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P35546 (RET_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proto-oncogene tyrosine-protein kinase receptor Ret

EC=2.7.10.1
Alternative name(s):
Proto-oncogene c-Ret
Gene names
Name:Ret
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1115 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10

Catalytic activity

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

Enzyme regulation

Repressed by withaferin A (WA). Ref.11

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

Expressed in peripheral nerve cells, hematopoietic cells and podocytes. Ref.9

Post-translational modification

Autophosphorylated on C-terminal tyrosine residues upon ligand stimulation. Dephosphorylated by PTPRJ on Tyr-906, Tyr-1016 and Tyr-1063 By similarity. Ref.7 Ref.12

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.

Disruption phenotype

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. Ref.10

Miscellaneous

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

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family.

Contains 1 cadherin domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from genetic interaction PubMed 15569713. Source: MGI

Peyer's patch morphogenesis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

anatomical structure morphogenesis

Traceable author statement PubMed 11731455. Source: MGI

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

embryonic epithelial tube formation

Inferred from direct assay PubMed 15569713. Source: MGI

enteric nervous system development

Inferred from mutant phenotype PubMed 9834195. Source: MGI

homophilic cell adhesion

Inferred from electronic annotation. Source: InterPro

innervation

Inferred from electronic annotation. Source: Ensembl

membrane protein proteolysis

Inferred from electronic annotation. Source: Ensembl

nervous system development

Inferred from mutant phenotype PubMed 11069590. Source: MGI

neural crest cell migration

Inferred from mutant phenotype PubMed 15242795. Source: MGI

neuron cell-cell adhesion

Inferred from direct assay PubMed 21357690. Source: UniProtKB

neuron differentiation

Inferred from mutant phenotype PubMed 17553423. Source: MGI

neuron maturation

Inferred from mutant phenotype PubMed 15233745. Source: MGI

peptidyl-tyrosine phosphorylation

Traceable author statement PubMed 11731455. Source: GOC

positive regulation of cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell size

Inferred from mutant phenotype PubMed 17553423. Source: MGI

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

positive regulation of metanephric glomerulus development

Inferred from mutant phenotype PubMed 17047028. Source: UniProtKB

positive regulation of neuron maturation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 17047028. Source: UniProtKB

regulation of axonogenesis

Inferred from mutant phenotype PubMed 17553423. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

response to pain

Inferred from mutant phenotype Ref.10. Source: UniProtKB

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from genetic interaction PubMed 9576965. Source: MGI

ureter maturation

Inferred from mutant phenotype PubMed 21521737. Source: MGI

ureteric bud development

Inferred from mutant phenotype PubMed 12195422. Source: MGI

   Cellular_componentendosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

membrane raft

Inferred from electronic annotation. Source: Ensembl

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 22304922. Source: IntAct

transmembrane receptor protein tyrosine kinase activity

Traceable author statement PubMed 11731455. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Epha5Q606295EBI-5548911,EBI-1267609

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35546-1)

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.
Isoform 2 (identifier: P35546-2)

Also known as: Ret9;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 11151087Proto-oncogene tyrosine-protein kinase receptor Ret
PRO_0000024451
Chain29 – 708680Extracellular cell-membrane anchored RET cadherin 120 kDa fragment By similarity
PRO_0000415294
Chain709 – 1018310Soluble RET kinase fragment By similarity
PRO_0000415295

Regions

Topological domain29 – 637609Extracellular Potential
Transmembrane638 – 65922Helical; Potential
Topological domain660 – 1115456Cytoplasmic Potential
Domain168 – 273106Cadherin
Domain725 – 1017293Protein kinase
Nucleotide binding731 – 7399ATP By similarity
Region806 – 8083Inhibitors binding By similarity

Sites

Active site8751Proton acceptor By similarity
Binding site7591ATP By similarity
Binding site8931Inhibitor By similarity
Site708 – 7092Cleavage; by caspase-3 By similarity
Site1018 – 10192Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue6971Phosphoserine By similarity
Modified residue8071Phosphotyrosine; by autocatalysis By similarity
Modified residue8101Phosphotyrosine; by autocatalysis By similarity
Modified residue9011Phosphotyrosine; by autocatalysis By similarity
Modified residue9061Phosphotyrosine; by autocatalysis By similarity
Modified residue9821Phosphotyrosine; by autocatalysis By similarity
Modified residue10161Phosphotyrosine; by autocatalysis By similarity
Modified residue10631Phosphotyrosine; by autocatalysis Ref.12
Modified residue10911Phosphotyrosine; by autocatalysis By similarity
Modified residue10971Phosphotyrosine; by autocatalysis By similarity
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation1511N-linked (GlcNAc...) By similarity
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation1991N-linked (GlcNAc...) Potential
Glycosylation3451N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation4501N-linked (GlcNAc...) Potential
Glycosylation4701N-linked (GlcNAc...) Potential
Glycosylation5561N-linked (GlcNAc...) Potential
Disulfide bond137 ↔ 142 By similarity

Natural variations

Alternative sequence1065 – 111551MSDPN…DTFDS → RISHAFTRF in isoform 2.
VSP_011304

Experimental info

Mutagenesis10631Y → F: Abolishes interaction with DOK proteins. Ref.7
Sequence conflict1741F → S in CAA48013. Ref.1

Secondary structure

..... 1115
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Ret51) [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: A5CF1EF45A640413

FASTA1,115123,874
        10         20         30         40         50         60 
MAKATSGAAG LGLKLILLLP LLGEAPLGLY FSRDAYWERL YVDQPAGTPL LYVHALRDAP 

        70         80         90        100        110        120 
GEVPSFRLGQ HLYGVYRTRL HENDWIRINE TTGLLYLNQS LDHSSWEQLS IRNGGFPLLT 

       130        140        150        160        170        180 
IFLQVFLGST AQREGECHWP GCTRVYFSFI NDTFPNCSSF KAQDLCIPET AVSFRVRENR 

       190        200        210        220        230        240 
PPGTFYHFHM LPVQFLCPNI SVKYSLLGGD SLPFRCDPDC LEVSTRWALD RELREKYVLE 

       250        260        270        280        290        300 
ALCIVAGPGA NKETVTLSFP VTVYDEDDSA PTFSGGVGTA SAVVEFKRKE GTVVATLQVF 

       310        320        330        340        350        360 
DADVVPASGE LVRRYTNTLL SGDSWAQQTF RVEHSPIETL VQVNNNSVRA TMHNYKLILN 

       370        380        390        400        410        420 
RSLSISESRV LQLAVLVNDS DFQGPGAGGI LVLHFNVSVL PVTLNLPRAY SFPVNKRARR 

       430        440        450        460        470        480 
YAQIGKVCVE NCQEFSGVSI QYKLQPSSIN CTALGVVTSP EDTSGTLFVN DTEALRRPEC 

       490        500        510        520        530        540 
TKLQYTVVAT DRQTRRQTQA SLVVTVEGTS ITEEVGCPKS CAVNKRRPEC EECGGLGSPT 

       550        560        570        580        590        600 
GRCEWRQGDG KGITRNFSTC SPSTRTCPDG HCDAVESRDA NICPQDCLRA DIVGGHERGE 

       610        620        630        640        650        660 
RQGIKAGYGI CNCFPDEKKC FCEPEDSQGP LCDALCRTII TAALFSLIIS ILLSIFCVCH 

       670        680        690        700        710        720 
HHKHGHKPPI ASAEMTFCRP AQGFPISYSS SGTRRPSLDS TENQVPVDSF KIPEDPKWEF 

       730        740        750        760        770        780 
PRKNLVLGKT LGEGEFGKVV KATAFRLKGR AGYTTVAVKM LKENASQSEL RDLLSEFNLL 

       790        800        810        820        830        840 
KQVNHPHVIK LYGACSQDGP LLLIVEYAKY GSLRGFLRDS RKIGPAYVSG GGSRNSSSLD 

       850        860        870        880        890        900 
HPDERVLTMG DLISFAWQIS RGMQYLAEMK LVHRDLAARN ILVAEGRKMK ISDFGLSRDV 

       910        920        930        940        950        960 
YEEDSYVKKS KGRIPVKWMA IESLFDHIYT TQSDVWSFGV LLWEIVTLGG NPYPGIPPER 

       970        980        990       1000       1010       1020 
LFNLLKTGHR MERPDNCSEE MYRLMLQCWK QEPDKRPVFA DISKDLEKMM VKSRDYLDLA 

      1030       1040       1050       1060       1070       1080 
ASTPSDSLLY DDGLSEEETP LVDCNNAPLP RSLPSTWIEN KLYGMSDPNW PGESPVPLTR 

      1090       1100       1110 
ADGTSTGFPR YANDSVYANW MVSPSAAKLM DTFDS 

« Hide

Isoform 2 (Ret9) [UniParc].

Checksum: DB582E8D490C4A62
Show »

FASTA1,073119,469

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS20470.1. [P35546-1]
CCDS39608.1. [P35546-2]
PIRS29926. I48735.
RefSeqNP_001074249.1. NM_001080780.1. [P35546-2]
NP_033076.2. NM_009050.2. [P35546-1]
UniGeneMm.57199.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UEFX-ray2.50C/D1055-1067[»]
ProteinModelPortalP35546.
SMRP35546. Positions 29-273, 714-1012.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202865. 2 interactions.
IntActP35546. 10 interactions.
MINTMINT-5313433.

Chemistry

ChEMBLCHEMBL2034799.

PTM databases

PhosphoSiteP35546.

Proteomic databases

PRIDEP35546.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032201; ENSMUSP00000032201; ENSMUSG00000030110. [P35546-1]
ENSMUST00000088790; ENSMUSP00000086169; ENSMUSG00000030110. [P35546-2]
GeneID19713.
KEGGmmu:19713.
UCSCuc009dlm.1. mouse. [P35546-1]
uc009dln.1. mouse. [P35546-2]

Organism-specific databases

CTD5979.
MGIMGI:97902. Ret.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00670000097694.
HOGENOMHOG000010301.
HOVERGENHBG002609.
InParanoidP35546.
KOK05126.
OMASMENQVS.
OrthoDBEOG7NGQ9N.
PhylomeDBP35546.
TreeFamTF317640.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

BgeeP35546.
CleanExMM_RET.
GenevestigatorP35546.

Family and domain databases

Gene3D2.60.40.60. 1 hit.
InterProIPR002126. 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]
PfamPF00028. Cadherin. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000631. TyrPK_receptor_Ret. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00112. CA. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49313. SSF49313. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50268. CADHERIN_2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP35546.
NextBio297098.
PROP35546.
SOURCESearch...

Entry information

Entry nameRET_MOUSE
AccessionPrimary (citable) accession number: P35546
Secondary accession number(s): Q8BQ34, Q9QXH9
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot