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Q16288

- NTRK3_HUMAN

UniProt

Q16288 - NTRK3_HUMAN

Protein

NT-3 growth factor receptor

Gene

NTRK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 2 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Receptor for neurotrophin-3 (NT-3). This is a tyrosine-protein kinase receptor. Known substrates for the trk receptors are SHC1, PI-3 kinase, and PLCG1. The different isoforms do not have identical signaling properties.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei516 – 5161Interaction with SHC1By similarity
    Binding sitei572 – 5721ATPPROSITE-ProRule annotation
    Active sitei679 – 6791Proton acceptorPROSITE-ProRule annotation
    Sitei834 – 8341Interaction with PLC-gamma-1By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi544 – 5529ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. neurotrophin binding Source: ProtInc
    3. neurotrophin receptor activity Source: BHF-UCL
    4. p53 binding Source: BHF-UCL
    5. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. activation of MAPK activity Source: BHF-UCL
    2. activation of protein kinase B activity Source: BHF-UCL
    3. activation of Ras GTPase activity Source: BHF-UCL
    4. cellular response to retinoic acid Source: Ensembl
    5. cochlea development Source: Ensembl
    6. mechanoreceptor differentiation Source: Ensembl
    7. modulation by virus of host transcription Source: Ensembl
    8. negative regulation of astrocyte differentiation Source: Ensembl
    9. negative regulation of cell death Source: Ensembl
    10. negative regulation of protein phosphorylation Source: BHF-UCL
    11. neuron fate specification Source: Ensembl
    12. neuron migration Source: Ensembl
    13. neurotrophin signaling pathway Source: GOC
    14. positive regulation of actin cytoskeleton reorganization Source: BHF-UCL
    15. positive regulation of axon extension involved in regeneration Source: Ensembl
    16. positive regulation of cell migration Source: BHF-UCL
    17. positive regulation of cell proliferation Source: BHF-UCL
    18. positive regulation of gene expression Source: BHF-UCL
    19. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    20. positive regulation of positive chemotaxis Source: BHF-UCL
    21. protein autophosphorylation Source: Ensembl
    22. response to axon injury Source: Ensembl
    23. response to corticosterone Source: Ensembl
    24. response to ethanol Source: Ensembl
    25. transmembrane receptor protein tyrosine kinase signaling pathway Source: BHF-UCL

    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.
    SignaLinkiQ16288.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NT-3 growth factor receptor (EC:2.7.10.1)
    Alternative name(s):
    GP145-TrkC
    Short name:
    Trk-C
    Neurotrophic tyrosine kinase receptor type 3
    TrkC tyrosine kinase
    Gene namesi
    Name:NTRK3
    Synonyms:TRKC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:8033. NTRK3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. integral component of plasma membrane Source: ProtInc
    3. receptor complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti2665. Congenital mesoblastic nephroma.
    2030. Fibrosarcoma.
    PharmGKBiPA31819.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Add
    BLAST
    Chaini32 – 839808NT-3 growth factor receptorPRO_0000016731Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi272 – 2721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi320 ↔ 3621 PublicationPROSITE-ProRule annotation
    Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
    Modified residuei516 – 5161Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei705 – 7051Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei709 – 7091Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei710 – 7101Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Ligand-mediated auto-phosphorylation.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ16288.
    PaxDbiQ16288.
    PRIDEiQ16288.

    PTM databases

    PhosphoSiteiQ16288.

    Expressioni

    Tissue specificityi

    Widely expressed but mainly in nervous tissue. Isoform 2 is expressed at higher levels in adult brain than in fetal brain.

    Gene expression databases

    ArrayExpressiQ16288.
    BgeeiQ16288.
    CleanExiHS_NTRK3.
    GenevestigatoriQ16288.

    Organism-specific databases

    HPAiCAB009233.

    Interactioni

    Subunit structurei

    Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures. Binds SH2B2. Interacts with SQSTM1 and KIDINS220 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi110971. 9 interactions.
    DIPiDIP-5723N.
    IntActiQ16288. 4 interactions.
    MINTiMINT-188514.
    STRINGi9606.ENSP00000354207.

    Structurei

    Secondary structure

    1
    839
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi318 – 3269
    Beta strandi332 – 3376
    Beta strandi345 – 35410
    Beta strandi356 – 36712
    Helixi370 – 3723
    Beta strandi374 – 3829
    Beta strandi385 – 3939
    Helixi535 – 5373
    Beta strandi538 – 5436
    Beta strandi552 – 5598
    Beta strandi562 – 57312
    Helixi579 – 59416
    Beta strandi603 – 61210
    Beta strandi614 – 6185
    Helixi625 – 6317
    Helixi653 – 67220
    Helixi682 – 6843
    Beta strandi685 – 6873
    Helixi689 – 6913
    Beta strandi693 – 6953
    Helixi706 – 7083
    Helixi734 – 7363
    Helixi739 – 7446
    Helixi749 – 76315
    Turni764 – 7663
    Turni770 – 7734
    Helixi776 – 78510
    Helixi797 – 80610
    Helixi811 – 8133
    Helixi817 – 82913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WWCX-ray1.90A297-422[»]
    3V5QX-ray2.20A/B530-832[»]
    ProteinModelPortaliQ16288.
    SMRiQ16288. Positions 28-401, 529-832.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16288.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 429398ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini454 – 839386CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati104 – 12522LRR 1Add
    BLAST
    Repeati128 – 14922LRR 2Add
    BLAST
    Domaini160 – 20950LRRCTAdd
    BLAST
    Domaini210 – 30091Ig-like C2-type 1Add
    BLAST
    Domaini309 – 38274Ig-like C2-type 2Add
    BLAST
    Domaini538 – 839302Protein 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 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000264255.
    HOVERGENiHBG056735.
    InParanoidiQ16288.
    KOiK05101.
    OMAiNFVSIYE.
    OrthoDBiEOG7GTT32.
    PhylomeDBiQ16288.
    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.
    IPR003599. Ig_sub.
    IPR013151. Immunoglobulin.
    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.
    IPR020446. Tyr_kin_neurotrophic_rcpt_3.
    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. 1 hit.
    PF00047. ig. 1 hit.
    PF13855. LRR_8. 1 hit.
    PF01462. LRRNT. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR01939. NTKRECEPTOR.
    PR01942. NTKRECEPTOR3.
    PR00109. TYRKINASE.
    SMARTiSM00409. IG. 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.
    PS51450. LRR. 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 (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q16288-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MDVSLCPAKC SFWRIFLLGS VWLDYVGSVL ACPANCVCSK TEINCRRPDD    50
    GNLFPLLEGQ DSGNSNGNAS INITDISRNI TSIHIENWRS LHTLNAVDME 100
    LYTGLQKLTI KNSGLRSIQP RAFAKNPHLR YINLSSNRLT TLSWQLFQTL 150
    SLRELQLEQN FFNCSCDIRW MQLWQEQGEA KLNSQNLYCI NADGSQLPLF 200
    RMNISQCDLP EISVSHVNLT VREGDNAVIT CNGSGSPLPD VDWIVTGLQS 250
    INTHQTNLNW TNVHAINLTL VNVTSEDNGF TLTCIAENVV GMSNASVALT 300
    VYYPPRVVSL EEPELRLEHC IEFVVRGNPP PTLHWLHNGQ PLRESKIIHV 350
    EYYQEGEISE GCLLFNKPTH YNNGNYTLIA KNPLGTANQT INGHFLKEPF 400
    PESTDNFILF DEVSPTPPIT VTHKPEEDTF GVSIAVGLAA FACVLLVVLF 450
    VMINKYGRRS KFGMKGPVAV ISGEEDSASP LHHINHGITT PSSLDAGPDT 500
    VVIGMTRIPV IENPQYFRQG HNCHKPDTYV QHIKRRDIVL KRELGEGAFG 550
    KVFLAECYNL SPTKDKMLVA VKALKDPTLA ARKDFQREAE LLTNLQHEHI 600
    VKFYGVCGDG DPLIMVFEYM KHGDLNKFLR AHGPDAMILV DGQPRQAKGE 650
    LGLSQMLHIA SQIASGMVYL ASQHFVHRDL ATRNCLVGAN LLVKIGDFGM 700
    SRDVYSTDYY RLFNPSGNDF CIWCEVGGHT MLPIRWMPPE SIMYRKFTTE 750
    SDVWSFGVIL WEIFTYGKQP WFQLSNTEVI ECITQGRVLE RPRVCPKEVY 800
    DVMLGCWQRE PQQRLNIKEI YKILHALGKA TPIYLDILG 839
    Length:839
    Mass (Da):94,428
    Last modified:March 6, 2007 - v2
    Checksum:i7FE8846830083C08
    GO
    Isoform 2 (identifier: Q16288-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         529-612: YVQHIKRRDI...FYGVCGDGDP → WVFSNIDNHG...VYFSKGRHGF
         613-839: Missing.

    Show »
    Length:612
    Mass (Da):68,452
    Checksum:iF2E84DC71B8E4DB3
    GO
    Isoform 3 (identifier: Q16288-3) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         712-725: Missing.

    Show »
    Length:825
    Mass (Da):92,801
    Checksum:i7ADBE1AF6DB280BF
    GO
    Isoform 4 (identifier: Q16288-4) [UniParc]FASTAAdd to Basket

    Also known as: D

    The sequence of this isoform differs from the canonical sequence as follows:
         402-410: ESTDNFILF → V

    Show »
    Length:831
    Mass (Da):93,460
    Checksum:i4823FA200F88433F
    GO
    Isoform 5 (identifier: Q16288-5) [UniParc]FASTAAdd to Basket

    Also known as: E

    The sequence of this isoform differs from the canonical sequence as follows:
         402-410: ESTDNFILF → V
         712-725: Missing.

    Note: No experimental confirmation.

    Show »
    Length:817
    Mass (Da):91,833
    Checksum:i674CC49828F86789
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651S → G in BAH12511. (PubMed:14702039)Curated
    Sequence conflicti70 – 701S → N in AAB33111. (PubMed:7823156)Curated
    Sequence conflicti70 – 701S → N in AAB33112. (PubMed:7823156)Curated
    Sequence conflicti635 – 6351D → N in AAA75374. (PubMed:7806211)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti149 – 1491T → R in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041471
    Natural varianti306 – 3061R → C.1 Publication
    Corresponds to variant rs56386352 [ dbSNP | Ensembl ].
    VAR_041472
    Natural varianti307 – 3071V → L in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041473
    Natural varianti336 – 3361L → Q in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041474
    Natural varianti664 – 6641A → S in a lung carcinoma sample; somatic mutation. 1 Publication
    VAR_046521
    Natural varianti677 – 6771H → Y in a lung adenocarcinoma sample; somatic mutation. 2 Publications
    VAR_041475
    Natural varianti678 – 6781R → Q.1 Publication
    Corresponds to variant rs55890138 [ dbSNP | Ensembl ].
    VAR_041476
    Natural varianti735 – 7351R → F in a lung large cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions.
    VAR_046770
    Natural varianti736 – 7361W → C in a lung carcinoma sample; somatic mutation. 1 Publication
    VAR_046522
    Natural varianti745 – 7451R → P in a lung carcinoma sample; somatic mutation. 1 Publication
    VAR_046523
    Natural varianti766 – 7661Y → F in a lung carcinoma sample; somatic mutation. 1 Publication
    VAR_046524
    Natural varianti768 – 7681K → R.1 Publication
    Corresponds to variant rs55770052 [ dbSNP | Ensembl ].
    VAR_046771
    Natural varianti781 – 7811E → K.1 Publication
    Corresponds to variant rs56393451 [ dbSNP | Ensembl ].
    VAR_046772

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei402 – 4109ESTDNFILF → V in isoform 4 and isoform 5. 1 PublicationVSP_002924
    Alternative sequencei529 – 61284YVQHI…GDGDP → WVFSNIDNHGILNLKDNRDH LVPSTHYIYEEPEVQSGEVS YPRSHGFREIMLNPISLPGH SKPLNHGIYVEDVNVYFSKG RHGF in isoform 2. 1 PublicationVSP_002925Add
    BLAST
    Alternative sequencei613 – 839227Missing in isoform 2. 1 PublicationVSP_002926Add
    BLAST
    Alternative sequencei712 – 72514Missing in isoform 3 and isoform 5. 3 PublicationsVSP_002927Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05012 mRNA. Translation: AAA75374.1.
    S76475 mRNA. Translation: AAB33111.1.
    S76476 mRNA. Translation: AAB33112.1.
    AJ224521
    , AJ224522, AJ224523, AJ224524, AJ224525, AJ224526, AJ224527, AJ224528, AJ224529, AJ224530, AJ224531, AJ224532, AJ224533, AJ224534, AJ224535 Genomic DNA. Translation: CAA12029.1.
    AK297160 mRNA. Translation: BAH12511.1.
    AC009711 Genomic DNA. No translation available.
    AC011966 Genomic DNA. No translation available.
    AC021677 Genomic DNA. No translation available.
    CCDSiCCDS10340.1. [Q16288-3]
    CCDS32322.1. [Q16288-1]
    CCDS32323.1. [Q16288-2]
    CCDS58399.1. [Q16288-5]
    PIRiA55178.
    I73632.
    I73633.
    RefSeqiNP_001012338.1. NM_001012338.2. [Q16288-1]
    NP_002521.2. NM_002530.3.
    UniGeneiHs.410969.
    Hs.706364.

    Genome annotation databases

    EnsembliENST00000317501; ENSP00000318328; ENSG00000140538. [Q16288-2]
    ENST00000355254; ENSP00000347397; ENSG00000140538. [Q16288-3]
    ENST00000357724; ENSP00000350356; ENSG00000140538. [Q16288-4]
    ENST00000360948; ENSP00000354207; ENSG00000140538. [Q16288-1]
    ENST00000394480; ENSP00000377990; ENSG00000140538. [Q16288-3]
    ENST00000540489; ENSP00000444673; ENSG00000140538. [Q16288-2]
    ENST00000557856; ENSP00000453959; ENSG00000140538. [Q16288-5]
    GeneIDi4916.
    KEGGihsa:4916.
    UCSCiuc002bme.2. human. [Q16288-1]
    uc002bmf.2. human. [Q16288-3]

    Polymorphism databases

    DMDMi134035335.

    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
    U05012 mRNA. Translation: AAA75374.1 .
    S76475 mRNA. Translation: AAB33111.1 .
    S76476 mRNA. Translation: AAB33112.1 .
    AJ224521
    , AJ224522 , AJ224523 , AJ224524 , AJ224525 , AJ224526 , AJ224527 , AJ224528 , AJ224529 , AJ224530 , AJ224531 , AJ224532 , AJ224533 , AJ224534 , AJ224535 Genomic DNA. Translation: CAA12029.1 .
    AK297160 mRNA. Translation: BAH12511.1 .
    AC009711 Genomic DNA. No translation available.
    AC011966 Genomic DNA. No translation available.
    AC021677 Genomic DNA. No translation available.
    CCDSi CCDS10340.1. [Q16288-3 ]
    CCDS32322.1. [Q16288-1 ]
    CCDS32323.1. [Q16288-2 ]
    CCDS58399.1. [Q16288-5 ]
    PIRi A55178.
    I73632.
    I73633.
    RefSeqi NP_001012338.1. NM_001012338.2. [Q16288-1 ]
    NP_002521.2. NM_002530.3.
    UniGenei Hs.410969.
    Hs.706364.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WWC X-ray 1.90 A 297-422 [» ]
    3V5Q X-ray 2.20 A/B 530-832 [» ]
    ProteinModelPortali Q16288.
    SMRi Q16288. Positions 28-401, 529-832.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110971. 9 interactions.
    DIPi DIP-5723N.
    IntActi Q16288. 4 interactions.
    MINTi MINT-188514.
    STRINGi 9606.ENSP00000354207.

    Chemistry

    BindingDBi Q16288.
    ChEMBLi CHEMBL5608.
    GuidetoPHARMACOLOGYi 1819.

    PTM databases

    PhosphoSitei Q16288.

    Polymorphism databases

    DMDMi 134035335.

    Proteomic databases

    MaxQBi Q16288.
    PaxDbi Q16288.
    PRIDEi Q16288.

    Protocols and materials databases

    DNASUi 4916.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317501 ; ENSP00000318328 ; ENSG00000140538 . [Q16288-2 ]
    ENST00000355254 ; ENSP00000347397 ; ENSG00000140538 . [Q16288-3 ]
    ENST00000357724 ; ENSP00000350356 ; ENSG00000140538 . [Q16288-4 ]
    ENST00000360948 ; ENSP00000354207 ; ENSG00000140538 . [Q16288-1 ]
    ENST00000394480 ; ENSP00000377990 ; ENSG00000140538 . [Q16288-3 ]
    ENST00000540489 ; ENSP00000444673 ; ENSG00000140538 . [Q16288-2 ]
    ENST00000557856 ; ENSP00000453959 ; ENSG00000140538 . [Q16288-5 ]
    GeneIDi 4916.
    KEGGi hsa:4916.
    UCSCi uc002bme.2. human. [Q16288-1 ]
    uc002bmf.2. human. [Q16288-3 ]

    Organism-specific databases

    CTDi 4916.
    GeneCardsi GC15M088402.
    HGNCi HGNC:8033. NTRK3.
    HPAi CAB009233.
    MIMi 191316. gene.
    neXtProti NX_Q16288.
    Orphaneti 2665. Congenital mesoblastic nephroma.
    2030. Fibrosarcoma.
    PharmGKBi PA31819.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000264255.
    HOVERGENi HBG056735.
    InParanoidi Q16288.
    KOi K05101.
    OMAi NFVSIYE.
    OrthoDBi EOG7GTT32.
    PhylomeDBi Q16288.
    TreeFami TF106465.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki Q16288.

    Miscellaneous databases

    ChiTaRSi NTRK3. human.
    EvolutionaryTracei Q16288.
    GeneWikii TrkC_receptor.
    GenomeRNAii 4916.
    NextBioi 18927.
    PROi Q16288.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16288.
    Bgeei Q16288.
    CleanExi HS_NTRK3.
    Genevestigatori Q16288.

    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.
    IPR003599. Ig_sub.
    IPR013151. Immunoglobulin.
    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.
    IPR020446. Tyr_kin_neurotrophic_rcpt_3.
    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. 1 hit.
    PF00047. ig. 1 hit.
    PF13855. LRR_8. 1 hit.
    PF01462. LRRNT. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR01939. NTKRECEPTOR.
    PR01942. NTKRECEPTOR3.
    PR00109. TYRKINASE.
    SMARTi SM00409. IG. 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.
    PS51450. LRR. 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. "Molecular cloning of the cDNA for human TrkC (NTRK3), chromosomal assignment, and evidence for a splice variant."
      McGregor L.M., Baylin S.B., Griffin C.A., Hawkins A.L., Nelkin B.D.
      Genomics 22:267-272(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
      Tissue: Fetal brain.
    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 1; 2 AND 3), PARTIAL PROTEIN SEQUENCE.
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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 5).
      Tissue: Brain.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 (1.9 ANGSTROMS) OF 297-401, DISULFIDE BOND.
    7. "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: VARIANTS [LARGE SCALE ANALYSIS] ARG-149; CYS-306; LEU-307; GLN-336; TYR-677; GLN-678; ARG-768 AND LYS-781.
    8. "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 SER-664; TYR-677; CYS-736; PRO-745 AND PHE-766.

    Entry informationi

    Entry nameiNTRK3_HUMAN
    AccessioniPrimary (citable) accession number: Q16288
    Secondary accession number(s): B7Z4C5
    , E9PG56, H0YND1, O75682, Q12827, Q16289
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 168 of the entry and version 2 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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