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Protein

Tumor necrosis factor receptor superfamily member 16

Gene

NGFR

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

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

  • death receptor activity Source: Ensembl
  • Rab GTPase binding Source: UniProtKB
  • receptor activity Source: ProtInc
  • signal transducer activity Source: ProtInc
  • transmembrane signaling receptor activity Source: ProtInc
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:7809. NGFR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 250222ExtracellularSequence AnalysisAdd
BLAST
Transmembranei251 – 27222HelicalSequence AnalysisAdd
BLAST
Topological domaini273 – 427155CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31615.

Polymorphism and mutation databases

BioMutaiNGFR.
DMDMi128156.

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
Modified residuei311 – 3111Phosphoserine1 Publication

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

BgeeiP08138.
CleanExiHS_NGFR.
GenevisibleiP08138. HS.

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.
NGFP011382EBI-1387782,EBI-1028250
SALL2Q9Y4673EBI-1387782,EBI-746180

Protein-protein interaction databases

BioGridi110870. 38 interactions.
DIPiDIP-406N.
IntActiP08138. 20 interactions.
MINTiMINT-107412.
STRINGi9606.ENSP00000172229.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EWVX-ray2.60E396-412[»]
ProteinModelPortaliP08138.
SMRiP08138. Positions 32-189, 243-283, 335-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08138.

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.
GeneTreeiENSGT00730000110974.
HOGENOMiHOG000059587.
HOVERGENiHBG060431.
InParanoidiP08138.
KOiK02583.
OMAiRECTRWA.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P08138-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGAGATGRAM DGPRLLLLLL LGVSLGGAKE ACPTGLYTHS GECCKACNLG
60 70 80 90 100
EGVAQPCGAN QTVCEPCLDS VTFSDVVSAT EPCKPCTECV GLQSMSAPCV
110 120 130 140 150
EADDAVCRCA YGYYQDETTG RCEACRVCEA GSGLVFSCQD KQNTVCEECP
160 170 180 190 200
DGTYSDEANH VDPCLPCTVC EDTERQLREC TRWADAECEE IPGRWITRST
210 220 230 240 250
PPEGSDSTAP STQEPEAPPE QDLIASTVAG VVTTVMGSSQ PVVTRGTTDN
260 270 280 290 300
LIPVYCSILA AVVVGLVAYI AFKRWNSCKQ NKQGANSRPV NQTPPPEGEK
310 320 330 340 350
LHSDSGISVD SQSLHDQQPH TQTASGQALK GDGGLYSSLP PAKREEVEKL
360 370 380 390 400
LNGSAGDTWR HLAGELGYQP EHIDSFTHEA CPVRALLASW ATQDSATLDA
410 420
LLAALRRIQR ADLVESLCSE STATSPV
Length:427
Mass (Da):45,183
Last modified:August 1, 1988 - v1
Checksum:iB09FA143FB3D625B
GO
Isoform 2 (identifier: P08138-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.

Note: No experimental confirmation available.
Show »
Length:333
Mass (Da):35,767
Checksum:iFC38A7379D84CB28
GO

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9494Missing in isoform 2. 1 PublicationVSP_056850Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14764 mRNA. Translation: AAB59544.1.
AK303278 mRNA. Translation: BAG64358.1.
AK313654 mRNA. Translation: BAG36408.1.
AC006487 Genomic DNA. No translation available.
AC015656 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94677.1.
BC050309 mRNA. Translation: AAH50309.1.
M21621 Genomic DNA. Translation: AAA36363.1.
CCDSiCCDS11549.1. [P08138-1]
PIRiA25218. GQHUN.
RefSeqiNP_002498.1. NM_002507.3. [P08138-1]
UniGeneiHs.415768.
Hs.681726.

Genome annotation databases

EnsembliENST00000172229; ENSP00000172229; ENSG00000064300. [P08138-1]
ENST00000504201; ENSP00000421731; ENSG00000064300. [P08138-2]
GeneIDi4804.
KEGGihsa:4804.
UCSCiuc002ioz.4. human. [P08138-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14764 mRNA. Translation: AAB59544.1.
AK303278 mRNA. Translation: BAG64358.1.
AK313654 mRNA. Translation: BAG36408.1.
AC006487 Genomic DNA. No translation available.
AC015656 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94677.1.
BC050309 mRNA. Translation: AAH50309.1.
M21621 Genomic DNA. Translation: AAA36363.1.
CCDSiCCDS11549.1. [P08138-1]
PIRiA25218. GQHUN.
RefSeqiNP_002498.1. NM_002507.3. [P08138-1]
UniGeneiHs.415768.
Hs.681726.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EWVX-ray2.60E396-412[»]
ProteinModelPortaliP08138.
SMRiP08138. Positions 32-189, 243-283, 335-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110870. 38 interactions.
DIPiDIP-406N.
IntActiP08138. 20 interactions.
MINTiMINT-107412.
STRINGi9606.ENSP00000172229.

Chemistry

BindingDBiP08138.
ChEMBLiCHEMBL4762.
GuidetoPHARMACOLOGYi1888.

PTM databases

PhosphoSiteiP08138.
UniCarbKBiP08138.

Polymorphism and mutation databases

BioMutaiNGFR.
DMDMi128156.

Proteomic databases

MaxQBiP08138.
PaxDbiP08138.
PeptideAtlasiP08138.
PRIDEiP08138.

Protocols and materials databases

DNASUi4804.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000172229; ENSP00000172229; ENSG00000064300. [P08138-1]
ENST00000504201; ENSP00000421731; ENSG00000064300. [P08138-2]
GeneIDi4804.
KEGGihsa:4804.
UCSCiuc002ioz.4. human. [P08138-1]

Organism-specific databases

CTDi4804.
GeneCardsiGC17P047572.
HGNCiHGNC:7809. NGFR.
HPAiCAB000143.
CAB001995.
HPA004765.
MIMi162010. gene.
neXtProtiNX_P08138.
PharmGKBiPA31615.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39106.
GeneTreeiENSGT00730000110974.
HOGENOMiHOG000059587.
HOVERGENiHBG060431.
InParanoidiP08138.
KOiK02583.
OMAiRECTRWA.
OrthoDBiEOG77T14T.
PhylomeDBiP08138.
TreeFamiTF106466.

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.

Miscellaneous databases

ChiTaRSiNGFR. human.
EvolutionaryTraceiP08138.
GeneWikiiLow-affinity_nerve_growth_factor_receptor.
GenomeRNAii4804.
NextBioi18518.
PMAP-CutDBP08138.
PROiP08138.
SOURCEiSearch...

Gene expression databases

BgeeiP08138.
CleanExiHS_NGFR.
GenevisibleiP08138. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Cerebellum and Thymus.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. "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.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. Cited for: INTERACTION WITH RANBP9.
    Tissue: Brain.
  12. Cited for: FUNCTION, INTERACTION WITH LINGO1.
  13. "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.
  14. "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.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTNR16_HUMAN
AccessioniPrimary (citable) accession number: P08138
Secondary accession number(s): B2R961, B4E096
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 24, 2015
This is version 172 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.