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NGFR (nerve growth factor receptor)

Written2015-12Nobuyuki Tanaka
Cancer Immunobiology, Miyagi Cancer Center Research Institute;

Abstract Review on NGFR, with data on DNA, on the protein encoded, and where the gene is implicated.

(Note : for Links provided by Atlas : click)


Alias_namesnerve growth factor receptor (TNFR superfamily, member 16)
Alias_symbol (synonym)TNFRSF16
Other aliasp75(NTR)
LocusID (NCBI) 4804
Atlas_Id 41535
Location 17q21.33 Size: 19,728 bases; orientation: plus strand.  [Link to chromosome band 17q21]
Location_base_pair Starts at 49495293 and ends at 49515020 bp from pter ( according to hg19-Feb_2009)  [Mapping NGFR.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
CD248 (11q13.2) / NGFR (17q21.33)NGFR (17q21.33) / SPAG9 (17q21.33)SMURF2 (17q23.3) / NGFR (17q21.33)
SPAG9 (17q21.33) / NGFR (17q21.33)


Note NGFR is a member of the Tumor Necrosis Factor receptor (TNFR) superfamily. It serves as a low-affinity common receptor subunit for multiple neurotrohins (NGF, BDNF, NTF3 (NT-3) and NTF4 (NT-4/5)) (Tomellini et al. et al., 2014). It lacks any enzymatic activity, and mediates signals through interacting protein partners.
Transcription The transcript encodes 427 amino acids, including a signal peptide sequence.


Description Nerve growth factor receptor (NGFR) is a low affinity cell surface receptor for NGF. It is a member of the Tumor Necrosis Factor receptor (TNFR) superfamily, and thus anonymously called TNFRSF16. NGFR not only serves as a common receptor subunit for neurotrophins (NGF, BDNF, NT-3 and NT-4/5), but also binds their precursors (pro-neurotrophins), pro-NGF, pro-BDNF, pro-NT-3 and pro-NT-4/5. It also works as a co-receptor with other receptor partners, such as SORT1 (Sortilin), LINGO1 and RTN4R (Nogo receptor/NOGO-R)(Wang et al. et al., 2002; Bronfman et al. et al., 2004; Mi et al. et al., 2004; Meabon et al. et al., 2015).
NGFR consists of 427-amino-acid in overall length, and possesses an extracellular region with four 40 amino acid repeats with 6 cysteins at conserved positions followed by a serine/threonine-rich region, a single transmembrane domain, and a 155 amino acid cytoplasmic domain. The extracellular receives N- and O- glycosylations, and the cysteine-rich region conserved among the TNFR superfamily is licensing it as a similar receptor. The intracellular region lacks any catalytic domain, instead it possesses a death domain implicated in protein-protein interaction. Therefore, its signaling potential is dependent on protein-protein interactions.
NGFR receives proteolytic processing. Extracellular cleavage is mediated by ADAM17/TACE, which modifies NGFR to a smaller 28-kDa membrane-bound C-terminal fragment (p75-CTF). Further processing of p75-CTF by γ-secretase releases the intracellular domain (p75-ICD), which is implicated in cell death (Underwood et al. et al., 2008). Recent report indicates that the most abundant homotypic arrangement for NGFR is a trimer, and both of the monomers and trimers coexist (Anastasia et al. et al., 2015). In neurons, the trimers are not required for NGFR activation irrespective of ligand stimulation, whereas monomers are capable of conferring acute responses. Activation of NGFR is context-dependent, where the oligomerization status and expression amount determine the biological effect, and the trimers seem to sequester NGFR from an active form.
Expression NGFR is expressed in a wide variety of tissues, such as brain, peripheral neurons, schwann cells, liver, esophagus and oral epithelium and the mesenchyme. In development, it is expressed in neural crest stem cells, and is regarded as a neural crest stem (NCS) cell marker. NGFR is also expressed in adult tissue stem cells and cancer stem cells, derived from ectoderm, neural crest and mesoderm.
  NGFR is localized on cellular membrane, either as a monomer or a trimer. NGFR forms a receptor heterodomer complex with TrkA, TrkB and TrkC. Also, NGFR associates with cell surface receptors such as Lingo-1, NogoR and Sortilin.
Localisation NGFR is localized on the cell surface, endosomes and caveolae (Bilderback et al. et al., 1999; Huang et al. et al., 1999). It also shows cytoplasmic and nuclear localization. Intracellular domain (ICD), a cleaved product of NGFR, is present in intracellular compartments (Parkhurst et al. et al., 2010).
Function NGFR forms disulfide-linked dimers independently of ligand binding (Vilar et al. et al., 2009). Variety of functions mediated by NGFR owes to co-receptors. NGFR cooperates with tyrosine kinase receptors of neurophilins; NTRK1 (TrkA) for NGF binding, NTRK2 (TrkB) for BDNF and NT-4/5 and NTRK3 (TrkC) for NT-3. NGFR also cooperates with non-tyrosine kinase receptors, sortilin, Lingo-1 and NOGO-R. A trimetric receptor complex with Lingo-1 and NOGO-R binds RTN4 (Nogo-66), MAG (myelin associated glycoprotein) and OMG (oligodendrocyte myelin glycoprotein).
NGFR confers diverse functions to cells, which is totally dependent on cell types, differentiation status, binding to neurotrophins, neurotrophin maturation status, availability of co-receptors, accessibility to intracytoplasmic effectors, post-translation modification and cleavages. A variety of NGFR-mediated signals mediate cell proliferation and survival (Gentry et al. et al., 2000), differentiation, cell cycle progression (Chittka et al. et al., 2004), apoptosis (Rabizadeh et al. et al., 1993) (Nykjaer et al. et al., 2004), neurite outgrowth and retraction (Rabizadeh et al. et al., 1999), myelination (Notterpek et al., 2003), cell migration and invasion.
NGFR lacks its own enzymatic activity. Instead, it associates with a variety of intracellular proteins to mediate signals. TRAF2 , TRAF4 and TRAF6 mediate NF-κB activation (Khursigara et al. et al., 1999; Ye et al. et al., 1999). NGFR, through its death domain (DD), binds RIPK2 (RIP2) by a neurotrophin-dependent manner, activates NF-κB and supports Schwann cell survival (Khursigara et al. et al., 2001). Similarly, PTPN13 (Fas-associated phosphatase-1/FAP-1) and FAIM (Fas apoptosis inhibitory molecule) associate NGFR, and activates NF-κB and mediate neurite outgrowth (Irie et al. et al., 1999) (Sole et al. et al., 2004). NGFR activates RAC1, which leads to JNK activation and cell death (Harrington et al. et al., 2002). Pro-neurotrophin such as pro-BDNF activates CASP3 (Caspase-3) and JNK, leading to neuronal cell death (Charalampopoulos et al. et al., 2012). JNK is necessary but not sufficient for NGFR-mediated cell death. NGFR constitutively associates with ARHGDIA (RhoGDI), preventing its inhibition towards RHOA. RIP2 recruitment to DD and RhoGDI release from it, is mechanistically linked, and RhoGDI prevents RhoA activity upon release from NGFR. RIP2 has another competitor BEX1 for NGFR binding; BEX1 inhibits NF-κB activation and cell cycle progression. Association of MAGED1 (Neurotrophin receptor-interacting MAGE homolog/NRAGE), NGFRAP1 (p75NTR-associated cell death executor/NADE) and neurotrophin receptor interacting factor (NRIF) is related with pro-apoptotic signaling (Sasaki et al. et al., 2005; Bertrand et al. et al., 2008) (Mukai et al. et al., 2000) (Linggi et al. et al., 2005). Other binding partners include Schwann cell factor 1 (SC1) (Chittka et al. et al., 2004) and SALL2 (Pincheira et al. et al., 2009) both inducing cell cycle arrest, PARD3 (Par-3) which is involved in polarized myelination, and PDE4A4/5 implicated in enhanced cAMP degradation (Sachs et al. et al., 2007). NGFR also binds MAGI1 , which induces neurite outgrowth (Ito et al. et al., 2013). SHC1 is constitutively bound with NGFR, which may play a role in activation of phosphoinositide 3-kinase (PI3K) and Akt (protein kinase B) (Epa et al. et al., 2004). PI3K-Akt pathway supports survival of many types of cells (So et al. et al., 2013). Rab5 Family GTPases RAB5A and RAB31 directly associate with the DD of NGFR, and NGFR regulates glucose homeostasis and insulin sensitivity.
Stem cell Marker:
A variety of stem/progenitor cells express NGFR (Tomellini et al. et al., 2014). Inner cell mass of blastocysts is NGFR-positive, indicating that embryonic stem cells express NGFR. Later in the development, neural crest stem cells (NCSC) express NGFR (Schuldiner et al. et al., 2000), where three neutrophins, BDNF, NT-3 and NT-4, mediate their survival (Pyle et al. et al., 2006). NGFR also marks adult stem cells. Tissue stem cells originating from NCSCs express NGFR, and NGFR seemingly maintains their undifferentiated phenotypes and survival via NT-3(Kruger et al. et al., 2002) (Chalazonitis et al., 2004). Mesenchymal stem cells (MSCs) also express NGFR, where NGFR inhibits the differentiation of MSCs into osteogenic, adipogenic, chondrogenic and myogenic lineages (Mikami et al. et al., 2011). NGFR is a marker for precursors of hepatic stellate cells and portal fibloblast in the liver (Suzuki et al. et al., 2008). Likewise, keratinocyte of the basal layer of epidermis, and esophageal and oropharyngeal mucosa's basal layer cells possessing tissue stem cell properties, are NGFR-positive.

Implicated in

Entity Melanoma
Note Tumor tissues are often heterogeneous and contain a population of cells with stem-like properties, referred as cancer stem cells (CSCs). NGFR is a CSC-marker of Melanoma which arise from Melanocytes, neural crest derived cells (Boiko et al. et al., 2010). NGFR+ Melanoma CSCs are not only tumorigenic, but also prone to make metastasis.
Entity Hypopharyngeal cancer
Note Squamous cell carcinoma (SCS) is also tightly associated with NGFR. NGFR defines CSC-like cells in hypopharyngeal cancer (Imai et al. et al., 2013).
Prognosis The degree of NGFR+ cells within a tumor is significantly associated with patients' prognosis
Entity Head and neck squamous cancer and esophageal cancer
Note Squamous cell carcinoma arising in the oral cancer is also tightly associated with NGFR. Higher NGFR expression is also associated with poor prognosis of other SCCs such as esophageal, oral and head and neck cancers, suggesting its CSC-like phenotypes (Okumura et al. et al., 2006; Murillo-Sauca et al. et al., 2014).
Entity Breast cancer
Note GFR mediates breast CSC self-renewal by regulating the expression of pluripotency transcription factors (Tomellini et al. et al., 2015).


Detection of p75NTR Trimers: Implications for Receptor Stoichiometry and Activation
Anastasia A, Barker PA, Chao MV, Hempstead BL
J Neurosci 2015 Aug 26;35(34):11911-20
PMID 26311773
NRAGE, a p75NTR adaptor protein, is required for developmental apoptosis in vivo
Bertrand MJ, Kenchappa RS, Andrieu D, Leclercq-Smekens M, Nguyen HN, Carter BD, Muscatelli F, Barker PA, De Backer O
Cell Death Differ 2008 Dec;15(12):1921-9
PMID 18772898
Caveolin interacts with Trk A and p75(NTR) and regulates neurotrophin signaling pathways
Bilderback TR, Gazula VR, Lisanti MP, Dobrowsky RT
J Biol Chem 1999 Jan 1;274(1):257-63
PMID 9867838
Human melanoma-initiating cells express neural crest nerve growth factor receptor CD271
Boiko AD, Razorenova OV, van de Rijn M, Swetter SM, Johnson DL, Ly DP, Butler PD, Yang GP, Joshua B, Kaplan MJ, Longaker MT, Weissman IL
Nature 2010 Jul 1;466(7302):133-7
PMID 20596026
Multi-tasking by the p75 neurotrophin receptor: sortilin things out? EMBO Rep
Bronfman FC, Fainzilber M
2004 Sep;5(9):867-71 Review
PMID 15470383
Neurotrophin-3 in the development of the enteric nervous system
Chalazonitis A
Prog Brain Res 2004;146:243-63
PMID 14699968
Genetic dissection of neurotrophin signaling through the p75 neurotrophin receptor
Charalampopoulos I, Vicario A, Pediaditakis I, Gravanis A, Simi A, Ibáñez CF
Cell Rep 2012 Dec 27;2(6):1563-70
PMID 23260665
The p75NTR-interacting protein SC1 inhibits cell cycle progression by transcriptional repression of cyclin E
Chittka A, Arevalo JC, Rodriguez-Guzman M, Pérez P, Chao MV, Sendtner M
J Cell Biol 2004 Mar 29;164(7):985-96
PMID 15051733
The p75 neurotrophin receptor enhances TrkA signalling by binding to Shc and augmenting its phosphorylation
Epa WR, Markovska K, Barrett GL
J Neurochem 2004 Apr;89(2):344-53
PMID 15056278
Nerve growth factor activation of nuclear factor kappaB through its p75 receptor is an anti-apoptotic signal in RN22 schwannoma cells
Gentry JJ, Casaccia-Bonnefil P, Carter BD
J Biol Chem 2000 Mar 17;275(11):7558-65
PMID 10713062
Activation of Rac GTPase by p75 is necessary for c-jun N-terminal kinase-mediated apoptosis
Harrington AW, Kim JY, Yoon SO
J Neurosci 2002 Jan 1;22(1):156-66
PMID 11756498
Nerve growth factor signaling in caveolae-like domains at the plasma membrane
Huang CS, Zhou J, Feng AK, Lynch CC, Klumperman J, DeArmond SJ, Mobley WC
J Biol Chem 1999 Dec 17;274(51):36707-14
PMID 10593976
CD271 defines a stem cell-like population in hypopharyngeal cancer
Imai T, Tamai K, Oizumi S, Oyama K, Yamaguchi K, Sato I, Satoh K, Matsuura K, Saijo S, Sugamura K, Tanaka N
PLoS One 2013 Apr 23;8(4):e62002
PMID 23626764
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 JC, Bredesen DE, Sato TA
FEBS Lett 1999 Oct 29;460(2):191-8
PMID 10544233
MAGI-1 acts as a scaffolding molecule for NGF receptor-mediated signaling pathway
Ito H, Morishita R, Iwamoto I, Mizuno M, Nagata K
Biochim Biophys Acta 2013 Oct;1833(10):2302-10
PMID 23769981
A prosurvival function for the p75 receptor death domain mediated via the caspase recruitment domain receptor-interacting protein 2
Khursigara G, Bertin J, Yano H, Moffett H, DiStefano PS, Chao MV
J Neurosci 2001 Aug 15;21(16):5854-63
PMID 11487608
Neural crest stem cells persist in the adult gut but undergo changes in self-renewal, neuronal subtype potential, and factor responsiveness
Kruger GM, Mosher JT, Bixby S, Joseph N, Iwashita T, Morrison SJ
Neuron 2002 Aug 15;35(4):657-69
PMID 12194866
Neurotrophin receptor interacting factor (NRIF) is an essential mediator of apoptotic signaling by the p75 neurotrophin receptor
Linggi MS, Burke TL, Williams BB, Harrington A, Kraemer R, Hempstead BL, Yoon SO, Carter BD
J Biol Chem 2005 Apr 8;280(14):13801-8
PMID 15668238
LINGO-1 protein interacts with the p75 neurotrophin receptor in intracellular membrane compartments
Meabon JS, De Laat R, Ieguchi K, Wiley JC, Hudson MP, Bothwell M
J Biol Chem 2015 Apr 10;290(15):9511-20
PMID 25666623
LINGO-1 is a component of the Nogo-66 receptor/p75 signaling complex
Mi S, Lee X, Shao Z, Thill G, Ji B, Relton J, Levesque M, Allaire N, Perrin S, Sands B, Crowell T, Cate RL, McCoy JM, Pepinsky RB
Nat Neurosci 2004 Mar;7(3):221-8
PMID 14966521
CD271/p75(NTR) inhibits the differentiation of mesenchymal stem cells into osteogenic, adipogenic, chondrogenic, and myogenic lineages
Mikami Y, Ishii Y, Watanabe N, Shirakawa T, Suzuki S, Irie S, Isokawa K, Honda MJ
Stem Cells Dev 2011 May;20(5):901-13
PMID 21142793
NADE, a p75NTR-associated cell death executor, is involved in signal transduction mediated by the common neurotrophin receptor p75NTR
Mukai J, Hachiya T, Shoji-Hoshino S, Kimura MT, Nadano D, Suvanto P, Hanaoka T, Li Y, Irie S, Greene LA, Sato TA
J Biol Chem 2000 Jun 9;275(23):17566-70
PMID 10764727
CD271 is a functional and targetable marker of tumor-initiating cells in head and neck squamous cell carcinoma
Murillo-Sauca O, Chung MK, Shin JH, Karamboulas C, Kwok S, Jung YH, Oakley R, Tysome JR, Farnebo LO, Kaplan MJ, Sirjani D, Divi V, Holsinger FC, Tomeh C, Nichols A, Le QT, Colevas AD, Kong CS, Uppaluri R, Lewis JS Jr, Ailles LE, Sunwoo JB
Oncotarget 2014 Aug 30;5(16):6854-66
PMID 25149537
Neurotrophins in myelination: a new role for a puzzling receptor
Notterpek L
Trends Neurosci 2003 May;26(5):232-4
PMID 12744836
Sortilin is essential for proNGF-induced neuronal cell death
Nykjaer A, Lee R, Teng KK, Jansen P, Madsen P, Nielsen MS, Jacobsen C, Kliemannel M, Schwarz E, Willnow TE, Hempstead BL, Petersen CM
Nature 2004 Feb 26;427(6977):843-8
PMID 14985763
The biological role of the low-affinity p75 neurotrophin receptor in esophageal squamous cell carcinoma
Okumura T, Tsunoda S, Mori Y, Ito T, Kikuchi K, Wang TC, Yasumoto S, Shimada Y
Clin Cancer Res 2006 Sep 1;12(17):5096-103
PMID 16951226
Nuclear localization of the p75 neurotrophin receptor intracellular domain
Parkhurst CN, Zampieri N, Chao MV
J Biol Chem 2010 Feb 19;285(8):5361-8
PMID 20022966
Sall2 is a novel p75NTR-interacting protein that links NGF signalling to cell cycle progression and neurite outgrowth
Pincheira R, Baerwald M, Dunbar JD, Donner DB
EMBO J 2009 Feb 4;28(3):261-73
PMID 19131967
Neurotrophins mediate human embryonic stem cell survival
Pyle AD, Lock LF, Donovan PJ
Nat Biotechnol 2006 Mar;24(3):344-50
PMID 16444268
Neurotrophin dependence mediated by p75NTR: contrast between rescue by BDNF and NGF
Rabizadeh S, Rabizadeh S, Ye X, Wang JJ, Bredesen DE
Cell Death Differ 1999 Dec;6(12):1222-7
PMID 10637439
p75 neurotrophin receptor regulates tissue fibrosis through inhibition of plasminogen activation via a PDE4/cAMP/PKA pathway
Sachs BD, Baillie GS, McCall JR, Passino MA, Schachtrup C, Wallace DA, Dunlop AJ, MacKenzie KF, Klussmann E, Lynch MJ, Sikorski SL, Nuriel T, Tsigelny I, Zhang J, Houslay MD, Chao MV, Akassoglou K
J Cell Biol 2007 Jun 18;177(6):1119-32
PMID 17576803
RumMAGE-D the members: structure and function of a new adaptor family of MAGE-D proteins
Sasaki A, Hinck L, Watanabe K
J Recept Signal Transduct Res 2005;25(3):181-98
PMID 16194933
Effects of eight growth factors on the differentiation of cells derived from human embryonic stem cells
Schuldiner M, Yanuka O, Itskovitz-Eldor J, Melton DA, Benvenisty N
Proc Natl Acad Sci U S A 2000 Oct 10;97(21):11307-12
PMID 11027332
Regulation of PI-3-Kinase and Akt Signaling in T Lymphocytes and Other Cells by TNFR Family Molecules
So T, Croft M
Front Immunol 2013 Jun 7;4:139
PMID 23760533
The death receptor antagonist FAIM promotes neurite outgrowth by a mechanism that depends on ERK and NF-kapp B signaling
Sole C, Dolcet X, Segura MF, Gutierrez H, Diaz-Meco MT, Gozzelino R, Sanchis D, Bayascas JR, Gallego C, Moscat J, Davies AM, Comella JX
J Cell Biol 2004 Nov 8;167(3):479-92
PMID 15520226
p75 Neurotrophin receptor is a marker for precursors of stellate cells and portal fibroblasts in mouse fetal liver
Suzuki K, Tanaka M, Watanabe N, Saito S, Nonaka H, Miyajima A
Gastroenterology 2008 Jul;135(1):270-281
PMID 18515089
Nerve growth factor and proNGF simultaneously promote symmetric self-renewal, quiescence, and epithelial to mesenchymal transition to enlarge the breast cancer stem cell compartment
Tomellini E, Touil Y, Lagadec C, Julien S, Ostyn P, Ziental-Gelus N, Meignan S, Lengrand J, Adriaenssens E, Polakowska R, Le Bourhis X
Stem Cells 2015 Feb;33(2):342-53
PMID 25286822
Palmitoylation of the C-terminal fragment of p75(NTR) regulates death signaling and is required for subsequent cleavage by gamma-secretase
Underwood CK, Reid K, May LM, Bartlett PF, Coulson EJ
Mol Cell Neurosci 2008 Feb;37(2):346-58
PMID 18055214
Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers
Vilar M, Charalampopoulos I, Kenchappa RS, Simi A, Karaca E, Reversi A, Choi S, Bothwell M, Mingarro I, Friedman WJ, Schiavo G, Bastiaens PI, Verveer PJ, Carter BD, Ibáñez CF
Neuron 2009 Apr 16;62(1):72-83
PMID 19376068
P75 interacts with the Nogo receptor as a co-receptor for Nogo, MAG and OMgp
Wang KC, Kim JA, Sivasankaran R, Segal R, He Z
Nature 2002 Nov 7;420(6911):74-8
PMID 12422217
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 JJ, Leo E, Zapata J, Hauser CA, Reed JC, Bredesen DE
J Biol Chem 1999 Oct 15;274(42):30202-8
PMID 10514511


This paper should be referenced as such :
Tanaka N
NGFR (nerve growth factor receptor);
Atlas Genet Cytogenet Oncol Haematol. in press
On line version :

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 2 ]

Solid Tumors TT_t1417q24q21ID101871 TT_t1717q21q24ID102665

External links

HGNC (Hugo)NGFR   7809
Entrez_Gene (NCBI)NGFR  4804  nerve growth factor receptor
AliasesCD271; Gp80-LNGFR; TNFRSF16; p75(NTR); 
GeneCards (Weizmann)NGFR
Ensembl hg19 (Hinxton)ENSG00000064300 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000064300 [Gene_View]  ENSG00000064300 [Sequence]  chr17:49495293-49515020 [Contig_View]  NGFR [Vega]
ICGC DataPortalENSG00000064300
Genatlas (Paris)NGFR
SOURCE (Princeton)NGFR
Genetics Home Reference (NIH)NGFR
Genomic and cartography
GoldenPath hg38 (UCSC)NGFR  -     chr17:49495293-49515020 +  17q21.33   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)NGFR  -     17q21.33   [Description]    (hg19-Feb_2009)
GoldenPathNGFR - 17q21.33 [CytoView hg19]  NGFR - 17q21.33 [CytoView hg38]
Mapping of homologs : NCBINGFR [Mapview hg19]  NGFR [Mapview hg38]
Gene and transcription
Genbank (Entrez)AK303278 AK313654 BC050309 BC052797 BQ639556
RefSeq transcript (Entrez)NM_002507
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)NGFR
Alternative Splicing GalleryENSG00000064300
Gene ExpressionNGFR [ NCBI-GEO ]   NGFR [ EBI - ARRAY_EXPRESS ]   NGFR [ SEEK ]   NGFR [ MEM ]
Gene Expression Viewer (FireBrowse)NGFR [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
BioGPS (Tissue expression)4804
GTEX Portal (Tissue expression)NGFR
Human Protein AtlasENSG00000064300-NGFR [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Conserved Domain (NCBI)NGFR
DMDM Disease mutations4804
Blocks (Seattle)NGFR
Human Protein Atlas [tissue]ENSG00000064300-NGFR [tissue]
IPIIPI00027436   IPI00964934   IPI00964654   
Protein Interaction databases
Ontologies - Pathways
Huge Navigator NGFR [HugePedia]
snp3D : Map Gene to Disease4804
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD4804
Chemical/Pharm GKB GenePA31615
Clinical trialNGFR
canSAR (ICR)NGFR (select the gene name)
DataMed IndexNGFR
PubMed325 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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