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Protein

Proto-oncogene tyrosine-protein kinase receptor Ret

Gene

Ret

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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: MGI
  3. transmembrane receptor protein tyrosine kinase activity Source: MGI

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  2. anatomical structure morphogenesis Source: MGI
  3. cellular response to retinoic acid Source: MGI
  4. embryonic epithelial tube formation Source: MGI
  5. enteric nervous system development Source: MGI
  6. homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  7. innervation Source: Ensembl
  8. MAPK cascade Source: MGI
  9. membrane protein proteolysis Source: MGI
  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: MGI
  18. positive regulation of cell migration Source: MGI
  19. positive regulation of cell size Source: MGI
  20. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  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: MGI
  24. positive regulation of transcription, DNA-templated Source: UniProtKB
  25. regulation of axonogenesis Source: MGI
  26. regulation of cell adhesion Source: MGI
  27. response to drug Source: Ensembl
  28. response to pain Source: UniProtKB
  29. retina development in camera-type eye Source: Ensembl
  30. transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI
  31. ureteric bud development Source: MGI
  32. ureter maturation Source: MGI
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 637609ExtracellularSequence AnalysisAdd
BLAST
Transmembranei638 – 65922HelicalSequence AnalysisAdd
BLAST
Topological domaini660 – 1115456CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. endosome membrane Source: MGI
  3. integral component of plasma membrane Source: MGI
  4. intracellular membrane-bounded organelle Source: MGI
  5. membrane raft Source: Ensembl
  6. plasma membrane Source: MGI
  7. receptor complex Source: MGI
Complete GO annotation...

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 autocatalysis1 Publication
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

MaxQBiP35546.
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 – 10593Combined sources
Turni1061 – 10644Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP35546.

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.
GeneTreeiENSGT00760000118923.
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. AlignAdd to basket

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

        10         20         30         40         50
MAKATSGAAG LGLKLILLLP LLGEAPLGLY FSRDAYWERL YVDQPAGTPL
60 70 80 90 100
LYVHALRDAP GEVPSFRLGQ HLYGVYRTRL HENDWIRINE TTGLLYLNQS
110 120 130 140 150
LDHSSWEQLS IRNGGFPLLT IFLQVFLGST AQREGECHWP GCTRVYFSFI
160 170 180 190 200
NDTFPNCSSF KAQDLCIPET AVSFRVRENR PPGTFYHFHM LPVQFLCPNI
210 220 230 240 250
SVKYSLLGGD SLPFRCDPDC LEVSTRWALD RELREKYVLE ALCIVAGPGA
260 270 280 290 300
NKETVTLSFP VTVYDEDDSA PTFSGGVGTA SAVVEFKRKE GTVVATLQVF
310 320 330 340 350
DADVVPASGE LVRRYTNTLL SGDSWAQQTF RVEHSPIETL VQVNNNSVRA
360 370 380 390 400
TMHNYKLILN RSLSISESRV LQLAVLVNDS DFQGPGAGGI LVLHFNVSVL
410 420 430 440 450
PVTLNLPRAY SFPVNKRARR YAQIGKVCVE NCQEFSGVSI QYKLQPSSIN
460 470 480 490 500
CTALGVVTSP EDTSGTLFVN DTEALRRPEC TKLQYTVVAT DRQTRRQTQA
510 520 530 540 550
SLVVTVEGTS ITEEVGCPKS CAVNKRRPEC EECGGLGSPT GRCEWRQGDG
560 570 580 590 600
KGITRNFSTC SPSTRTCPDG HCDAVESRDA NICPQDCLRA DIVGGHERGE
610 620 630 640 650
RQGIKAGYGI CNCFPDEKKC FCEPEDSQGP LCDALCRTII TAALFSLIIS
660 670 680 690 700
ILLSIFCVCH HHKHGHKPPI ASAEMTFCRP AQGFPISYSS SGTRRPSLDS
710 720 730 740 750
TENQVPVDSF KIPEDPKWEF PRKNLVLGKT LGEGEFGKVV KATAFRLKGR
760 770 780 790 800
AGYTTVAVKM LKENASQSEL RDLLSEFNLL KQVNHPHVIK LYGACSQDGP
810 820 830 840 850
LLLIVEYAKY GSLRGFLRDS RKIGPAYVSG GGSRNSSSLD HPDERVLTMG
860 870 880 890 900
DLISFAWQIS RGMQYLAEMK LVHRDLAARN ILVAEGRKMK ISDFGLSRDV
910 920 930 940 950
YEEDSYVKKS KGRIPVKWMA IESLFDHIYT TQSDVWSFGV LLWEIVTLGG
960 970 980 990 1000
NPYPGIPPER LFNLLKTGHR MERPDNCSEE MYRLMLQCWK QEPDKRPVFA
1010 1020 1030 1040 1050
DISKDLEKMM VKSRDYLDLA ASTPSDSLLY DDGLSEEETP LVDCNNAPLP
1060 1070 1080 1090 1100
RSLPSTWIEN KLYGMSDPNW PGESPVPLTR ADGTSTGFPR YANDSVYANW
1110
MVSPSAAKLM DTFDS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBiP35546.
ChEMBLiCHEMBL2034799.

PTM databases

PhosphoSiteiP35546.

Proteomic databases

MaxQBiP35546.
PRIDEiP35546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi5979.
MGIiMGI:97902. Ret.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000010301.
HOVERGENiHBG002609.
InParanoidiP35546.
KOiK05126.
OMAiSMENQVS.
OrthoDBiEOG7NGQ9N.
PhylomeDBiP35546.
TreeFamiTF317640.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.

Miscellaneous databases

EvolutionaryTraceiP35546.
NextBioi297098.
PROiP35546.
SOURCEiSearch...

Gene expression databases

BgeeiP35546.
CleanExiMM_RET.
GenevestigatoriP35546.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 147 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.