X-ray 3.21 A 42-348 [» ]
3U3V X-ray 2.96 A 42-348 [» ]
ProteinModelPortali O75509.
SMRi O75509. Positions 51-214, 569-655.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118090. 7 interactions.
DIPi DIP-53299N.
IntActi O75509. 5 interactions.
MINTi MINT-8247609.
STRINGi 9606.ENSP00000296861.

PTM databases

PhosphoSitei O75509.

Proteomic databases

MaxQBi O75509.
PaxDbi O75509.
PRIDEi O75509.

Protocols and materials databases

DNASUi 27242.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296861 ; ENSP00000296861 ; ENSG00000146072 .
GeneIDi 27242.
KEGGi hsa:27242.
UCSCi uc003oyv.3. human.

Organism-specific databases

CTDi 27242.
GeneCardsi GC06M047246.
HGNCi HGNC:13469. TNFRSF21.
HPAi CAB009805.
HPA006746.
MIMi 605732. gene.
neXtProti NX_O75509.
PharmGKBi PA37775.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42658.
GeneTreei ENSGT00760000119204.
HOGENOMi HOG000136852.
HOVERGENi HBG054218.
InParanoidi O75509.
KOi K05157.
OMAi TKLENST.
OrthoDBi EOG786H2Q.
PhylomeDBi O75509.
TreeFami TF331157.

Enzyme and pathway databases

Reactomei REACT_116145. PPARA activates gene expression.

Miscellaneous databases

ChiTaRSi TNFRSF21. human.
EvolutionaryTracei O75509.
GeneWikii TNFRSF21.
GenomeRNAii 27242.
NextBioi 50139.
PROi O75509.
SOURCEi Search...

Gene expression databases

Bgeei O75509.
CleanExi HS_TNFRSF21.
Genevestigatori O75509.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
InterProi IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022330. TNFR_21.
[Graphical view ]
Pfami PF00531. Death. 1 hit.
[Graphical view ]
PRINTSi PR01971. TNFACTORR21.
SMARTi SM00005. DEATH. 1 hit.
SM00208. TNFR. 4 hits.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
PROSITEi PS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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.

Entry informationi

Entry nameiTNR21_HUMAN
AccessioniPrimary (citable) accession number: O75509
Secondary accession number(s): B2RDI9, Q0D2P5, Q96D86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 140 of the entry and version 1 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

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3