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Q16620

- NTRK2_HUMAN

UniProt

Q16620 - NTRK2_HUMAN

Protein

BDNF/NT-3 growth factors receptor

Gene

NTRK2

Organism
Homo sapiens (Human)
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 Nov 1996)
      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. May also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia.1 Publication

    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei516 – 5161Interaction with SHC1By similarity
    Binding sitei572 – 5721ATPPROSITE-ProRule annotation
    Active sitei676 – 6761Proton acceptorPROSITE-ProRule annotation
    Sitei706 – 7061Interaction with SH2D1ABy similarity
    Sitei817 – 8171Interaction with PLCG1By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi544 – 5529ATPPROSITE-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. activation of adenylate cyclase activity Source: Reactome
    2. aging Source: Ensembl
    3. brain-derived neurotrophic factor receptor signaling pathway Source: UniProtKB
    4. calcium-mediated signaling using intracellular calcium source Source: Ensembl
    5. central nervous system neuron development Source: UniProtKB
    6. cerebral cortex development Source: UniProtKB
    7. feeding behavior Source: Ensembl
    8. glutamate secretion Source: Ensembl
    9. learning Source: UniProtKB
    10. long-term memory Source: Ensembl
    11. long-term synaptic potentiation Source: Ensembl
    12. mechanoreceptor differentiation Source: Ensembl
    13. negative regulation of anoikis Source: Ensembl
    14. negative regulation of neuron apoptotic process Source: UniProtKB
    15. neuromuscular junction development Source: Ensembl
    16. neuron differentiation Source: UniProtKB
    17. neuron migration Source: UniProtKB
    18. neurotrophin TRK receptor signaling pathway Source: Reactome
    19. oligodendrocyte differentiation Source: Ensembl
    20. peripheral nervous system neuron development Source: Ensembl
    21. positive regulation of axonogenesis Source: UniProtKB
    22. positive regulation of cell proliferation Source: UniProtKB
    23. positive regulation of gene expression Source: UniProtKB
    24. positive regulation of MAPK cascade Source: UniProtKB
    25. positive regulation of neuron projection development Source: UniProtKB
    26. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    27. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
    28. protein autophosphorylation Source: UniProtKB
    29. regulation of dendrite development Source: Ensembl
    30. regulation of neurotransmitter secretion Source: Ensembl
    31. regulation of protein kinase B signaling Source: Ensembl
    32. regulation of Rac GTPase activity Source: UniProtKB
    33. response to auditory stimulus Source: Ensembl
    34. retinal rod cell development Source: Ensembl
    35. transmembrane receptor protein tyrosine kinase signaling pathway Source: Reactome
    36. vasculogenesis Source: Ensembl

    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. 2681.
    ReactomeiREACT_11046. NGF-independant TRKA activation.
    SignaLinkiQ16620.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    BDNF/NT-3 growth factors receptor (EC:2.7.10.1)
    Alternative name(s):
    GP145-TrkB
    Short name:
    Trk-B
    Neurotrophic tyrosine kinase receptor type 2
    TrkB tyrosine kinase
    Tropomyosin-related kinase B
    Gene namesi
    Name:NTRK2
    Synonyms:TRKB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:8032. NTRK2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. cytosol Source: Ensembl
    3. dendritic spine Source: Ensembl
    4. endosome membrane Source: UniProtKB-SubCell
    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. postsynaptic density Source: Ensembl
    10. postsynaptic membrane Source: Ensembl
    11. presynaptic active zone Source: Ensembl
    12. receptor complex Source: MGI
    13. terminal bouton Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Obesity hyperphagia and developmental delay (OHPDD) [MIM:613886]: A disorder characterized by early-onset obesity, hyperphagia, and severe developmental delay in motor function, speech, and language.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti706 – 7061Y → C in OHPDD; expressed normally on the cell surface; results in markedly impaired ligand-induced phosphorylation as well as impaired downstream MAPK1 phosphorylation. 1 Publication
    VAR_065890

    Keywords - Diseasei

    Disease mutation, Obesity

    Organism-specific databases

    MIMi613886. phenotype.
    Orphaneti251612. Pilocytic astrocytoma.
    PharmGKBiPA31818.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Add
    BLAST
    Chaini32 – 822791BDNF/NT-3 growth factors receptorPRO_0000016727Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 381 PublicationPROSITE-ProRule annotation
    Disulfide bondi36 ↔ 451 PublicationPROSITE-ProRule annotation
    Glycosylationi67 – 671N-linked (GlcNAc...)2 Publications
    Glycosylationi95 – 951N-linked (GlcNAc...)1 Publication
    Glycosylationi121 – 1211N-linked (GlcNAc...)2 Publications
    Disulfide bondi152 ↔ 1761 PublicationPROSITE-ProRule annotation
    Disulfide bondi154 ↔ 1941 PublicationPROSITE-ProRule annotation
    Glycosylationi178 – 1781N-linked (GlcNAc...)1 Publication
    Glycosylationi205 – 2051N-linked (GlcNAc...)1 Publication
    Disulfide bondi218 ↔ 2661 PublicationPROSITE-ProRule annotation
    Glycosylationi241 – 2411N-linked (GlcNAc...)1 Publication
    Glycosylationi254 – 2541N-linked (GlcNAc...)2 Publications
    Glycosylationi280 – 2801N-linked (GlcNAc...)1 Publication
    Disulfide bondi302 ↔ 3451 PublicationPROSITE-ProRule annotation
    Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi338 – 3381N-linked (GlcNAc...)1 Publication
    Glycosylationi412 – 4121N-linked (GlcNAc...)1 Publication
    Modified residuei516 – 5161Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei702 – 7021Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei706 – 7061Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei707 – 7071Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei817 – 8171Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Phosphorylated. Undergoes ligand-mediated autophosphorylation that is required for interaction with SHC1 and PLCG1 and other downstream effectors. Isoform TrkB-T-Shc is not phosphorylated.1 Publication
    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

    PaxDbiQ16620.
    PRIDEiQ16620.

    PTM databases

    PhosphoSiteiQ16620.

    Expressioni

    Tissue specificityi

    Isoform TrkB is expressed in the central and peripheral nervous system. In the central nervous system (CNS), expression is observed in the cerebral cortex, hippocampus, thalamus, choroid plexus, granular layer of the cerebellum, brain stem, and spinal cord. In the peripheral nervous system, it is expressed in many cranial ganglia, the ophthalmic nerve, the vestibular system, multiple facial structures, the submaxillary glands, and dorsal root ganglia. Isoform TrkB-T1 is mainly expressed in the brain but also detected in other tissues including pancreas, kidney and heart. Isoform TrkB-T-Shc is predominantly expressed in the brain.2 Publications

    Developmental stagei

    Widely expressed in fetal brain.1 Publication

    Gene expression databases

    ArrayExpressiQ16620.
    BgeeiQ16620.
    CleanExiHS_NTRK2.
    GenevestigatoriQ16620.

    Organism-specific databases

    HPAiCAB010346.
    HPA007637.

    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 By similarity. Interacts (phosphorylated upon ligand-binding) with FRS2; activates the MAPK signaling pathway.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi110970. 22 interactions.
    DIPiDIP-5720N.
    IntActiQ16620. 6 interactions.
    MINTiMINT-156841.
    STRINGi9606.ENSP00000277120.

    Structurei

    Secondary structure

    1
    822
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi286 – 2927
    Beta strandi300 – 3089
    Beta strandi314 – 3196
    Beta strandi322 – 3243
    Beta strandi328 – 33710
    Beta strandi339 – 35012
    Helixi353 – 3553
    Beta strandi357 – 3648
    Beta strandi369 – 3768
    Beta strandi500 – 5034
    Beta strandi506 – 5127
    Turni515 – 5173
    Helixi535 – 5373
    Beta strandi538 – 5458
    Beta strandi552 – 5576
    Beta strandi567 – 5748
    Helixi579 – 59214
    Beta strandi603 – 6075
    Beta strandi609 – 61810
    Helixi625 – 6317
    Helixi634 – 6385
    Beta strandi641 – 6433
    Helixi650 – 66920
    Helixi679 – 6813
    Beta strandi682 – 6843
    Helixi686 – 6883
    Beta strandi690 – 6923
    Helixi698 – 7014
    Helixi703 – 7053
    Beta strandi707 – 7093
    Turni710 – 7123
    Beta strandi713 – 7153
    Helixi717 – 7193
    Helixi722 – 7276
    Helixi732 – 74716
    Turni748 – 7503
    Turni753 – 7564
    Helixi759 – 76810
    Helixi780 – 78910
    Helixi794 – 7963
    Helixi800 – 81314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HCFX-ray2.70X/Y286-383[»]
    1WWBX-ray2.10X283-385[»]
    2MFQNMR-B497-519[»]
    4ASZX-ray1.70A527-822[»]
    4AT3X-ray1.77A527-822[»]
    4AT4X-ray2.36A527-822[»]
    4AT5X-ray1.71A527-822[»]
    ProteinModelPortaliQ16620.
    SMRiQ16620. Positions 29-385, 527-822.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16620.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 430399ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini455 – 822368CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei431 – 45424HelicalSequence 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
    Domaini295 – 36571Ig-like C2-type 2Add
    BLAST
    Domaini538 – 807270Protein 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.
    HOGENOMiHOG000264255.
    HOVERGENiHBG056735.
    KOiK04360.
    OMAiCEIMWIK.
    OrthoDBiEOG7QG43C.
    PhylomeDBiQ16620.
    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 (7)i

    Sequence statusi: Complete.

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

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform TrkB (identifier: Q16620-1) [UniParc]FASTAAdd to Basket

    Also known as: gp145-TrkB

    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

    MSSWIRWHGP AMARLWGFCW LVVGFWRAAF ACPTSCKCSA SRIWCSDPSP    50
    GIVAFPRLEP NSVDPENITE IFIANQKRLE IINEDDVEAY VGLRNLTIVD 100
    SGLKFVAHKA FLKNSNLQHI NFTRNKLTSL SRKHFRHLDL SELILVGNPF 150
    TCSCDIMWIK TLQEAKSSPD TQDLYCLNES SKNIPLANLQ IPNCGLPSAN 200
    LAAPNLTVEE GKSITLSCSV AGDPVPNMYW DVGNLVSKHM NETSHTQGSL 250
    RITNISSDDS GKQISCVAEN LVGEDQDSVN LTVHFAPTIT FLESPTSDHH 300
    WCIPFTVKGN PKPALQWFYN GAILNESKYI CTKIHVTNHT EYHGCLQLDN 350
    PTHMNNGDYT LIAKNEYGKD EKQISAHFMG WPGIDDGANP NYPDVIYEDY 400
    GTAANDIGDT TNRSNEIPST DVTDKTGREH LSVYAVVVIA SVVGFCLLVM 450
    LFLLKLARHS KFGMKGPASV ISNDDDSASP LHHISNGSNT PSSSEGGPDA 500
    VIIGMTKIPV IENPQYFGIT NSQLKPDTFV QHIKRHNIVL KRELGEGAFG 550
    KVFLAECYNL CPEQDKILVA VKTLKDASDN ARKDFHREAE LLTNLQHEHI 600
    VKFYGVCVEG DPLIMVFEYM KHGDLNKFLR AHGPDAVLMA EGNPPTELTQ 650
    SQMLHIAQQI AAGMVYLASQ HFVHRDLATR NCLVGENLLV KIGDFGMSRD 700
    VYSTDYYRVG GHTMLPIRWM PPESIMYRKF TTESDVWSLG VVLWEIFTYG 750
    KQPWYQLSNN EVIECITQGR VLQRPRTCPQ EVYELMLGCW QREPHMRKNI 800
    KGIHTLLQNL AKASPVYLDI LG 822
    Length:822
    Mass (Da):91,999
    Last modified:November 1, 1996 - v1
    Checksum:i2FEB9159948F0D13
    GO
    Isoform TrkB-T1 (identifier: Q16620-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         467-477: PASVISNDDDS → FVLFHKIPLDG
         478-822: Missing.

    Note: Non-catalytic isoform.

    Show »
    Length:477
    Mass (Da):53,051
    Checksum:iC4A7F565BC88372F
    GO
    Isoform TrkB-T-Shc (identifier: Q16620-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         529-537: FVQHIKRHN → WPRGSPKTA
         538-822: Missing.

    Show »
    Length:537
    Mass (Da):59,167
    Checksum:i5A8FA252A3871CC1
    GO
    Isoform 4 (identifier: Q16620-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         465-465: K → KDFSWFGFGKVKSRQGV

    Show »
    Length:838
    Mass (Da):93,826
    Checksum:i130C95A9D8895432
    GO
    Isoform 5 (identifier: Q16620-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         465-465: K → KDFSWFGFGKVKSRQGV
         529-537: FVQHIKRHN → WPRGSPKTA
         538-822: Missing.

    Show »
    Length:553
    Mass (Da):60,994
    Checksum:iBD98221B9EE1A6C1
    GO
    Isoform TrkB-T-TK (identifier: Q16620-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         710-735: GGHTMLPIRWMPPESIMYRKFTTESD → SSCADQRPQGPLSLRDPCCICLLRLS
         736-822: Missing.

    Show »
    Length:735
    Mass (Da):81,569
    Checksum:i5E0746BCCA281069
    GO
    Isoform TrkB-N-T1 (identifier: Q16620-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-156: Missing.
         467-477: PASVISNDDDS → FVLFHKIPLDG
         478-822: Missing.

    Show »
    Length:321
    Mass (Da):35,332
    Checksum:i64C146AAB494744E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381L → F in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041470
    Natural varianti309 – 3091G → R.1 Publication
    VAR_016320
    Natural varianti338 – 3381N → Y.
    Corresponds to variant rs1047856 [ dbSNP | Ensembl ].
    VAR_011973
    Natural varianti545 – 5451G → V.
    Corresponds to variant rs1075108 [ dbSNP | Ensembl ].
    VAR_049715
    Natural varianti697 – 6971M → I in a lung carcinoma sample; somatic mutation. 1 Publication
    VAR_046518
    Natural varianti699 – 6991R → G in a lung carcinoma sample; somatic mutation. 1 Publication
    VAR_046519
    Natural varianti706 – 7061Y → C in OHPDD; expressed normally on the cell surface; results in markedly impaired ligand-induced phosphorylation as well as impaired downstream MAPK1 phosphorylation. 1 Publication
    VAR_065890
    Natural varianti718 – 7181R → C in a lung carcinoma sample; somatic mutation. 1 Publication
    VAR_046520

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 156156Missing in isoform TrkB-N-T1. 1 PublicationVSP_042177Add
    BLAST
    Alternative sequencei465 – 4651K → KDFSWFGFGKVKSRQGV in isoform 4 and isoform 5. 1 PublicationVSP_041942
    Alternative sequencei467 – 47711PASVISNDDDS → FVLFHKIPLDG in isoform TrkB-T1 and isoform TrkB-N-T1. 6 PublicationsVSP_002901Add
    BLAST
    Alternative sequencei478 – 822345Missing in isoform TrkB-T1 and isoform TrkB-N-T1. 6 PublicationsVSP_002902Add
    BLAST
    Alternative sequencei529 – 5379FVQHIKRHN → WPRGSPKTA in isoform TrkB-T-Shc and isoform 5. 1 PublicationVSP_002903
    Alternative sequencei538 – 822285Missing in isoform TrkB-T-Shc and isoform 5. 1 PublicationVSP_002904Add
    BLAST
    Alternative sequencei710 – 73526GGHTM…TTESD → SSCADQRPQGPLSLRDPCCI CLLRLS in isoform TrkB-T-TK. 1 PublicationVSP_042178Add
    BLAST
    Alternative sequencei736 – 82287Missing in isoform TrkB-T-TK. 1 PublicationVSP_042179Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12140 mRNA. Translation: AAC51371.1.
    S76473 mRNA. Translation: AAB33109.1.
    S76474 mRNA. Translation: AAB33110.1.
    X75958 mRNA. Translation: CAA53571.1.
    AF410899 mRNA. Translation: AAL67965.1.
    AF410900 mRNA. Translation: AAL67966.1.
    AF410901 mRNA. Translation: AAL67967.1.
    AF508964 mRNA. Translation: AAM77876.1.
    AB209118 mRNA. Translation: BAD92355.1.
    AK294285 mRNA. Translation: BAG57570.1.
    AL445532, AL390777, AL596132 Genomic DNA. Translation: CAH71816.1.
    AL390777, AL596132 Genomic DNA. Translation: CAH72193.1.
    AL390777, AL596132 Genomic DNA. Translation: CAH72194.1.
    AL390777, AL445532, AL596132 Genomic DNA. Translation: CAH72195.1.
    AL596132, AL390777 Genomic DNA. Translation: CAH72313.1.
    AL596132, AL390777 Genomic DNA. Translation: CAH72314.1.
    AL596132, AL390777, AL445532 Genomic DNA. Translation: CAH72316.1.
    CH471089 Genomic DNA. Translation: EAW62688.1.
    BC031835 mRNA. Translation: AAH31835.1.
    CCDSiCCDS35050.1. [Q16620-1]
    CCDS35051.1. [Q16620-5]
    CCDS35052.1. [Q16620-3]
    CCDS35053.1. [Q16620-2]
    CCDS6671.1. [Q16620-4]
    PIRiA56853.
    I73631.
    RefSeqiNP_001007098.1. NM_001007097.2. [Q16620-2]
    NP_001018074.1. NM_001018064.2. [Q16620-1]
    NP_001018075.1. NM_001018065.2. [Q16620-5]
    NP_001018076.1. NM_001018066.2. [Q16620-3]
    NP_006171.2. NM_006180.4. [Q16620-4]
    XP_005252058.1. XM_005252001.1. [Q16620-4]
    XP_005252060.1. XM_005252003.1. [Q16620-4]
    XP_005252061.1. XM_005252004.1. [Q16620-4]
    XP_005252063.1. XM_005252006.2. [Q16620-5]
    XP_005252064.1. XM_005252007.1. [Q16620-2]
    UniGeneiHs.494312.
    Hs.712776.

    Genome annotation databases

    EnsembliENST00000277120; ENSP00000277120; ENSG00000148053. [Q16620-4]
    ENST00000304053; ENSP00000306167; ENSG00000148053. [Q16620-5]
    ENST00000323115; ENSP00000314586; ENSG00000148053. [Q16620-1]
    ENST00000359847; ENSP00000352906; ENSG00000148053. [Q16620-2]
    ENST00000376208; ENSP00000365381; ENSG00000148053. [Q16620-3]
    ENST00000376213; ENSP00000365386; ENSG00000148053. [Q16620-1]
    ENST00000376214; ENSP00000365387; ENSG00000148053. [Q16620-4]
    ENST00000395882; ENSP00000379221; ENSG00000148053. [Q16620-2]
    GeneIDi4915.
    KEGGihsa:4915.
    UCSCiuc004any.1. human. [Q16620-6]
    uc004anz.1. human. [Q16620-4]
    uc004aoa.1. human. [Q16620-1]
    uc011lsz.2. human. [Q16620-5]
    uc011lta.2. human. [Q16620-3]
    uc011ltb.1. human. [Q16620-7]

    Polymorphism databases

    DMDMi2497560.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12140 mRNA. Translation: AAC51371.1 .
    S76473 mRNA. Translation: AAB33109.1 .
    S76474 mRNA. Translation: AAB33110.1 .
    X75958 mRNA. Translation: CAA53571.1 .
    AF410899 mRNA. Translation: AAL67965.1 .
    AF410900 mRNA. Translation: AAL67966.1 .
    AF410901 mRNA. Translation: AAL67967.1 .
    AF508964 mRNA. Translation: AAM77876.1 .
    AB209118 mRNA. Translation: BAD92355.1 .
    AK294285 mRNA. Translation: BAG57570.1 .
    AL445532 , AL390777 , AL596132 Genomic DNA. Translation: CAH71816.1 .
    AL390777 , AL596132 Genomic DNA. Translation: CAH72193.1 .
    AL390777 , AL596132 Genomic DNA. Translation: CAH72194.1 .
    AL390777 , AL445532 , AL596132 Genomic DNA. Translation: CAH72195.1 .
    AL596132 , AL390777 Genomic DNA. Translation: CAH72313.1 .
    AL596132 , AL390777 Genomic DNA. Translation: CAH72314.1 .
    AL596132 , AL390777 , AL445532 Genomic DNA. Translation: CAH72316.1 .
    CH471089 Genomic DNA. Translation: EAW62688.1 .
    BC031835 mRNA. Translation: AAH31835.1 .
    CCDSi CCDS35050.1. [Q16620-1 ]
    CCDS35051.1. [Q16620-5 ]
    CCDS35052.1. [Q16620-3 ]
    CCDS35053.1. [Q16620-2 ]
    CCDS6671.1. [Q16620-4 ]
    PIRi A56853.
    I73631.
    RefSeqi NP_001007098.1. NM_001007097.2. [Q16620-2 ]
    NP_001018074.1. NM_001018064.2. [Q16620-1 ]
    NP_001018075.1. NM_001018065.2. [Q16620-5 ]
    NP_001018076.1. NM_001018066.2. [Q16620-3 ]
    NP_006171.2. NM_006180.4. [Q16620-4 ]
    XP_005252058.1. XM_005252001.1. [Q16620-4 ]
    XP_005252060.1. XM_005252003.1. [Q16620-4 ]
    XP_005252061.1. XM_005252004.1. [Q16620-4 ]
    XP_005252063.1. XM_005252006.2. [Q16620-5 ]
    XP_005252064.1. XM_005252007.1. [Q16620-2 ]
    UniGenei Hs.494312.
    Hs.712776.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HCF X-ray 2.70 X/Y 286-383 [» ]
    1WWB X-ray 2.10 X 283-385 [» ]
    2MFQ NMR - B 497-519 [» ]
    4ASZ X-ray 1.70 A 527-822 [» ]
    4AT3 X-ray 1.77 A 527-822 [» ]
    4AT4 X-ray 2.36 A 527-822 [» ]
    4AT5 X-ray 1.71 A 527-822 [» ]
    ProteinModelPortali Q16620.
    SMRi Q16620. Positions 29-385, 527-822.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110970. 22 interactions.
    DIPi DIP-5720N.
    IntActi Q16620. 6 interactions.
    MINTi MINT-156841.
    STRINGi 9606.ENSP00000277120.

    Chemistry

    BindingDBi Q16620.
    ChEMBLi CHEMBL4898.
    GuidetoPHARMACOLOGYi 1818.

    PTM databases

    PhosphoSitei Q16620.

    Polymorphism databases

    DMDMi 2497560.

    Proteomic databases

    PaxDbi Q16620.
    PRIDEi Q16620.

    Protocols and materials databases

    DNASUi 4915.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000277120 ; ENSP00000277120 ; ENSG00000148053 . [Q16620-4 ]
    ENST00000304053 ; ENSP00000306167 ; ENSG00000148053 . [Q16620-5 ]
    ENST00000323115 ; ENSP00000314586 ; ENSG00000148053 . [Q16620-1 ]
    ENST00000359847 ; ENSP00000352906 ; ENSG00000148053 . [Q16620-2 ]
    ENST00000376208 ; ENSP00000365381 ; ENSG00000148053 . [Q16620-3 ]
    ENST00000376213 ; ENSP00000365386 ; ENSG00000148053 . [Q16620-1 ]
    ENST00000376214 ; ENSP00000365387 ; ENSG00000148053 . [Q16620-4 ]
    ENST00000395882 ; ENSP00000379221 ; ENSG00000148053 . [Q16620-2 ]
    GeneIDi 4915.
    KEGGi hsa:4915.
    UCSCi uc004any.1. human. [Q16620-6 ]
    uc004anz.1. human. [Q16620-4 ]
    uc004aoa.1. human. [Q16620-1 ]
    uc011lsz.2. human. [Q16620-5 ]
    uc011lta.2. human. [Q16620-3 ]
    uc011ltb.1. human. [Q16620-7 ]

    Organism-specific databases

    CTDi 4915.
    GeneCardsi GC09P087283.
    HGNCi HGNC:8032. NTRK2.
    HPAi CAB010346.
    HPA007637.
    MIMi 600456. gene.
    613886. phenotype.
    neXtProti NX_Q16620.
    Orphaneti 251612. Pilocytic astrocytoma.
    PharmGKBi PA31818.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000264255.
    HOVERGENi HBG056735.
    KOi K04360.
    OMAi CEIMWIK.
    OrthoDBi EOG7QG43C.
    PhylomeDBi Q16620.
    TreeFami TF106465.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_11046. NGF-independant TRKA activation.
    SignaLinki Q16620.

    Miscellaneous databases

    EvolutionaryTracei Q16620.
    GeneWikii TrkB_receptor.
    GenomeRNAii 4915.
    NextBioi 18915.
    PROi Q16620.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16620.
    Bgeei Q16620.
    CleanExi HS_NTRK2.
    Genevestigatori Q16620.

    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

    1. "Cloning and chromosomal localization of the human TRK-B tyrosine kinase receptor gene (NTRK2)."
      Nakagawara A., Liu X.-G., Ikegaki N., White P.S., Yamashiro D.J., Nycum L.M., Biegel J.A., Brodeur G.M.
      Genomics 25:538-546(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKB).
      Tissue: Hippocampus.
    2. "Human trks: molecular cloning, tissue distribution, and expression of extracellular domain immunoadhesins."
      Shelton D.L., Sutherland J., Gripp J., Camerato T., Armanini M.P., Phillips H.S., Carroll K., Spencer S.D., Levinson A.D.
      J. Neurosci. 15:477-491(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TRKB AND TRKB-T1).
      Tissue: Brain.
    3. "Cloning of a non-catalytic form of human trkB and distribution of messenger RNA for trkB in human brain."
      Allen S.J., Dawbarn D., Eckford S.D., Wilcock G.K., Ashcroft M., Colebrook S.M., Feeney R., Macgowan S.H.
      Neuroscience 60:825-834(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKB-T1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Hippocampus.
    4. "Analysis of the human TrkB gene genomic organization reveals novel TrkB isoforms, unusual gene length, and splicing mechanism."
      Stoilov P., Castren E., Stamm S.
      Biochem. Biophys. Res. Commun. 290:1054-1065(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TRKB; TRKB-T1; TRKB-T-SHC; 4 AND 5), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    5. "Full length truncated TrkB sequence identified in a screen for genes regulated by ischemic preconditioning."
      Steinbeck J.A., Thomsen S., Wessig J., Leypoldt F., Lewerenz J., Methner A.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TRKB-T1), VARIANT ARG-309.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TRKB-N-T1).
      Tissue: Amygdala.
    7. "Homo sapiens protein coding cDNA."
      Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TRKB-T-TK).
      Tissue: Brain.
    8. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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 TRKB-T1).
      Tissue: Brain.
    11. "Extracellular domain of neurotrophin receptor trkB: disulfide structure, N-glycosylation sites, and ligand binding."
      Haniu M., Talvenheimo J., Le J., Katta V., Welcher A., Rohde M.F.
      Arch. Biochem. Biophys. 322:256-264(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS, GLYCOSYLATION AT ASN-67; ASN-95; ASN-121; ASN-178; ASN-205; ASN-241; ASN-254; ASN-280; ASN-338 AND ASN-412.
    12. "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.
    13. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-67; ASN-121 AND ASN-254.
      Tissue: Plasma.
    14. "Human TrkB gene: novel alternative transcripts, protein isoforms and expression pattern in the prefrontal cerebral cortex during postnatal development."
      Luberg K., Wong J., Weickert C.S., Timmusk T.
      J. Neurochem. 113:952-964(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS TRKB-T-TK AND TRKB-N-T1).
    15. "Crystal structures of the neurotrophin-binding domain of TrkA, TrkB and TrkC."
      Ultsch M.H., Wiesmann C., Simmons L.C., Henrich J., Yang M., Reilly D., Bass S.H., de Vos A.M.
      J. Mol. Biol. 290:149-159(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 283-385.
    16. "Specificity in Trk receptor:neurotrophin interactions: the crystal structure of TrkB-d5 in complex with neurotrophin-4/5."
      Banfield M.J., Naylor R.L., Robertson A.G., Allen S.J., Dawbarn D., Brady R.L.
      Structure 9:1191-1199(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 284-383 IN COMPLEX WITH NTF4.
    17. "A de novo mutation affecting human TrkB associated with severe obesity and developmental delay."
      Yeo G.S., Connie Hung C.C., Rochford J., Keogh J., Gray J., Sivaramakrishnan S., O'Rahilly S., Farooqi I.S.
      Nat. Neurosci. 7:1187-1189(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OHPDD CYS-706, CHARACTERIZATION OF VARIANT OHPDD CYS-706, FUNCTION AS A BDNF-ACTIVATED RECEPTOR, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    18. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-138.
    19. "Frequent mutations in the neurotrophic tyrosine receptor kinase gene family in large cell neuroendocrine carcinoma of the lung."
      Marchetti A., Felicioni L., Pelosi G., Del Grammastro M., Fumagalli C., Sciarrotta M., Malatesta S., Chella A., Barassi F., Mucilli F., Camplese P., D'Antuono T., Sacco R., Buttitta F.
      Hum. Mutat. 29:609-616(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ILE-697; GLY-699 AND CYS-718.

    Entry informationi

    Entry nameiNTRK2_HUMAN
    AccessioniPrimary (citable) accession number: Q16620
    Secondary accession number(s): B1ANZ4
    , B4DFV9, Q16675, Q59GJ1, Q8WXJ5, Q8WXJ6, Q8WXJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    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
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Trk also stands for tropomyosin-related kinase since the first Trk was isolated as an oncogenic protein which was the result of a fusion between the tropomyosin gene TPM3 and NTRK1.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3