Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Proto-oncogene tyrosine-protein kinase receptor Ret  

UniProtKB / Swiss-Prot ID :  RET_HUMAN

Gene Name (Synonyms) : 
RET, CDHF12, CDHR16, PTC, RET51  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. 

Protein 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. Act 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. 

Transmembrane Topology (topPTM) : RET_HUMAN 

Protein Sequence MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQ...
Predicted Secondary Structure CCCCCCCCHHHHHHHHHHHHHHHHHHHCEEECCCCCEEEEEEECCCCCCEEEEEEECCCCCCCCCHHHHH...
Protein Variant
LocationDescription
20P -> L (in HSCR1; sporadic form). VAR_009459
32S -> L (in HSCR1; familial form;dbSNP:rs76764689).
40L -> P (in HSCR1). VAR_009492
64P -> L (in HSCR1; familial form;dbSNP:rs77596424).
67R -> H (in CCHS; dbSNP:rs192489011). VAR_018153
77R -> C (in HSCR1). VAR_009460
93G -> S (in HSCR1; unknown pathologicalsignificance).
114R -> C (in HSCR1). VAR_067101
114R -> H (in CCHS and HSCR1). VAR_018154
142C -> S (in HSCR1; sporadic form). VAR_006298
145V -> G (in HSCR1; also in a colorectalcancer sample; somatic mutation).
155P -> L (in HSCR1). VAR_067102
157C -> Y (in HSCR1; unknown pathologicalsignificance).
163R -> Q (in a colorectal adenocarcinomasample; somatic mutation;
174F -> S (in HSCR1; sporadic form). VAR_009462
175R -> P (in HSCR1). VAR_067103
180R -> P (in HSCR1; sporadic form). VAR_009463
197C -> Y (in HSCR1; sporadic form). VAR_009464
198P -> T (in RADYS; preventsphosphorylation in response to GDNF;
231R -> H (in HSCR1; familial form;dbSNP:rs79661516).
251E -> K (in HSCR1; familial form). VAR_006300
278T -> A (in HSCR1). VAR_067104
278T -> N (found in two patients withHirschsprung disease; dbSNP:rs35118262).
278T -> P (in HSCR1). VAR_067105
287R -> Q (in HSCR1; sporadic form). VAR_006301
292V -> M (found in patients withHirschsprung disease; unknown
300D -> N (in HSCR1). VAR_067106
313R -> Q (in HSCR1; dbSNP:rs77702891). VAR_009465
316S -> I (in HSCR1). VAR_067107
330R -> Q (in HSCR1; dbSNP:rs80236571). VAR_006302
339S -> L (in HSCR1). VAR_067108
353D -> Y (in HSCR1). VAR_067109
359N -> K (in HSCR1; unknown pathologicalsignificance).
360R -> Q (in HSCR1). VAR_067110
360R -> W (in HSCR1). VAR_009467
376V -> A (in RADYS; constitutivelyphosphorylated; expressed only the
393F -> L (in HSCR1; familial form;dbSNP:rs78098482).
394N -> H (in RADYS; preventsphosphorylation in response to GDNF).
394N -> K (in HSCR1). VAR_009468
397V -> M (in HSCR1; dbSNP:rs183729115). VAR_067111
399P -> L (in HSCR1; sporadic form). VAR_006304
412V -> M (in HSCR1). VAR_067112
423G -> R (in HSCR1). VAR_067113
432A -> E (in CCHS). VAR_018155
475R -> Q (in HSCR1; sporadic form;dbSNP:rs138624658).
480E -> K (in HSCR1). VAR_067114
489D -> N (in dbSNP:rs9282834). VAR_018156
531C -> CEEC (in MTC; familial form). VAR_009469
549Missing (in HSCR1). VAR_067115
593G -> E (in a colorectal cancer sample;somatic mutation).
595E -> Q (in HSCR1). VAR_067116
600R -> Q. VAR_008966
609C -> G (in MEN2A). VAR_009470
609C -> R (in MEN2A; dbSNP:rs77558292). VAR_009471
609C -> W (in HSCR1; familial form). VAR_006307
609C -> Y (in MTC, MEN2A and HSCR1; familialand sporadic forms; dbSNP:rs77939446).
611C -> G (in MTC; familial form). VAR_009472
611C -> R (in MEN2A). VAR_009473
611C -> S (in MEN2A). VAR_009474
611C -> W (in MEN2A and MTC; familial form;dbSNP:rs80069458).
611C -> Y (in MEN2A). VAR_006309
618C -> F (in MEN2A and MTC; familial form). VAR_006312
618C -> G (in MEN2A). VAR_006310
618C -> R (in MEN2A, MTC and HSCR1;dbSNP:rs76262710).
618C -> S (in MEN2A, HSCR1 and MTC; familialand sporadic forms; dbSNP:rs79781594).
618C -> Y (in MEN2A and MTC; familial form). VAR_006314
620C -> F (in MEN2A and MTC; familial form;dbSNP:rs77503355).
620C -> G (in MEN2A and MTC; familial andsporadic forms).
620C -> R (in MEN2A, MTC and HSCR1; familialand sporadic forms).
620C -> S (in MEN2A and MTC; familial form). VAR_006317
620C -> W (in MEN2A and HSCR1). VAR_009475
620C -> Y (in MEN2A). VAR_006319
626Q -> K (in HSCR1; sporadic form). VAR_009476
630C -> F (in MEN2A and MTC; familial form). VAR_006320
630C -> S (in MTC; sporadic form). VAR_009477
630C -> Y (in MTC; familial and sporadicforms).
631D -> G (in thyroid carcinoma; somaticmutation; dbSNP:rs121913308).
632ELC -> DVR (in MEN2A). VAR_006322
634CR -> WG (in MEN2A). VAR_006329
634C -> CHELC (in MEN2A). VAR_009479
634C -> F (in MEN2A and pheochromocytoma). VAR_006324
634C -> G (in MEN2A and pheochromocytoma). VAR_006323
634C -> R (in MEN2A, pheochromocytoma andMTC; familial form; also found as somatic
634C -> S (in MEN2A, pheochromocytoma andMTC; familial form).
634C -> W (in MEN2A, pheochromocytoma andMTC; familial form).
634C -> Y (in MEN2A, pheochromocytoma andMTC; familial form).
636T -> TCRT (in MEN2A). VAR_006330
639A -> G (in MTC; sporadic form). VAR_012743
640A -> G (in MEN2A; dbSNP:rs78935588). VAR_009480
641A -> G (in MTC; sporadic form). VAR_012744
679P -> L (in HSCR1). VAR_067117
690S -> P (in HSCR1; sporadic form). VAR_006331
691G -> S (in dbSNP:rs1799939). VAR_006332
694R -> Q (in HSCR1; dbSNP:rs141185224). VAR_067118
749R -> T (in dbSNP:rs34288963). VAR_041765
762E -> Q (in HSCR1; sporadic form). VAR_009481
765S -> P (in HSCR1; dbSNP:rs75075748). VAR_009493
767S -> R (in HSCR1; sporadic form). VAR_006334
768E -> D (in MTC; familial and sporadicforms; dbSNP:rs78014899).
778V -> I (in RADYS; constitutivelyphosphorylated; dbSNP:rs75686697).
783N -> S (in HSCR1). VAR_067119
790L -> F (in MEN2A and MTC; familial form;dbSNP:rs75030001).
791Y -> F (in HSCR1, pheochromocytoma, MTCand MEN2A; familial form;
804V -> L (in MTC; familial form;dbSNP:rs79658334).
804V -> M (in MTC; familial form;dbSNP:rs79658334).
813R -> Q (in HSCR1; sporadic form). VAR_009484
826Y -> S (in dbSNP:rs34617196). VAR_041766
830G -> R (in HSCR1). VAR_067120
844R -> L (in MTC; familial form;dbSNP:rs55947360).
873R -> Q (in HSCR1; sporadic form). VAR_006338
883A -> F (in MEN2B; somatic mutation insporadic medullary thyroid carcinoma;
891S -> A (in MTC; familial form;dbSNP:rs75234356).
893F -> L (in HSCR1; sporadic form). VAR_006339
894G -> S (in RADYS; constitutivelyphosphorylated; expressed only the
897R -> Q (in HSCR1; sporadic form;dbSNP:rs76087194).
907K -> E (in HSCR1; sporadic form). VAR_006341
907K -> T (in HSCR1). VAR_067121
918M -> T (in RADYS, MEN2B and MTC; sporadicform; somatic mutation;
921E -> K (in HSCR1; sporadic form). VAR_006343
922S -> F (in MTC; sporadic form). VAR_012745
922S -> Y (rare polymorphism). VAR_009487
946T -> M (in MEN2B and MTC; familial form). VAR_006345
961F -> L (in HSCR1). VAR_067122
972R -> G (in HSCR1; familial form;dbSNP:rs76534745).
973P -> L (in HSCR1; familial form). VAR_006347
980M -> T (in HSCR1; sporadic form). VAR_006348
982R -> C (in dbSNP:rs17158558). VAR_006349
1039P -> L (in CCHS; with colonicaganglionosis; dbSNP:rs79853121).
1039P -> Q. VAR_009488
1049P -> L (in RADYS; preventsphosphorylation in response to GDNF).
1052L -> V (in HSCR1). VAR_067123
1059Missing (in HSCR1). VAR_009489
1061L -> P (in HSCR1). VAR_009490
1062Y -> C (in HSCR1). VAR_067124
1064M -> T (in HSCR1; familial form). VAR_009491
1067P -> S (in RADYS; preventsphosphorylation in response to GDNF).
1112F -> Y (in a bladder transitional cellcarcinoma sample; somatic mutation).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
151N-linked (GlcNAc...).FSFFNTSFP
HEEHHCCCC
32.57UniProtKB
Link-
675PhosphothreonineSAEMTFRRP
CCCCCCCCC
12.90Phosphositeplus
Link-
687PhosphotyrosineFPVSYSSSG
CCCCCCCCC
16.89Phosphositeplus
Link-
687Phosphotyrosine (RET)FPVSYSSSG
CCCCCCCCC
16.89HPRD
Link-
687Phosphotyrosine (RET;RET)FPVSYSSSG
CCCCCCCCC
16.89PhosphoELM
Link-
696PhosphoserineARRPSLDSM
CCCCCCCCC
42.89PhosphoELM
Link-
696PhosphoserineARRPSLDSM
CCCCCCCCC
42.89Phosphositeplus
Link-
696Phosphoserine.ARRPSLDSM
CCCCCCCCC
42.89UniProtKB
Link-
752PhosphotyrosineGRAGYTTVA
CCCCCEEEE
9.76Phosphositeplus
Link
753PhosphothreonineRAGYTTVAV
CCCCEEEEE
17.55HPRD
Link
754PhosphothreonineAGYTTVAVK
CCCEEEEEE
9.66HPRD
Link
791PhosphotyrosineVIKLYGACS
EEEEEEEEE
9.55PhosphoELM
Link
791PhosphotyrosineVIKLYGACS
EEEEEEEEE
9.55Phosphositeplus
Link
806PhosphotyrosineLIVEYAKYG
EEEEECCCC
9.48Phosphositeplus
Link
806Phosphotyrosine (RET)LIVEYAKYG
EEEEECCCC
9.48HPRD
Link
806Phosphotyrosine (RET)LIVEYAKYG
EEEEECCCC
9.48PhosphoELM
Link
806Phosphotyrosine; by autocatalysis.LIVEYAKYG
EEEEECCCC
9.48UniProtKB
Link
809PhosphotyrosineEYAKYGSLR
EECCCCCHH
12.08Phosphositeplus
Link
809Phosphotyrosine (RET)EYAKYGSLR
EECCCCCHH
12.08HPRD
Link
809Phosphotyrosine (RET)EYAKYGSLR
EECCCCCHH
12.08PhosphoELM
Link
809Phosphotyrosine; by autocatalysis.EYAKYGSLR
EECCCCCHH
12.08UniProtKB
Link
826PhosphotyrosineVGPGYLGSG
CCCCCCCCC
15.83Phosphositeplus
Link
826Phosphotyrosine (RET)VGPGYLGSG
CCCCCCCCC
15.83HPRD
Link
826Phosphotyrosine (RET)VGPGYLGSG
CCCCCCCCC
15.83PhosphoELM
Link
864PhosphotyrosineQGMQYLAEM
HHHHHHHHC
10.05Phosphositeplus
Link
891PhosphoserineKMKISDFGL
EEEEEECCE
22.74PhosphoELM
Link
891PhosphoserineKMKISDFGL
EEEEEECCE
22.74Phosphositeplus
Link
900PhosphotyrosineSRDVYEEDS
EEECCCCCC
20.21Phosphositeplus
Link
900Phosphotyrosine (RET)SRDVYEEDS
EEECCCCCC
20.21HPRD
Link
900Phosphotyrosine (RET)SRDVYEEDS
EEECCCCCC
20.21PhosphoELM
Link
900Phosphotyrosine; by autocatalysis.SRDVYEEDS
EEECCCCCC
20.21UniProtKB
Link
905PhosphotyrosineEEDSYVKRS
CCCCEEEEE
23.47Phosphositeplus
Link
905Phosphotyrosine (RET)EEDSYVKRS
CCCCEEEEE
23.47HPRD
Link
905Phosphotyrosine (RET)EEDSYVKRS
CCCCEEEEE
23.47HPRD
Link
905Phosphotyrosine (RET)EEDSYVKRS
CCCCEEEEE
23.47PhosphoELM
Link
905Phosphotyrosine; by autocatalysis.EEDSYVKRS
CCCCEEEEE
23.47UniProtKB
Link
928PhosphotyrosineFDHIYTTQS
HCCCCCCHH
10.58Phosphositeplus
Link
952PhosphotyrosineGGNPYPGIP
CCCCCCCCC
20.35Phosphositeplus
Link
981PhosphotyrosineSEEMYRLML
CHHHHHHHH
12.13Phosphositeplus
Link
981Phosphotyrosine (RET)SEEMYRLML
CHHHHHHHH
12.13HPRD
Link
981Phosphotyrosine (RET;RET)SEEMYRLML
CHHHHHHHH
12.13PhosphoELM
Link
981Phosphotyrosine; by autocatalysis.SEEMYRLML
CHHHHHHHH
12.13UniProtKB
Link
1015PhosphotyrosineKRRDYLDLA
CCCCCCCCC
10.58Phosphositeplus
Link-
1015Phosphotyrosine (RET)KRRDYLDLA
CCCCCCCCC
10.58HPRD
Link-
1015Phosphotyrosine (RET)KRRDYLDLA
CCCCCCCCC
10.58PhosphoELM
Link-
1015Phosphotyrosine; by autocatalysis.KRRDYLDLA
CCCCCCCCC
10.58UniProtKB
Link-
1029PhosphotyrosineDSLIYDDGL
CCCCCCCCC
17.18Phosphositeplus
Link-
1029Phosphotyrosine (RET)DSLIYDDGL
CCCCCCCCC
17.18HPRD
Link-
1029Phosphotyrosine (RET;RET)DSLIYDDGL
CCCCCCCCC
17.18PhosphoELM
Link-
1062PhosphotyrosineENKLYGMSD
HHHHHCCCC
16.64Phosphositeplus
Link-
1062Phosphotyrosine (RET)ENKLYGMSD
HHHHHCCCC
16.64HPRD
Link-
1062Phosphotyrosine (RET)ENKLYGMSD
HHHHHCCCC
16.64HPRD
Link-
1062Phosphotyrosine (RET;RET)ENKLYGMSD
HHHHHCCCC
16.64PhosphoELM
Link-
1062Phosphotyrosine; by autocatalysis.ENKLYGMSD
HHHHHCCCC
16.64UniProtKB
Link-
1090PhosphotyrosineGFPRYPNDS
CCCCCCCCC
13.46Phosphositeplus
Link-
1090Phosphotyrosine (RET)GFPRYPNDS
CCCCCCCCC
13.46HPRD
Link-
1090Phosphotyrosine (RET)GFPRYPNDS
CCCCCCCCC
13.46PhosphoELM
Link-
1090Phosphotyrosine; by autocatalysis.GFPRYPNDS
CCCCCCCCC
13.46UniProtKB
Link-
1096PhosphotyrosineNDSVYANWM
CCCCCCCCE
9.73Phosphositeplus
Link-
1096Phosphotyrosine (RET)NDSVYANWM
CCCCCCCCE
9.73HPRD
Link-
1096Phosphotyrosine (RET;RET)NDSVYANWM
CCCCCCCCE
9.73PhosphoELM
Link-
1096Phosphotyrosine; by autocatalysis.NDSVYANWM
CCCCCCCCE
9.73UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CBL_HUMANphysical interactionMINT-50071MINT12727845
CBL_HUMANphysical interactionMINT-60968MINT15677445
CBL_HUMANphysical interactionMINT-60969MINT15677445
CBL_HUMANphysical interactionMINT-60976MINT15677445
CBL_HUMANphysical interactionMINT-60970MINT15677445
SHC1_HUMANphysical interactionMINT-60981MINT15677445
STAT3_HUMANin vitro
in vivo
HPRD:01266HPRD11536047
12637586
15485908
GRB2_HUMANin vivoHPRD:01266HPRD9393871
RET_HUMANin vitro
in vivo
HPRD:01266HPRD8621380
11121408
15588985
14711813
10445857
DOK6_HUMANin vitroHPRD:01266HPRD15286081
CBLB_HUMANin vivoHPRD:01266HPRD16525057
AKAP5_HUMANin vivoHPRD:01266HPRD11886862
CRK_HUMANin vitroHPRD:01266HPRD10208419
KAP2_HUMANin vitro
in vivo
HPRD:01266HPRD11886862
GDNF_HUMANin vitroHPRD:01266HPRD8674117
FAK1_HUMANin vitroHPRD:01266HPRD16153436
MK01_HUMANin vitroHPRD:01266HPRD16153436
MK08_HUMANin vitroHPRD:01266HPRD16153436
MK14_HUMANin vitroHPRD:01266HPRD16153436
MK03_HUMANin vitroHPRD:01266HPRD16153436
GOGA5_HUMANENSP00000344798STRING
PHX2B_HUMANENSP00000344798STRING
PSPN_HUMANENSP00000344798STRING
VHL_HUMANENSP00000344798STRING
CBL_HUMANENSP00000344798STRING
STAT3_HUMANENSP00000344798STRING
DOK2_HUMANENSP00000344798STRING
FRS2_HUMANENSP00000344798STRING
CRK_HUMANENSP00000344798STRING
CRK_HUMANENSP00000344798STRING
NRTN_HUMANENSP00000344798STRING
GFRA2_HUMANENSP00000344798STRING
GRB7_HUMANENSP00000344798STRING
GFRA4_HUMANENSP00000344798STRING
GDNF_HUMANENSP00000344798STRING
PTC1_HUMANENSP00000344798STRING
EDN3_HUMANENSP00000344798STRING
DOK4_HUMANENSP00000344798STRING
GFRA1_HUMANENSP00000344798STRING
NF1_HUMANENSP00000344798STRING
TRI33_HUMANENSP00000344798STRING
SOX10_HUMANENSP00000344798STRING
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Disease Reference
Kegg disease
H00032 Thyroid cancer
H00822 Renal agenesis and Renal adysplasia
H00910 Hirschsprung disease (HD)
H00916 Congenital central hypoventilation syndrome (CCHS)
OMIM disease
114500Colorectal cancer (CRC)
142623Hirschsprung disease 1 (HSCR1)
155240Medullary thyroid carcinoma (MTC)
162300Multiple neoplasia 2B (MEN2B)
171300Pheochromocytoma (PCC)
171400Multiple neoplasia 2A (MEN2A)
188550Thyroid papillary carcinoma (TPC)
Note=Mutations in RET have been detected in patients with renal agenesis suggesting a possible involvement of this gene in disease pathogenesis.
209880
Drug Reference
Kegg drug
D06402 Sunitinib malate (JAN/USAN); Sutent (TN)
D06678 Motesanib; AMG 706
D08552 Sunitinib (INN)
D08947 Motesanib phosphate (JAN); Motesanib diphosphate (USAN)
D10062 Cabozantinib (USAN)
D10095 Cabozantinib s-malate (USAN); Cometriq (TN)
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mammal-restricted elements predispose human RET to folding impairmentby HSCR mutations.";
Kjaer S., Hanrahan S., Totty N., McDonald N.Q.;
Nat. Struct. Mol. Biol. 17:726-731(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-270, GLYCOSYLATION ATASN-151, AND DISULFIDE BOND.
Phosphorylation
ReferencePubMed
"Tyrosines 1015 and 1062 are in vivo autophosphorylation sites in retand ret-derived oncoproteins.";
Salvatore D., Barone M.V., Salvatore G., Melillo R.M., Chiappetta G.,Mineo A., Fenzi G., Vecchio G., Fusco A., Santoro M.;
J. Clin. Endocrinol. Metab. 85:3898-3907(2000).
Cited for: PHOSPHORYLATION AT TYR-1015 AND TYR-1062.
"Identification of RET autophosphorylation sites by massspectrometry.";
Kawamoto Y., Takeda K., Okuno Y., Yamakawa Y., Ito Y., Taguchi R.,Kato M., Suzuki H., Takahashi M., Nakashima I.;
J. Biol. Chem. 279:14213-14224(2004).
Cited for: PHOSPHORYLATION AT TYR-806; TYR-809; TYR-900; TYR-905; TYR-981;TYR-1015; TYR-1062; TYR-1090 AND TYR-1096.
"The receptor-type protein tyrosine phosphatase J antagonizes thebiochemical and biological effects of RET-derived oncoproteins.";
Iervolino A., Iuliano R., Trapasso F., Viglietto G., Melillo R.M.,Carlomagno F., Santoro M., Fusco A.;
Cancer Res. 66:6280-6287(2006).
Cited for: AUTOPHOSPHORYLATION AT TYR-905; TYR-1015 AND TYR-1062, ANDDEPHOSPHORYLATION BY PTPRJ AT TYR-905; TYR-1015 AND TYR-1062.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696, AND MASSSPECTROMETRY.
"Structure and chemical inhibition of the RET tyrosine kinasedomain.";
Knowles P.P., Murray-Rust J., Kjaer S., Scott R.P., Hanrahan S.,Santoro M., Ibanez C.F., McDonald N.Q.;
J. Biol. Chem. 281:33577-33587(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 705-1013 ALONE AND IN COMPLEXWITH INHIBITORS, MASS SPECTROMETRY, AND PHOSPHORYLATION AT TYR-900 ANDTYR-905.
"Synthesis, structure-activity relationship and crystallographicstudies of 3-substituted indolin-2-one RET inhibitors.";
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.;
Bioorg. Med. Chem. 18:1482-1496(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 705-1013 IN COMPLEX WITHINHIBITORS, ENZYME REGULATION, AND PHOSPHORYLATION AT TYR-905.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures