RET_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RET_RAT
• UniProt AC: G3V9H8
• Protein Name: Proto-oncogene tyrosine-protein kinase receptor Ret
• Gene Name: Ret
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 1115
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Endosome membrane ; Single-pass type I membrane protein .
• Protein Description: 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 (By similarity). Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways (By similarity)..
• Protein Sequence: MAKARSGAAGLGLKLFLLLPLLGEAPLGLYFSRDAYWERLYVDQPAGTPLLYVHALRDAPGEVPSFRLGQYLYGVYRTRLHENDWIHIDSGTGLLYLNQSLDHSSWEQLSIRNGGFPLLTVFLQVFLGSTAQREGECHWPGCARVYFSFINDTFPNCSSFKARDLCTPETGVSFRIRENRPPGTFYQFRMLPVQFLCPNISVKYKLLEGDGLPFRCDPDCLEVSTRWALDRELQEKYVLEAECAVAGPGANKEKVAVSFPVTVYDEDDSPPTFSGGVGTASAVVEFKRKEGTVVATLQVFDADVVPASGELVRRYTSTLLSGDSWAQQTFRVEHTPNETLVQSNNNSVRATMHNYKLVLNRSLSISESRVLQLVVLVNDSDFQGPGSGVLFLHFNVSVLPVTLNLPMAYSFPVNRRARRYAQIGKVCVENCQEFSGVSIQYKLQPSSTNCSALGVVTSTEDTSGTLYVNDTEALRRPECTELQYTVVATDRQTRRQTQASLVVTVEGTYIAEEVGCPKSCAVNKRRPECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTRTCPDGHCDALESRDINICPQDCLRGPIVGGHERGERQGIKAGYGICNCFPDEKKCFCEPEDSQGPLCDELCRTVITAAVLFSFIISVLLSTFCIHRYHKHAHKPPIASAEMTFCRPAQGFPISYSSSGTRRPSLDSMENQVSVDSFKIPEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASQSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRDSRKIGPAYVSSGGSRNSSSLDHPDERVLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKKSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKSRDYLDLAASTPSDSLLYDDGLSEEETPLVDCNSAPLPRSLPSTWIENKLYGMSDPNWPGESPVPLTRADGTSTGFPRYANDSVYANWMVSPSAAKLMDTFDS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
98	N-linked_Glycosylation	GTGLLYLNQSLDHSS CCEEEEECCCCCCCC		-
151	N-linked_Glycosylation	RVYFSFINDTFPNCS EEEEEECCCCCCCCH		-
156	N-linked_Glycosylation	FINDTFPNCSSFKAR ECCCCCCCCHHCCHH		-
199	N-linked_Glycosylation	PVQFLCPNISVKYKL CHHHCCCCEEEEEEE		-
378	N-linked_Glycosylation	LQLVVLVNDSDFQGP EEEEEEECCCCCCCC		-
395	N-linked_Glycosylation	GVLFLHFNVSVLPVT EEEEEEEEEEEEEEE		-
449	N-linked_Glycosylation	KLQPSSTNCSALGVV EECCCCCCCCEEEEE		-
469	N-linked_Glycosylation	TSGTLYVNDTEALRR CCCEEEECCCHHHHC		-
555	N-linked_Glycosylation	DGKGITRNFSTCSPS CCCCCCCCEECCCCC		-
687	Phosphorylation	PAQGFPISYSSSGTR CCCCCCCCCCCCCCC		25575281
688	Phosphorylation	AQGFPISYSSSGTRR CCCCCCCCCCCCCCC		25575281
689	Phosphorylation	QGFPISYSSSGTRRP CCCCCCCCCCCCCCC		25575281
690	Phosphorylation	GFPISYSSSGTRRPS CCCCCCCCCCCCCCC		25575281
691	Phosphorylation	FPISYSSSGTRRPSL CCCCCCCCCCCCCCH		25575281
693	Phosphorylation	ISYSSSGTRRPSLDS CCCCCCCCCCCCHHH		25575281
697	Phosphorylation	SSGTRRPSLDSMENQ CCCCCCCCHHHHCCC		28551015
700	Phosphorylation	TRRPSLDSMENQVSV CCCCCHHHHCCCCCC		28551015
807	Phosphorylation	PLLLIVEYAKYGSLR CEEEEEEHHHHCCHH		-
810	Phosphorylation	LIVEYAKYGSLRGFL EEEEHHHHCCHHHHH		-
901	Phosphorylation	FGLSRDVYEEDSYVK CCCCCCCCCCCHHCC		-
906	Phosphorylation	DVYEEDSYVKKSKGR CCCCCCHHCCCCCCC		-
982	Phosphorylation	DNCSEEMYRLMLQCW CCCCHHHHHHHHHHH		-
1016	Phosphorylation	MMVKSRDYLDLAAST HHHHCHHHHHHHCCC		-
1063	Phosphorylation	TWIENKLYGMSDPNW CHHHCCCCCCCCCCC		-
1091	Phosphorylation	TSTGFPRYANDSVYA CCCCCCCCCCCCEEC		-
1097	Phosphorylation	RYANDSVYANWMVSP CCCCCCEECCEEECH		-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
906	Y	Phosphorylation	Kinase	RET	G3V9H8	PSP
1016	Y	Phosphorylation	Kinase	RET	G3V9H8	PSP
1063	Y	Phosphorylation	Kinase	RET	G3V9H8	PSP
1097	Y	Phosphorylation	Kinase	RET	G3V9H8	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RET_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RET_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC_RAT	Ubc	physical	16525057
AIP_RAT	Aip	physical	19366855

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.