TGFR2_HUMAN - dbPTM
TGFR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TGFR2_HUMAN
UniProt AC P37173
Protein Name TGF-beta receptor type-2
Gene Name TGFBR2
Organism Homo sapiens (Human).
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..
Protein Sequence MGRGLLRGLWPLHIVLWTRIASTIPPHVQKSVNNDMIVTDNNGAVKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPDLLLVIFQVTGISLLPPLGVAISVIIIFYCYRVNRQQKLSSTWETGKTRKLMEFSEHCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYASWKTEKDIFSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLESRMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVESMKDNVLRDRGRPEIPSFWLNHQGIQMVCETLTECWDHDPEARLTAQCVAERFSELEHLDRLSGRSCSEEKIPEDGSLNTTK
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
31O-linked_GlycosylationIPPHVQKSVNNDMIV
CCHHHHHHCCCCEEE		17.00OGP
31 (in isoform 2)Phosphorylation-17.00-
39O-linked_GlycosylationVNNDMIVTDNNGAVK
CCCCEEEECCCCCCC		23.2955833639
64 (in isoform 2)O-linked_Glycosylation-26.28OGP
70N-linked_GlycosylationNQKSCMSNCSITSIC
CCHHHHCCCEEEHHC		9.18UniProtKB CARBOHYD
94N-linked_GlycosylationVWRKNDENITLETVC
EEEECCCCEEEEEEE		35.09UniProtKB CARBOHYD
118PhosphorylationFILEDAASPKCIMKE
HHCCCCCCCCCEECC		26.9826091039
154N-linked_GlycosylationIIFSEEYNTSNPDLL
EEEECCCCCCCCCEE		40.07UniProtKB CARBOHYD
205UbiquitinationSSTWETGKTRKLMEF
HHHHCCCCHHHHHHH		53.21-
208UbiquitinationWETGKTRKLMEFSEH
HCCCCHHHHHHHHHH		58.37-
213PhosphorylationTRKLMEFSEHCAIIL
HHHHHHHHHHEEEEE		17.089155023
225PhosphorylationIILEDDRSDISSTCA
EEECCCCCHHHHHHC		46.418947046
228PhosphorylationEDDRSDISSTCANNI
CCCCCHHHHHHCCCC		25.288947046
229PhosphorylationDDRSDISSTCANNIN
CCCCHHHHHHCCCCC		28.048947046
259PhosphorylationKGRFAEVYKAKLKQN
CCCHHHHHHHHHHCC		9.209169454
260UbiquitinationGRFAEVYKAKLKQNT
CCHHHHHHHHHHCCC		44.19-
264UbiquitinationEVYKAKLKQNTSEQF
HHHHHHHHCCCCHHH		40.57-
268PhosphorylationAKLKQNTSEQFETVA
HHHHCCCCHHHCEEE		36.6323403867
284PhosphorylationKIFPYEEYASWKTEK
EEECHHHHCCCCCHH		8.269169454
286PhosphorylationFPYEEYASWKTEKDI
ECHHHHCCCCCHHHH		28.3624719451
291UbiquitinationYASWKTEKDIFSDIN
HCCCCCHHHHHHCCC		62.45-
295PhosphorylationKTEKDIFSDINLKHE
CCHHHHHHCCCCCHH		37.6028102081
300UbiquitinationIFSDINLKHENILQF
HHHCCCCCHHHHHHH		44.37-
336PhosphorylationAKGNLQEYLTRHVIS
CCCCHHHHHHHHCCC		10.629169454
352PhosphorylationEDLRKLGSSLARGIA
HHHHHHHHHHHHHHH		32.3923927012
353PhosphorylationDLRKLGSSLARGIAH
HHHHHHHHHHHHHHH		25.0123927012
381UbiquitinationPIVHRDLKSSNILVK
CEEECCCCCCCEEEE		57.01-
383PhosphorylationVHRDLKSSNILVKND
EECCCCCCCEEEECC		26.7122210691
392PhosphorylationILVKNDLTCCLCDFG
EEEECCEEEEECCCC		12.2022210691
409PhosphorylationLRLDPTLSVDDLANS
EECCCCCCHHHHHHC		26.4426657352
416PhosphorylationSVDDLANSGQVGTAR
CHHHHHHCCCCCCHH		25.629169454
424PhosphorylationGQVGTARYMAPEVLE
CCCCCHHHCCHHHHH		8.6528152594
441PhosphorylationMNLENVESFKQTDVY
CCCCCHHHHHHCCHH		33.209169454
445PhosphorylationNVESFKQTDVYSMAL
CHHHHHHCCHHHHHH		28.20-
448PhosphorylationSFKQTDVYSMALVLW
HHHHCCHHHHHHHHH		8.7826074081
449PhosphorylationFKQTDVYSMALVLWE
HHHCCHHHHHHHHHH		9.4526074081
470PhosphorylationAVGEVKDYEPPFGSK
CCEECCCCCCCCCCC		25.3130576142
476PhosphorylationDYEPPFGSKVREHPC
CCCCCCCCCCCCCCC		28.4930576142
477UbiquitinationYEPPFGSKVREHPCV
CCCCCCCCCCCCCCH		45.77-
486PhosphorylationREHPCVESMKDNVLR
CCCCCHHHHHHHCHH		15.6723403867
488UbiquitinationHPCVESMKDNVLRDR
CCCHHHHHHHCHHCC		56.27-
539PhosphorylationQCVAERFSELEHLDR
HHHHHHHHHHHHHHH		47.7123403867
548PhosphorylationLEHLDRLSGRSCSEE
HHHHHHHCCCCCCCC		32.8130266825
551PhosphorylationLDRLSGRSCSEEKIP
HHHHCCCCCCCCCCC		26.068947046
553PhosphorylationRLSGRSCSEEKIPED
HHCCCCCCCCCCCCC		50.4623401153
556NeddylationGRSCSEEKIPEDGSL
CCCCCCCCCCCCCCC		60.55-
556UbiquitinationGRSCSEEKIPEDGSL
CCCCCCCCCCCCCCC		60.55-
562PhosphorylationEKIPEDGSLNTTK--
CCCCCCCCCCCCC--		30.6723403867
565PhosphorylationPEDGSLNTTK-----
CCCCCCCCCC-----		41.0523403867
566PhosphorylationEDGSLNTTK------
CCCCCCCCC------		33.4125159151
567NeddylationDGSLNTTK-------
CCCCCCCC-------		57.19-
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
213SPhosphorylationKinaseTGFR2P37173
PhosphoELM
259YPhosphorylationKinaseTGFR2P37173
PhosphoELM
284YPhosphorylationKinaseSRCP12931
PSP
284YPhosphorylationKinaseSRCP05480
PSP
336YPhosphorylationKinaseTGFR2P37173
PhosphoELM
409SPhosphorylationKinaseTGFR2P37173
PhosphoELM
416SPhosphorylationKinaseTGFR2P37173
PhosphoELM
424YPhosphorylationKinaseTGFR2P37173
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:15817471
-KUbiquitinationE3 ubiquitin ligaseWWP1Q9H0M0
PMID:15817471
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:15817471
-KUbiquitinationE3 ubiquitin ligaseSMURF2Q9HAU4
PMID:22848678
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGFR2_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFB3_HUMANTGFB3physical
11850637
EGLN_HUMANENGphysical
12015308
AP2B1_HUMANAP2B1physical
12429842
EGLN_HUMANENGphysical
9872992
TGFB3_HUMANTGFB3physical
9872992
TGBR3_HUMANTGFBR3physical
8106553
TGFB1_HUMANTGFB1physical
11157754
TGFB2_HUMANTGFB2physical
11157754
TGFB3_HUMANTGFB3physical
11157754
CCNB2_HUMANCCNB2physical
9926943
CCNB1_HUMANCCNB1physical
9926943
P85A_HUMANPIK3R1physical
9435577
P85B_HUMANPIK3R2physical
9435577
STRAP_HUMANSTRAPphysical
10757800
CLUS_HUMANCLUphysical
8555189
ACVR1_HUMANACVR1physical
7890683
HS90A_HUMANHSP90AA1physical
18591668
T22D1_HUMANTSC22D1physical
21791611
HS90A_HUMANHSP90AA1physical
22848678
TRAF6_HUMANTRAF6physical
18922473
HS90A_RATHsp90aa1physical
22964853
UBC_RATUbcphysical
22964853
M3K7_HUMANMAP3K7physical
19556242
TGFR1_HUMANTGFBR1physical
19556242
A4_HUMANAPPphysical
21832049
IQGA1_HUMANIQGAP1physical
23454766
PEG10_HUMANPEG10physical
15611116
TGFB1_HUMANTGFB1physical
8242742
NRP1_HUMANNRP1physical
21186301
TRAF4_HUMANTRAF4physical
23973329
CBL_HUMANCBLphysical
23290524
PK3CB_HUMANPIK3CBphysical
26186194
CDC6_HUMANCDC6physical
26186194
PKN3_HUMANPKN3physical
26186194
PKHH3_HUMANPLEKHH3physical
26186194
AVR2B_HUMANACVR2Bphysical
26186194
AVR2A_HUMANACVR2Aphysical
26186194
PKN2_HUMANPKN2physical
26186194
TYK2_HUMANTYK2physical
26186194
JAK1_HUMANJAK1physical
26186194
P85B_HUMANPIK3R2physical
26186194
P85A_HUMANPIK3R1physical
26186194
P55G_HUMANPIK3R3physical
26186194
LSR_HUMANLSRphysical
26186194
RAB6B_HUMANRAB6Bphysical
26186194
RAB6A_HUMANRAB6Aphysical
26186194
WDR44_HUMANWDR44physical
26186194
MARH7_HUMANMARCH7physical
26186194
CD320_HUMANCD320physical
26186194
TR19L_HUMANRELTphysical
26186194
BMR1A_HUMANBMPR1Aphysical
26186194
ERBB2_HUMANERBB2physical
26186194
DEN6A_HUMANDENND6Aphysical
26186194
FGFR1_HUMANFGFR1physical
26186194
DIP2A_HUMANDIP2Aphysical
26186194
PTPRS_HUMANPTPRSphysical
26186194
PTPRF_HUMANPTPRFphysical
26186194
EHD4_HUMANEHD4physical
26186194
ACV1B_HUMANACVR1Bphysical
26186194
NFIP1_HUMANNDFIP1physical
26186194
MFAP3_HUMANMFAP3physical
26186194
MYADM_HUMANMYADMphysical
26186194
MTMR5_HUMANSBF1physical
26186194
FMN2_HUMANFMN2physical
26186194
F1712_HUMANFAM171A2physical
26186194
LRP10_HUMANLRP10physical
26186194
CNEP1_HUMANCTDNEP1physical
26186194
SPSB1_HUMANSPSB1physical
26032413
EIF3I_HUMANEIF3Iphysical
9813058
TGFR1_HUMANTGFBR1physical
11483955
DAXX_HUMANDAXXphysical
11483955
DAXX_MOUSEDaxxphysical
11483955
TGFA1_HUMANTGFBRAP1physical
11278302
TRAF6_HUMANTRAF6physical
26807171
SMUF2_HUMANSMURF2physical
25149540
SMAD7_HUMANSMAD7physical
25149540
SH3K1_HUMANSH3KBP1physical
26169354
FMN2_HUMANFMN2physical
28514442
AVR2B_HUMANACVR2Bphysical
28514442
BMR1A_HUMANBMPR1Aphysical
28514442
MYADM_HUMANMYADMphysical
28514442
DEN6A_HUMANDENND6Aphysical
28514442
TR19L_HUMANRELTphysical
28514442
RAB6B_HUMANRAB6Bphysical
28514442
JAK1_HUMANJAK1physical
28514442
PKHH3_HUMANPLEKHH3physical
28514442
P85A_HUMANPIK3R1physical
28514442
CDC6_HUMANCDC6physical
28514442
MARH7_HUMANMARCH7physical
28514442
PTPRS_HUMANPTPRSphysical
28514442
LRP10_HUMANLRP10physical
28514442
ERBB2_HUMANERBB2physical
28514442
P55G_HUMANPIK3R3physical
28514442
PKN2_HUMANPKN2physical
28514442
NFIP1_HUMANNDFIP1physical
28514442
MTMR5_HUMANSBF1physical
28514442
FGFR1_HUMANFGFR1physical
28514442
P85B_HUMANPIK3R2physical
28514442
PKN3_HUMANPKN3physical
28514442
PK3CB_HUMANPIK3CBphysical
28514442
MFAP3_HUMANMFAP3physical
28514442
Drug and Disease Associations
Kegg Disease
H00020 Colorectal cancer
H00800 Loeys-Dietz syndrome (LDS)
H00801 Familial thoracic aortic aneurysm and dissection (TAAD); Aortic aneurysm familial thoracic type (AAT
OMIM Disease
614331Hereditary non-polyposis colorectal cancer 6 (HNPCC6)
133239Esophageal cancer (ESCR)
610168Loeys-Dietz syndrome 2 (LDS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TGFR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-409; SER-548; SER-551AND SER-553, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND MASSSPECTROMETRY.

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