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Q3UFB7

- NTRK1_MOUSE

UniProt

Q3UFB7 - NTRK1_MOUSE

Protein

High affinity nerve growth factor receptor

Gene

Ntrk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (20 Feb 2007)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand, it can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival. Upon dimeric NGF 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 driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors.3 Publications

    Catalytic activityi

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

    Enzyme regulationi

    The pro-survival signaling effect of NTRK1 in neurons requires its endocytosis into signaling early endosomes and its retrograde axonal transport. This is regulated by different proteins including CFL1, RAC1 and SORT1. NTF3 is unable to induce this signaling probably due to the lability of the NTF3-NTRK1 complex in endosomes. SH2D1A inhibits the autophosphorylation of the receptor, and alters the recruitment and activation of downstream effectors and signaling cascades. Regulated by NGFR.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei499 – 4991Interaction with SHC1By similarity
    Binding sitei547 – 5471ATPPROSITE-ProRule annotation
    Active sitei653 – 6531Proton acceptorPROSITE-ProRule annotation
    Sitei794 – 7941Interaction with PLCG1By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi519 – 5279ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. nerve growth factor binding Source: UniProtKB
    3. nerve growth factor receptor activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. protein tyrosine kinase activity Source: MGI
    7. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. axon guidance Source: Ensembl
    3. axonogenesis involved in innervation Source: UniProtKB
    4. B cell differentiation Source: MGI
    5. cellular response to growth factor stimulus Source: MGI
    6. cellular response to nerve growth factor stimulus Source: UniProtKB
    7. cellular response to nicotine Source: Ensembl
    8. circadian rhythm Source: UniProtKB
    9. detection of mechanical stimulus involved in sensory perception of pain Source: Ensembl
    10. detection of temperature stimulus involved in sensory perception of pain Source: Ensembl
    11. developmental programmed cell death Source: UniProtKB
    12. learning or memory Source: Ensembl
    13. mechanoreceptor differentiation Source: MGI
    14. negative regulation of cell proliferation Source: UniProtKB
    15. negative regulation of neuron apoptotic process Source: UniProtKB
    16. nerve growth factor signaling pathway Source: UniProtKB
    17. nervous system development Source: MGI
    18. neurotrophin TRK receptor signaling pathway Source: UniProtKB
    19. olfactory nerve development Source: Ensembl
    20. peptidyl-tyrosine phosphorylation Source: GOC
    21. positive regulation of angiogenesis Source: Ensembl
    22. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    23. positive regulation of neuron projection development Source: UniProtKB
    24. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    25. positive regulation of programmed cell death Source: UniProtKB
    26. positive regulation of Ras GTPase activity Source: UniProtKB
    27. positive regulation of Ras protein signal transduction Source: UniProtKB
    28. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
    29. protein autophosphorylation Source: UniProtKB
    30. protein phosphorylation Source: MGI
    31. response to activity Source: Ensembl
    32. response to axon injury Source: Ensembl
    33. response to drug Source: Ensembl
    34. response to electrical stimulus Source: Ensembl
    35. response to ethanol Source: Ensembl
    36. response to hydrostatic pressure Source: Ensembl
    37. response to nutrient levels Source: Ensembl
    38. response to radiation Source: Ensembl
    39. Sertoli cell development Source: Ensembl
    40. sympathetic nervous system development Source: UniProtKB

    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

    ReactomeiREACT_202778. Retrograde neurotrophin signalling.
    REACT_205300. PI3K/AKT activation.
    REACT_209347. NGF-independant TRKA activation.
    REACT_212952. Signalling to STAT3.
    REACT_213333. TRKA activation by NGF.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    High affinity nerve growth factor receptor (EC:2.7.10.1)
    Alternative name(s):
    Neurotrophic tyrosine kinase receptor type 1
    Gene namesi
    Name:Ntrk1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:97383. Ntrk1.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type I membrane protein By similarity. Early endosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Late endosome membrane By similarity; Single-pass type I membrane protein By similarity
    Note: Localized at cell membrane and early endosomes before nerve growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with RAPGEF2 at late endosomes By similarity. Internalized to endosomes upon binding of NGF or NTF3 and further transported to the cell body via a retrograde axonal transport.By similarity

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cell surface Source: MGI
    3. cytoplasm Source: MGI
    4. cytoplasmic vesicle Source: Ensembl
    5. dendrite Source: Ensembl
    6. early endosome Source: UniProtKB
    7. early endosome membrane Source: UniProtKB-SubCell
    8. integral component of plasma membrane Source: UniProtKB
    9. late endosome Source: UniProtKB
    10. late endosome membrane Source: UniProtKB-SubCell
    11. neuronal cell body Source: Ensembl
    12. plasma membrane Source: UniProtKB
    13. protein complex Source: UniProtKB
    14. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice die early after birth due to severe sensory and sympathetic neuropathies characterized by extensive neuronal cell loss in trigeminal, sympathetic and dorsal root ganglia, as well as a decrease in the cholinergic basal forebrain projections to the hippocampus and cortex. There are for instance 35% fewer cells by E17.5 in the superior cervical ganglion, a major component of the sympathetic system.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 799766High affinity nerve growth factor receptorPRO_0000278537Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi154 ↔ 193PROSITE-ProRule annotation
    Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi217 ↔ 267PROSITE-ProRule annotation
    Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi320 – 3201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi361 – 3611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
    Modified residuei499 – 4991Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei679 – 6791Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei683 – 6831Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei684 – 6841Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei794 – 7941Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Ligand-mediated autophosphorylation. Interaction with SQSTM1 is phosphotyrosine-dependent. Autophosphorylation at Tyr-499 mediates interaction and phosphorylation of SHC1.
    N-glycosylated.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

    PaxDbiQ3UFB7.
    PRIDEiQ3UFB7.

    PTM databases

    PhosphoSiteiQ3UFB7.

    Expressioni

    Developmental stagei

    First detected at E13.5, a time coinciding with the requirement of sympathetic neurons for NGF.1 Publication

    Inductioni

    Expression oscillates in a circadian manner in the suprachiasmatic nucleus (SCN) of the brain.1 Publication

    Gene expression databases

    BgeeiQ3UFB7.
    CleanExiMM_NTRK1.
    GenevestigatoriQ3UFB7.

    Interactioni

    Subunit structurei

    Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. Homodimerization is induced by binding of a NGF dimer. Interacts with SQSTM1; bridges NTRK1 to NGFR. Forms a ternary complex with NGFR and KIDINS220; this complex is affected by the expression levels of KIDINS220 and an increase in KIDINS220 expression leads to a decreased association of NGFR and NTRK1. Interacts (phosphorylated upon activation by NGF) with SHC1; mediates SHC1 phosphorylation and activation. Interacts (phosphorylated upon activation by NGF) with PLCG1; mediates PLCG1 phosphorylation and activation. Interacts (phosphorylated) with SH2B1 and SH2B2. Interacts with GRB2. Interacts with PIK3R1. Interacts with FRS2. Interacts with SORT1; may regulate NTRK1 anterograde axonal transport. Interacts with NRADD By similarity. Interacts with SH2D1A; regulates NTRK1. Interacts with RAB7A By similarity. Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a nerve growth factor (NGF)-dependent manner By similarity. Interacts with RAPGEF2; the interaction is strengthened after NGF stimulation By similarity.By similarity

    Protein-protein interaction databases

    BioGridi201868. 7 interactions.
    DIPiDIP-60900N.
    STRINGi10090.ENSMUSP00000029712.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3UFB7.
    SMRiQ3UFB7. Positions 36-391, 504-797.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini34 – 420387ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini442 – 799358CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei421 – 44121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati90 – 11324LRR 1Add
    BLAST
    Repeati116 – 13722LRR 2Add
    BLAST
    Domaini148 – 21972LRRCTAdd
    BLAST
    Domaini196 – 28590Ig-like C2-type 1Add
    BLAST
    Domaini205 – 368164Ig-like C2-type 2Add
    BLAST
    Domaini513 – 784272Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni472 – 49322Interaction with SQSTM1By similarityAdd
    BLAST

    Domaini

    The transmembrane domain mediates interaction with KIDINS220.By similarity
    The extracellular domain mediates interaction with NGFR.By similarity

    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 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110657.
    HOGENOMiHOG000264255.
    HOVERGENiHBG056735.
    InParanoidiQ3UFB7.
    KOiK03176.
    OMAiKNVTCWA.
    OrthoDBiEOG7GTT32.
    PhylomeDBiQ3UFB7.
    TreeFamiTF106465.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR011009. Kinase-like_dom.
    IPR001611. Leu-rich_rpt.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR020461. Tyr_kinase_neurotrophic_rcpt_1.
    IPR020777. Tyr_kinase_NGF_rcpt.
    IPR002011. Tyr_kinase_rcpt_2_CS.
    [Graphical view]
    PfamiPF13855. LRR_8. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR01939. NTKRECEPTOR.
    PR01940. NTKRECEPTOR1.
    PR00109. TYRKINASE.
    SMARTiSM00409. IG. 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q3UFB7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRGQRLGQL GWHRPAAGLG SLMTSLMLAC ASAASCREVC CPVGPSGLRC    50
    TRAGSLDTLR GLRGAGNLTE LYVENQQHLQ RLEFEDLQGL GELRSLTIVK 100
    SGLRFVAPDA FRFTPRLSHL NLSSNALESL SWKTVQGLSL QDLTLSGNPL 150
    HCSCALFWLQ RWEQEGLCGV HTQTLHDSGP GDQFLPLGHN TSCGVPTVKI 200
    QMPNDSVEVG DDVFLQCQVE GLALQQADWI LTELEGAATV KKFGDLPSLG 250
    LILVNVTSDL NKKNVTCWAE NDVGRAEVSV QVSVSFPASV HLGLAVEQHH 300
    WCIPFSVDGQ PAPSLRWLFN GSVLNETSFI FTQFLESALT NETMRHGCLR 350
    LNQPTHVNNG NYTLLAANPY GQAAASVMAA FMDNPFEFNP EDPIPVSFSP 400
    VDGNSTSRDP VEKKDETPFG VSVAVGLAVS AALFLSALLL VLNKCGQRSK 450
    FGINRPAVLA PEDGLAMSLH FMTLGGSSLS PTEGKGSGLQ GHIMENPQYF 500
    SDTCVHHIKR QDIILKWELG EGAFGKVFLA ECYNLLNDQD KMLVAVKALK 550
    EASENARQDF QREAELLTML QHQHIVRFFG VCTEGGPLLM VFEYMRHGDL 600
    NRFLRSHGPD AKLLAGGEDV APGPLGLGQL LAVASQVAAG MVYLASLHFV 650
    HRDLATRNCL VGQGLVVKIG DFGMSRDIYS TDYYRVGGRT MLPIRWMPPE 700
    SILYRKFSTE SDVWSFGVVL WEIFTYGKQP WYQLSNTEAI ECITQGRELE 750
    RPRACPPDVY AIMRGCWQRE PQQRLSMKDV HARLQALAQA PPSYLDVLG 799
    Length:799
    Mass (Da):87,738
    Last modified:February 20, 2007 - v2
    Checksum:i1A37F76A63564603
    GO

    Sequence cautioni

    The sequence BAE28644.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK081588 mRNA. No translation available.
    AK148691 mRNA. Translation: BAE28644.1. Different initiation.
    CCDSiCCDS50947.1.
    RefSeqiNP_001028296.1. NM_001033124.1.
    UniGeneiMm.80682.

    Genome annotation databases

    EnsembliENSMUST00000029712; ENSMUSP00000029712; ENSMUSG00000028072.
    GeneIDi18211.
    KEGGimmu:18211.
    UCSCiuc008psw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK081588 mRNA. No translation available.
    AK148691 mRNA. Translation: BAE28644.1 . Different initiation.
    CCDSi CCDS50947.1.
    RefSeqi NP_001028296.1. NM_001033124.1.
    UniGenei Mm.80682.

    3D structure databases

    ProteinModelPortali Q3UFB7.
    SMRi Q3UFB7. Positions 36-391, 504-797.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201868. 7 interactions.
    DIPi DIP-60900N.
    STRINGi 10090.ENSMUSP00000029712.

    PTM databases

    PhosphoSitei Q3UFB7.

    Proteomic databases

    PaxDbi Q3UFB7.
    PRIDEi Q3UFB7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029712 ; ENSMUSP00000029712 ; ENSMUSG00000028072 .
    GeneIDi 18211.
    KEGGi mmu:18211.
    UCSCi uc008psw.1. mouse.

    Organism-specific databases

    CTDi 4914.
    MGIi MGI:97383. Ntrk1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110657.
    HOGENOMi HOG000264255.
    HOVERGENi HBG056735.
    InParanoidi Q3UFB7.
    KOi K03176.
    OMAi KNVTCWA.
    OrthoDBi EOG7GTT32.
    PhylomeDBi Q3UFB7.
    TreeFami TF106465.

    Enzyme and pathway databases

    Reactomei REACT_202778. Retrograde neurotrophin signalling.
    REACT_205300. PI3K/AKT activation.
    REACT_209347. NGF-independant TRKA activation.
    REACT_212952. Signalling to STAT3.
    REACT_213333. TRKA activation by NGF.

    Miscellaneous databases

    NextBioi 293598.
    PROi Q3UFB7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3UFB7.
    CleanExi MM_NTRK1.
    Genevestigatori Q3UFB7.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR011009. Kinase-like_dom.
    IPR001611. Leu-rich_rpt.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR020461. Tyr_kinase_neurotrophic_rcpt_1.
    IPR020777. Tyr_kinase_NGF_rcpt.
    IPR002011. Tyr_kinase_rcpt_2_CS.
    [Graphical view ]
    Pfami PF13855. LRR_8. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR01939. NTKRECEPTOR.
    PR01940. NTKRECEPTOR1.
    PR00109. TYRKINASE.
    SMARTi SM00409. IG. 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. "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].
      Strain: C57BL/6J.
      Tissue: Embryo and Sympathetic ganglion.
    2. "Severe sensory and sympathetic neuropathies in mice carrying a disrupted Trk/NGF receptor gene."
      Smeyne R.J., Klein R., Schnapp A., Long L.K., Bryant S., Lewin A., Lira S.A., Barbacid M.
      Nature 368:246-249(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN DEVELOPMENT OF THE NERVOUS SYSTEM.
    3. "TrkA, but not TrkC, receptors are essential for survival of sympathetic neurons in vivo."
      Fagan A.M., Zhang H., Landis S., Smeyne R.J., Silos-Santiago I., Barbacid M.
      J. Neurosci. 16:6208-6218(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SYMPATHETIC NEURONS SURVIVAL, DEVELOPMENTAL STAGE.
    4. "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.
    5. "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.
    6. "Recruitment of actin modifiers to TrkA endosomes governs retrograde NGF signaling and survival."
      Harrington A.W., St Hillaire C., Zweifel L.S., Glebova N.O., Philippidou P., Halegoua S., Ginty D.D.
      Cell 146:421-434(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NGF AND NTF3 SIGNALING, ENZYME REGULATION, SUBCELLULAR LOCATION.
    7. "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 nameiNTRK1_MOUSE
    AccessioniPrimary (citable) accession number: Q3UFB7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 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