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P08138

- TNR16_HUMAN

UniProt

P08138 - TNR16_HUMAN

Protein

Tumor necrosis factor receptor superfamily member 16

Gene

NGFR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake By similarity. Low affinity receptor which can bind to NGF, BDNF, NT-3, and NT-4. Can mediate cell survival as well as cell death of neural cells. Necessary for the circadian oscillation of the clock genes ARNTL/BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver.By similarity2 Publications

    GO - Molecular functioni

    1. death receptor activity Source: Ensembl
    2. protein binding Source: IntAct
    3. Rab GTPase binding Source: UniProtKB
    4. receptor activity Source: ProtInc
    5. signal transducer activity Source: ProtInc
    6. transmembrane signaling receptor activity Source: ProtInc
    7. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic signaling pathway Source: Reactome
    2. axon guidance Source: Ensembl
    3. central nervous system development Source: Ensembl
    4. circadian regulation of gene expression Source: UniProtKB
    5. detection of temperature stimulus Source: Ensembl
    6. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    7. glucose homeostasis Source: UniProtKB
    8. hair follicle morphogenesis Source: Ensembl
    9. intracellular protein transport Source: UniProtKB
    10. membrane protein intracellular domain proteolysis Source: Reactome
    11. negative regulation of apoptotic process Source: Reactome
    12. negative regulation of axonogenesis Source: Reactome
    13. negative regulation of cell cycle Source: Reactome
    14. negative regulation of fibroblast growth factor receptor signaling pathway Source: Ensembl
    15. negative regulation of hair follicle development Source: Ensembl
    16. nerve development Source: Ensembl
    17. neurotrophin TRK receptor signaling pathway Source: Reactome
    18. positive regulation of apoptotic process Source: Reactome
    19. positive regulation of apoptotic signaling pathway Source: Ensembl
    20. positive regulation of axonogenesis Source: Reactome
    21. positive regulation of fibroblast proliferation Source: Ensembl
    22. positive regulation of odontogenesis of dentin-containing tooth Source: Ensembl
    23. regulation of axonogenesis Source: Reactome
    24. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
    25. regulation of glucose import in response to insulin stimulus Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Receptor

    Keywords - Biological processi

    Apoptosis, Biological rhythms, Differentiation, Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_13415. p75NTR recruits signalling complexes.
    REACT_13443. Regulated proteolysis of p75NTR.
    REACT_13526. NADE modulates death signalling.
    REACT_13638. NRAGE signals death through JNK.
    REACT_13643. NRIF signals cell death from the nucleus.
    REACT_13695. p75NTR negatively regulates cell cycle via SC1.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_13724. NFG and proNGF binds to p75NTR.
    REACT_13779. Axonal growth stimulation.
    REACT_13806. Ceramide signalling.
    REACT_13815. Axonal growth inhibition (RHOA activation).
    SignaLinkiP08138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor receptor superfamily member 16
    Alternative name(s):
    Gp80-LNGFR
    Low affinity neurotrophin receptor p75NTR
    Low-affinity nerve growth factor receptor
    Short name:
    NGF receptor
    p75 ICD
    CD_antigen: CD271
    Gene namesi
    Name:NGFR
    Synonyms:TNFRSF16
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7809. NGFR.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. cytosol Source: Reactome
    3. endosome Source: Reactome
    4. extracellular region Source: Reactome
    5. integral component of plasma membrane Source: ProtInc
    6. nucleoplasm Source: Reactome
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31615.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Add
    BLAST
    Chaini29 – 427399Tumor necrosis factor receptor superfamily member 16PRO_0000034591Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 43PROSITE-ProRule annotation
    Disulfide bondi44 ↔ 57PROSITE-ProRule annotation
    Disulfide bondi47 ↔ 64PROSITE-ProRule annotation
    Glycosylationi60 – 601N-linked (GlcNAc...)CuratedCAR_000231
    Disulfide bondi67 ↔ 83PROSITE-ProRule annotation
    Disulfide bondi86 ↔ 99PROSITE-ProRule annotation
    Disulfide bondi89 ↔ 107PROSITE-ProRule annotation
    Disulfide bondi109 ↔ 122PROSITE-ProRule annotation
    Disulfide bondi125 ↔ 138PROSITE-ProRule annotation
    Disulfide bondi128 ↔ 146PROSITE-ProRule annotation
    Disulfide bondi149 ↔ 164PROSITE-ProRule annotation
    Disulfide bondi167 ↔ 180PROSITE-ProRule annotation
    Disulfide bondi170 ↔ 188PROSITE-ProRule annotation

    Post-translational modificationi

    N- and O-glycosylated.
    O-linked glycans consist of Gal1-3GalNAc core elongated by 1 or 2 NeuNAc.
    Phosphorylated on serine residues.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP08138.
    PaxDbiP08138.
    PeptideAtlasiP08138.
    PRIDEiP08138.

    PTM databases

    PhosphoSiteiP08138.
    UniCarbKBiP08138.

    Miscellaneous databases

    PMAP-CutDBP08138.

    Expressioni

    Gene expression databases

    ArrayExpressiP08138.
    BgeeiP08138.
    CleanExiHS_NGFR.
    GenevestigatoriP08138.

    Organism-specific databases

    HPAiCAB000143.
    CAB001995.
    HPA004765.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Interacts with p75NTR-associated cell death executor. Interacts with TRAF2, TRAF4, TRAF6, PTPN13 and RANBP9. Interacts through TRAF6 with SQSTM1 which bridges NGFR to NTRK1. Interacts with BEX1 and NGFRAP1/BEX3. Interacts with KIDINS220 and NTRK1. Can form a ternary complex with NTRK1 and KIDINS220 and this complex is affected by the expression levels of KIDINS220. An increase in KIDINS220 expression leads to a decreased association of NGFR and NTRK1. Interacts with NTRK2; may regulate the ligand specificity of the NTRK2 receptor. Interacts (via death domain) with RAB31. Interacts with LINGO1 and NRADD. Interacts with MAGED1; the interaction antagonizes the association NGFR:NTRK1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APPP050672EBI-1387782,EBI-77613
    CD80P336813EBI-1387782,EBI-1031024
    NdnP252333EBI-1387782,EBI-1801080From a different organism.
    Ndnl2Q9CPR83EBI-1387782,EBI-5529102From a different organism.
    SALL2Q9Y4673EBI-1387782,EBI-8541433

    Protein-protein interaction databases

    BioGridi110870. 38 interactions.
    DIPiDIP-406N.
    IntActiP08138. 17 interactions.
    MINTiMINT-107412.
    STRINGi9606.ENSP00000172229.

    Structurei

    Secondary structure

    1
    427
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi398 – 40912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EWVX-ray2.60E396-412[»]
    ProteinModelPortaliP08138.
    SMRiP08138. Positions 32-189, 335-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08138.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 250222ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini273 – 427155CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei251 – 27222HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati31 – 6434TNFR-Cys 1Add
    BLAST
    Repeati66 – 10742TNFR-Cys 2Add
    BLAST
    Repeati108 – 14639TNFR-Cys 3Add
    BLAST
    Repeati148 – 18841TNFR-Cys 4Add
    BLAST
    Domaini344 – 42178DeathPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni326 – 34116Mediates interaction with KIDINS220By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi197 – 24852Ser/Thr-richAdd
    BLAST

    Domaini

    Death domain is responsible for interaction with RANBP9.
    The extracellular domain is responsible for interaction with NTRK1.By similarity

    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

    eggNOGiNOG39106.
    HOGENOMiHOG000059587.
    HOVERGENiHBG060431.
    InParanoidiP08138.
    KOiK02583.
    OMAiRQLRECT.
    OrthoDBiEOG77T14T.
    PhylomeDBiP08138.
    TreeFamiTF106466.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    InterProiIPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR022325. TNFR_16.
    [Graphical view]
    PfamiPF00531. Death. 1 hit.
    PF00020. TNFR_c6. 3 hits.
    [Graphical view]
    PRINTSiPR01966. TNFACTORR16.
    SMARTiSM00005. DEATH. 1 hit.
    SM00208. TNFR. 4 hits.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
    PS00652. TNFR_NGFR_1. 3 hits.
    PS50050. TNFR_NGFR_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08138-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAGATGRAM DGPRLLLLLL LGVSLGGAKE ACPTGLYTHS GECCKACNLG    50
    EGVAQPCGAN QTVCEPCLDS VTFSDVVSAT EPCKPCTECV GLQSMSAPCV 100
    EADDAVCRCA YGYYQDETTG RCEACRVCEA GSGLVFSCQD KQNTVCEECP 150
    DGTYSDEANH VDPCLPCTVC EDTERQLREC TRWADAECEE IPGRWITRST 200
    PPEGSDSTAP STQEPEAPPE QDLIASTVAG VVTTVMGSSQ PVVTRGTTDN 250
    LIPVYCSILA AVVVGLVAYI AFKRWNSCKQ NKQGANSRPV NQTPPPEGEK 300
    LHSDSGISVD SQSLHDQQPH TQTASGQALK GDGGLYSSLP PAKREEVEKL 350
    LNGSAGDTWR HLAGELGYQP EHIDSFTHEA CPVRALLASW ATQDSATLDA 400
    LLAALRRIQR ADLVESLCSE STATSPV 427
    Length:427
    Mass (Da):45,183
    Last modified:August 1, 1988 - v1
    Checksum:iB09FA143FB3D625B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti205 – 2051S → L.
    Corresponds to variant rs2072446 [ dbSNP | Ensembl ].
    VAR_020010

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14764 mRNA. Translation: AAB59544.1.
    AK313654 mRNA. Translation: BAG36408.1.
    CH471109 Genomic DNA. Translation: EAW94677.1.
    BC050309 mRNA. Translation: AAH50309.1.
    M21621 Genomic DNA. Translation: AAA36363.1.
    CCDSiCCDS11549.1.
    PIRiA25218. GQHUN.
    RefSeqiNP_002498.1. NM_002507.3.
    UniGeneiHs.415768.
    Hs.681726.

    Genome annotation databases

    EnsembliENST00000172229; ENSP00000172229; ENSG00000064300.
    GeneIDi4804.
    KEGGihsa:4804.
    UCSCiuc002ioz.4. human.

    Polymorphism databases

    DMDMi128156.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14764 mRNA. Translation: AAB59544.1 .
    AK313654 mRNA. Translation: BAG36408.1 .
    CH471109 Genomic DNA. Translation: EAW94677.1 .
    BC050309 mRNA. Translation: AAH50309.1 .
    M21621 Genomic DNA. Translation: AAA36363.1 .
    CCDSi CCDS11549.1.
    PIRi A25218. GQHUN.
    RefSeqi NP_002498.1. NM_002507.3.
    UniGenei Hs.415768.
    Hs.681726.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EWV X-ray 2.60 E 396-412 [» ]
    ProteinModelPortali P08138.
    SMRi P08138. Positions 32-189, 335-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110870. 38 interactions.
    DIPi DIP-406N.
    IntActi P08138. 17 interactions.
    MINTi MINT-107412.
    STRINGi 9606.ENSP00000172229.

    Chemistry

    BindingDBi P08138.
    ChEMBLi CHEMBL4762.
    GuidetoPHARMACOLOGYi 1888.

    PTM databases

    PhosphoSitei P08138.
    UniCarbKBi P08138.

    Polymorphism databases

    DMDMi 128156.

    Proteomic databases

    MaxQBi P08138.
    PaxDbi P08138.
    PeptideAtlasi P08138.
    PRIDEi P08138.

    Protocols and materials databases

    DNASUi 4804.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000172229 ; ENSP00000172229 ; ENSG00000064300 .
    GeneIDi 4804.
    KEGGi hsa:4804.
    UCSCi uc002ioz.4. human.

    Organism-specific databases

    CTDi 4804.
    GeneCardsi GC17P047572.
    HGNCi HGNC:7809. NGFR.
    HPAi CAB000143.
    CAB001995.
    HPA004765.
    MIMi 162010. gene.
    neXtProti NX_P08138.
    PharmGKBi PA31615.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39106.
    HOGENOMi HOG000059587.
    HOVERGENi HBG060431.
    InParanoidi P08138.
    KOi K02583.
    OMAi RQLRECT.
    OrthoDBi EOG77T14T.
    PhylomeDBi P08138.
    TreeFami TF106466.

    Enzyme and pathway databases

    Reactomei REACT_13415. p75NTR recruits signalling complexes.
    REACT_13443. Regulated proteolysis of p75NTR.
    REACT_13526. NADE modulates death signalling.
    REACT_13638. NRAGE signals death through JNK.
    REACT_13643. NRIF signals cell death from the nucleus.
    REACT_13695. p75NTR negatively regulates cell cycle via SC1.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_13724. NFG and proNGF binds to p75NTR.
    REACT_13779. Axonal growth stimulation.
    REACT_13806. Ceramide signalling.
    REACT_13815. Axonal growth inhibition (RHOA activation).
    SignaLinki P08138.

    Miscellaneous databases

    ChiTaRSi NGFR. human.
    EvolutionaryTracei P08138.
    GeneWikii Low-affinity_nerve_growth_factor_receptor.
    GenomeRNAii 4804.
    NextBioi 18518.
    PMAP-CutDB P08138.
    PROi P08138.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08138.
    Bgeei P08138.
    CleanExi HS_NGFR.
    Genevestigatori P08138.

    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.
    IPR022325. TNFR_16.
    [Graphical view ]
    Pfami PF00531. Death. 1 hit.
    PF00020. TNFR_c6. 3 hits.
    [Graphical view ]
    PRINTSi PR01966. TNFACTORR16.
    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. 3 hits.
    PS50050. TNFR_NGFR_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Cerebellum.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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.
    5. "A constitutive promoter directs expression of the nerve growth factor receptor gene."
      Sehgal A., Patil N., Chao M.
      Mol. Cell. Biol. 8:3160-3167(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
    6. "TRAF family proteins interact with the common neurotrophin receptor and modulate apoptosis induction."
      Ye X., Mehlen P., Rabizadeh S., VanArsdale T., Zhang H., Shin H., Wang J.J.L., Leo E., Zapata J.M., Hauser C.A., Reed J.C., Bredesen D.E.
      J. Biol. Chem. 274:30202-30208(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF2; TRAF4 AND TRAF6.
    7. "Association of the p75 neurotrophin receptor with TRAF6."
      Khursigara G., Orlinick J.R., Chao M.V.
      J. Biol. Chem. 274:2597-2600(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF6.
    8. "Functional interaction of Fas-associated phosphatase-1 (FAP-1) with p75(NTR) and their effect on NF-kappaB activation."
      Irie S., Hachiya T., Rabizadeh S., Maruyama W., Mukai J., Li Y., Reed J.C., Bredesen D.E., Sato T.A.
      FEBS Lett. 460:191-198(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPN13.
    9. "The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor."
      Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T., Barker P.A., Moscat J.
      J. Biol. Chem. 276:7709-7712(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF6 AND SQSTM1.
    10. Cited for: INTERACTION WITH RANBP9.
      Tissue: Brain.
    11. Cited for: FUNCTION, INTERACTION WITH LINGO1.
    12. "O-linked oligosaccharide on the 75-kDa neurotrophin receptor."
      Chapman B.S., Eckart M.R., Kaufman S.E., Lapointe G.R.
      J. Neurochem. 66:1707-1716(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF O-LINKED CARBOHYDRATE.
    13. "p75 neurotrophin receptor is a clock gene that regulates oscillatory components of circadian and metabolic networks."
      Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F., Sassone-Corsi P., Ptacek L.J., Akassoglou K.
      J. Neurosci. 33:10221-10234(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiTNR16_HUMAN
    AccessioniPrimary (citable) accession number: P08138
    Secondary accession number(s): B2R961
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 164 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

    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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3