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O75509

- TNR21_HUMAN

UniProt

O75509 - TNR21_HUMAN

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
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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 - Molecular functioni

    1. protein binding Source: IntAct

    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

    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

    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

    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...)2 Publications
    Disulfide bondi91 ↔ 106
    Disulfide bondi109 ↔ 123
    Disulfide bondi113 ↔ 131
    Disulfide bondi133 ↔ 144
    Glycosylationi141 – 1411N-linked (GlcNAc...)2 Publications
    Disulfide bondi150 ↔ 168
    Disulfide bondi171 ↔ 186
    Disulfide bondi192 ↔ 211
    Glycosylationi252 – 2521N-linked (GlcNAc...)2 Publications
    Glycosylationi257 – 2571N-linked (GlcNAc...)2 Publications
    Glycosylationi278 – 2781N-linked (GlcNAc...)2 Publications
    Glycosylationi289 – 2891N-linked (GlcNAc...)2 Publications
    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 – 575
    Turni59 – 613
    Beta strandi64 – 685
    Beta strandi74 – 785
    Beta strandi82 – 843
    Beta strandi87 – 904
    Beta strandi99 – 1013
    Beta strandi118 – 1214
    Beta strandi130 – 1323
    Beta strandi137 – 1404
    Beta strandi143 – 1464
    Beta strandi154 – 1585
    Beta strandi162 – 1643
    Beta strandi167 – 1704
    Beta strandi181 – 1833
    Helixi193 – 1953
    Beta strandi198 – 2014
    Beta strandi205 – 2073
    Beta strandi210 – 2123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei350 – 37021HelicalSequence AnalysisAdd
    BLAST

    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.
    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

    MGTSPSSSTA LASCSRIARR ATATMIAGSL LLLGFLSTTT AQPEQKASNL    50
    IGTYRHVDRA TGQVLTCDKC PAGTYVSEHC TNTSLRVCSS CPVGTFTRHE 100
    NGIEKCHDCS QPCPWPMIEK LPCAALTDRE CTCPPGMFQS NATCAPHTVC 150
    PVGWGVRKKG TETEDVRCKQ CARGTFSDVP SSVMKCKAYT DCLSQNLVVI 200
    KPGTKETDNV CGTLPSFSSS TSPSPGTAIF PRPEHMETHE VPSSTYVPKG 250
    MNSTESNSSA SVRPKVLSSI QEGTVPDNTS SARGKEDVNK TLPNLQVVNH 300
    QQGPHHRHIL KLLPSMEATG GEKSSTPIKG PKRGHPRQNL HKHFDINEHL 350
    PWMIVLFLLL VLVVIVVCSI RKSSRTLKKG PRQDPSAIVE KAGLKKSMTP 400
    TQNREKWIYY CNGHGIDILK LVAAQVGSQW KDIYQFLCNA SEREVAAFSN 450
    GYTADHERAY AALQHWTIRG PEASLAQLIS ALRQHRRNDV VEKIRGLMED 500
    TTQLETDKLA LPMSPSPLSP SPIPSPNAKL ENSALLTVEP SPQDKNKGFF 550
    VDESEPLLRC DSTSSGSSAL SRNGSFITKE KKDTVLRQVR LDPCDLQPIF 600
    DDMLHFLNPE ELRVIEEIPQ AEDKLDRLFE IIGVKSQEAS QTLLDSVYSH 650
    LPDLL 655
    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 138 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