TGBR3_MOUSE - dbPTM
TGBR3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
143N-linked_GlycosylationVVQFSSGNFSLTAET
EEEECCCCEEEEEEE
25.86-
207PhosphorylationNIGKNFLSLNYLAEY
CCCCCCCCHHHHHHH
15.4925293948
210PhosphorylationKNFLSLNYLAEYLQP
CCCCCHHHHHHHHCH
16.7525293948
214PhosphorylationSLNYLAEYLQPKAAE
CHHHHHHHHCHHHHC
12.6725293948
491N-linked_GlycosylationPSCKAKMNGTHFVLE
HHHCCEECCCEEEEE
52.05-
533O-linked_GlycosylationAPSPGDSSGWPDGYE
CCCCCCCCCCCCCCC
50.019659379
544O-linked_GlycosylationDGYEDLESGDNGFPG
CCCCCCCCCCCCCCC
59.769659379
570N-linked_GlycosylationRAGVVVFNCSLRQLR
CCEEEEEECCCHHCC
11.67-
589N-linked_GlycosylationFQDQLDGNATFNMEL
CCCCCCCCCEEEEEE
35.16-
696N-linked_GlycosylationFVFKSVFNTSLLFLH
EEHHHHCCHHHHHHH
26.97-
720UbiquitinationKGSQKLPKCVTPDDA
CCCCCCCCCCCCCHH
52.34-
830PhosphorylationSPPASENSSAAHSIG
CCCCCCCCCCCCCCC
19.8025338131
849PhosphorylationTPCSSSSTA------
CCCCCCCCC------
38.0325338131

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 TGBR3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGBR3_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 TGBR3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TGBR3_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TGBR3_MOUSE

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"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.

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