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Protein

BDNF/NT-3 growth factors receptor

Gene

Ntrk2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin-dependent calcium signaling in glial cells.4 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Enzyme regulationi

The neuronal activity and the influx of calcium positively regulate the kinase activity and the internalization of the receptor which are both important for active signaling. Regulated by NGFR that may control the internalization of the receptor. NGFR may also stimulate the activation by BDNF compared to NTF3 and NTF4. SH2D1A inhibits the autophosphorylation of the receptor, and alters the recruitment and activation of downstream effectors and signaling cascades. The formation of active receptors dimers able to fully transduce the ligand-mediated signal, may be negatively regulated by the formation of inactive heterodimers with the non-catalytic isoforms.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei571 – 5711ATPPROSITE-ProRule annotation
Active sitei675 – 6751Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi543 – 5519ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • brain-derived neurotrophic factor-activated receptor activity Source: UniProtKB
  • brain-derived neurotrophic factor binding Source: UniProtKB
  • neurotrophin binding Source: UniProtKB
  • neurotrophin receptor activity Source: RGD
  • protein homodimerization activity Source: UniProtKB
  • receptor tyrosine kinase binding Source: RGD
  • transmembrane receptor protein tyrosine kinase activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • brain-derived neurotrophic factor receptor signaling pathway Source: UniProtKB
  • cellular response to brain-derived neurotrophic factor stimulus Source: RGD
  • cellular response to nerve growth factor stimulus Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • central nervous system neuron development Source: UniProtKB
  • cerebral cortex development Source: UniProtKB
  • inflammatory response Source: RGD
  • learning Source: UniProtKB
  • long-term memory Source: RGD
  • negative regulation of neuron apoptotic process Source: UniProtKB
  • neuron differentiation Source: UniProtKB
  • neuron migration Source: UniProtKB
  • neurotrophin signaling pathway Source: GOC
  • peptidyl-tyrosine phosphorylation Source: GOC
  • positive regulation of axonogenesis Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of glucocorticoid receptor signaling pathway Source: MGI
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of neuron projection development Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • positive regulation of synaptic transmission, glutamatergic Source: RGD
  • protein autophosphorylation Source: UniProtKB
  • regulation of dendrite development Source: RGD
  • regulation of GTPase activity Source: UniProtKB
  • regulation of MAPK cascade Source: UniProtKB
  • regulation of neurotransmitter secretion Source: RGD
  • response to auditory stimulus Source: RGD
  • response to light stimulus Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
BDNF/NT-3 growth factors receptor (EC:2.7.10.1)
Alternative name(s):
Neurotrophic tyrosine kinase receptor type 2
TrkB tyrosine kinase
Short name:
Trk-B
Gene namesi
Name:Ntrk2
Synonyms:Trkb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi3213. Ntrk2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 429398ExtracellularSequence analysisAdd
BLAST
Transmembranei430 – 45324HelicalSequence analysisAdd
BLAST
Topological domaini454 – 821368CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: RGD
  • axon terminus Source: RGD
  • cell surface Source: RGD
  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • dendritic spine Source: RGD
  • endosome membrane Source: UniProtKB-SubCell
  • excitatory synapse Source: RGD
  • Golgi membrane Source: Reactome
  • growth cone Source: RGD
  • integral component of plasma membrane Source: UniProtKB
  • neuronal cell body Source: RGD
  • perikaryon Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic density Source: RGD
  • presynaptic active zone Source: RGD
  • rough endoplasmic reticulum Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi515 – 5151Y → F: Loss of interaction with SHC1. 1 Publication
Mutagenesisi571 – 5711K → A: Loss of kinase activity. 1 Publication
Mutagenesisi701 – 7011Y → F: Loss of autophosphorylation and altered interaction with SHC1 and PLCG1; when associated with F-705 and F-706. 1 Publication
Mutagenesisi705 – 7051Y → F: Loss of autophosphorylation; when associated with F-701 and F-706. 2 Publications
Mutagenesisi706 – 7061Y → F: Loss of autophosphorylation; when associated with F-701 and F-705. 1 Publication

Chemistry

ChEMBLiCHEMBL1795111.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131By similarityAdd
BLAST
Chaini32 – 821790BDNF/NT-3 growth factors receptorPRO_0000016729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 38PROSITE-ProRule annotation
Disulfide bondi36 ↔ 45PROSITE-ProRule annotation
Glycosylationi67 – 671N-linked (GlcNAc...)By similarity
Glycosylationi95 – 951N-linked (GlcNAc...)By similarity
Glycosylationi121 – 1211N-linked (GlcNAc...)By similarity
Disulfide bondi152 ↔ 176PROSITE-ProRule annotation
Disulfide bondi154 ↔ 194PROSITE-ProRule annotation
Glycosylationi178 – 1781N-linked (GlcNAc...)By similarity
Glycosylationi205 – 2051N-linked (GlcNAc...)By similarity
Disulfide bondi218 ↔ 266PROSITE-ProRule annotation
Glycosylationi241 – 2411N-linked (GlcNAc...)By similarity
Glycosylationi254 – 2541N-linked (GlcNAc...)By similarity
Glycosylationi280 – 2801N-linked (GlcNAc...)By similarity
Disulfide bondi302 ↔ 345PROSITE-ProRule annotation
Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence analysis
Glycosylationi338 – 3381N-linked (GlcNAc...)By similarity
Glycosylationi411 – 4111N-linked (GlcNAc...)By similarity
Modified residuei515 – 5151Phosphotyrosine; by autocatalysisBy similarity
Modified residuei701 – 7011Phosphotyrosine; by autocatalysis1 Publication
Modified residuei705 – 7051Phosphotyrosine; by autocatalysis1 Publication
Modified residuei706 – 7061Phosphotyrosine; by autocatalysis1 Publication
Modified residuei816 – 8161Phosphotyrosine; by autocatalysis1 Publication

Post-translational modificationi

Phosphorylated. Undergoes ligand-mediated autophosphorylation that is required for interaction with SHC1 and PLCG1 and other downstream effectors. Some isoforms are not phosphorylated.2 Publications
Ubiquitinated. Undergoes polyubiquitination upon activation; regulated by NGFR. Ubiquitination regulates the internalization of the receptor (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ63604.
PRIDEiQ63604.

PTM databases

iPTMnetiQ63604.
PhosphoSiteiQ63604.
UniCarbKBiQ63604.

Expressioni

Tissue specificityi

Widely expressed in the central and peripheral nervous system. The different forms are differentially expressed in various cell types. Isoform T2 is primarily expressed in neurons.

Gene expression databases

ExpressionAtlasiQ63604. baseline and differential.
GenevisibleiQ63604. RN.

Interactioni

Subunit structurei

Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. Interacts (phosphorylated upon activation by BDNF) with SHC1; mediates SHC1 phosphorylation and activation. Interacts (phosphorylated upon activation by BDNF) with PLCG1 and/or PLCG2; mediates PLCG1 phosphorylation and activation. Interacts with SH2B1 and SH2B2. Interacts with NGFR; may regulate the ligand specificity of the receptor. Interacts (phosphorylated upon ligand-binding) with SH2D1A; regulates NTRK2. Interacts with SQSTM1 and KIDINS220. Interacts (phosphorylated upon ligand-binding) with FRS2; activates the MAPK signaling pathway.8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei515 – 5151Interaction with SHC1
Sitei705 – 7051Interaction with SH2D1A
Sitei816 – 8161Interaction with PLCG1By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PirbQ8K4V63EBI-7287667,EBI-8602514From a different organism.

GO - Molecular functioni

  • brain-derived neurotrophic factor binding Source: UniProtKB
  • neurotrophin binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor tyrosine kinase binding Source: RGD

Protein-protein interaction databases

BioGridi247131. 6 interactions.
DIPiDIP-5717N.
IntActiQ63604. 4 interactions.
MINTiMINT-1204365.
STRINGi10116.ENSRNOP00000045635.

Structurei

3D structure databases

ProteinModelPortaliQ63604.
SMRiQ63604. Positions 283-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 6130LRRNTAdd
BLAST
Repeati92 – 11322LRR 1Add
BLAST
Repeati116 – 13722LRR 2Add
BLAST
Domaini148 – 19649LRRCTAdd
BLAST
Domaini197 – 28286Ig-like C2-type 1Add
BLAST
Domaini295 – 36571Ig-like C2-type 2Add
BLAST
Domaini537 – 806270Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 2 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1026. Eukaryota.
ENOG410YGKQ. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000264255.
HOVERGENiHBG056735.
InParanoidiQ63604.
KOiK04360.
OMAiCSCEIMW.
OrthoDBiEOG7QG43C.
PhylomeDBiQ63604.
TreeFamiTF106465.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
3.80.10.10. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR000372. LRRNT.
IPR031635. NTRK_C2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR020455. Tyr_kin_neurotrophic_rcpt_2.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR020777. Tyr_kinase_NGF_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamiPF07679. I-set. 2 hits.
PF13855. LRR_8. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF16920. TPKR_C2. 1 hit.
[Graphical view]
PRINTSiPR01939. NTKRECEPTOR.
PR01941. NTKRECEPTOR2.
PR00109. TYRKINASE.
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
SSF52058. SSF52058. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform GP145-TrkB (identifier: Q63604-1) [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
MSPWPRWHGP AMARLWGLCL LVLGFWRASL ACPMSCKCST TRIWCTEPSP
60 70 80 90 100
GIVAFPRLEP NSIDPENITE ILIANQKRLE IINEDDVEAY VGLKNLTIVD
110 120 130 140 150
SGLKFVAYKA FLKNGNLRHI NFTRNKLTSL SRRHFRHLDL SDLILTGNPF
160 170 180 190 200
TCSCDIMWLK TLQETKSSPD TQDLYCLNES SKNTPLANLQ IPNCGLPSAR
210 220 230 240 250
LAAPNLTVEE GKSVTISCSV GGDPLPTLYW DVGNLVSKHM NETSHTQGSL
260 270 280 290 300
RITNISSDDS GKQISCVAEN LVGEDQDSVN LTVHFAPTIT FLESPTSDHH
310 320 330 340 350
WCIPFTVRGN PKPALQWFYN GAILNESKYI CTKIHVTNHT EYHGCLQLDN
360 370 380 390 400
PTHMNNGDYT LMAKNEYGKD ERQISAHFMG RPGVDYETNP NYPEVLYEDW
410 420 430 440 450
TTPTDIGDTT NKSNEIPSTD VADQTNREHL SVYAVVVIAS VVGFCLLVML
460 470 480 490 500
LLLKLARHSK FGMKGPASVI SNDDDSASPL HHISNGSNTP SSSEGGPDAV
510 520 530 540 550
IIGMTKIPVI ENPQYFGITN SQLKPDTFVQ HIKRHNIVLK RELGEGAFGK
560 570 580 590 600
VFLAECYNLC PEQDKILVAV KTLKDASDNA RKDFHREAEL LTNLQHEHIV
610 620 630 640 650
KFYGVCVEGD PLIMVFEYMK HGDLNKFLRA HGPDAVLMAE GNPPTELTQS
660 670 680 690 700
QMLHIAQQIA AGMVYLASQH FVHRDLATRN CLVGENLLVK IGDFGMSRDV
710 720 730 740 750
YSTDYYRVGG HTMLPIRWMP PESIMYRKFT TESDVWSLGV VLWEIFTYGK
760 770 780 790 800
QPWYQLSNNE VIECITQGRV LQRPRTCPQE VYELMLGCWQ REPHTRKNIK
810 820
NIHTLLQNLA KASPVYLDIL G
Length:821
Mass (Da):92,186
Last modified:November 1, 1996 - v1
Checksum:i0DDACDA212CDAA0E
GO
Isoform T1 (identifier: Q63604-2) [UniParc]FASTAAdd to basket

Also known as: GP95-TrkB

The sequence of this isoform differs from the canonical sequence as follows:
     466-476: PASVISNDDDS → FVLFHKIPLDG
     477-821: Missing.

Note: Non-catalytic isoform.
Show »
Length:476
Mass (Da):53,212
Checksum:i79AFCD9CA0AB13A8
GO
Isoform T2 (identifier: Q63604-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     466-474: PASVISNDD → KQKCAYFAS
     475-821: Missing.

Note: Non-catalytic isoform.
Show »
Length:474
Mass (Da):52,971
Checksum:i2A6F19237F9F692A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei466 – 47611PASVISNDDDS → FVLFHKIPLDG in isoform T1. CuratedVSP_002910Add
BLAST
Alternative sequencei466 – 4749PASVISNDD → KQKCAYFAS in isoform T2. CuratedVSP_002912
Alternative sequencei475 – 821347Missing in isoform T2. CuratedVSP_002913Add
BLAST
Alternative sequencei477 – 821345Missing in isoform T1. CuratedVSP_002911Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55291 mRNA. Translation: AAA42279.1.
M55292 mRNA. Translation: AAA42280.1.
M55293 mRNA. Translation: AAA42281.1.
PIRiA39667.
B39667.
C39667.
RefSeqiNP_001156640.1. NM_001163168.2. [Q63604-2]
NP_036863.1. NM_012731.2. [Q63604-1]
UniGeneiRn.11246.

Genome annotation databases

EnsembliENSRNOT00000042145; ENSRNOP00000045635; ENSRNOG00000018839. [Q63604-1]
ENSRNOT00000090914; ENSRNOP00000070128; ENSRNOG00000018839. [Q63604-2]
GeneIDi25054.
KEGGirno:25054.
UCSCiRGD:3213. rat. [Q63604-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55291 mRNA. Translation: AAA42279.1.
M55292 mRNA. Translation: AAA42280.1.
M55293 mRNA. Translation: AAA42281.1.
PIRiA39667.
B39667.
C39667.
RefSeqiNP_001156640.1. NM_001163168.2. [Q63604-2]
NP_036863.1. NM_012731.2. [Q63604-1]
UniGeneiRn.11246.

3D structure databases

ProteinModelPortaliQ63604.
SMRiQ63604. Positions 283-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247131. 6 interactions.
DIPiDIP-5717N.
IntActiQ63604. 4 interactions.
MINTiMINT-1204365.
STRINGi10116.ENSRNOP00000045635.

Chemistry

ChEMBLiCHEMBL1795111.

PTM databases

iPTMnetiQ63604.
PhosphoSiteiQ63604.
UniCarbKBiQ63604.

Proteomic databases

PaxDbiQ63604.
PRIDEiQ63604.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000042145; ENSRNOP00000045635; ENSRNOG00000018839. [Q63604-1]
ENSRNOT00000090914; ENSRNOP00000070128; ENSRNOG00000018839. [Q63604-2]
GeneIDi25054.
KEGGirno:25054.
UCSCiRGD:3213. rat. [Q63604-1]

Organism-specific databases

CTDi4915.
RGDi3213. Ntrk2.

Phylogenomic databases

eggNOGiKOG1026. Eukaryota.
ENOG410YGKQ. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000264255.
HOVERGENiHBG056735.
InParanoidiQ63604.
KOiK04360.
OMAiCSCEIMW.
OrthoDBiEOG7QG43C.
PhylomeDBiQ63604.
TreeFamiTF106465.

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Miscellaneous databases

NextBioi605258.
PROiQ63604.

Gene expression databases

ExpressionAtlasiQ63604. baseline and differential.
GenevisibleiQ63604. RN.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
3.80.10.10. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR000372. LRRNT.
IPR031635. NTRK_C2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR020455. Tyr_kin_neurotrophic_rcpt_2.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR020777. Tyr_kinase_NGF_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamiPF07679. I-set. 2 hits.
PF13855. LRR_8. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF16920. TPKR_C2. 1 hit.
[Graphical view]
PRINTSiPR01939. NTKRECEPTOR.
PR01941. NTKRECEPTOR2.
PR00109. TYRKINASE.
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
SSF52058. SSF52058. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "trkB, a neural receptor protein-tyrosine kinase: evidence for a full-length and two truncated receptors."
    Middlemas D.S., Lindberg R.A., Hunter T.
    Mol. Cell. Biol. 11:143-153(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Cerebellum.
  2. "The neurotrophic factors brain-derived neurotrophic factor and neurotrophin-3 are ligands for the trkB tyrosine kinase receptor."
    Soppet D., Escandon E., Maragos J., Middlemas D.S., Reid S.W., Blair J., Burton L.E., Stanton B.R., Kaplan D.R., Hunter T., Nicolics K., Parada L.F.
    Cell 65:895-903(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BDNF AND NTF3 SIGNALING, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  3. "Identification of TrkB autophosphorylation sites and evidence that phospholipase C-gamma 1 is a substrate of the TrkB receptor."
    Middlemas D.S., Meisenhelder J., Hunter T.
    J. Biol. Chem. 269:5458-5466(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-701; TYR-705; TYR-706 AND TYR-816.
  4. "Naturally occurring truncated trkB receptors have dominant inhibitory effects on brain-derived neurotrophic factor signaling."
    Eide F.F., Vining E.R., Eide B.L., Zang K., Wang X.Y., Reichardt L.F.
    J. Neurosci. 16:3123-3129(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, HOMODIMERIZATION, AUTOPHOSPHORYLATION.
  5. "Identification and characterization of novel substrates of Trk receptors in developing neurons."
    Qian X., Riccio A., Zhang Y., Ginty D.D.
    Neuron 21:1017-1029(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2B1 AND SH2B2.
  6. "Activation loop tyrosines contribute varying roles to TrkB autophosphorylation and signal transduction."
    McCarty J.H., Feinstein S.C.
    Oncogene 16:1691-1700(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL PROLIFERATION, FUNCTION IN PHOSPHORYLATION OF SHC1 AND PLCG1, AUTOPHOSPHORYLATION, INTERACTION WITH SHC1; PLCG1 AND PLCG2, MUTAGENESIS OF LYS-571; TYR-701; TYR-705 AND TYR-706.
  7. "Biochemical and functional interactions between the neurotrophin receptors trk and p75NTR."
    Bibel M., Hoppe E., Barde Y.A.
    EMBO J. 18:616-622(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NGFR.
  8. "The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation."
    Meakin S.O., MacDonald J.I.S., Gryz E.A., Kubu C.J., Verdi J.M.
    J. Biol. Chem. 274:9861-9870(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FRS2.
  9. "Brain-derived neurotrophic factor induces phosphorylation of fibroblast growth factor receptor substrate 2."
    Easton J.B., Moody N.M., Zhu X., Middlemas D.S.
    J. Biol. Chem. 274:11321-11327(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF FRS2, INTERACTION WITH SHC1, MUTAGENESIS OF TYR-515.
  10. "The TrkB-Shc site signals neuronal survival and local axon growth via MEK and P13-kinase."
    Atwal J.K., Massie B., Miller F.D., Kaplan D.R.
    Neuron 27:265-277(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AXONOGENESIS AND NEURON SURVIVAL.
  11. "Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve growth factor receptor TrkA regulates receptor trafficking and Erk5 signaling."
    Geetha T., Wooten M.W.
    J. Biol. Chem. 278:4730-4739(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1.
  12. "A unique pathway for sustained neurotrophin signaling through an ankyrin-rich membrane-spanning protein."
    Arevalo J.C., Yano H., Teng K.K., Chao M.V.
    EMBO J. 23:2358-2368(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIDINS220.
  13. "SLAM-associated protein as a potential negative regulator in Trk signaling."
    Lo K.Y., Chin W.H., Ng Y.P., Cheng A.W., Cheung Z.H., Ip N.Y.
    J. Biol. Chem. 280:41744-41752(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH SH2D1A, MUTAGENESIS OF TYR-705.

Entry informationi

Entry nameiNTRK2_RAT
AccessioniPrimary (citable) accession number: Q63604
Secondary accession number(s): Q63605, Q63606
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.