Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Transforming growth factor beta receptor type 3  

UniProtKB / Swiss-Prot ID :  TGBR3_RAT

Gene Name (Synonyms) : 
Tgfbr3  

Species :  Rattus norvegicus (Rat). 

Subcellular Localization :  Cell membrane; Single-pass type I membrane protein. Secreted. Secreted, extracellular space, extracellular matrix. Note=Exists both as a membrane-bound form and as soluble form in serum and in the extracellular matrix. 

Protein Function :  Binds to TGF-beta. Could be involved in capturing and retaining TGF-beta for presentation to the signaling receptors. 

Transmembrane Topology (topPTM) : TGBR3_RAT 

Protein Sequence MAVTSHHMIPVMVVLMSACLATAGPEPSTRCELSPINASHPVQALMESFTVLSGCASRGTTGLPREVHVL...
Predicted Secondary Structure CCCCCHHHHHHHHHHHHHHCCCCCCCCCCEEEEEECCCCCCCEEEEEEEHHHHHHHHHCCCCCEEEEEEE...
Protein Variant -
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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
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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
535O-linked (Xyl...) (glycosaminoglycan) (ByPGDSSGWPD
CCCCCEECC
50.01UniProtKB
Link-
546O-linked (Xyl...) (glycosaminoglycan) (ByEDLESGDNG
CCEEEEECC
59.76UniProtKB
Link-
591N-linked (GlcNAc...).QLDGNATFN
CCCCEEEEE
35.16UniProtKB
Link
698N-linked (GlcNAc...).KSVFNTSLL
EECCCCCEE
26.97UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structure of betaglycan zona pellucida (ZP)-C domain providesinsights into ZP-mediated protein polymerization and TGF-betabinding.";
Lin S.J., Hu Y., Zhu J., Woodruff T.K., Jardetzky T.S.;
Proc. Natl. Acad. Sci. U.S.A. 108:5232-5236(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 591-763, GLYCOSYLATION ATASN-591 AND ASN-698, AND DISULFIDE BONDS.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures