| UniProt ID | TGBR3_MOUSE | |
|---|---|---|
| UniProt AC | O88393 | |
| Protein Name | Transforming growth factor beta receptor type 3 | |
| Gene Name | Tgfbr3 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 850 | |
| Subcellular Localization |
Cell membrane Single-pass type I membrane protein. Secreted. Secreted, extracellular space, extracellular matrix. Exists both as a membrane-bound form and as soluble form in serum and in the extracellular matrix.. |
|
| Protein Description | Binds to TGF-beta. Could be involved in capturing and retaining TGF-beta for presentation to the signaling receptors (By similarity).. | |
| Protein Sequence | MAVTSHHMVPVFVLMSACLATAGPEPSTRCELSPISASHPVQALMESFTVLSGCASRGTTGLPREVHILNLRSTDQGLGQPQREVTLHLNPIASVHTHHKPVVFLLNSPQPLVWHVKTERLAAGVPRLFLVSEGSVVQFSSGNFSLTAETEERSFPQENEHLLHWAQKEYGAVTSFTELKIARNIYIKVGEDQVFPPTCNIGKNFLSLNYLAEYLQPKAAEGCVLASQPHEKEVHIIELISPNSNPYSTFQVDIIIDIRPAREDPEVVKNLVLILKCKKSVNWVIKSFDVKGNLKVIAPDSIGFGKESERSMTVTKLVRNDYPSTQENLMKWALDNGYSPVTSYTIAPVANRFHLRLENNEEMRDEEVHTIPPELRILLGPDHLPALDSPPFQGEIPNGGFPFPFPDIPRRGWKEGEDRIPRPKEPIIPRVQLLPDHREPEEVQGGVNIALSVKCDNEKMVVAVDKDSFQTNGYSGMELTLLDPSCKAKMNGTHFVLESPLNGCGTRHRRSAPDGVVYYNSIVVQAPSPGDSSGWPDGYEDLESGDNGFPGDTDEGETAPLSRAGVVVFNCSLRQLRSPSGFQDQLDGNATFNMELYNTDLFLVPSPGVFSVAENEHVYVEVSVTKADQDLGFAIQTCFISPYSNPDRMSDYTIIENICPKDDSVKFYSSKRVHFPIPHAEVDKKRFSFVFKSVFNTSLLFLHCELTLCSRNKGSQKLPKCVTPDDACTSLDATMIWTMMQNKKTFTKPLAVVLQVDYKENVPNMKESSPVPPPPQIFHGLDTLTVMGIAFAAFVIGALLTGALWYIYSHTGETARRQQVPTSPPASENSSAAHSIGSTQSTPCSSSSTA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 143 | N-linked_Glycosylation | VVQFSSGNFSLTAET EEEECCCCEEEEEEE | 25.86 | - | |
| 207 | Phosphorylation | NIGKNFLSLNYLAEY CCCCCCCCHHHHHHH | 15.49 | 25293948 | |
| 210 | Phosphorylation | KNFLSLNYLAEYLQP CCCCCHHHHHHHHCH | 16.75 | 25293948 | |
| 214 | Phosphorylation | SLNYLAEYLQPKAAE CHHHHHHHHCHHHHC | 12.67 | 25293948 | |
| 491 | N-linked_Glycosylation | PSCKAKMNGTHFVLE HHHCCEECCCEEEEE | 52.05 | - | |
| 533 | O-linked_Glycosylation | APSPGDSSGWPDGYE CCCCCCCCCCCCCCC | 50.01 | 9659379 | |
| 544 | O-linked_Glycosylation | DGYEDLESGDNGFPG CCCCCCCCCCCCCCC | 59.76 | 9659379 | |
| 570 | N-linked_Glycosylation | RAGVVVFNCSLRQLR CCEEEEEECCCHHCC | 11.67 | - | |
| 589 | N-linked_Glycosylation | FQDQLDGNATFNMEL CCCCCCCCCEEEEEE | 35.16 | - | |
| 696 | N-linked_Glycosylation | FVFKSVFNTSLLFLH EEHHHHCCHHHHHHH | 26.97 | - | |
| 720 | Ubiquitination | KGSQKLPKCVTPDDA CCCCCCCCCCCCCHH | 52.34 | - | |
| 830 | Phosphorylation | SPPASENSSAAHSIG CCCCCCCCCCCCCCC | 19.80 | 25338131 | |
| 849 | Phosphorylation | TPCSSSSTA------ CCCCCCCCC------ | 38.03 | 25338131 |
| 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 TGBR3_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TGBR3_MOUSE !! | ||||||
* 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 TGBR3_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of TGBR3_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| O-linked Glycosylation | |
| Reference | PubMed |
| "Murine betaglycan primary structure, expression and glycosaminoglycanattachment sites."; Ponce-Castaneda M.V., Esparza-Lopez J., Vilchis-Landeros M.M.,Mendoza V., Lopez-Casillas F.; Biochim. Biophys. Acta 1384:189-196(1998). Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION AT SER-533 AND SER-544, ANDMUTAGENESIS OF SER-533 AND SER-544. | |