TGFR2_MOUSE - dbPTM
TGFR2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TGFR2_MOUSE
UniProt AC Q62312
Protein Name TGF-beta receptor type-2
Gene Name Tgfbr2
Organism Mus musculus (Mouse).
Sequence Length 592
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 MGRGLLRGLWPLHIVLWTRIASTIPPHVPKSDVEMEAQKDASIHLSCNRTIHPLKHFNSDVMASDNGGAVKLPQLCKFCDVRLSTCDNQKSCMSNCSITAICEKPHEVCVAVWRKNDKNITLETVCHDPKLTYHGFTLEDAASPKCVMKEKKRAGETFFMCACNMEECNDYIIFSEEYTTSSPDLLLVIIQVTGVSLLPPLGIAIAVIIIFYCYRVHRQQKLSPSWESSKPRKLMDFSDNCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYSSWKTEKDIFSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLESRMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVESMKDSVLRDRGRPEIPSFWLNHQGIQIVCETLTECWDHDPEARLTAQCVAERFSELEHPERLSGRSCSQEKIPEDGSLNTTK
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 Orthologous
Protein Cluster
48N-linked_GlycosylationASIHLSCNRTIHPLK
CEEEEECCCEECCCC		40.53-
59PhosphorylationHPLKHFNSDVMASDN
CCCCCCCCCEECCCC		30.5528059163
64PhosphorylationFNSDVMASDNGGAVK
CCCCEECCCCCCCCC		17.3228059163
76S-nitrosylationAVKLPQLCKFCDVRL
CCCHHHHHHHCCEEE		2.4021278135
76S-nitrosocysteineAVKLPQLCKFCDVRL
CCCHHHHHHHCCEEE		2.40-
95N-linked_GlycosylationNQKSCMSNCSITAIC
CCCHHHCCCEEEEEE		9.18-
119N-linked_GlycosylationVWRKNDKNITLETVC
EEEECCCCEEEEEEE		35.03-
225PhosphorylationRQQKLSPSWESSKPR
HHCCCCCCCCCCCCC		39.8525338131
228PhosphorylationKLSPSWESSKPRKLM
CCCCCCCCCCCCCCC		37.0927149854
229PhosphorylationLSPSWESSKPRKLMD
CCCCCCCCCCCCCCC		34.8525338131
230UbiquitinationSPSWESSKPRKLMDF
CCCCCCCCCCCCCCC		59.11-
250PhosphorylationIILEDDRSDISSTCA
EEECCCHHHCHHHHC		46.418947046
253PhosphorylationEDDRSDISSTCANNI
CCCHHHCHHHHCCCC		25.288947046
254PhosphorylationDDRSDISSTCANNIN
CCHHHCHHHHCCCCC		28.048947046
309PhosphorylationKIFPYEEYSSWKTEK
EEECHHHHCCCCCHH		8.9622817900
377PhosphorylationEDLRKLGSSLARGIA
HHHHHHHHHHHHHHH		32.3921743459
378PhosphorylationDLRKLGSSLARGIAH
HHHHHHHHHHHHHHH		25.0121743459
434PhosphorylationLRLDPTLSVDDLANS
EECCCCCCHHHHHHC		26.4429233185
441PhosphorylationSVDDLANSGQVGTAR
CHHHHHHCCCCCCHH		25.6227566939
457PhosphorylationMAPEVLESRMNLENV
CCHHHHHHCCCCCCH		32.4429514104
501PhosphorylationDYEPPFGSKVREHPC
CCCCCCCCCCCCCCC		28.4925338131
511PhosphorylationREHPCVESMKDSVLR
CCCCCCHHHHHHHHH		15.6726060331
573PhosphorylationLEHPERLSGRSCSQE
CCCHHHHCCCCCCCC		38.0825266776
576PhosphorylationPERLSGRSCSQEKIP
HHHHCCCCCCCCCCC		22.968947046
578PhosphorylationRLSGRSCSQEKIPED
HHCCCCCCCCCCCCC		42.498947046
587PhosphorylationEKIPEDGSLNTTK--
CCCCCCCCCCCCC--		30.6725619855
590PhosphorylationPEDGSLNTTK-----
CCCCCCCCCC-----		41.0525619855
591PhosphorylationEDGSLNTTK------
CCCCCCCCC------		33.4125619855
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

Oops, there are no upstream regulatory protein records of TGFR2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGFR2_MOUSE !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TGFR2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFR1_MOUSETgfbr1physical
12070302
TGBR3_MOUSETgfbr3physical
12070302
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TGFR2_MOUSE

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Related Literatures of Post-Translational Modification

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