Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P35546

- RET_MOUSE

UniProt

P35546 - RET_MOUSE

Protein

Proto-oncogene tyrosine-protein kinase receptor Ret

Gene

Ret

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration.2 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Repressed by withaferin A (WA).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei708 – 7092Cleavage; by caspase-3By similarity
    Binding sitei759 – 7591ATPPROSITE-ProRule annotation
    Active sitei875 – 8751Proton acceptorPROSITE-ProRule annotation
    Binding sitei893 – 8931InhibitorBy similarity
    Sitei1018 – 10192Cleavage; by caspase-3By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi731 – 7399ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: Ensembl
    3. protein binding Source: IntAct
    4. transmembrane receptor protein tyrosine kinase activity Source: MGI

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    2. anatomical structure morphogenesis Source: MGI
    3. cellular response to retinoic acid Source: Ensembl
    4. embryonic epithelial tube formation Source: MGI
    5. enteric nervous system development Source: MGI
    6. homophilic cell adhesion Source: InterPro
    7. innervation Source: Ensembl
    8. MAPK cascade Source: MGI
    9. membrane protein proteolysis Source: Ensembl
    10. nervous system development Source: MGI
    11. neural crest cell migration Source: MGI
    12. neuron cell-cell adhesion Source: UniProtKB
    13. neuron differentiation Source: MGI
    14. neuron maturation Source: MGI
    15. peptidyl-tyrosine phosphorylation Source: GOC
    16. Peyer's patch morphogenesis Source: UniProtKB
    17. positive regulation of cell adhesion mediated by integrin Source: Ensembl
    18. positive regulation of cell migration Source: Ensembl
    19. positive regulation of cell size Source: MGI
    20. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    21. positive regulation of metanephric glomerulus development Source: UniProtKB
    22. positive regulation of neuron maturation Source: Ensembl
    23. positive regulation of neuron projection development Source: Ensembl
    24. positive regulation of transcription, DNA-templated Source: UniProtKB
    25. regulation of axonogenesis Source: MGI
    26. response to drug Source: Ensembl
    27. response to pain Source: UniProtKB
    28. retina development in camera-type eye Source: Ensembl
    29. transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI
    30. ureteric bud development Source: MGI
    31. ureter maturation Source: MGI

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proto-oncogene tyrosine-protein kinase receptor Ret (EC:2.7.10.1)
    Alternative name(s):
    Proto-oncogene c-Ret
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Ret
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:97902. Ret.

    Subcellular locationi

    GO - Cellular componenti

    1. endosome membrane Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: Ensembl
    3. membrane raft Source: Ensembl
    4. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Exclusive loss in nociceptors results in a reduction in nociceptor number and size with a reduced epidermal innervation, but increased sensitivity to cold and increased formalin-induced pain.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1063 – 10631Y → F: Abolishes interaction with DOK proteins. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 11151087Proto-oncogene tyrosine-protein kinase receptor RetPRO_0000024451Add
    BLAST
    Chaini29 – 708680Extracellular cell-membrane anchored RET cadherin 120 kDa fragmentBy similarityPRO_0000415294Add
    BLAST
    Chaini709 – 1018310Soluble RET kinase fragmentBy similarityPRO_0000415295Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi137 ↔ 142By similarity
    Glycosylationi151 – 1511N-linked (GlcNAc...)By similarity
    Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi556 – 5561N-linked (GlcNAc...)Sequence Analysis
    Modified residuei697 – 6971PhosphoserineBy similarity
    Modified residuei807 – 8071Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei810 – 8101Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei901 – 9011Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei906 – 9061Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei982 – 9821Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1016 – 10161Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1063 – 10631Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei1091 – 10911Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1097 – 10971Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated on C-terminal tyrosine residues upon ligand stimulation. Dephosphorylated by PTPRJ on Tyr-906, Tyr-1016 and Tyr-1063 By similarity.By similarity
    Proteolytically cleaved by caspase-3. The soluble RET kinase fragment is able to induce cell death. The extracellular cell-membrane anchored RET cadherin fragment accelerates cell adhesion in sympathetic neurons By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiP35546.

    PTM databases

    PhosphoSiteiP35546.

    Expressioni

    Tissue specificityi

    Expressed in peripheral nerve cells, hematopoietic cells and podocytes.1 Publication

    Gene expression databases

    BgeeiP35546.
    CleanExiMM_RET.
    GenevestigatoriP35546.

    Interactioni

    Subunit structurei

    Phosphorylated form interacts with the PBT domain of DOK2, DOK4 and DOK5. The phosphorylated form interacts with PLCG1 and GRB7. Interacts (not phosphorylated) with PTK2/FAK1 (via FERM domain). Extracellular cell-membrane anchored RET cadherin fragments form complex in neurons with reduced trophic status, preferentially at the contact sites between somas. Interacts with AIP in the pituitary gland; this interaction prevents the formation of the AIP-survivin complex. Binds to ARTN. Interacts (inactive) with CBLC and CD2AP; dissociates upon activation by GDNF which increases CBLC:CD2AP interaction.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Epha5Q606295EBI-5548911,EBI-1267609

    Protein-protein interaction databases

    BioGridi202865. 2 interactions.
    IntActiP35546. 10 interactions.
    MINTiMINT-5313433.

    Structurei

    Secondary structure

    1
    1115
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1057 – 10593
    Turni1061 – 10644

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UEFX-ray2.50C/D1055-1067[»]
    ProteinModelPortaliP35546.
    SMRiP35546. Positions 29-273, 714-1012.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35546.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 637609ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini660 – 1115456CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei638 – 65922HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini168 – 273106CadherinPROSITE-ProRule annotationAdd
    BLAST
    Domaini725 – 1017293Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni806 – 8083Inhibitors bindingBy similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
    Contains 1 cadherin domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00670000097694.
    HOGENOMiHOG000010301.
    HOVERGENiHBG002609.
    InParanoidiP35546.
    KOiK05126.
    OMAiSMENQVS.
    OrthoDBiEOG7NGQ9N.
    PhylomeDBiP35546.
    TreeFamiTF317640.

    Family and domain databases

    Gene3Di2.60.40.60. 1 hit.
    InterProiIPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR011009. Kinase-like_dom.
    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.
    IPR016249. Tyr_kinase_Ret_rcpt.
    [Graphical view]
    PfamiPF00028. Cadherin. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000631. TyrPK_receptor_Ret. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00112. CA. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49313. SSF49313. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50268. CADHERIN_2. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35546-1) [UniParc]FASTAAdd to Basket

    Also known as: Ret51

    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

    MAKATSGAAG LGLKLILLLP LLGEAPLGLY FSRDAYWERL YVDQPAGTPL     50
    LYVHALRDAP GEVPSFRLGQ HLYGVYRTRL HENDWIRINE TTGLLYLNQS 100
    LDHSSWEQLS IRNGGFPLLT IFLQVFLGST AQREGECHWP GCTRVYFSFI 150
    NDTFPNCSSF KAQDLCIPET AVSFRVRENR PPGTFYHFHM LPVQFLCPNI 200
    SVKYSLLGGD SLPFRCDPDC LEVSTRWALD RELREKYVLE ALCIVAGPGA 250
    NKETVTLSFP VTVYDEDDSA PTFSGGVGTA SAVVEFKRKE GTVVATLQVF 300
    DADVVPASGE LVRRYTNTLL SGDSWAQQTF RVEHSPIETL VQVNNNSVRA 350
    TMHNYKLILN RSLSISESRV LQLAVLVNDS DFQGPGAGGI LVLHFNVSVL 400
    PVTLNLPRAY SFPVNKRARR YAQIGKVCVE NCQEFSGVSI QYKLQPSSIN 450
    CTALGVVTSP EDTSGTLFVN DTEALRRPEC TKLQYTVVAT DRQTRRQTQA 500
    SLVVTVEGTS ITEEVGCPKS CAVNKRRPEC EECGGLGSPT GRCEWRQGDG 550
    KGITRNFSTC SPSTRTCPDG HCDAVESRDA NICPQDCLRA DIVGGHERGE 600
    RQGIKAGYGI CNCFPDEKKC FCEPEDSQGP LCDALCRTII TAALFSLIIS 650
    ILLSIFCVCH HHKHGHKPPI ASAEMTFCRP AQGFPISYSS SGTRRPSLDS 700
    TENQVPVDSF KIPEDPKWEF PRKNLVLGKT LGEGEFGKVV KATAFRLKGR 750
    AGYTTVAVKM LKENASQSEL RDLLSEFNLL KQVNHPHVIK LYGACSQDGP 800
    LLLIVEYAKY GSLRGFLRDS RKIGPAYVSG GGSRNSSSLD HPDERVLTMG 850
    DLISFAWQIS RGMQYLAEMK LVHRDLAARN ILVAEGRKMK ISDFGLSRDV 900
    YEEDSYVKKS KGRIPVKWMA IESLFDHIYT TQSDVWSFGV LLWEIVTLGG 950
    NPYPGIPPER LFNLLKTGHR MERPDNCSEE MYRLMLQCWK QEPDKRPVFA 1000
    DISKDLEKMM VKSRDYLDLA ASTPSDSLLY DDGLSEEETP LVDCNNAPLP 1050
    RSLPSTWIEN KLYGMSDPNW PGESPVPLTR ADGTSTGFPR YANDSVYANW 1100
    MVSPSAAKLM DTFDS 1115
    Length:1,115
    Mass (Da):123,874
    Last modified:August 16, 2004 - v2
    Checksum:iA5CF1EF45A640413
    GO
    Isoform 2 (identifier: P35546-2) [UniParc]FASTAAdd to Basket

    Also known as: Ret9

    The sequence of this isoform differs from the canonical sequence as follows:
         1065-1115: MSDPNWPGESPVPLTRADGTSTGFPRYANDSVYANWMVSPSAAKLMDTFDS → RISHAFTRF

    Show »
    Length:1,073
    Mass (Da):119,469
    Checksum:iDB582E8D490C4A62
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti174 – 1741F → S in CAA48013. (PubMed:8455936)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1065 – 111551MSDPN…DTFDS → RISHAFTRF in isoform 2. 3 PublicationsVSP_011304Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67812 mRNA. Translation: CAA48013.1.
    AF209436 mRNA. Translation: AAF21033.1.
    AY326397 mRNA. Translation: AAP88379.1.
    AK051633 mRNA. Translation: BAC34699.1.
    BC059012 mRNA. Translation: AAH59012.1.
    CCDSiCCDS20470.1. [P35546-1]
    CCDS39608.1. [P35546-2]
    PIRiI48735. S29926.
    RefSeqiNP_001074249.1. NM_001080780.1. [P35546-2]
    NP_033076.2. NM_009050.2. [P35546-1]
    UniGeneiMm.57199.

    Genome annotation databases

    EnsembliENSMUST00000032201; ENSMUSP00000032201; ENSMUSG00000030110. [P35546-1]
    ENSMUST00000088790; ENSMUSP00000086169; ENSMUSG00000030110. [P35546-2]
    GeneIDi19713.
    KEGGimmu:19713.
    UCSCiuc009dlm.1. mouse. [P35546-1]
    uc009dln.1. mouse. [P35546-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67812 mRNA. Translation: CAA48013.1 .
    AF209436 mRNA. Translation: AAF21033.1 .
    AY326397 mRNA. Translation: AAP88379.1 .
    AK051633 mRNA. Translation: BAC34699.1 .
    BC059012 mRNA. Translation: AAH59012.1 .
    CCDSi CCDS20470.1. [P35546-1 ]
    CCDS39608.1. [P35546-2 ]
    PIRi I48735. S29926.
    RefSeqi NP_001074249.1. NM_001080780.1. [P35546-2 ]
    NP_033076.2. NM_009050.2. [P35546-1 ]
    UniGenei Mm.57199.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UEF X-ray 2.50 C/D 1055-1067 [» ]
    ProteinModelPortali P35546.
    SMRi P35546. Positions 29-273, 714-1012.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202865. 2 interactions.
    IntActi P35546. 10 interactions.
    MINTi MINT-5313433.

    Chemistry

    ChEMBLi CHEMBL2034799.

    PTM databases

    PhosphoSitei P35546.

    Proteomic databases

    PRIDEi P35546.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032201 ; ENSMUSP00000032201 ; ENSMUSG00000030110 . [P35546-1 ]
    ENSMUST00000088790 ; ENSMUSP00000086169 ; ENSMUSG00000030110 . [P35546-2 ]
    GeneIDi 19713.
    KEGGi mmu:19713.
    UCSCi uc009dlm.1. mouse. [P35546-1 ]
    uc009dln.1. mouse. [P35546-2 ]

    Organism-specific databases

    CTDi 5979.
    MGIi MGI:97902. Ret.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00670000097694.
    HOGENOMi HOG000010301.
    HOVERGENi HBG002609.
    InParanoidi P35546.
    KOi K05126.
    OMAi SMENQVS.
    OrthoDBi EOG7NGQ9N.
    PhylomeDBi P35546.
    TreeFami TF317640.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    EvolutionaryTracei P35546.
    NextBioi 297098.
    PROi P35546.
    SOURCEi Search...

    Gene expression databases

    Bgeei P35546.
    CleanExi MM_RET.
    Genevestigatori P35546.

    Family and domain databases

    Gene3Di 2.60.40.60. 1 hit.
    InterProi IPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR011009. Kinase-like_dom.
    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.
    IPR016249. Tyr_kinase_Ret_rcpt.
    [Graphical view ]
    Pfami PF00028. Cadherin. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000631. TyrPK_receptor_Ret. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00112. CA. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49313. SSF49313. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50268. CADHERIN_2. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of mouse ret proto-oncogene and its sequence similarity to the cadherin superfamily."
      Iwamoto T., Taniguchi M., Asai N., Ohkusu K., Nakashima I., Takahashi M.
      Oncogene 8:1087-1091(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular characterization of mouse neuro-2a c-ret proto-oncogene."
      Phua C.Y.D., Too H.P.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Wang Y.-Z., Yoong L.-F., Too H.-P.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: BALB/c.
    4. "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] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Spinal ganglion.
    5. "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 2).
      Strain: C57BL/6.
      Tissue: Brain.
    6. "Direct association between the Ret receptor tyrosine kinase and the Src homology 2-containing adapter protein Grb7."
      Pandey A., Liu X., Dixon J.E., Di Fiore P.P., Dixit V.M.
      J. Biol. Chem. 271:10607-10610(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB7 AND PLCG1.
    7. "Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation."
      Grimm J., Sachs M., Britsch S., Di Cesare S., Schwarz-Romond T., Alitalo K., Birchmeier W.
      J. Cell Biol. 154:345-354(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOK2; DOK4 AND DOK5, PHOSPHORYLATION, MUTAGENESIS OF TYR-1063.
    8. "Tyrosine kinase receptor RET is a key regulator of Peyer's patch organogenesis."
      Veiga-Fernandes H., Coles M.C., Foster K.E., Patel A., Williams A., Natarajan D., Barlow A., Pachnis V., Kioussis D.
      Nature 446:547-551(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PEYER'S PATCH ORGANOGENESIS, INTERACTION WITH ARTN.
    9. "CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the regulation of ret signal transduction."
      Tsui C.C., Pierchala B.A.
      J. Neurosci. 28:8789-8800(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RET, TISSUE SPECIFICITY.
    10. "RET signaling is required for survival and normal function of nonpeptidergic nociceptors."
      Golden J.P., Hoshi M., Nassar M.A., Enomoto H., Wood J.N., Milbrandt J., Gereau R.W. IV, Johnson E.M. Jr., Jain S.
      J. Neurosci. 30:3983-3994(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NOCICEPTORS REGULATION, DISRUPTION PHENOTYPE.
    11. "A novel RET inhibitor with potent efficacy against medullary thyroid cancer in vivo."
      Samadi A.K., Mukerji R., Shah A., Timmermann B.N., Cohen M.S.
      Surgery 148:1228-1236(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    12. "Structural basis for the specific recognition of RET by the Dok1 phosphotyrosine binding domain."
      Shi N., Ye S., Bartlam M., Yang M., Wu J., Liu Y., Sun F., Han X., Peng X., Qiang B., Yuan J., Rao Z.
      J. Biol. Chem. 279:4962-4969(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1055-1067, PHOSPHORYLATION AT TYR-1063.

    Entry informationi

    Entry nameiRET_MOUSE
    AccessioniPrimary (citable) accession number: P35546
    Secondary accession number(s): Q8BQ34, Q9QXH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Treatment with withaferin A (WA) leads tumor regression in medullary thyroid carcinomas (MTC).

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3