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P15209

- NTRK2_MOUSE

UniProt

P15209 - NTRK2_MOUSE

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
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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 binding Source: UniProtKB
    6. 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

    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.

    GO - Cellular componenti

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

    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

    ArrayExpressiP15209.
    BgeeiP15209.
    CleanExiMM_NTRK2.
    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...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei430 – 45324HelicalSequence AnalysisAdd
    BLAST

    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.
    GeneTreeiENSGT00730000110657.
    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

    MSPWLKWHGP AMARLWGLCL LVLGFWRASL ACPTSCKCSS ARIWCTEPSP    50
    GIVAFPRLEP NSVDPENITE ILIANQKRLE IINEDDVEAY VGLRNLTIVD 100
    SGLKFVAYKA FLKNSNLRHI NFTRNKLTSL SRRHFRHLDL SDLILTGNPF 150
    TCSCDIMWLK TLQETKSSPD TQDLYCLNES SKNMPLANLQ IPNCGLPSAR 200
    LAAPNLTVEE GKSVTLSCSV GGDPLPTLYW DVGNLVSKHM NETSHTQGSL 250
    RITNISSDDS GKQISCVAEN LVGEDQDSVN LTVHFAPTIT FLESPTSDHH 300
    WCIPFTVRGN PKPALQWFYN GAILNESKYI CTKIHVTNHT EYHGCLQLDN 350
    PTHMNNGDYT LMAKNEYGKD ERQISAHFMG RPGVDYETNP NYPEVLYEDW 400
    TTPTDIGDTT NKSNEIPSTD VADQSNREHL SVYAVVVIAS VVGFCLLVML 450
    LLLKLARHSK FGMKGPASVI SNDDDSASPL HHISNGSNTP SSSEGGPDAV 500
    IIGMTKIPVI ENPQYFGITN SQLKPDTFVQ HIKRHNIVLK RELGEGAFGK 550
    VFLAECYNLC PEQDKILVAV KTLKDASDNA RKDFHREAEL LTNLQHEHIV 600
    KFYGVCVEGD PLIMVFEYMK HGDLNKFLRA HGPDAVLMAE GNPPTELTQS 650
    QMLHIAQQIA AGMVYLASQH FVHRDLATRN CLVGENLLVK IGDFGMSRDV 700
    YSTDYYRVGG HTMLPIRWMP PESIMYRKFT TESDVWSLGV VLWEIFTYGK 750
    QPWYQLSNNE VIECITQGRV LQRPRTCPQE VYELMLGCWQ REPHTRKNIK 800
    SIHTLLQNLA KASPVYLDIL G 821
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 ENSGT00730000110657.
    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

    ArrayExpressi P15209.
    Bgeei P15209.
    CleanExi MM_NTRK2.
    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 ]
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    Publicationsi

    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: October 1, 2014
    This is version 169 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

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