P35546 (RET_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proto-oncogene tyrosine-protein kinase receptor Ret
EC=2.7.10.1

Alternative name(s):
Proto-oncogene c-Ret

Cleaved into the following 2 chains:

1. Soluble RET kinase fragment
2. Extracellular cell-membrane anchored RET cadherin 120 kDa fragment

Gene names

Name:

Ret

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1115 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.9
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	Repressed by withaferin A (WA). Ref.10
Subunit structure	Interacts (not phosphorylated) with CC 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 By similarity. Phosphorylated form interacts with the PBT domain of DOK2, DOK4 and DOK5. The phosphorylated form interacts with PLCG1 and GRB7. Binds to ARTN. Ref.6 Ref.7 Ref.8
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 and hematopoietic cells.
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.11 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.9
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 process	Cell adhesion
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Inferred from genetic interaction PubMed 15569713. Source: MGI Peyer's patch morphogenesis Inferred from mutant phenotype Ref.8. Source: UniProtKB cellular response to retinoic acid Inferred from electronic annotation. Source: Compara 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 membrane protein proteolysis Inferred from electronic annotation. Source: Compara 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 maturation Inferred from mutant phenotype PubMed 15233745. Source: MGI positive regulation of cell adhesion mediated by integrin Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of metanephric glomerulus development Inferred from mutant phenotype PubMed 17047028. Source: UniProtKB positive regulation of neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 17047028. Source: UniProtKB response to pain Inferred from mutant phenotype Ref.9. Source: UniProtKB 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_component	endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: Compara transmembrane receptor protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Epha5	Q60629	5	EBI-5548911,EBI-1267609

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P35546-1)

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Chain

29 – 1115

1087

Proto-oncogene tyrosine-protein kinase receptor Ret

PRO_0000024451

Chain

29 – 708

680

Extracellular cell-membrane anchored RET cadherin 120 kDa fragment By similarity

PRO_0000415294

Chain

709 – 1018

310

Soluble RET kinase fragment By similarity

PRO_0000415295

Regions

Topological domain

29 – 637

609

Extracellular Potential

Transmembrane

638 – 659

22

Helical; Potential

Topological domain

660 – 1115

456

Cytoplasmic Potential

Domain

168 – 273

106

Cadherin

Domain

725 – 1017

293

Protein kinase

Nucleotide binding

731 – 739

9

ATP By similarity

Region

806 – 808

3

Inhibitors binding By similarity

Sites

Active site

875

1

Proton acceptor By similarity

Binding site

759

1

ATP By similarity

Binding site

893

1

Inhibitors By similarity

Site

708 – 709

2

Cleavage; by caspase-3 By similarity

Site

1018 – 1019

2

Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue

697

1

Phosphoserine By similarity

Modified residue

807

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

810

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

901

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

906

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

982

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

1016

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

1063

1

Phosphotyrosine; by autocatalysis Ref.11

Modified residue

1091

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

1097

1

Phosphotyrosine; by autocatalysis By similarity

Glycosylation

89

1

N-linked (GlcNAc...) Potential

Glycosylation

98

1

N-linked (GlcNAc...) Potential

Glycosylation

151

1

N-linked (GlcNAc...) By similarity

Glycosylation

156

1

N-linked (GlcNAc...) Potential

Glycosylation

199

1

N-linked (GlcNAc...) Potential

Glycosylation

345

1

N-linked (GlcNAc...) Potential

Glycosylation

360

1

N-linked (GlcNAc...) Potential

Glycosylation

378

1

N-linked (GlcNAc...) Potential

Glycosylation

396

1

N-linked (GlcNAc...) Potential

Glycosylation

450

1

N-linked (GlcNAc...) Potential

Glycosylation

470

1

N-linked (GlcNAc...) Potential

Glycosylation

556

1

N-linked (GlcNAc...) Potential

Disulfide bond

137 ↔ 142

By similarity

Natural variations

Alternative sequence

1065 – 1115

51

MSDPN…DTFDS → RISHAFTRF in isoform 2.

VSP_011304

Experimental info

Mutagenesis

1063

1

Y → F: Abolishes interaction with DOK proteins. Ref.7

Sequence conflict

174

1

F → S in CAA48013. Ref.1

Secondary structure

1

.

.

.

.

.

1115

Helix Strand Turn

Details...

Beta strand

1057 – 1059

3

Turn

1061 – 1064

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: A5CF1EF45A640413	FASTA	1,115	123,874
	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
	Isoform 2 (Ret9) [UniParc]. Checksum: DB582E8D490C4A62	FASTA	1,073	119,469
	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 ASTPSDSLLY DDGLSEEETP LVDCNNAPLP RSLPSTWIEN KLYGRISHAF TRF

References

	« Hide 'large scale' referencesShow '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). Strain: A.
[3]	Wang Y.-Z., Yoong L.-F., Too H.-P. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: BALB/c.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Spinal ganglion.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6. Tissue: Brain.
[6]	"Direct association between the Ret receptor tyrosine kinase and the Src homology 2-containing adapter protein Grb7." Pandey A., Liu X., Dixon J.E., Di Fiore P.P., Dixit V.M. J. Biol. Chem. 271:10607-10610(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB7 AND PLCG1.
[7]	"Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation." Grimm J., Sachs M., Britsch S., Di Cesare S., Schwarz-Romond T., Alitalo K., Birchmeier W. J. Cell Biol. 154:345-354(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DOK2; DOK4 AND DOK5, PHOSPHORYLATION, MUTAGENESIS OF TYR-1063.
[8]	"Tyrosine kinase receptor RET is a key regulator of Peyer's patch organogenesis." Veiga-Fernandes H., Coles M.C., Foster K.E., Patel A., Williams A., Natarajan D., Barlow A., Pachnis V., Kioussis D. Nature 446:547-551(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PEYER'S PATCH ORGANOGENESIS, INTERACTION WITH ARTN.
[9]	"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.
[10]	"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.
[11]	"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.

IPI

IPI00463765.
IPI00463766.

PIR

S29926. I48735.

RefSeq

NP_001074249.1. NM_001080780.1.
NP_033076.2. NM_009050.2.

UniGene

Mm.57199.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UEF	X-ray	2.50	C/D	1055-1067	[»]

ProteinModelPortal

P35546.

SMR

P35546. Positions 29-273, 714-1055.

ModBase

Search...

Protein-protein interaction databases

IntAct

P35546. 7 interactions.

PTM databases

PhosphoSite

P35546.

Proteomic databases

PRIDE

P35546.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000032201; ENSMUSP00000032201; ENSMUSG00000030110.
ENSMUST00000088790; ENSMUSP00000086169; ENSMUSG00000030110.

GeneID

19713.

KEGG

mmu:19713.

UCSC

uc009dlm.1. mouse.
uc009dln.1. mouse.

Organism-specific databases

CTD

5979.

MGI

MGI:97902. Ret.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00670000097694.

HOGENOM

HOG000010301.

HOVERGEN

HBG002609.

InParanoid

P35546.

KO

K05126.

OMA

TVHDYRL.

OrthoDB

EOG4P2Q1H.

Enzyme and pathway databases

BRENDA

2.7.10.1. 3474.

Gene expression databases

Bgee

P35546.

CleanEx

MM_RET.

Genevestigator

P35546.

GermOnline

ENSMUSG00000030110. Mus musculus.

Family and domain databases

Gene3D

2.60.40.60. 1 hit.

InterPro

IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]

Pfam

PF00028. Cadherin. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF000631. TyrPK_receptor_Ret. 1 hit.

PRINTS

PR00109. TYRKINASE.

SMART

SM00112. CA. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF49313. Cadherin. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS50268. CADHERIN_2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P35546.

NextBio

297098.

SOURCE

Search...

Entry information

Entry name

RET_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program