TGFR2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TGFR2_RAT
• UniProt AC: P38438
• Protein Name: TGF-beta receptor type-2
• Gene Name: Tgfbr2
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 567
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Membrane raft .
• Protein Description: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways (By similarity)..
• Protein Sequence: MGRGLLRGLWPLHIVLWTRIASTIPPHVPKSVNSDLMAGDNSGAVKLPQLCKFCDVTLSTCDNQKSCMSNCSVTSICEKPQEVCVAVWRKNDKNITLETVCHDPKFTYHGFTLEDATSPTCVMKEKKRAGETFFMCSCNTEECNDYIIFNEEYTTSSPDLLLVIIQVTGVSLLPPLGIAIAVIAIFYCYRVHRQQKLSPSWESSKPRKLMDFSDNCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYSSWKTEKDIFSDINLKHENILQFLTAEERKTEMGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLESRMNLENMESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVESMKDNVLRDRGRPEIPSFWLNHQGIQIVCETLTECWDHDPEARLTAQCVAERFSELEHPDRLSGRSCSQEKIPEDGSLNTTK

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
70	N-linked_Glycosylation	NQKSCMSNCSVTSIC CCCHHHCCCEEEECC	8.66	-
94	N-linked_Glycosylation	VWRKNDKNITLETVC EEEECCCCEEEEEEE	35.03	-
200	Phosphorylation	RQQKLSPSWESSKPR HHCCCCCCCCCCCCC	39.85	30181290
203	Phosphorylation	KLSPSWESSKPRKLM CCCCCCCCCCCCCCC	37.09	30181290
204	Phosphorylation	LSPSWESSKPRKLMD CCCCCCCCCCCCCCC	34.85	30181290
213	Phosphorylation	PRKLMDFSDNCAIIL CCCCCCCCCCEEEEE	24.53	30181290
277	Sumoylation	QFETVAVKIFPYEEY HHCEEEEEEECHHHH	28.97	-
352	Phosphorylation	EDLRKLGSSLARGIA HHHHHHHHHHHHHHH	32.39	25532521
407	Phosphorylation	LSLRLDPTLSVDDLA CCEECCCCCCHHHHH	31.19	25575281
409	Phosphorylation	LRLDPTLSVDDLANS EECCCCCCHHHHHHC	26.44	25575281
486	Phosphorylation	REHPCVESMKDNVLR CCCCCHHHHHHHCHH	15.67	25575281
548	Phosphorylation	LEHPDRLSGRSCSQE CCCCCCCCCCCCCCC	32.81	25532521
551	Phosphorylation	PDRLSGRSCSQEKIP CCCCCCCCCCCCCCC	22.96	22668510
553	Phosphorylation	RLSGRSCSQEKIPED CCCCCCCCCCCCCCC	42.49	25532521
562	Phosphorylation	EKIPEDGSLNTTK-- CCCCCCCCCCCCC--	30.67	25575281
565	Phosphorylation	PEDGSLNTTK----- CCCCCCCCCC-----	41.05	25575281
566	Phosphorylation	EDGSLNTTK------ CCCCCCCCC------	33.41	25575281

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

Oops, there are no upstream regulatory protein records of TGFR2_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TGFR2_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 TGFR2_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of TGFR2_RAT !!

Drug and Disease Associations

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