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P35546

- RET_MOUSE

UniProt

P35546 - RET_MOUSE

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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

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.

Enzyme regulationi

Repressed by withaferin A (WA).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei708 – 7092Cleavage; by caspase-3 By similarity
Binding sitei759 – 7591ATP By similarity
Active sitei875 – 8751Proton acceptor By similarity
Binding sitei893 – 8931Inhibitor By similarity
Sitei1018 – 10192Cleavage; by caspase-3 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi731 – 7399ATP By similarity

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. MAPK cascade Source: MGI
  2. Peyer's patch morphogenesis Source: UniProtKB
  3. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  4. anatomical structure morphogenesis Source: MGI
  5. cellular response to retinoic acid Source: Ensembl
  6. embryonic epithelial tube formation Source: MGI
  7. enteric nervous system development Source: MGI
  8. homophilic cell adhesion Source: InterPro
  9. innervation Source: Ensembl
  10. membrane protein proteolysis Source: Ensembl
  11. nervous system development Source: MGI
  12. neural crest cell migration Source: MGI
  13. neuron cell-cell adhesion Source: UniProtKB
  14. neuron differentiation Source: MGI
  15. neuron maturation Source: MGI
  16. peptidyl-tyrosine phosphorylation Source: GOC
  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. ureter maturation Source: MGI
  31. ureteric bud development 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 – 637609Extracellular Reviewed prediction
Add
BLAST
Transmembranei638 – 65922Helical; Reviewed prediction
Add
BLAST
Topological domaini660 – 1115456Cytoplasmic Reviewed prediction
Add
BLAST

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
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 – 2828 Reviewed prediction
Add
BLAST
Chaini29 – 11151087Proto-oncogene tyrosine-protein kinase receptor Ret
PRO_0000024451Add
BLAST
Chaini29 – 708680Extracellular cell-membrane anchored RET cadherin 120 kDa fragment By similarity
PRO_0000415294Add
BLAST
Chaini709 – 1018310Soluble RET kinase fragment By similarity
PRO_0000415295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi89 – 891N-linked (GlcNAc...) Reviewed prediction
Glycosylationi98 – 981N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi137 ↔ 142 By similarity
Glycosylationi151 – 1511N-linked (GlcNAc...) By similarity
Glycosylationi156 – 1561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi199 – 1991N-linked (GlcNAc...) Reviewed prediction
Glycosylationi345 – 3451N-linked (GlcNAc...) Reviewed prediction
Glycosylationi360 – 3601N-linked (GlcNAc...) Reviewed prediction
Glycosylationi378 – 3781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi396 – 3961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi450 – 4501N-linked (GlcNAc...) Reviewed prediction
Glycosylationi470 – 4701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi556 – 5561N-linked (GlcNAc...) Reviewed prediction
Modified residuei697 – 6971Phosphoserine By similarity
Modified residuei807 – 8071Phosphotyrosine; by autocatalysis By similarity
Modified residuei810 – 8101Phosphotyrosine; by autocatalysis By similarity
Modified residuei901 – 9011Phosphotyrosine; by autocatalysis By similarity
Modified residuei906 – 9061Phosphotyrosine; by autocatalysis By similarity
Modified residuei982 – 9821Phosphotyrosine; by autocatalysis By similarity
Modified residuei1016 – 10161Phosphotyrosine; by autocatalysis By similarity
Modified residuei1063 – 10631Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1091 – 10911Phosphotyrosine; by autocatalysis By similarity
Modified residuei1097 – 10971Phosphotyrosine; by autocatalysis By 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.2 Publications
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.

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

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.

Miscellaneous databases

EvolutionaryTraceiP35546.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 273106Cadherin
Add
BLAST
Domaini725 – 1017293Protein kinase
Add
BLAST

Region

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

Sequence similaritiesi

Contains 1 cadherin domain.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1065 – 111551MSDPN…DTFDS → RISHAFTRF in isoform 2.
VSP_011304Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741F → S in CAA48013. 1 Publication

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

« 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: July 9, 2014
This is version 141 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

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