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Proto-oncogene tyrosine-protein kinase receptor Ret (EC 2.7.10.1) (Cadherin family member 12) (Proto-oncogene c-Ret) [Cleaved into: Soluble RET kinase fragment; Extracellular cell-membrane anchored RET cadherin 120 kDa fragment]

 RET_HUMAN               Reviewed;        1114 AA.
P07949; A8K6Z2; Q15250; Q9BTB0; Q9H4A2;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 3.
30-AUG-2017, entry version 230.
RecName: Full=Proto-oncogene tyrosine-protein kinase receptor Ret;
EC=2.7.10.1;
AltName: Full=Cadherin family member 12;
AltName: Full=Proto-oncogene c-Ret;
Contains:
RecName: Full=Soluble RET kinase fragment;
Contains:
RecName: Full=Extracellular cell-membrane anchored RET cadherin 120 kDa fragment;
Flags: Precursor;
Name=RET; Synonyms=CDHF12, CDHR16, PTC, RET51;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
CYS-982.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-280 (ISOFORMS 1/2).
PubMed=2660074;
Takahashi M.;
"Isolation of ret proto-oncogene cDNA with an amino-terminal signal
sequence.";
Oncogene 4:805-806(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 255-1114 (ISOFORM 1).
PubMed=3078962;
Takahashi M., Buma Y., Iwamoto T., Inaguma Y., Ikeda H., Hiai H.;
"Cloning and expression of the ret proto-oncogene encoding a tyrosine
kinase with two potential transmembrane domains.";
Oncogene 3:571-578(1988).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 588-1063 (ISOFORM 2), AND CHROMOSOMAL
TRANSLOCATION WITH TRIM27.
PubMed=3037315; DOI=10.1128/MCB.7.4.1378;
Takahashi M., Cooper G.M.;
"ret transforming gene encodes a fusion protein homologous to tyrosine
kinases.";
Mol. Cell. Biol. 7:1378-1385(1987).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 713-1114 (ISOFORM 1), AND CHROMOSOMAL
TRANSLOCATION WITH GOLGA5.
TISSUE=Fibroblast;
PubMed=2734021;
Ishizaka Y., Ochiai M., Tahira T., Suhimura T., Nahao M.;
"Activation of the ret-II oncogene without a sequence encoding a
transmembrane domain and transforming activity of two ret-II oncogene
products differing in carboxy-termini due to alternative splicing.";
Oncogene 4:789-794(1989).
[8]
ERRATUM.
Ishizaka Y., Ochiai M., Tahira T., Suhimura T., Nahao M.;
Oncogene 4:1415-1415(1989).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 713-1114 (ISOFORM 1), AND CHROMOSOMAL
TRANSLOCATION WITH CCDC6.
TISSUE=Thyroid papillary carcinoma;
PubMed=2406025; DOI=10.1016/0092-8674(90)90659-3;
Grieco M., Santoro M., Berlingieri M.T., Melillo R.M., Donghi R.,
Bongarzone I., Pierotti M.A., Della Porta G., Fusco A., Vecchio G.;
"PTC is a novel rearranged form of the ret proto-oncogene and is
frequently detected in vivo in human thyroid papillary carcinomas.";
Cell 60:557-563(1990).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 713-770 (ISOFORMS 1/2), AND CHROMOSOMAL
TRANSLOCATION WITH PCM1.
PubMed=10980597; DOI=10.1038/sj.onc.1203772;
Corvi R., Berger N., Balczon R., Romeo G.;
"RET/PCM-1: a novel fusion gene in papillary thyroid carcinoma.";
Oncogene 19:4236-4242(2000).
[11]
CHROMOSOMAL TRANSLOCATION WITH TRIM33 AND TRIM24.
PubMed=10439047; DOI=10.1038/sj.onc.1202824;
Klugbauer S., Rabes H.M.;
"The transcription coactivator HTIF1 and a related protein are fused
to the RET receptor tyrosine kinase in childhood papillary thyroid
carcinomas.";
Oncogene 18:4388-4393(1999).
[12]
PHOSPHORYLATION AT TYR-1015 AND TYR-1062.
PubMed=11061555; DOI=10.1210/jcem.85.10.6882;
Salvatore D., Barone M.V., Salvatore G., Melillo R.M., Chiappetta G.,
Mineo A., Fenzi G., Vecchio G., Fusco A., Santoro M.;
"Tyrosines 1015 and 1062 are in vivo autophosphorylation sites in ret
and ret-derived oncoproteins.";
J. Clin. Endocrinol. Metab. 85:3898-3907(2000).
[13]
PHOSPHORYLATION AT TYR-806; TYR-809; TYR-900; TYR-905; TYR-981;
TYR-1015; TYR-1062; TYR-1090 AND TYR-1096.
PubMed=14711813; DOI=10.1074/jbc.M312600200;
Kawamoto Y., Takeda K., Okuno Y., Yamakawa Y., Ito Y., Taguchi R.,
Kato M., Suzuki H., Takahashi M., Nakashima I.;
"Identification of RET autophosphorylation sites by mass
spectrometry.";
J. Biol. Chem. 279:14213-14224(2004).
[14]
CHROMOSOMAL TRANSLOCATION WITH TRIM27.
PubMed=12787916; DOI=10.1016/S0027-5107(03)00056-3;
Saenko V., Rogounovitch T., Shimizu-Yoshida Y., Abrosimov A.,
Lushnikov E., Roumiantsev P., Matsumoto N., Nakashima M.,
Meirmanov S., Ohtsuru A., Namba H., Tsyb A., Yamashita S.;
"Novel tumorigenic rearrangement, Delta rfp/ret, in a papillary
thyroid carcinoma from externally irradiated patient.";
Mutat. Res. 527:81-90(2003).
[15]
PHOSPHORYLATION AT TYR-905; TYR-1015 AND TYR-1062, AND
DEPHOSPHORYLATION AT TYR-905; TYR-1015 AND TYR-1062 BY PTPRJ.
PubMed=16778204; DOI=10.1158/0008-5472.CAN-06-0228;
Iervolino A., Iuliano R., Trapasso F., Viglietto G., Melillo R.M.,
Carlomagno F., Santoro M., Fusco A.;
"The receptor-type protein tyrosine phosphatase J antagonizes the
biochemical and biological effects of RET-derived oncoproteins.";
Cancer Res. 66:6280-6287(2006).
[16]
ENZYME REGULATION.
PubMed=17884497; DOI=10.1016/j.bmcl.2007.07.104;
Graham Robinett R., Freemerman A.J., Skinner M.A., Shewchuk L.,
Lackey K.;
"The discovery of substituted 4-(3-hydroxyanilino)-quinolines as
potent RET kinase inhibitors.";
Bioorg. Med. Chem. Lett. 17:5886-5893(2007).
[17]
ENZYME REGULATION BY SORAFENIB.
PubMed=17664273; DOI=10.1074/jbc.M703461200;
Plaza-Menacho I., Mologni L., Sala E., Gambacorti-Passerini C.,
Magee A.I., Links T.P., Hofstra R.M.W., Barford D., Isacke C.M.;
"Sorafenib functions to potently suppress RET tyrosine kinase activity
by direct enzymatic inhibition and promoting RET lysosomal degradation
independent of proteasomal targeting.";
J. Biol. Chem. 282:29230-29240(2007).
[18]
ENZYME REGULATION BY 3- AND 4-SUBSTITUTED BETA-CARBOLIN-1-ONES.
PubMed=19053769; DOI=10.1021/jm8007823;
Cincinelli R., Cassinelli G., Dallavalle S., Lanzi C., Merlini L.,
Botta M., Tuccinardi T., Martinelli A., Penco S., Zunino F.;
"Synthesis, modeling, and RET protein kinase inhibitory activity of
3- and 4-substituted beta-carbolin-1-ones.";
J. Med. Chem. 51:7777-7787(2008).
[19]
INTERACTION WITH CD2AP, AND MUTAGENESIS OF LYS-758.
PubMed=18753381; DOI=10.1523/JNEUROSCI.2738-08.2008;
Tsui C.C., Pierchala B.A.;
"CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the
regulation of ret signal transduction.";
J. Neurosci. 28:8789-8800(2008).
[20]
INTERACTION WITH AIP.
PubMed=19366855; DOI=10.1210/jc.2008-1980;
Vargiolu M., Fusco D., Kurelac I., Dirnberger D., Baumeister R.,
Morra I., Melcarne A., Rimondini R., Romeo G., Bonora E.;
"The tyrosine kinase receptor RET interacts in vivo with aryl
hydrocarbon receptor-interacting protein to alter survivin
availability.";
J. Clin. Endocrinol. Metab. 94:2571-2578(2009).
[21]
INDUCTION BY NKX2-1; PHOX2B; SOX10 AND PAX3.
PubMed=19853745; DOI=10.1016/j.jpedsurg.2008.11.055;
Leon T.Y.Y., Ngan E.S.W., Poon H.-C., So M.-T., Lui V.C.H.,
Tam P.K.H., Garcia-Barcelo M.M.;
"Transcriptional regulation of RET by Nkx2-1, Phox2b, Sox10, and
Pax3.";
J. Pediatr. Surg. 44:1904-1912(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[23]
FUNCTION IN DEVELOPMENT OF MECHANORECEPTORS.
PubMed=20064382; DOI=10.1016/j.neuron.2009.12.014;
Ma Q.;
"RETouching upon mechanoreceptors.";
Neuron 64:773-776(2009).
[24]
ENZYME REGULATION, AND REVIEW ON KINASE INHIBITORS.
PubMed=20605972; DOI=10.1210/er.2009-0031;
Ye L., Santarpia L., Gagel R.F.;
"The evolving field of tyrosine kinase inhibitors in the treatment of
endocrine tumors.";
Endocr. Rev. 31:578-599(2010).
[25]
ENZYME REGULATION.
PubMed=20409618; DOI=10.1016/j.ejmech.2010.03.017;
Brandt W., Mologni L., Preu L., Lemcke T., Gambacorti-Passerini C.,
Kunick C.;
"Inhibitors of the RET tyrosine kinase based on a 2-(alkylsulfanyl)-4-
(3-thienyl)nicotinonitrile scaffold.";
Eur. J. Med. Chem. 45:2919-2927(2010).
[26]
FUNCTION IN PITUITARY.
PubMed=20616503; DOI=10.1159/000318502;
Garcia-Lavandeira M., Diaz-Rodriguez E., Garcia-Rendueles M.E.,
Rodrigues J.S., Perez-Romero S., Bravo S.B., Alvarez C.V.;
"Functional role of the RET dependence receptor, GFRa co-receptors and
ligands in the pituitary.";
Front. Horm. Res. 38:127-138(2010).
[27]
FUNCTION IN CELL ADHESION/MIGRATION.
PubMed=20702524; DOI=10.1210/jc.2010-0771;
Cockburn J.G., Richardson D.S., Gujral T.S., Mulligan L.M.;
"RET-mediated cell adhesion and migration require multiple integrin
subunits.";
J. Clin. Endocrinol. Metab. 95:E342-E346(2010).
[28]
SUBCELLULAR LOCATION.
PubMed=19823924; DOI=10.1007/s10895-009-0548-x;
Richardson D.S., Mulligan L.M.;
"Direct visualization of vesicle maturation and plasma membrane
protein trafficking.";
J. Fluoresc. 20:401-405(2010).
[29]
ENZYME REGULATION.
PubMed=21134556; DOI=10.1016/j.surg.2010.09.026;
Samadi A.K., Mukerji R., Shah A., Timmermann B.N., Cohen M.S.;
"A novel RET inhibitor with potent efficacy against medullary thyroid
cancer in vivo.";
Surgery 148:1228-1236(2010).
[30]
FUNCTION IN CELL ADHESION, FUNCTION IN APOPTOSIS, PROTEOLYTIC
PROCESSING BY CASPASE-3 AT ASP-707 AND ASP-1017, MUTAGENESIS OF
ASP-707; LYS-758 AND 708-ALA--SER-1114, AND SUBUNIT.
PubMed=21357690; DOI=10.1074/jbc.M110.195461;
Cabrera J.R., Bouzas-Rodriguez J., Tauszig-Delamasure S., Mehlen P.;
"RET modulates cell adhesion via its cleavage by caspase in
sympathetic neurons.";
J. Biol. Chem. 286:14628-14638(2011).
[31]
INTERACTION WITH PTK2/FAK1, AND FUNCTION IN PTK2/FAK1 PHOSPHORYLATION.
PubMed=21454698; DOI=10.1074/jbc.M110.168500;
Plaza-Menacho I., Morandi A., Mologni L., Boender P.,
Gambacorti-Passerini C., Magee A.I., Hofstra R.M.W., Knowles P.,
McDonald N.Q., Isacke C.M.;
"Focal adhesion kinase (FAK) binds RET kinase via its FERM domain,
priming a direct and reciprocal RET-FAK transactivation mechanism.";
J. Biol. Chem. 286:17292-17302(2011).
[32]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 705-1013 ALONE AND IN COMPLEX
WITH INHIBITORS, IDENTIFICATION BY MASS SPECTROMETRY, AND
PHOSPHORYLATION AT TYR-900 AND TYR-905.
PubMed=16928683; DOI=10.1074/jbc.M605604200;
Knowles P.P., Murray-Rust J., Kjaer S., Scott R.P., Hanrahan S.,
Santoro M., Ibanez C.F., McDonald N.Q.;
"Structure and chemical inhibition of the RET tyrosine kinase
domain.";
J. Biol. Chem. 281:33577-33587(2006).
[33]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 705-1013 IN COMPLEX WITH
INHIBITORS, ENZYME REGULATION, AND PHOSPHORYLATION AT TYR-905.
PubMed=20117004; DOI=10.1016/j.bmc.2010.01.011;
Mologni L., Rostagno R., Brussolo S., Knowles P.P., Kjaer S.,
Murray-Rust J., Rosso E., Zambon A., Scapozza L., McDonald N.Q.,
Lucchini V., Gambacorti-Passerini C.;
"Synthesis, structure-activity relationship and crystallographic
studies of 3-substituted indolin-2-one RET inhibitors.";
Bioorg. Med. Chem. 18:1482-1496(2010).
[34]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-270, GLYCOSYLATION AT
ASN-151, AND DISULFIDE BOND.
PubMed=20473317; DOI=10.1038/nsmb.1808;
Kjaer S., Hanrahan S., Totty N., McDonald N.Q.;
"Mammal-restricted elements predispose human RET to folding impairment
by HSCR mutations.";
Nat. Struct. Mol. Biol. 17:726-731(2010).
[35]
REVIEW ON HSCR VARIANTS.
PubMed=9359036;
Hofstra R.M.W., Osinga J., Buys C.H.C.M.;
"Mutations in Hirschsprung disease: when does a mutation contribute to
the phenotype.";
Eur. J. Hum. Genet. 5:180-185(1997).
[36]
REVIEW ON VARIANTS.
PubMed=9067749;
DOI=10.1002/(SICI)1098-1004(1997)9:2<97::AID-HUMU1>3.0.CO;2-M;
Eng C., Mulligan L.M.;
"Mutations of the RET proto-oncogene in the multiple endocrine
neoplasia type 2 syndromes, related sporadic tumours, and Hirschsprung
disease.";
Hum. Mutat. 9:97-109(1997).
[37]
VARIANTS MEN2A/MTC TRP-611; SER-618; ARG-620; TYR-620 AND ARG-634.
PubMed=8103403; DOI=10.1093/hmg/2.7.851;
Donis-Keller H., Dou S., Chi D., Carlson K.M., Toshima K.,
Lairmore T.C., Howe J.R., Moley J.F., Goodfellow P., Wells S.A. Jr.;
"Mutations in the RET proto-oncogene are associated with MEN 2A and
FMTC.";
Hum. Mol. Genet. 2:851-856(1993).
[38]
VARIANTS MEN2A GLY-618; 632-ASP--ARG-634; GLY-634; PHE-634; TYR-634
AND SER-634.
PubMed=8099202; DOI=10.1038/363458a0;
Mulligan L.M., Kwok J.B.J., Healey C.S., Elsdon M.J., Eng C.,
Gardner E., Love D.R., Mole S.E., Moore J.K., Papi L., Ponder M.A.,
Telenius H., Tunnacliffe A., Ponder B.A.J.;
"Germ-line mutations of the RET proto-oncogene in multiple endocrine
neoplasia type 2A.";
Nature 363:458-460(1993).
[39]
VARIANTS HSCR1 PRO-40; LEU-399; GLN-762; PRO-765; GLN-897; GLY-972 AND
LEU-973.
PubMed=7704557;
Yin L., Barone V., Seri M., Bolino A., Bocciardi R., Ceccherini I.,
Pasini B., Tocco T., Lerone M., Cywes S., Moore S.,
Vanderwinden J.-M., Abramowicz M.J., Kristoffersson U., Larsson L.T.,
Hamel B.C.J., Silengo M., Martucciello G., Romeo G.;
"Heterogeneity and low detection rate of RET mutations in Hirschsprung
disease.";
Eur. J. Hum. Genet. 2:272-280(1994).
[40]
VARIANT MEN2B THR-918.
PubMed=7911697; DOI=10.1093/hmg/3.2.237;
Eng C., Smith D.P., Mulligan L.M., Nagai M.A., Healey C.S.,
Ponder M.A., Gardner E., Scheumann G.F., Jackson C.E., Tunnacliffe A.,
Ponder B.A.J.;
"Point mutation within the tyrosine kinase domain of the RET proto-
oncogene in multiple endocrine neoplasia type 2B and related sporadic
tumours.";
Hum. Mol. Genet. 3:237-241(1994).
[41]
VARIANTS MEN2A/MTC ARG-618; SER-618; PHE-620; ARG-620; PHE-634;
GLY-634 AND TYR-634.
PubMed=7915165; DOI=10.1093/hmg/3.4.635;
Xue F., Yu H., Maurer L.H., Memoli V.A., Nutile-Mcmenemy N.,
Schuster M.K., Browden D.W., Mao J.-I., Noll W.W.;
"Germline RET mutations in MEN 2A and FMTC and their detection by
simple DNA diagnostic tests.";
Hum. Mol. Genet. 3:635-638(1994).
[42]
VARIANTS MTC/MEN2A TYR-609; ARG-618; SER-618 AND SER-620.
PubMed=7849720; DOI=10.1093/hmg/3.10.1895;
Blaugrund J.E., Johns M.M. Jr., Eby Y.J., Ball D.W., Baylin S.B.,
Hruban R.H., Sidransky D.;
"RET proto-oncogene mutations in inherited and sporadic medullary
thyroid cancer.";
Hum. Mol. Genet. 3:1895-1897(1994).
[43]
VARIANTS MTC, AND VARIANTS MEN2A.
PubMed=7874109; DOI=10.1093/hmg/3.11.1939;
Schuffenecker I., Billaud M., Calender A., Chambe B., Ginet N.,
Calmettes C., Modigliani E., Lenoir G.M.;
"RET proto-oncogene mutations in French MEN 2A and FMTC families.";
Hum. Mol. Genet. 3:1939-1943(1994).
[44]
VARIANTS HSCR1 TRP-609; ARG-618 AND ARG-620, VARIANT MEN2A ARG-618,
AND VARIANT MTC ARG-620.
PubMed=7881414; DOI=10.1093/hmg/3.12.2163;
Mulligan L.M., Eng C., Attie T., Lyonnet S., Marsh D.J., Hyland V.J.,
Robinson B.G., Frilling A., Verellen-Dumoulin C., Safar A.,
Venter D.J., Munnich A., Ponder B.A.J.;
"Diverse phenotypes associated with exon 10 mutations of the RET
proto-oncogene.";
Hum. Mol. Genet. 3:2163-2167(1994).
[45]
VARIANT MEN2B THR-918.
PubMed=7906866; DOI=10.1038/367375a0;
Hofstra R.M.W., Landsvater R.M., Ceccherini I., Stulp R.P.,
Stelwagen T., Luo Y., Pasini B., Hoeppener J.W.M.,
Ploos van Amstel H.K., Romeo G., Lips C.J.M., Buys C.H.C.M.;
"A mutation in the RET proto-oncogene associated with multiple
endocrine neoplasia type 2B and sporadic medullary thyroid
carcinoma.";
Nature 367:375-376(1994).
[46]
VARIANTS HSCR1 PRO-765; GLN-897 AND GLY-972.
PubMed=8114938; DOI=10.1038/367377a0;
Romeo G., Ronchetto P., Luo Y., Barone V., Seri M., Ceccherini I.,
Pasini B., Bocciardi R., Lerone M., Kaarlainen H., Martucciello G.;
"Point mutations affecting the tyrosine kinase domain of the RET
proto-oncogene in Hirschsprung's disease.";
Nature 367:377-378(1994).
[47]
VARIANTS HSCR1 LEU-32; LEU-64; GLN-330 AND LEU-393.
PubMed=8114939; DOI=10.1038/367378a0;
Edery P., Lyonnet S., Mulligan L.M., Pelet A., Dow E., Abel L.,
Holder S., Nihoul-Fkete C., Ponder B.A.J., Munnich A.;
"Mutations of the RET proto-oncogene in Hirschsprung's disease.";
Nature 367:378-380(1994).
[48]
VARIANT MEN2B THR-918.
PubMed=7906417; DOI=10.1073/pnas.91.4.1579;
Carlson K.M., Dou S., Chi D., Scavarda N., Toshima K., Jackson C.E.,
Wells S.A. Jr., Goodfellow P.J., Donis-Keller H.;
"Single missense mutation in the tyrosine kinase catalytic domain of
the RET protooncogene is associated with multiple endocrine neoplasia
type 2B.";
Proc. Natl. Acad. Sci. U.S.A. 91:1579-1583(1994).
[49]
VARIANTS MTC; MEN2A AND MEN2B.
PubMed=8625130;
DOI=10.1002/1097-0142(19950801)76:3<479::AID-CNCR2820760319>3.0.CO;2-M;
Komminoth P., Kunz E.K., Matias-Guiu X., Hiort O., Christiansen G.,
Colomer A., Roth J., Heitz P.U.;
"Analysis of RET protooncogene point mutations distinguishes heritable
from nonheritable medullary thyroid carcinomas.";
Cancer 76:479-489(1995).
[50]
VARIANTS MEN2A SER-618; SER-620; ARG-634 AND TYR-634.
PubMed=7860065; DOI=10.1007/BF00209399;
Takiguchi-Shirahama S., Koyama K., Miyauchi A., Wakasugi T., Oishi S.,
Takami H., Hikiji K., Nakamura Y.;
"Germline mutations of the RET proto-oncogene in eight Japanese
patients with multiple endocrine neoplasia type 2A (MEN2A).";
Hum. Genet. 95:187-190(1995).
[51]
VARIANTS HSCR1 LEU-20; SER-93; GLN-330; TYR-609 AND ARG-620, AND
VARIANT CYS-982.
TISSUE=Blood;
PubMed=7633441; DOI=10.1093/hmg/4.5.821;
Angrist M., Bolk S., Thiel B., Puffenberger E.G., Hofstra R.M.W.,
Buys C.H.C.M., Cass D.T., Chakravarti A.;
"Mutation analysis of the RET receptor tyrosine kinase in Hirschsprung
disease.";
Hum. Mol. Genet. 4:821-830(1995).
[52]
VARIANTS HSCR1.
TISSUE=Leukocyte;
PubMed=7581377; DOI=10.1093/hmg/4.8.1381;
Attie T., Pelet A., Edery P., Eng C., Mulligan L.M., Amiel J.,
Boutrand L., Beldjord C., Nihoul-Fekete C., Munnich A., Ponder B.A.J.,
Lyonnet S.;
"Diversity of RET proto-oncogene mutations in familial and sporadic
Hirschsprung disease.";
Hum. Mol. Genet. 4:1381-1386(1995).
[53]
VARIANT MEN2B THR-918, AND VARIANT TYR-922.
PubMed=8595427; DOI=10.1093/hmg/4.10.1987;
Kitamura Y., Scavarda N., Wells S.A. Jr., Jackson C.E.,
Goodfellow P.J.;
"Two maternally derived missense mutations in the tyrosine kinase
domain of the RET protooncogene in a patient with de novo MEN 2B.";
Hum. Mol. Genet. 4:1987-1988(1995).
[54]
VARIANT MTC ASP-768.
PubMed=7845675;
Eng C., Smith D.P., Mulligan L.M., Healey C.S., Zvelebil M.J.,
Stonehouse T.J., Ponder M.A., Jackson C.E., Waterfield M.D.,
Ponder B.A.J.;
"A novel point mutation in the tyrosine kinase domain of the RET
proto-oncogene in sporadic medullary thyroid carcinoma and in a family
with FMTC.";
Oncogene 10:509-513(1995).
[55]
VARIANTS MTC ASP-768 AND LEU-804.
PubMed=7784092;
Bolino A., Schuffenecker I., Luo Y., Seri M., Silengo M., Tocco T.,
Chabrier G., Houdent C., Murat A., Schlumberger M., Tournaire J.,
Lenoir G.M., Romeo G.;
"RET mutations in exons 13 and 14 of FMTC patients.";
Oncogene 10:2415-2419(1995).
[56]
VARIANTS HSCR1 TYR-157; LYS-359; TYR-609; ARG-620; ASN-1059 DEL AND
PRO-1061.
Hofstra R.M.W., Osinga J., Stulp R.P., Scheffer H., Meijers C.,
Buys C.H.C.M.;
"Mutations in three genes are found associated with the development of
Hirschsprung disease: RET, EDNRB and EDN3.";
Am. J. Hum. Genet. 59:A263-A263(1996).
[57]
VARIANTS HSCR1 PRO-40 AND PRO-765.
PubMed=9043870;
Yin L., Seri M., Barone V., Tocco T., Scaranari M., Romeo G.;
"Prevalence and parental origin of de novo RET mutations in
Hirschsprung's disease.";
Eur. J. Hum. Genet. 4:356-358(1996).
[58]
VARIANTS MTC/MEN2A.
PubMed=8557249; DOI=10.1007/BF00218825;
Landsvater R.M., Jansen R.P.M., Hofstra R.M.W., Buys C.H.C.M.,
Lips C.J.M., van Amstel H.K.P.;
"Mutation analysis of the RET proto-oncogene in Dutch families with
MEN 2A, MEN 2B and FMTC: two novel mutations and one de novo mutation
for MEN 2A.";
Hum. Genet. 97:11-14(1996).
[59]
VARIANTS MEN2A, VARIANT MTC ASP-768, AND VARIANT MEN2B THR-918.
PubMed=8807338;
DOI=10.1002/(SICI)1098-1004(1996)8:1<64::AID-HUMU9>3.3.CO;2-N;
Kambouris M., Jackson C.E., Feldman G.L.;
"Diagnosis of multiple endocrine neoplasia [MEN] 2A, 2B and familial
medullary thyroid cancer [FMTC] by multiplex PCR and heteroduplex
analyses of RET proto-oncogene mutations.";
Hum. Mutat. 8:64-70(1996).
[60]
VARIANTS MEN2A.
PubMed=8626834; DOI=10.1210/jcem.81.5.8626834;
Frank-Raue K., Hoeppner W., Frilling A., Kotzerke J., Dralle H.,
Haase R., Mann K., Seif F., Kirchner R., Rendl J., Deckart H.F.,
Ritter M.M., Hampel R., Klempa J., Scholz G.H., Raue F., Bogner U.,
Brabant G., Grussendorf M., Hartenstein C.H., Heidemann P., Hensen J.,
Doerr A.G., Hoehne T., Hoernig-Franz I., Huefner M., Kress J.,
Langer H.J., Lottermoser K., Schweikert H.U., Kusterer K., Menken U.,
Mercier J., Oelkers W., Sauer J., Simon D., Starrach G., Ziegler R.;
"Mutations of the ret protooncogene in German multiple endocrine
neoplasia families: relation between genotype and phenotype.";
J. Clin. Endocrinol. Metab. 81:1780-1783(1996).
[61]
VARIANT MEN2A HIS-GLU-LEU-CYS-634 INS.
PubMed=9097963; DOI=10.1093/hmg/6.4.587;
Hoeppner W., Ritter M.M.;
"A duplication of 12 bp in the critical cysteine rich domain of the
RET proto-oncogene results in a distinct phenotype of multiple
endocrine neoplasia type 2A.";
Hum. Mol. Genet. 6:587-590(1997).
[62]
VARIANTS HSCR1 PRO-180; GLN-313; ARG-620 AND PHE-791.
PubMed=9090527;
DOI=10.1002/(SICI)1098-1004(1997)9:3<243::AID-HUMU5>3.3.CO;2-N;
Seri M., Yin L., Barone V., Bolino A., Celli I., Bocciardi R.,
Pasini B., Ceccherini I., Lerone M., Kristoffersson U., Larsson L.T.,
Casasa J.M., Cass D.T., Abramowicz M.J., Vanderwinden J.-M.,
Kravcenkiene I., Baric I., Silengo M., Martucciello G., Romeo G.;
"Frequency of RET mutations in long- and short-segment Hirschsprung
disease.";
Hum. Mutat. 9:243-249(1997).
[63]
VARIANT MTC ARG-618, AND VARIANT HSCR1 ARG-618.
PubMed=9259198;
DOI=10.1002/(SICI)1098-1004(1997)10:2<155::AID-HUMU7>3.3.CO;2-G;
Peretz H., Luboshitsky R., Baron E., Biton A., Gershoni R., Usher S.,
Grynberg E., Yakobson E., Graff E., Lapidot M.;
"Cys 618 Arg mutation in the RET proto-oncogene associated with
familial medullary thyroid carcinoma and maternally transmitted
Hirschsprung's disease suggesting a role for imprinting.";
Hum. Mutat. 10:155-159(1997).
[64]
VARIANT MEN2B PHE-883.
TISSUE=Peripheral blood leukocyte;
PubMed=9360560; DOI=10.1210/jcem.82.11.4508;
Gimm O., Marsh D.J., Andrew S.D., Frilling A., Dahia P.L.M.,
Mulligan L.M., Zajac J.D., Robinson B.G., Eng C.;
"Germline dinucleotide mutation in codon 883 of the RET proto-oncogene
in multiple endocrine neoplasia type 2B without codon 918 mutation.";
J. Clin. Endocrinol. Metab. 82:3902-3904(1997).
[65]
VARIANT MTC ALA-891.
PubMed=9398735; DOI=10.1210/jcem.82.12.4439;
Hofstra R.M.W., Fattoruso O., Quadro L., Wu Y., Libroia A., Verga U.,
Colantuoni V., Buys C.H.C.M.;
"A novel point mutation in the intracellular domain of the ret
protooncogene in a family with medullary thyroid carcinoma.";
J. Clin. Endocrinol. Metab. 82:4176-4178(1997).
[66]
VARIANTS HSCR1 SER-174 AND TYR-197.
PubMed=9094028; DOI=10.1016/S0022-3468(97)90616-3;
Kusafuka T., Wang Y., Puri P.;
"Mutation analysis of the RET, the endothelin-B receptor, and the
endothelin-3 genes in sporadic cases of Hirschsprung's disease.";
J. Pediatr. Surg. 32:501-504(1997).
[67]
VARIANTS MTC; MEN2A AND MEN2B, AND VARIANT SER-691.
PubMed=9223675; DOI=10.1038/sj.onc.1201102;
Kitamura Y., Goodfellow P.J., Shimizu K., Nagahama M., Ito K.,
Kitagawa W., Akasu H., Takami H., Tanaka S., Wells S.A. Jr.;
"Novel germline RET proto-oncogene mutations associated with medullary
thyroid carcinoma (MTC): mutation analysis in Japanese patients with
MTC.";
Oncogene 14:3103-3106(1997).
[68]
VARIANT MEN2B PHE-883.
PubMed=9294615; DOI=10.1038/sj.onc.1201481;
Smith D.P., Houghton C., Ponder B.A.J.;
"Germline mutation of RET codon 883 in two cases of de novo MEN 2B.";
Oncogene 15:1213-1217(1997).
[69]
VARIANT CCHS LEU-1039, AND VARIANT SER-691.
PubMed=9497256; DOI=10.1086/301759;
Amiel J., Salomon R., Attie T., Pelet A., Trang H., Mokhtari M.,
Gaultier C., Munnich A., Lyonnet S.;
"Mutations of the RET-GDNF signaling pathway in Ondine's curse.";
Am. J. Hum. Genet. 62:715-717(1998).
[70]
VARIANT MTC GLY-611.
PubMed=9677065;
DOI=10.1002/(SICI)1096-8628(19980707)78:3<271::AID-AJMG13>3.0.CO;2-C;
Oriola J., Paramo C., Halperin I., Garcia-Mayor R.V.,
Rivera-Fillat F.;
"Novel point mutation in exon 10 of the RET proto-oncogene in a family
with medullary thyroid carcinoma.";
Am. J. Med. Genet. 78:271-273(1998).
[71]
VARIANT CYS-982.
PubMed=9760196; DOI=10.1007/s004390050797;
Svensson P.J., Anvret M., Molander M.L., Nordenskjold A.;
"Phenotypic variation in a family with mutations in two Hirschsprung-
related genes (RET and endothelin receptor B).";
Hum. Genet. 103:145-148(1998).
[72]
VARIANTS MEN2A TYR-609; SER-618; ARG-620 AND TRP-620, AND VARIANTS
HSCR1 TYR-609; SER-618; ARG-620 AND TRP-620.
PubMed=9384613; DOI=10.1093/hmg/7.1.129;
Decker R.A., Peacock M.L., Watson P.;
"Hirschsprung disease in MEN 2A: increased spectrum of RET exon 10
genotypes and strong genotype-phenotype correlation.";
Hum. Mol. Genet. 7:129-134(1998).
[73]
VARIANT MEN2A CYS-ARG-THR-636 INS.
PubMed=9452064;
Hoeppner W., Dralle H., Brabant G.;
"Duplication of 9 base pairs in the critical cysteine-rich domain of
the RET proto-oncogene causes multiple endocrine neoplasia type 2A.";
Hum. Mutat. Suppl. 1:S128-S130(1998).
[74]
VARIANT MTC MET-804.
PubMed=9452077;
Fattoruso O., Quadro L., Libroia A., Verga U., Lupoli G., Cascone E.,
Colantuoni V.;
"A GTG to ATG novel point mutation at codon 804 in exon 14 of the RET
proto-oncogene in two families affected by familial medullary thyroid
carcinoma.";
Hum. Mutat. Suppl. 1:S167-S171(1998).
[75]
VARIANTS MTC/MEN2A PHE-790 AND PHE-791.
PubMed=9506724; DOI=10.1210/jcem.83.3.4619;
Berndt I., Reuter M., Saller B., Frank-Raue K., Groth P.,
Grussendorf M., Raue F., Ritter M.M., Hoeppner W.;
"A new hot spot for mutations in the ret protooncogene causing
familial medullary thyroid carcinoma and multiple endocrine neoplasia
type 2A.";
J. Clin. Endocrinol. Metab. 83:770-774(1998).
[76]
VARIANTS MTC AND MEN2A.
PubMed=9621513; DOI=10.1007/s100380050048;
Shirahama S., Ogura K., Takami H., Ito K., Tohsen T., Miyauchi A.,
Nakamura Y.;
"Mutational analysis of the RET proto-oncogene in 71 Japanese patients
with medullary thyroid carcinoma.";
J. Hum. Genet. 43:101-106(1998).
[77]
VARIANTS HSCR1 LYS-626 AND GLN-813.
PubMed=10090908; DOI=10.1086/302329;
Auricchio A., Griseri P., Carpentieri M.L., Betsos N., Staiano A.,
Tozzi A., Priolo M., Thompson H., Bocciardi R., Romeo G., Ballabio A.,
Ceccherini I.;
"Double heterozygosity for a RET substitution interfering with
splicing and an EDNRB missense mutation in Hirschsprung disease.";
Am. J. Hum. Genet. 64:1216-1221(1999).
[78]
VARIANTS HSCR1 ASN-1059 DEL AND PRO-1061.
PubMed=10484767; DOI=10.1093/hmg/8.11.1989;
Geneste O., Bidaud C., De Vita G., Hofstra R.M.W., Tartare-Deckert S.,
Buys C.H.C.M., Lenoir G.M., Santoro M., Billaud M.;
"Two distinct mutations of the RET receptor causing Hirschsprung's
disease impair the binding of signalling effectors to a
multifunctional docking site.";
Hum. Mol. Genet. 8:1989-1999(1999).
[79]
VARIANT MTC GLU-GLU-CYS-531 INS.
PubMed=10323403; DOI=10.1210/jcem.84.5.5665;
Pigny P., Bauters C., Wemeau J.-L., Houcke M.L., Crepin M., Caron P.,
Giraud S., Calender A., Buisine M.-P., Kerckaert J.-P., Porchet N.;
"A novel 9-base pair duplication in RET exon 8 in familial medullary
thyroid carcinoma.";
J. Clin. Endocrinol. Metab. 84:1700-1704(1999).
[80]
VARIANT MEN2A GLY-640.
PubMed=10522989; DOI=10.1210/jcem.84.10.6056;
Tessitore A., Sinisi A.A., Pasquali D., Cardone M., Vitale D.,
Bellastella A., Colantuoni V.;
"A novel case of multiple endocrine neoplasia type 2A associated with
two de novo mutations of the RET protooncogene.";
J. Clin. Endocrinol. Metab. 84:3522-3527(1999).
[81]
VARIANTS MTC MET-804 AND LEU-844.
PubMed=10826520; DOI=10.1055/s-2000-5806;
Bartsch D.K., Hasse C., Schug C., Barth P., Rothmund M., Hoeppner W.;
"A RET double mutation in the germline of a kindred with FMTC.";
Exp. Clin. Endocrinol. Diabetes 108:128-132(2000).
[82]
VARIANT GLN-600.
PubMed=10612852;
DOI=10.1002/(SICI)1098-1004(200001)15:1<122::AID-HUMU41>3.0.CO;2-7;
Saez M.E., Ruiz A., Cebrian A., Morales F., Robledo M., Antinolo G.,
Borrego S.;
"A new germline mutation, R600Q, within the coding region of RET
proto-oncogene: a rare polymorphism or a MEN 2 causing mutation?";
Hum. Mutat. 15:122-122(2000).
[83]
VARIANTS HSCR1 LEU-32; CYS-77; TRP-360 AND LYS-394.
PubMed=10618407; DOI=10.1073/pnas.97.1.268;
Bolk S., Pelet A., Hofstra R.M.W., Angrist M., Salomon R., Croaker D.,
Buys C.H.C.M., Lyonnet S., Chakravarti A.;
"A human model for multigenic inheritance: phenotypic expression in
Hirschsprung disease requires both the RET gene and a new 9q31
locus.";
Proc. Natl. Acad. Sci. U.S.A. 97:268-273(2000).
[84]
VARIANTS MTC GLY-639; GLY-641 AND PHE-922.
PubMed=11692159; DOI=10.1007/s001090100250;
Kalinin V.N., Amosenko F.A., Shabanov M.A., Lubchenko L.N.,
Hosch S.B., Garkavtseva R.F., Izbicki J.R.;
"Three novel mutations in the RET proto-oncogene.";
J. Mol. Med. 79:609-612(2001).
[85]
VARIANTS PHEOCHROMOCYTOMA ARG-634; GLY-634; TYR-634; SER-634; PHE-634;
TRP-634 AND PHE-791.
PubMed=12000816; DOI=10.1056/NEJMoa020152;
The Freiburg-Warsaw-Columbus pheochromocytoma study group;
Neumann H.P.H., Bausch B., McWhinney S.R., Bender B.U., Gimm O.,
Franke G., Schipper J., Klisch J., Altehoefer C., Zerres K.,
Januszewicz A., Smith W.M., Munk R., Manz T., Glaesker S., Apel T.W.,
Treier M., Reineke M., Walz M.K., Hoang-Vu C., Brauckhoff M.,
Klein-Franke A., Klose P., Schmidt H., Maier-Woelfle M.,
Peczkowska M., Szmigielski C., Eng C.;
"Germ-line mutations in nonsyndromic pheochromocytoma.";
N. Engl. J. Med. 346:1459-1466(2002).
[86]
VARIANT CCHS HIS-114.
PubMed=12086152; DOI=10.1620/tjem.196.241;
Kanai M., Numakura C., Sasaki A., Shirahata E., Akaba K.,
Hashimoto M., Hasegawa H., Shirasawa S., Hayasaka K.;
"Congenital central hypoventilation syndrome: a novel mutation of the
RET gene in an isolated case.";
Tohoku J. Exp. Med. 196:241-246(2002).
[87]
VARIANTS ASN-489; SER-691 AND CYS-982, AND VARIANTS CCHS HIS-67;
HIS-114 AND GLU-432.
PubMed=14566559; DOI=10.1007/s00439-003-1036-z;
Sasaki A., Kanai M., Kijima K., Akaba K., Hashimoto M., Hasegawa H.,
Otaki S., Koizumi T., Kusuda S., Ogawa Y., Tuchiya K., Yamamoto W.,
Nakamura T., Hayasaka K.;
"Molecular analysis of congenital central hypoventilation syndrome.";
Hum. Genet. 114:22-26(2003).
[88]
VARIANTS [LARGE SCALE ANALYSIS] GLY-145; TRP-360 AND GLU-593.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[89]
VARIANTS [LARGE SCALE ANALYSIS] GLN-163; ASN-278; MET-292; ASN-489;
SER-691; THR-749; SER-826; LEU-844; CYS-982 AND TYR-1112.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[90]
VARIANTS THR-198; ALA-376; HIS-394; ILE-778; SER-894; THR-918;
LEU-1049 AND SER-1067, POSSIBLE INVOLVEMENT IN RENAL AGENESIS, AND
CHARACTERIZATION OF VARIANTS THR-198; ALA-376; HIS-394; ILE-778;
SER-894; LEU-1049 AND SER-1067.
PubMed=18252215; DOI=10.1016/j.ajhg.2007.10.008;
Skinner M.A., Safford S.D., Reeves J.G., Jackson M.E.,
Freemerman A.J.;
"Renal aplasia in humans is associated with RET mutations.";
Am. J. Hum. Genet. 82:344-351(2008).
[91]
VARIANTS HSCR1 549-LYS-GLY-550 DEL; CYS-114; HIS-114; GLY-145;
LEU-155; PRO-175; ALA-278; PRO-278; ASN-300; GLN-313; ILE-316;
LEU-339; TYR-353; GLN-360; MET-397; MET-412; ARG-423; LYS-480;
GLN-595; LEU-679; GLN-694; SER-783; ARG-830; THR-907; LEU-961;
VAL-1052; CYS-1062 AND THR-1064, AND VARIANTS ASN-278 AND MET-292.
PubMed=22174939; DOI=10.1371/journal.pone.0028986;
So M.T., Leon T.Y., Cheng G., Tang C.S., Miao X.P., Cornes B.K.,
Diem N.N., Cui L., Ngan E.S., Lui V.C., Wu X.Z., Wang B., Wang H.,
Yuan Z.W., Huang L.M., Li L., Xia H., Zhu D., Liu J., Nguyen T.L.,
Chan I.H., Chung P.H., Liu X.L., Zhang R., Wong K.K., Sham P.C.,
Cherny S.S., Tam P.K., Garcia-Barcelo M.M.;
"RET mutational spectrum in Hirschsprung disease: evaluation of 601
Chinese patients.";
PLoS ONE 6:E28986-E28986(2011).
-!- 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.
{ECO:0000269|PubMed:20064382, ECO:0000269|PubMed:20616503,
ECO:0000269|PubMed:20702524, ECO:0000269|PubMed:21357690,
ECO:0000269|PubMed:21454698}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Repressed by 4-(3-hydroxyanilino)-quinolines
derivatives, indolin-2-one-derivatives, 2-(alkylsulfanyl)-4-(3-
thienyl) nicotinonitrile analogs, 3- and 4-substituted beta-
carbolin-1-ones, vandetanib, motesanib, sorafenib (BAY 43-9006),
cabozantinib (XL184), sunitinib, and withaferin A (WA).
Inactivation by sorafenib both reduces kinase activity and
promotes lysosomal degradation. {ECO:0000269|PubMed:17664273,
ECO:0000269|PubMed:17884497, ECO:0000269|PubMed:19053769,
ECO:0000269|PubMed:20117004, ECO:0000269|PubMed:20409618,
ECO:0000269|PubMed:20605972, ECO:0000269|PubMed:21134556}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:18753381,
ECO:0000269|PubMed:19366855, ECO:0000269|PubMed:20117004,
ECO:0000269|PubMed:21357690, ECO:0000269|PubMed:21454698}.
-!- INTERACTION:
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-2480756, EBI-945833;
P19174:PLCG1; NbExp=2; IntAct=EBI-2480756, EBI-79387;
Q62985:Sh2b1 (xeno); NbExp=3; IntAct=EBI-2480756, EBI-7395583;
P40763:STAT3; NbExp=3; IntAct=EBI-2480756, EBI-518675;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19823924};
Single-pass type I membrane protein {ECO:0000269|PubMed:19823924}.
Endosome membrane {ECO:0000269|PubMed:19823924}; Single-pass type
I membrane protein {ECO:0000269|PubMed:19823924}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=RET51;
IsoId=P07949-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2; Synonyms=RET9;
IsoId=P07949-2; Sequence=VSP_040735;
-!- INDUCTION: Positively regulated by NKX2-1, PHOX2B, SOX10 and PAX3.
{ECO:0000269|PubMed:19853745}.
-!- PTM: Autophosphorylated on C-terminal tyrosine residues upon
ligand stimulation. Dephosphorylated by PTPRJ on Tyr-905, Tyr-1015
and Tyr-1062. {ECO:0000269|PubMed:11061555,
ECO:0000269|PubMed:14711813, ECO:0000269|PubMed:16778204,
ECO:0000269|PubMed:16928683, ECO:0000269|PubMed:20117004}.
-!- PTM: 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. {ECO:0000269|PubMed:21357690}.
-!- POLYMORPHISM: The Cys-982 polymorphism may be associated with an
increased risk for developing Hirschsprung disease.
-!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
characterized by malignant lesions arising from the inner wall of
the large intestine (the colon) and the rectum. Genetic
alterations are often associated with progression from
premalignant lesion (adenoma) to invasive adenocarcinoma. Risk
factors for cancer of the colon and rectum include colon polyps,
long-standing ulcerative colitis, and genetic family history.
Note=The disease may be caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Hirschsprung disease 1 (HSCR1) [MIM:142623]: A disorder
of neural crest development characterized by absence of enteric
ganglia along a variable length of the intestine. It is the most
common cause of congenital intestinal obstruction. Early symptoms
range from complete acute neonatal obstruction, characterized by
vomiting, abdominal distention and failure to pass stool, to
chronic constipation in the older child.
{ECO:0000269|PubMed:10090908, ECO:0000269|PubMed:10484767,
ECO:0000269|PubMed:10618407, ECO:0000269|PubMed:22174939,
ECO:0000269|PubMed:7581377, ECO:0000269|PubMed:7633441,
ECO:0000269|PubMed:7704557, ECO:0000269|PubMed:7881414,
ECO:0000269|PubMed:8114938, ECO:0000269|PubMed:8114939,
ECO:0000269|PubMed:9043870, ECO:0000269|PubMed:9090527,
ECO:0000269|PubMed:9094028, ECO:0000269|PubMed:9259198,
ECO:0000269|PubMed:9384613, ECO:0000269|Ref.56}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Medullary thyroid carcinoma (MTC) [MIM:155240]: Rare
tumor derived from the C cells of the thyroid. Three hereditary
forms are known, that are transmitted in an autosomal dominant
fashion: (a) multiple neoplasia type 2A (MEN2A), (b) multiple
neoplasia type IIB (MEN2B) and (c) familial MTC (FMTC), which
occurs in 25-30% of MTC cases and where MTC is the only clinical
manifestation. {ECO:0000269|PubMed:10323403,
ECO:0000269|PubMed:10826520, ECO:0000269|PubMed:11692159,
ECO:0000269|PubMed:7784092, ECO:0000269|PubMed:7845675,
ECO:0000269|PubMed:7849720, ECO:0000269|PubMed:7874109,
ECO:0000269|PubMed:7881414, ECO:0000269|PubMed:7915165,
ECO:0000269|PubMed:8103403, ECO:0000269|PubMed:8557249,
ECO:0000269|PubMed:8625130, ECO:0000269|PubMed:8807338,
ECO:0000269|PubMed:9223675, ECO:0000269|PubMed:9259198,
ECO:0000269|PubMed:9398735, ECO:0000269|PubMed:9452077,
ECO:0000269|PubMed:9506724, ECO:0000269|PubMed:9621513,
ECO:0000269|PubMed:9677065}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Multiple neoplasia 2B (MEN2B) [MIM:162300]: Uncommon
inherited cancer syndrome characterized by predisposition to MTC
and phaeochromocytoma which is associated with marfanoid habitus,
mucosal neuromas, skeletal and ophthalmic abnormalities, and
ganglioneuromas of the intestine tract. Then the disease
progresses rapidly with the development of metastatic MTC and a
pheochromocytome in 50% of cases. {ECO:0000269|PubMed:7906417,
ECO:0000269|PubMed:7906866, ECO:0000269|PubMed:7911697,
ECO:0000269|PubMed:8595427, ECO:0000269|PubMed:8807338,
ECO:0000269|PubMed:9294615, ECO:0000269|PubMed:9360560}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Pheochromocytoma (PCC) [MIM:171300]: A catecholamine-
producing tumor of chromaffin tissue of the adrenal medulla or
sympathetic paraganglia. The cardinal symptom, reflecting the
increased secretion of epinephrine and norepinephrine, is
hypertension, which may be persistent or intermittent.
{ECO:0000269|PubMed:12000816}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Multiple neoplasia 2A (MEN2A) [MIM:171400]: The most
frequent form of medullary thyroid cancer (MTC). It is an
inherited cancer syndrome characterized by MTC, phaeochromocytoma
and/or hyperparathyroidism. {ECO:0000269|PubMed:10522989,
ECO:0000269|PubMed:7860065, ECO:0000269|PubMed:7874109,
ECO:0000269|PubMed:7881414, ECO:0000269|PubMed:7915165,
ECO:0000269|PubMed:8099202, ECO:0000269|PubMed:8103403,
ECO:0000269|PubMed:8626834, ECO:0000269|PubMed:8807338,
ECO:0000269|PubMed:9097963, ECO:0000269|PubMed:9384613,
ECO:0000269|PubMed:9452064}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Various chromosomal aberrations involving RET are
known. Some of them have been found in papillary thyroid
carcinomas (PTCs) (PubMed:12787916, PubMed:2406025,
PubMed:10980597, PubMed:10439047). Inversion inv(10)(q11.2;q21)
generates the RET/CCDC6 (PTC1) oncogene (PubMed:2406025).
Inversion inv(10)(q11.2;q11.2) generates the RET/NCOA4 (PTC3)
oncogene. Translocation t(10;14)(q11;q32) with GOLGA5 generates
the RET/GOLGA5 (PTC5) oncogene (PubMed:2734021). Translocation
t(8;10)(p21.3;q11.2) with PCM1 generates the PCM1/RET fusion
(PubMed:10980597). Translocation t(6;10)(p21.3;q11.2) with
TRIM27/RFP generates the Delta RFP/RET oncogene (PubMed:12787916).
Translocation t(1;10)(p13;q11) with TRIM33 generates the
TRIM33/RET (PTC7) oncogene (PubMed:10439047). Translocation
t(7;10)(q32;q11) with TRIM24/TIF1 generates the TRIM24/RET (PTC6)
oncogene (PubMed:10439047). Translocation t(6;10)(p21.3;q11.2)
with TRIM27/RFP generates the TRIM27/RET oncogene
(PubMed:3037315). {ECO:0000269|PubMed:10439047,
ECO:0000269|PubMed:10980597, ECO:0000269|PubMed:12787916,
ECO:0000269|PubMed:2406025, ECO:0000269|PubMed:2734021,
ECO:0000269|PubMed:3037315}.
-!- DISEASE: Note=Mutations in RET have been detected in patients with
renal agenesis suggesting a possible involvement of this gene in
disease pathogenesis.
-!- DISEASE: Congenital central hypoventilation syndrome (CCHS)
[MIM:209880]: Rare disorder characterized by abnormal control of
respiration in the absence of neuromuscular or lung disease, or an
identifiable brain stem lesion. A deficiency in autonomic control
of respiration results in inadequate or negligible ventilatory and
arousal responses to hypercapnia and hypoxemia.
{ECO:0000269|PubMed:12086152, ECO:0000269|PubMed:14566559,
ECO:0000269|PubMed:9497256}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Treatment with withaferin A (WA) leads tumor
regression in medullary thyroid carcinomas (MTC).
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAA36524.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAA36786.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA33787.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAC14882.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RETID76.html";
-!- WEB RESOURCE: Name=MEN2 RET database;
URL="http://www.arup.utah.edu/database/MEN2/MEN2_welcome.php";
-----------------------------------------------------------------------
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EMBL; AK291807; BAF84496.1; -; mRNA.
EMBL; AC010864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004257; AAH04257.1; -; mRNA.
EMBL; X15262; CAA33333.1; -; mRNA.
EMBL; X12949; CAA31408.1; -; mRNA.
EMBL; M16029; AAA36786.1; ALT_INIT; mRNA.
EMBL; X15786; CAA33787.1; ALT_INIT; mRNA.
EMBL; M31213; AAA36524.1; ALT_INIT; mRNA.
EMBL; AJ297349; CAC14882.1; ALT_INIT; mRNA.
CCDS; CCDS53525.1; -. [P07949-2]
CCDS; CCDS7200.1; -. [P07949-1]
PIR; A27203; TVHURE.
PIR; A34630; A34630.
PIR; B34735; B34735.
PIR; S05582; S05582.
RefSeq; NP_065681.1; NM_020630.4. [P07949-2]
RefSeq; NP_066124.1; NM_020975.4. [P07949-1]
UniGene; Hs.350321; -.
PDB; 1XPD; Model; -; A=709-1013.
PDB; 2IVS; X-ray; 2.00 A; A/B=705-1013.
PDB; 2IVT; X-ray; 2.60 A; A=705-1013.
PDB; 2IVU; X-ray; 2.50 A; A=705-1013.
PDB; 2IVV; X-ray; 2.25 A; A=705-1013.
PDB; 2X2K; X-ray; 2.60 A; A=705-1013.
PDB; 2X2L; X-ray; 2.00 A; A=705-1013.
PDB; 2X2M; X-ray; 2.50 A; A/B=705-1013.
PDB; 2X2U; X-ray; 2.00 A; A=29-270.
PDB; 4CKI; X-ray; 2.12 A; A=705-1013.
PDB; 4CKJ; X-ray; 1.65 A; A=705-1013.
PDB; 4UX8; EM; 24.00 A; A/B=29-635.
PDB; 5AMN; X-ray; 2.57 A; A=705-1012.
PDB; 5FM2; X-ray; 3.30 A; A=659-1013.
PDB; 5FM3; X-ray; 2.95 A; A=659-1013.
PDBsum; 1XPD; -.
PDBsum; 2IVS; -.
PDBsum; 2IVT; -.
PDBsum; 2IVU; -.
PDBsum; 2IVV; -.
PDBsum; 2X2K; -.
PDBsum; 2X2L; -.
PDBsum; 2X2M; -.
PDBsum; 2X2U; -.
PDBsum; 4CKI; -.
PDBsum; 4CKJ; -.
PDBsum; 4UX8; -.
PDBsum; 5AMN; -.
PDBsum; 5FM2; -.
PDBsum; 5FM3; -.
ProteinModelPortal; P07949; -.
SMR; P07949; -.
BioGrid; 111911; 44.
DIP; DIP-41449N; -.
IntAct; P07949; 29.
MINT; MINT-1217685; -.
STRING; 9606.ENSP00000347942; -.
BindingDB; P07949; -.
ChEMBL; CHEMBL2041; -.
DrugBank; DB08764; 4-BROMO-2-FLUORO-N-[(4E)-6-METHOXY-7-[(1-METHYLPIPERIDIN-4-YL)METHOXY]QUINAZOLIN-4(1H)-YLIDENE]ANILINE.
DrugBank; DB08875; Cabozantinib.
DrugBank; DB05216; MP470.
DrugBank; DB08901; Ponatinib.
DrugBank; DB08896; Regorafenib.
DrugBank; DB00398; Sorafenib.
GuidetoPHARMACOLOGY; 2185; -.
iPTMnet; P07949; -.
PhosphoSitePlus; P07949; -.
BioMuta; RET; -.
DMDM; 547807; -.
EPD; P07949; -.
MaxQB; P07949; -.
PaxDb; P07949; -.
PeptideAtlas; P07949; -.
PRIDE; P07949; -.
TopDownProteomics; P07949-2; -. [P07949-2]
DNASU; 5979; -.
Ensembl; ENST00000340058; ENSP00000344798; ENSG00000165731. [P07949-2]
Ensembl; ENST00000355710; ENSP00000347942; ENSG00000165731. [P07949-1]
GeneID; 5979; -.
KEGG; hsa:5979; -.
UCSC; uc001jak.2; human. [P07949-1]
CTD; 5979; -.
DisGeNET; 5979; -.
GeneCards; RET; -.
GeneReviews; RET; -.
HGNC; HGNC:9967; RET.
HPA; CAB002581; -.
HPA; CAB018342; -.
HPA; HPA008356; -.
HPA; HPA008495; -.
MalaCards; RET; -.
MIM; 114500; phenotype.
MIM; 142623; phenotype.
MIM; 155240; phenotype.
MIM; 162300; phenotype.
MIM; 164761; gene.
MIM; 171300; phenotype.
MIM; 171400; phenotype.
MIM; 209880; phenotype.
neXtProt; NX_P07949; -.
OpenTargets; ENSG00000165731; -.
Orphanet; 1848; Bilateral renal agenesis.
Orphanet; 99361; Familial medullary thyroid carcinoma.
Orphanet; 99803; Haddad syndrome.
Orphanet; 29072; Hereditary pheochromocytoma-paraganglioma.
Orphanet; 388; Hirschsprung disease.
Orphanet; 247698; Multiple endocrine neoplasia type 2A.
Orphanet; 247709; Multiple endocrine neoplasia type 2B.
Orphanet; 146; Papillary or follicular thyroid carcinoma.
Orphanet; 93100; Unilateral renal agenesis.
PharmGKB; PA34335; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000010301; -.
HOVERGEN; HBG002609; -.
InParanoid; P07949; -.
KO; K05126; -.
OMA; DSMENQV; -.
OrthoDB; EOG091G0CQZ; -.
PhylomeDB; P07949; -.
TreeFam; TF317640; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-8853659; RET signaling.
SignaLink; P07949; -.
SIGNOR; P07949; -.
ChiTaRS; RET; human.
EvolutionaryTrace; P07949; -.
GeneWiki; RET_proto-oncogene; -.
GenomeRNAi; 5979; -.
PRO; PR:P07949; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000165731; -.
CleanEx; HS_RET; -.
ExpressionAtlas; P07949; baseline and differential.
Genevisible; P07949; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0098797; C:plasma membrane protein complex; IDA:CAFA.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
GO; GO:0001838; P:embryonic epithelial tube formation; IEA:Ensembl.
GO; GO:0048484; P:enteric nervous system development; IEA:Ensembl.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0060384; P:innervation; IEA:Ensembl.
GO; GO:0097021; P:lymphocyte migration into lymphoid organs; ISS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
GO; GO:0007158; P:neuron cell-cell adhesion; IMP:UniProtKB.
GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
GO; GO:0061146; P:Peyer's patch morphogenesis; ISS:UniProtKB.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB.
GO; GO:0072300; P:positive regulation of metanephric glomerulus development; ISS:UniProtKB.
GO; GO:0014042; P:positive regulation of neuron maturation; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0007497; P:posterior midgut development; TAS:ProtInc.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0048265; P:response to pain; ISS:UniProtKB.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:Ensembl.
GO; GO:0035799; P:ureter maturation; IEA:Ensembl.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016249; Tyr_kinase_Ret_rcpt.
Pfam; PF00028; Cadherin; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF000631; TyrPK_receptor_Ret; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49313; SSF49313; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50268; CADHERIN_2; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell adhesion;
Cell membrane; Chromosomal rearrangement; Complete proteome;
Disease mutation; Disulfide bond; Endosome; Glycoprotein;
Hirschsprung disease; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome;
Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 1114 Proto-oncogene tyrosine-protein kinase
receptor Ret.
/FTId=PRO_0000024450.
CHAIN 29 707 Extracellular cell-membrane anchored RET
cadherin 120 kDa fragment.
/FTId=PRO_0000415292.
CHAIN 708 1017 Soluble RET kinase fragment.
/FTId=PRO_0000415293.
TOPO_DOM 29 635 Extracellular. {ECO:0000255}.
TRANSMEM 636 657 Helical. {ECO:0000255}.
TOPO_DOM 658 1114 Cytoplasmic. {ECO:0000255}.
DOMAIN 168 272 Cadherin. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 724 1016 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 730 738 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 805 807 Inhibitors binding.
ACT_SITE 874 874 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 758 758 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 892 892 Inhibitor.
SITE 587 588 Breakpoint for translocation to form the
TRIM27/RET oncogene.
SITE 707 708 Cleavage; by caspase-3.
SITE 712 713 Breakpoint for translocation to form
PCM1-RET; RET-CCDC6; RET-GOLGA5; RET-
TRIM24 and RET-TRIM33 oncogenes.
SITE 1017 1018 Cleavage; by caspase-3.
MOD_RES 696 696 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 806 806 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14711813}.
MOD_RES 809 809 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14711813}.
MOD_RES 900 900 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14711813,
ECO:0000269|PubMed:16928683}.
MOD_RES 905 905 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14711813,
ECO:0000269|PubMed:16778204,
ECO:0000269|PubMed:16928683,
ECO:0000269|PubMed:20117004}.
MOD_RES 981 981 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14711813}.
MOD_RES 1015 1015 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11061555,
ECO:0000269|PubMed:14711813,
ECO:0000269|PubMed:16778204}.
MOD_RES 1062 1062 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11061555,
ECO:0000269|PubMed:14711813,
ECO:0000269|PubMed:16778204}.
MOD_RES 1090 1090 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14711813}.
MOD_RES 1096 1096 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14711813}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20473317}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 343 343 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 361 361 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 377 377 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 394 394 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 554 554 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 137 142 {ECO:0000269|PubMed:20473317}.
VAR_SEQ 1064 1114 MSDPNWPGESPVPLTRADGTNTGFPRYPNDSVYANWMLSPS
AAKLMDTFDS -> RISHAFTRF (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:3037315}.
/FTId=VSP_040735.
VARIANT 20 20 P -> L (in HSCR1; sporadic form).
{ECO:0000269|PubMed:7633441}.
/FTId=VAR_009459.
VARIANT 32 32 S -> L (in HSCR1; familial form;
dbSNP:rs76764689).
{ECO:0000269|PubMed:10618407,
ECO:0000269|PubMed:8114939}.
/FTId=VAR_006295.
VARIANT 40 40 L -> P (in HSCR1).
{ECO:0000269|PubMed:7704557,
ECO:0000269|PubMed:9043870}.
/FTId=VAR_009492.
VARIANT 64 64 P -> L (in HSCR1; familial form;
dbSNP:rs77596424).
{ECO:0000269|PubMed:8114939}.
/FTId=VAR_006296.
VARIANT 67 67 R -> H (in CCHS; dbSNP:rs192489011).
{ECO:0000269|PubMed:14566559}.
/FTId=VAR_018153.
VARIANT 77 77 R -> C (in HSCR1).
{ECO:0000269|PubMed:10618407}.
/FTId=VAR_009460.
VARIANT 93 93 G -> S (in HSCR1; unknown pathological
significance).
{ECO:0000269|PubMed:7633441}.
/FTId=VAR_006297.
VARIANT 114 114 R -> C (in HSCR1; dbSNP:rs747483905).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067101.
VARIANT 114 114 R -> H (in CCHS and HSCR1;
dbSNP:rs76397662).
{ECO:0000269|PubMed:12086152,
ECO:0000269|PubMed:14566559,
ECO:0000269|PubMed:22174939}.
/FTId=VAR_018154.
VARIANT 142 142 C -> S (in HSCR1; sporadic form).
/FTId=VAR_006298.
VARIANT 145 145 V -> G (in HSCR1; also in a colorectal
cancer sample; somatic mutation).
{ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:22174939}.
/FTId=VAR_035711.
VARIANT 155 155 P -> L (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067102.
VARIANT 157 157 C -> Y (in HSCR1; unknown pathological
significance). {ECO:0000269|Ref.56}.
/FTId=VAR_009461.
VARIANT 163 163 R -> Q (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs149403911).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041762.
VARIANT 174 174 F -> S (in HSCR1; sporadic form).
{ECO:0000269|PubMed:9094028}.
/FTId=VAR_009462.
VARIANT 175 175 R -> P (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067103.
VARIANT 180 180 R -> P (in HSCR1; sporadic form).
{ECO:0000269|PubMed:9090527}.
/FTId=VAR_009463.
VARIANT 197 197 C -> Y (in HSCR1; sporadic form).
{ECO:0000269|PubMed:9094028}.
/FTId=VAR_009464.
VARIANT 198 198 P -> T (in a patient with renal agenesis;
unknown pathological significance;
prevents phosphorylation in response to
GDNF; dbSNP:rs76736111).
{ECO:0000269|PubMed:18252215}.
/FTId=VAR_044392.
VARIANT 231 231 R -> H (in HSCR1; familial form;
dbSNP:rs79661516).
/FTId=VAR_006299.
VARIANT 251 251 E -> K (in HSCR1; familial form;
dbSNP:rs562449603).
/FTId=VAR_006300.
VARIANT 278 278 T -> A (in HSCR1; dbSNP:rs541929171).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067104.
VARIANT 278 278 T -> N (found in two patients with
Hirschsprung disease; dbSNP:rs35118262).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:22174939}.
/FTId=VAR_041763.
VARIANT 278 278 T -> P (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067105.
VARIANT 287 287 R -> Q (in HSCR1; sporadic form).
/FTId=VAR_006301.
VARIANT 292 292 V -> M (found in patients with
Hirschsprung disease; unknown
pathological significance;
dbSNP:rs34682185).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:22174939}.
/FTId=VAR_041764.
VARIANT 300 300 D -> N (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067106.
VARIANT 313 313 R -> Q (in HSCR1; dbSNP:rs77702891).
{ECO:0000269|PubMed:22174939,
ECO:0000269|PubMed:9090527}.
/FTId=VAR_009465.
VARIANT 316 316 S -> I (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067107.
VARIANT 330 330 R -> Q (in HSCR1; dbSNP:rs80236571).
{ECO:0000269|PubMed:7633441,
ECO:0000269|PubMed:8114939}.
/FTId=VAR_006302.
VARIANT 339 339 S -> L (in HSCR1; dbSNP:rs774829203).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067108.
VARIANT 353 353 D -> Y (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067109.
VARIANT 359 359 N -> K (in HSCR1; unknown pathological
significance). {ECO:0000269|Ref.56}.
/FTId=VAR_009466.
VARIANT 360 360 R -> Q (in HSCR1; dbSNP:rs762472027).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067110.
VARIANT 360 360 R -> W (in HSCR1).
{ECO:0000269|PubMed:10618407,
ECO:0000269|PubMed:16959974}.
/FTId=VAR_009467.
VARIANT 376 376 V -> A (in a patient with renal agenesis;
unknown pathological significance;
constitutively phosphorylated; expressed
only the immature intracellular form).
{ECO:0000269|PubMed:18252215}.
/FTId=VAR_044393.
VARIANT 393 393 F -> L (in HSCR1; familial form;
dbSNP:rs78098482).
{ECO:0000269|PubMed:8114939}.
/FTId=VAR_006303.
VARIANT 394 394 N -> H (in a patient with renal agenesis;
unknown pathological significance;
prevents phosphorylation in response to
GDNF). {ECO:0000269|PubMed:18252215}.
/FTId=VAR_044394.
VARIANT 394 394 N -> K (in HSCR1).
{ECO:0000269|PubMed:10618407}.
/FTId=VAR_009468.
VARIANT 397 397 V -> M (in HSCR1; dbSNP:rs183729115).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067111.
VARIANT 399 399 P -> L (in HSCR1; sporadic form).
{ECO:0000269|PubMed:7704557}.
/FTId=VAR_006304.
VARIANT 412 412 V -> M (in HSCR1; dbSNP:rs746970700).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067112.
VARIANT 423 423 G -> R (in HSCR1; dbSNP:rs767601598).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067113.
VARIANT 432 432 A -> E (in CCHS; dbSNP:rs552057730).
{ECO:0000269|PubMed:14566559}.
/FTId=VAR_018155.
VARIANT 475 475 R -> Q (in HSCR1; sporadic form;
dbSNP:rs138624658).
/FTId=VAR_006305.
VARIANT 480 480 E -> K (in HSCR1; dbSNP:rs537874538).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067114.
VARIANT 489 489 D -> N (in dbSNP:rs9282834).
{ECO:0000269|PubMed:14566559,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_018156.
VARIANT 531 531 C -> CEEC (in MTC; familial form).
{ECO:0000269|PubMed:10323403}.
/FTId=VAR_009469.
VARIANT 549 550 Missing (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067115.
VARIANT 593 593 G -> E (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035712.
VARIANT 595 595 E -> Q (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067116.
VARIANT 600 600 R -> Q (in dbSNP:rs377767393).
{ECO:0000269|PubMed:10612852}.
/FTId=VAR_008966.
VARIANT 609 609 C -> G (in MEN2A; dbSNP:rs77558292).
/FTId=VAR_009470.
VARIANT 609 609 C -> R (in MEN2A; dbSNP:rs77558292).
/FTId=VAR_009471.
VARIANT 609 609 C -> W (in HSCR1; familial form;
dbSNP:rs377767396).
{ECO:0000269|PubMed:7881414}.
/FTId=VAR_006307.
VARIANT 609 609 C -> Y (in MTC, MEN2A and HSCR1; familial
and sporadic forms; dbSNP:rs77939446).
{ECO:0000269|PubMed:7633441,
ECO:0000269|PubMed:7849720,
ECO:0000269|PubMed:9384613,
ECO:0000269|Ref.56}.
/FTId=VAR_006306.
VARIANT 611 611 C -> G (in MTC; familial form;
dbSNP:rs377767391).
{ECO:0000269|PubMed:9677065}.
/FTId=VAR_009472.
VARIANT 611 611 C -> R (in MEN2A; dbSNP:rs377767391).
/FTId=VAR_009473.
VARIANT 611 611 C -> S (in MEN2A; dbSNP:rs377767391).
/FTId=VAR_009474.
VARIANT 611 611 C -> W (in MEN2A and MTC; familial form;
dbSNP:rs80069458).
{ECO:0000269|PubMed:8103403}.
/FTId=VAR_006308.
VARIANT 611 611 C -> Y (in MEN2A; dbSNP:rs377767397).
/FTId=VAR_006309.
VARIANT 618 618 C -> F (in MEN2A and MTC; familial form;
dbSNP:rs79781594).
/FTId=VAR_006312.
VARIANT 618 618 C -> G (in MEN2A; dbSNP:rs76262710).
{ECO:0000269|PubMed:8099202}.
/FTId=VAR_006310.
VARIANT 618 618 C -> R (in MEN2A, MTC and HSCR1;
dbSNP:rs76262710).
{ECO:0000269|PubMed:7849720,
ECO:0000269|PubMed:7881414,
ECO:0000269|PubMed:7915165,
ECO:0000269|PubMed:9259198}.
/FTId=VAR_006311.
VARIANT 618 618 C -> S (in MEN2A, HSCR1 and MTC; familial
and sporadic forms; dbSNP:rs79781594).
{ECO:0000269|PubMed:7849720,
ECO:0000269|PubMed:7860065,
ECO:0000269|PubMed:7915165,
ECO:0000269|PubMed:8103403,
ECO:0000269|PubMed:9384613}.
/FTId=VAR_006313.
VARIANT 618 618 C -> Y (in MEN2A and MTC; familial form;
dbSNP:rs79781594).
/FTId=VAR_006314.
VARIANT 620 620 C -> F (in MEN2A and MTC; familial form;
dbSNP:rs77503355).
{ECO:0000269|PubMed:7915165}.
/FTId=VAR_006318.
VARIANT 620 620 C -> G (in MEN2A and MTC; familial and
sporadic forms; dbSNP:rs77316810).
/FTId=VAR_006315.
VARIANT 620 620 C -> R (in MEN2A, MTC and HSCR1; familial
and sporadic forms; dbSNP:rs77316810).
{ECO:0000269|PubMed:7633441,
ECO:0000269|PubMed:7881414,
ECO:0000269|PubMed:7915165,
ECO:0000269|PubMed:8103403,
ECO:0000269|PubMed:9090527,
ECO:0000269|PubMed:9384613,
ECO:0000269|Ref.56}.
/FTId=VAR_006316.
VARIANT 620 620 C -> S (in MEN2A and MTC; familial form;
dbSNP:rs77503355).
{ECO:0000269|PubMed:7849720,
ECO:0000269|PubMed:7860065}.
/FTId=VAR_006317.
VARIANT 620 620 C -> W (in MEN2A and HSCR1;
dbSNP:rs79890926).
{ECO:0000269|PubMed:9384613}.
/FTId=VAR_009475.
VARIANT 620 620 C -> Y (in MEN2A; dbSNP:rs77503355).
{ECO:0000269|PubMed:8103403}.
/FTId=VAR_006319.
VARIANT 626 626 Q -> K (in HSCR1; sporadic form).
{ECO:0000269|PubMed:10090908}.
/FTId=VAR_009476.
VARIANT 630 630 C -> F (in MEN2A and MTC; familial form;
dbSNP:rs377767405).
/FTId=VAR_006320.
VARIANT 630 630 C -> S (in MTC; sporadic form;
dbSNP:rs377767405).
/FTId=VAR_009477.
VARIANT 630 630 C -> Y (in MTC; familial and sporadic
forms; dbSNP:rs377767405).
/FTId=VAR_009478.
VARIANT 631 631 D -> G (in thyroid carcinoma; somatic
mutation; dbSNP:rs121913308).
/FTId=VAR_006321.
VARIANT 632 634 ELC -> DVR (in MEN2A; dbSNP:rs377767408).
/FTId=VAR_006322.
VARIANT 634 635 CR -> WG (in MEN2A).
/FTId=VAR_006329.
VARIANT 634 634 C -> CHELC (in MEN2A).
{ECO:0000269|PubMed:9097963}.
/FTId=VAR_009479.
VARIANT 634 634 C -> F (in MEN2A and pheochromocytoma;
dbSNP:rs75996173).
{ECO:0000269|PubMed:12000816,
ECO:0000269|PubMed:7915165,
ECO:0000269|PubMed:8099202}.
/FTId=VAR_006324.
VARIANT 634 634 C -> G (in MEN2A and pheochromocytoma;
dbSNP:rs75076352).
{ECO:0000269|PubMed:12000816,
ECO:0000269|PubMed:7915165,
ECO:0000269|PubMed:8099202}.
/FTId=VAR_006323.
VARIANT 634 634 C -> R (in MEN2A, pheochromocytoma and
MTC; familial form; also found as somatic
mutation in a sporadic thyroid carcinoma;
dbSNP:rs75076352).
{ECO:0000269|PubMed:12000816,
ECO:0000269|PubMed:7860065,
ECO:0000269|PubMed:8103403}.
/FTId=VAR_006326.
VARIANT 634 634 C -> S (in MEN2A, pheochromocytoma and
MTC; familial form; dbSNP:rs75076352).
{ECO:0000269|PubMed:12000816,
ECO:0000269|PubMed:8099202}.
/FTId=VAR_006327.
VARIANT 634 634 C -> W (in MEN2A, pheochromocytoma and
MTC; familial form; dbSNP:rs77709286).
{ECO:0000269|PubMed:12000816}.
/FTId=VAR_006328.
VARIANT 634 634 C -> Y (in MEN2A, pheochromocytoma and
MTC; familial form; dbSNP:rs75996173).
{ECO:0000269|PubMed:12000816,
ECO:0000269|PubMed:7860065,
ECO:0000269|PubMed:7915165,
ECO:0000269|PubMed:8099202}.
/FTId=VAR_006325.
VARIANT 636 636 T -> TCRT (in MEN2A).
{ECO:0000269|PubMed:9452064}.
/FTId=VAR_006330.
VARIANT 639 639 A -> G (in MTC; sporadic form).
{ECO:0000269|PubMed:11692159}.
/FTId=VAR_012743.
VARIANT 640 640 A -> G (in MEN2A; dbSNP:rs78935588).
{ECO:0000269|PubMed:10522989}.
/FTId=VAR_009480.
VARIANT 641 641 A -> G (in MTC; sporadic form).
{ECO:0000269|PubMed:11692159}.
/FTId=VAR_012744.
VARIANT 679 679 P -> L (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067117.
VARIANT 690 690 S -> P (in HSCR1; sporadic form).
/FTId=VAR_006331.
VARIANT 691 691 G -> S (in dbSNP:rs1799939).
{ECO:0000269|PubMed:14566559,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9223675,
ECO:0000269|PubMed:9497256}.
/FTId=VAR_006332.
VARIANT 694 694 R -> Q (in HSCR1; dbSNP:rs141185224).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067118.
VARIANT 749 749 R -> T (in dbSNP:rs34288963).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041765.
VARIANT 762 762 E -> Q (in HSCR1; sporadic form).
{ECO:0000269|PubMed:7704557}.
/FTId=VAR_009481.
VARIANT 765 765 S -> P (in HSCR1; dbSNP:rs75075748).
{ECO:0000269|PubMed:7704557,
ECO:0000269|PubMed:8114938,
ECO:0000269|PubMed:9043870}.
/FTId=VAR_009493.
VARIANT 767 767 S -> R (in HSCR1; sporadic form).
/FTId=VAR_006334.
VARIANT 768 768 E -> D (in MTC; familial and sporadic
forms; dbSNP:rs78014899).
{ECO:0000269|PubMed:7784092,
ECO:0000269|PubMed:7845675,
ECO:0000269|PubMed:8807338}.
/FTId=VAR_006335.
VARIANT 778 778 V -> I (in a patient with renal agenesis;
unknown pathological significance;
constitutively phosphorylated;
dbSNP:rs75686697).
{ECO:0000269|PubMed:18252215}.
/FTId=VAR_044395.
VARIANT 783 783 N -> S (in HSCR1; dbSNP:rs587778656).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067119.
VARIANT 790 790 L -> F (in MEN2A and MTC; familial form;
dbSNP:rs75030001).
{ECO:0000269|PubMed:9506724}.
/FTId=VAR_009482.
VARIANT 791 791 Y -> F (in HSCR1, pheochromocytoma, MTC
and MEN2A; familial form;
dbSNP:rs77724903).
{ECO:0000269|PubMed:12000816,
ECO:0000269|PubMed:9090527,
ECO:0000269|PubMed:9506724}.
/FTId=VAR_009483.
VARIANT 804 804 V -> L (in MTC; familial form;
dbSNP:rs79658334).
{ECO:0000269|PubMed:7784092}.
/FTId=VAR_006336.
VARIANT 804 804 V -> M (in MTC; familial form;
dbSNP:rs79658334).
{ECO:0000269|PubMed:10826520,
ECO:0000269|PubMed:9452077}.
/FTId=VAR_006337.
VARIANT 813 813 R -> Q (in HSCR1; sporadic form).
{ECO:0000269|PubMed:10090908}.
/FTId=VAR_009484.
VARIANT 826 826 Y -> S (in dbSNP:rs34617196).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041766.
VARIANT 830 830 G -> R (in HSCR1; dbSNP:rs200127630).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067120.
VARIANT 844 844 R -> L (in MTC; familial form;
dbSNP:rs55947360).
{ECO:0000269|PubMed:10826520,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_011582.
VARIANT 873 873 R -> Q (in HSCR1; sporadic form).
/FTId=VAR_006338.
VARIANT 883 883 A -> F (in MEN2B; somatic mutation in
sporadic medullary thyroid carcinoma;
requires 2 nucleotide substitutions;
dbSNP:rs377767429).
{ECO:0000269|PubMed:9294615,
ECO:0000269|PubMed:9360560}.
/FTId=VAR_009485.
VARIANT 891 891 S -> A (in MTC; familial form;
dbSNP:rs75234356).
{ECO:0000269|PubMed:9398735}.
/FTId=VAR_009486.
VARIANT 893 893 F -> L (in HSCR1; sporadic form).
/FTId=VAR_006339.
VARIANT 894 894 G -> S (in a patient with renal agenesis;
unknown pathological significance;
constitutively phosphorylated; expressed
only the immature intracellular form).
{ECO:0000269|PubMed:18252215}.
/FTId=VAR_044396.
VARIANT 897 897 R -> Q (in HSCR1; sporadic form;
dbSNP:rs76087194).
{ECO:0000269|PubMed:7704557,
ECO:0000269|PubMed:8114938}.
/FTId=VAR_006340.
VARIANT 907 907 K -> E (in HSCR1; sporadic form;
dbSNP:rs377767430).
/FTId=VAR_006341.
VARIANT 907 907 K -> T (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067121.
VARIANT 918 918 M -> T (in MEN2B and MTC; sporadic form;
somatic mutation; also found in a patient
with renal agenesis; dbSNP:rs74799832).
{ECO:0000269|PubMed:18252215,
ECO:0000269|PubMed:7906417,
ECO:0000269|PubMed:7906866,
ECO:0000269|PubMed:7911697,
ECO:0000269|PubMed:8595427,
ECO:0000269|PubMed:8807338}.
/FTId=VAR_006342.
VARIANT 921 921 E -> K (in HSCR1; sporadic form).
/FTId=VAR_006343.
VARIANT 922 922 S -> F (in MTC; sporadic form;
dbSNP:rs377767432).
{ECO:0000269|PubMed:11692159}.
/FTId=VAR_012745.
VARIANT 922 922 S -> Y (rare polymorphism;
dbSNP:rs377767432).
{ECO:0000269|PubMed:8595427}.
/FTId=VAR_009487.
VARIANT 946 946 T -> M (in MEN2B and MTC; familial form).
/FTId=VAR_006345.
VARIANT 961 961 F -> L (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067122.
VARIANT 972 972 R -> G (in HSCR1; familial form;
dbSNP:rs76534745).
{ECO:0000269|PubMed:7704557,
ECO:0000269|PubMed:8114938}.
/FTId=VAR_006346.
VARIANT 973 973 P -> L (in HSCR1; familial form).
{ECO:0000269|PubMed:7704557}.
/FTId=VAR_006347.
VARIANT 980 980 M -> T (in HSCR1; sporadic form).
/FTId=VAR_006348.
VARIANT 982 982 R -> C (in dbSNP:rs17158558).
{ECO:0000269|PubMed:14566559,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:7633441,
ECO:0000269|PubMed:9760196}.
/FTId=VAR_006349.
VARIANT 1039 1039 P -> L (in CCHS; with colonic
aganglionosis; dbSNP:rs79853121).
{ECO:0000269|PubMed:9497256}.
/FTId=VAR_018157.
VARIANT 1039 1039 P -> Q (in dbSNP:rs79853121).
/FTId=VAR_009488.
VARIANT 1049 1049 P -> L (in a patient with renal agenesis;
unknown pathological significance;
prevents phosphorylation in response to
GDNF). {ECO:0000269|PubMed:18252215}.
/FTId=VAR_044397.
VARIANT 1052 1052 L -> V (in HSCR1).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067123.
VARIANT 1059 1059 Missing (in HSCR1).
{ECO:0000269|PubMed:10484767,
ECO:0000269|Ref.56}.
/FTId=VAR_009489.
VARIANT 1061 1061 L -> P (in HSCR1; dbSNP:rs536486113).
{ECO:0000269|PubMed:10484767,
ECO:0000269|Ref.56}.
/FTId=VAR_009490.
VARIANT 1062 1062 Y -> C (in HSCR1; dbSNP:rs587778659).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_067124.
VARIANT 1064 1064 M -> T (in HSCR1; familial form;
dbSNP:rs149513065).
{ECO:0000269|PubMed:22174939}.
/FTId=VAR_009491.
VARIANT 1067 1067 P -> S (in a patient with renal agenesis;
unknown pathological significance;
prevents phosphorylation in response to
GDNF; dbSNP:rs775583354).
{ECO:0000269|PubMed:18252215}.
/FTId=VAR_044398.
VARIANT 1112 1112 F -> Y (in a bladder transitional cell
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041767.
MUTAGEN 707 707 D->N: Impaired cleavage by caspase-3 and
loss of induced cell death.
{ECO:0000269|PubMed:21357690}.
MUTAGEN 708 1114 Missing: Loss of induced cell death, but
increased cell aggregation.
{ECO:0000269|PubMed:21357690}.
MUTAGEN 758 758 K->R: Loss of kinase activity. No effect
on interaction with and dissociation from
CBLC and CD2AP.
{ECO:0000269|PubMed:18753381,
ECO:0000269|PubMed:21357690}.
CONFLICT 647 647 I -> V (in Ref. 6; AAA36786).
{ECO:0000305}.
CONFLICT 664 664 A -> S (in Ref. 1; BAF84496).
{ECO:0000305}.
CONFLICT 750 750 A -> G (in Ref. 9; AAA36524).
{ECO:0000305}.
CONFLICT 904 904 S -> P (in Ref. 6; AAA36786).
{ECO:0000305}.
STRAND 30 32 {ECO:0000244|PDB:2X2U}.
STRAND 34 41 {ECO:0000244|PDB:2X2U}.
STRAND 49 52 {ECO:0000244|PDB:2X2U}.
STRAND 70 73 {ECO:0000244|PDB:2X2U}.
HELIX 75 77 {ECO:0000244|PDB:2X2U}.
STRAND 79 82 {ECO:0000244|PDB:2X2U}.
STRAND 85 88 {ECO:0000244|PDB:2X2U}.
TURN 90 92 {ECO:0000244|PDB:2X2U}.
STRAND 94 99 {ECO:0000244|PDB:2X2U}.
HELIX 103 111 {ECO:0000244|PDB:2X2U}.
STRAND 120 126 {ECO:0000244|PDB:2X2U}.
TURN 139 141 {ECO:0000244|PDB:2X2U}.
STRAND 142 152 {ECO:0000244|PDB:2X2U}.
HELIX 157 159 {ECO:0000244|PDB:2X2U}.
HELIX 162 166 {ECO:0000244|PDB:2X2U}.
STRAND 174 178 {ECO:0000244|PDB:2X2U}.
STRAND 184 187 {ECO:0000244|PDB:2X2U}.
HELIX 191 196 {ECO:0000244|PDB:2X2U}.
STRAND 202 208 {ECO:0000244|PDB:2X2U}.
STRAND 212 215 {ECO:0000244|PDB:2X2U}.
STRAND 222 227 {ECO:0000244|PDB:2X2U}.
TURN 231 233 {ECO:0000244|PDB:2X2U}.
STRAND 235 245 {ECO:0000244|PDB:2X2U}.
STRAND 252 263 {ECO:0000244|PDB:2X2U}.
HELIX 705 711 {ECO:0000244|PDB:4CKJ}.
TURN 715 717 {ECO:0000244|PDB:4CKJ}.
HELIX 721 723 {ECO:0000244|PDB:4CKJ}.
STRAND 724 732 {ECO:0000244|PDB:4CKJ}.
STRAND 734 744 {ECO:0000244|PDB:4CKJ}.
HELIX 746 748 {ECO:0000244|PDB:2IVS}.
STRAND 750 760 {ECO:0000244|PDB:4CKJ}.
HELIX 766 779 {ECO:0000244|PDB:4CKJ}.
STRAND 790 794 {ECO:0000244|PDB:4CKJ}.
STRAND 796 798 {ECO:0000244|PDB:4CKJ}.
STRAND 801 805 {ECO:0000244|PDB:4CKJ}.
HELIX 812 817 {ECO:0000244|PDB:4CKJ}.
TURN 819 821 {ECO:0000244|PDB:2IVS}.
STRAND 844 846 {ECO:0000244|PDB:4CKI}.
HELIX 848 867 {ECO:0000244|PDB:4CKJ}.
HELIX 877 879 {ECO:0000244|PDB:4CKJ}.
STRAND 880 883 {ECO:0000244|PDB:4CKJ}.
TURN 884 886 {ECO:0000244|PDB:4CKJ}.
STRAND 887 890 {ECO:0000244|PDB:4CKJ}.
HELIX 893 895 {ECO:0000244|PDB:2IVV}.
TURN 900 902 {ECO:0000244|PDB:4CKJ}.
HELIX 915 917 {ECO:0000244|PDB:4CKJ}.
HELIX 920 925 {ECO:0000244|PDB:4CKJ}.
HELIX 930 945 {ECO:0000244|PDB:4CKJ}.
HELIX 957 959 {ECO:0000244|PDB:4CKJ}.
HELIX 960 965 {ECO:0000244|PDB:4CKJ}.
HELIX 978 987 {ECO:0000244|PDB:4CKJ}.
HELIX 992 994 {ECO:0000244|PDB:4CKJ}.
HELIX 998 1012 {ECO:0000244|PDB:4CKJ}.
SEQUENCE 1114 AA; 124319 MW; A3DA0CE01A19A441 CRC64;
MAKATSGAAG LRLLLLLLLP LLGKVALGLY FSRDAYWEKL YVDQAAGTPL LYVHALRDAP
EEVPSFRLGQ HLYGTYRTRL HENNWICIQE DTGLLYLNRS LDHSSWEKLS VRNRGFPLLT
VYLKVFLSPT SLREGECQWP GCARVYFSFF NTSFPACSSL KPRELCFPET RPSFRIRENR
PPGTFHQFRL LPVQFLCPNI SVAYRLLEGE GLPFRCAPDS LEVSTRWALD REQREKYELV
AVCTVHAGAR EEVVMVPFPV TVYDEDDSAP TFPAGVDTAS AVVEFKRKED TVVATLRVFD
ADVVPASGEL VRRYTSTLLP GDTWAQQTFR VEHWPNETSV QANGSFVRAT VHDYRLVLNR
NLSISENRTM QLAVLVNDSD FQGPGAGVLL LHFNVSVLPV SLHLPSTYSL SVSRRARRFA
QIGKVCVENC QAFSGINVQY KLHSSGANCS TLGVVTSAED TSGILFVNDT KALRRPKCAE
LHYMVVATDQ QTSRQAQAQL LVTVEGSYVA EEAGCPLSCA VSKRRLECEE CGGLGSPTGR
CEWRQGDGKG ITRNFSTCSP STKTCPDGHC DVVETQDINI CPQDCLRGSI VGGHEPGEPR
GIKAGYGTCN CFPEEEKCFC EPEDIQDPLC DELCRTVIAA AVLFSFIVSV LLSAFCIHCY
HKFAHKPPIS SAEMTFRRPA QAFPVSYSSS GARRPSLDSM ENQVSVDAFK ILEDPKWEFP
RKNLVLGKTL GEGEFGKVVK ATAFHLKGRA GYTTVAVKML KENASPSELR DLLSEFNVLK
QVNHPHVIKL YGACSQDGPL LLIVEYAKYG SLRGFLRESR KVGPGYLGSG GSRNSSSLDH
PDERALTMGD LISFAWQISQ GMQYLAEMKL VHRDLAARNI LVAEGRKMKI SDFGLSRDVY
EEDSYVKRSQ GRIPVKWMAI ESLFDHIYTT QSDVWSFGVL LWEIVTLGGN PYPGIPPERL
FNLLKTGHRM ERPDNCSEEM YRLMLQCWKQ EPDKRPVFAD ISKDLEKMMV KRRDYLDLAA
STPSDSLIYD DGLSEEETPL VDCNNAPLPR ALPSTWIENK LYGMSDPNWP GESPVPLTRA
DGTNTGFPRY PNDSVYANWM LSPSAAKLMD TFDS


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