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P15209

- NTRK2_MOUSE

UniProt

P15209 - NTRK2_MOUSE

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Protein

BDNF/NT-3 growth factors receptor

Gene

Ntrk2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. Isoform GP95-TRKB may also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia.9 Publications

Catalytic activityi

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

Enzyme regulationi

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 (By similarity). 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.By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei515 – 5151Interaction with SHC1
Binding sitei571 – 5711ATPPROSITE-ProRule annotation
Active sitei675 – 6751Proton acceptorPROSITE-ProRule annotation
Sitei705 – 7051Interaction with SH2D1ABy similarity
Sitei816 – 8161Interaction with PLCG1

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. brain-derived neurotrophic factor-activated receptor activity Source: UniProtKB
  3. brain-derived neurotrophic factor binding Source: UniProtKB
  4. neurotrophin binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. brain-derived neurotrophic factor receptor signaling pathway Source: UniProtKB
  3. calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  4. central nervous system neuron development Source: UniProtKB
  5. cerebral cortex development Source: UniProtKB
  6. circadian rhythm Source: UniProtKB
  7. feeding behavior Source: MGI
  8. glutamate secretion Source: MGI
  9. learning Source: UniProtKB
  10. long-term memory Source: Ensembl
  11. long-term synaptic potentiation Source: UniProtKB
  12. mechanoreceptor differentiation Source: MGI
  13. negative regulation of anoikis Source: UniProtKB
  14. negative regulation of neuron apoptotic process Source: UniProtKB
  15. neuromuscular junction development Source: MGI
  16. neuron differentiation Source: UniProtKB
  17. neuron migration Source: UniProtKB
  18. oligodendrocyte differentiation Source: UniProtKB
  19. peripheral nervous system neuron development Source: UniProtKB
  20. positive regulation of axonogenesis Source: UniProtKB
  21. positive regulation of cell proliferation Source: UniProtKB
  22. positive regulation of gene expression Source: UniProtKB
  23. positive regulation of MAPK cascade Source: UniProtKB
  24. positive regulation of neuron projection development Source: UniProtKB
  25. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  26. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
  27. protein autophosphorylation Source: UniProtKB
  28. regulation of dendrite development Source: Ensembl
  29. regulation of metabolic process Source: MGI
  30. regulation of neurotransmitter secretion Source: Ensembl
  31. regulation of protein kinase B signaling Source: UniProtKB
  32. regulation of Rac GTPase activity Source: UniProtKB
  33. response to auditory stimulus Source: Ensembl
  34. retinal rod cell development Source: MGI
  35. vasculogenesis Source: MGI
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. 3474.
ReactomeiREACT_209347. NGF-independant TRKA activation.

Names & Taxonomyi

Protein namesi
Recommended name:
BDNF/NT-3 growth factors receptor (EC:2.7.10.1)
Alternative name(s):
GP145-TrkB/GP95-TrkB
Short name:
Trk-B
Neurotrophic tyrosine kinase receptor type 2
TrkB tyrosine kinase
Gene namesi
Name:Ntrk2
Synonyms:Trkb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:97384. Ntrk2.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication
Note: Internalized to endosomes upon ligand-binding.

Topology

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

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. cytosol Source: MGI
  3. dendritic spine Source: Ensembl
  4. endosome Source: MGI
  5. excitatory synapse Source: Ensembl
  6. growth cone Source: Ensembl
  7. integral component of plasma membrane Source: UniProtKB
  8. neuronal cell body Source: Ensembl
  9. neuronal postsynaptic density Source: MGI
  10. plasma membrane Source: MGI
  11. postsynaptic membrane Source: MGI
  12. presynaptic active zone Source: Ensembl
  13. receptor complex Source: MGI
  14. terminal bouton Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice lacking isoform GP145-TRKB, the catalytic isoform, do not display feeding activity and die at P1. This is associated neuronal deficiencies in the central and the peripheral nervous systems.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi515 – 5151Y → F: Loss of interaction with SHC1. 1 Publication
Mutagenesisi816 – 8161Y → F: Loss of interaction with PLCG1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Add
BLAST
Chaini32 – 821790BDNF/NT-3 growth factors receptorPRO_0000016728Add
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; alternate1 Publication
Modified residuei515 – 5151Phosphotyrosine; by autocatalysis; alternateBy similarity
Modified residuei701 – 7011Phosphotyrosine; by autocatalysisBy similarity
Modified residuei705 – 7051Phosphotyrosine; by autocatalysisBy similarity
Modified residuei706 – 7061Phosphotyrosine; by autocatalysisBy similarity
Modified residuei816 – 8161Phosphotyrosine; by autocatalysisBy similarity

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 (By similarity).By similarity
Ubiquitinated. Undergoes polyubiquitination upon activation; regulated by NGFR. Ubiquitination regulates the internalization of the receptor.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP15209.
PaxDbiP15209.
PRIDEiP15209.

PTM databases

PhosphoSiteiP15209.

Expressioni

Tissue specificityi

Widely expressed in the central and peripheral nervous system. The different forms are differentially expressed in various cell types. Isoform GP95-TRKB is specifically expressed in glial cells.

Inductioni

Expression oscillates in a circadian manner in the liver.1 Publication

Gene expression databases

BgeeiP15209.
CleanExiMM_NTRK2.
ExpressionAtlasiP15209. baseline and differential.
GenevestigatoriP15209.

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 (By similarity). Interacts (phosphorylated upon ligand-binding) with SH2D1A; regulates NTRK2. Interacts with SQSTM1 and KIDINS220 (By similarity). Interacts (phosphorylated upon ligand-binding) with FRS2; activates the MAPK signaling pathway (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PirbQ8K4V64EBI-309647,EBI-8602514
Ptpn11P352352EBI-309647,EBI-397236

Protein-protein interaction databases

BioGridi201869. 5 interactions.
DIPiDIP-5722N.
IntActiP15209. 4 interactions.
MINTiMINT-240722.

Structurei

3D structure databases

ProteinModelPortaliP15209.
SMRiP15209. Positions 32-385, 526-821.
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
Domaini301 – 36565Ig-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

eggNOGiCOG0515.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000264255.
HOVERGENiHBG056735.
InParanoidiP15209.
KOiK04360.
OMAiCEIMWIK.
OrthoDBiEOG7QG43C.
PhylomeDBiP15209.
TreeFamiTF106465.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
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.
PF01462. LRRNT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01939. NTKRECEPTOR.
PR01941. NTKRECEPTOR2.
PR00109. TYRKINASE.
SMARTiSM00408. IGc2. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. 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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform GP145-TRKB (identifier: P15209-1) [UniParc]FASTAAdd to Basket

Also known as: L3, TrkBTK+, TRKB-FL

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
MSPWLKWHGP AMARLWGLCL LVLGFWRASL ACPTSCKCSS ARIWCTEPSP
60 70 80 90 100
GIVAFPRLEP NSVDPENITE ILIANQKRLE IINEDDVEAY VGLRNLTIVD
110 120 130 140 150
SGLKFVAYKA FLKNSNLRHI NFTRNKLTSL SRRHFRHLDL SDLILTGNPF
160 170 180 190 200
TCSCDIMWLK TLQETKSSPD TQDLYCLNES SKNMPLANLQ IPNCGLPSAR
210 220 230 240 250
LAAPNLTVEE GKSVTLSCSV 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 VADQSNREHL 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
SIHTLLQNLA KASPVYLDIL G
Length:821
Mass (Da):92,133
Last modified:April 1, 1990 - v1
Checksum:i50E08D5FF86D8F30
GO
Isoform GP95-TRKB (identifier: P15209-2) [UniParc]FASTAAdd to Basket

Also known as: TRKB-T1, TrkBTK-

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):53,186
Checksum:i20A8B375ED397ACE
GO
Isoform L1 (identifier: P15209-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     72-120: Missing.

Show »
Length:772
Mass (Da):86,535
Checksum:iE3E800582F9D3FB6
GO
Isoform L10 (identifier: P15209-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-71: I → M
     72-143: Missing.

Show »
Length:749
Mass (Da):83,744
Checksum:i791E6861C97AA53F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei71 – 711I → M in isoform L10. CuratedVSP_002905
Alternative sequencei72 – 14372Missing in isoform L10. CuratedVSP_002906Add
BLAST
Alternative sequencei72 – 12049Missing in isoform L1. CuratedVSP_002907Add
BLAST
Alternative sequencei466 – 47611PASVISNDDDS → FVLFHKIPLDG in isoform GP95-TRKB. 3 PublicationsVSP_002908Add
BLAST
Alternative sequencei477 – 821345Missing in isoform GP95-TRKB. 3 PublicationsVSP_002909Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33385 mRNA. Translation: AAA40482.1.
X17647 mRNA. Translation: CAA35636.1.
AK018789 mRNA. Translation: BAB31412.1.
AK147391 mRNA. Translation: BAE27880.1.
AK160789 mRNA. Translation: BAE36012.1.
BC052014 mRNA. Translation: AAH52014.2.
CCDSiCCDS26573.1. [P15209-1]
CCDS36685.1. [P15209-2]
PIRiA35104.
S06943.
RefSeqiNP_001020245.1. NM_001025074.2. [P15209-1]
NP_001269890.1. NM_001282961.1. [P15209-1]
NP_032771.1. NM_008745.3. [P15209-2]
XP_006517212.1. XM_006517149.1. [P15209-1]
XP_006517215.1. XM_006517152.1. [P15209-2]
UniGeneiMm.130054.

Genome annotation databases

EnsembliENSMUST00000079828; ENSMUSP00000078757; ENSMUSG00000055254. [P15209-1]
ENSMUST00000109838; ENSMUSP00000105464; ENSMUSG00000055254. [P15209-2]
GeneIDi18212.
KEGGimmu:18212.
UCSCiuc007qui.1. mouse. [P15209-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33385 mRNA. Translation: AAA40482.1 .
X17647 mRNA. Translation: CAA35636.1 .
AK018789 mRNA. Translation: BAB31412.1 .
AK147391 mRNA. Translation: BAE27880.1 .
AK160789 mRNA. Translation: BAE36012.1 .
BC052014 mRNA. Translation: AAH52014.2 .
CCDSi CCDS26573.1. [P15209-1 ]
CCDS36685.1. [P15209-2 ]
PIRi A35104.
S06943.
RefSeqi NP_001020245.1. NM_001025074.2. [P15209-1 ]
NP_001269890.1. NM_001282961.1. [P15209-1 ]
NP_032771.1. NM_008745.3. [P15209-2 ]
XP_006517212.1. XM_006517149.1. [P15209-1 ]
XP_006517215.1. XM_006517152.1. [P15209-2 ]
UniGenei Mm.130054.

3D structure databases

ProteinModelPortali P15209.
SMRi P15209. Positions 32-385, 526-821.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201869. 5 interactions.
DIPi DIP-5722N.
IntActi P15209. 4 interactions.
MINTi MINT-240722.

PTM databases

PhosphoSitei P15209.

Proteomic databases

MaxQBi P15209.
PaxDbi P15209.
PRIDEi P15209.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000079828 ; ENSMUSP00000078757 ; ENSMUSG00000055254 . [P15209-1 ]
ENSMUST00000109838 ; ENSMUSP00000105464 ; ENSMUSG00000055254 . [P15209-2 ]
GeneIDi 18212.
KEGGi mmu:18212.
UCSCi uc007qui.1. mouse. [P15209-1 ]

Organism-specific databases

CTDi 4915.
MGIi MGI:97384. Ntrk2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118818.
HOGENOMi HOG000264255.
HOVERGENi HBG056735.
InParanoidi P15209.
KOi K04360.
OMAi CEIMWIK.
OrthoDBi EOG7QG43C.
PhylomeDBi P15209.
TreeFami TF106465.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.
Reactomei REACT_209347. NGF-independant TRKA activation.

Miscellaneous databases

ChiTaRSi Ntrk2. mouse.
NextBioi 293608.
PROi P15209.
SOURCEi Search...

Gene expression databases

Bgeei P15209.
CleanExi MM_NTRK2.
ExpressionAtlasi P15209. baseline and differential.
Genevestigatori P15209.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
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 ]
Pfami PF07679. I-set. 2 hits.
PF13855. LRR_8. 1 hit.
PF01462. LRRNT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR01939. NTKRECEPTOR.
PR01941. NTKRECEPTOR2.
PR00109. TYRKINASE.
SMARTi SM00408. IGc2. 1 hit.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50835. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "trkB, a novel tyrosine protein kinase receptor expressed during mouse neural development."
    Klein R., Parada L.F., Coulier F., Barbacid M.
    EMBO J. 8:3701-3709(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GP145-TRKB).
    Tissue: Brain.
  2. "The trkB tyrosine protein kinase gene codes for a second neurogenic receptor that lacks the catalytic kinase domain."
    Klein R., Conway D., Parada L.F., Barbacid M.
    Cell 61:647-656(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GP145-TRKB AND GP95-TRKB).
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GP145-TRKB AND GP95-TRKB).
    Strain: C57BL/6J and NOD.
    Tissue: Thymus.
  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] (ISOFORM GP95-TRKB).
    Strain: C57BL/6.
    Tissue: Brain.
  5. "TrkB variants with deletions in the leucine-rich motifs of the extracellular domain."
    Ninkina N., Grashchuck M., Buchman V.L., Davies A.M.
    J. Biol. Chem. 272:13019-13025(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS L1 AND L10).
    Tissue: Trigeminal ganglion.
  6. "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.
  7. "Targeted disruption of the trkB neurotrophin receptor gene results in nervous system lesions and neonatal death."
    Klein R., Smeyne R.J., Wurst W., Long L.K., Auerbach B.A., Joyner A.L., Barbacid M.
    Cell 75:113-122(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  8. "Characterization of neurotrophin and Trk receptor functions in developing sensory ganglia: direct NT-3 activation of TrkB neurons in vivo."
    Farinas I., Wilkinson G.A., Backus C., Reichardt L.F., Patapoutian A.
    Neuron 21:325-334(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NTF3-MEDIATED NEURON SURVIVAL.
  9. Cited for: FUNCTION IN LONG-TERM POTENTIATION AND LEARNING.
  10. "Mechanism of TrkB-mediated hippocampal long-term potentiation."
    Minichiello L., Calella A.M., Medina D.L., Bonhoeffer T., Klein R., Korte M.
    Neuron 36:121-137(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LONG-TERM POTENTIATION AND LEARNING, INTERACTION WITH SHC1 AND PLCG1, MUTAGENESIS OF TYR-515 AND TYR-816.
  11. "Regulation of TrkB receptor tyrosine kinase and its internalization by neuronal activity and Ca2+ influx."
    Du J., Feng L., Zaitsev E., Je H.S., Liu X.W., Lu B.
    J. Cell Biol. 163:385-395(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ENZYME REGULATION.
  12. "Truncated TrkB-T1 mediates neurotrophin-evoked calcium signalling in glia cells."
    Rose C.R., Blum R., Pichler B., Lepier A., Kafitz K.W., Konnerth A.
    Nature 426:74-78(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CALCIUM SIGNALING (ISOFORM GP95-TRKB).
  13. "TrkB regulates neocortex formation through the Shc/PLCgamma-mediated control of neuronal migration."
    Medina D.L., Sciarretta C., Calella A.M., Von Bohlen Und Halbach O., Unsicker K., Minichiello L.
    EMBO J. 23:3803-3814(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEURONAL MIGRATION AND DIFFERENTIATION.
  14. "Suppression of anoikis and induction of metastasis by the neurotrophic receptor TrkB."
    Douma S., Van Laar T., Zevenhoven J., Meuwissen R., Van Garderen E., Peeper D.S.
    Nature 430:1034-1039(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A SUPPRESSOR OF ANOIKIS.
  15. "p75 neurotrophin receptor reduces ligand-induced Trk receptor ubiquitination and delays Trk receptor internalization and degradation."
    Makkerh J.P., Ceni C., Auld D.S., Vaillancourt F., Dorval G., Barker P.A.
    EMBO Rep. 6:936-941(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, ENZYME REGULATION.
  16. "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.
  17. "TrkB binds and tyrosine-phosphorylates Tiam1, leading to activation of Rac1 and induction of changes in cellular morphology."
    Miyamoto Y., Yamauchi J., Tanoue A., Wu C., Mobley W.C.
    Proc. Natl. Acad. Sci. U.S.A. 103:10444-10449(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TIAM1, FUNCTION IN CELL DIFFERENTIATION, INTERACTION WITH TIAM1.
  18. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  19. "TrkB (tropomyosin-related kinase B) controls the assembly and maintenance of GABAergic synapses in the cerebellar cortex."
    Chen A.I., Nguyen C.N., Copenhagen D.R., Badurek S., Minichiello L., Ranscht B., Reichardt L.F.
    J. Neurosci. 31:2769-2780(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SYNAPSE FORMATION.
  20. "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: INDUCTION.

Entry informationi

Entry nameiNTRK2_MOUSE
AccessioniPrimary (citable) accession number: P15209
Secondary accession number(s): Q3TUF9, Q80WU0, Q91XJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 26, 2014
This is version 171 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3