TPBG_HUMAN - dbPTM
TPBG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPBG_HUMAN
UniProt AC Q13641
Protein Name Trophoblast glycoprotein
Gene Name TPBG
Organism Homo sapiens (Human).
Sequence Length 420
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description May function as an inhibitor of Wnt/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization..
Protein Sequence MPGGCSRGPAAGDGRLRLARLALVLLGWVSSSSPTSSASSFSSSAPFLASAVSAQPPLPDQCPALCECSEAARTVKCVNRNLTEVPTDLPAYVRNLFLTGNQLAVLPAGAFARRPPLAELAALNLSGSRLDEVRAGAFEHLPSLRQLDLSHNPLADLSPFAFSGSNASVSAPSPLVELILNHIVPPEDERQNRSFEGMVVAALLAGRALQGLRRLELASNHFLYLPRDVLAQLPSLRHLDLSNNSLVSLTYVSFRNLTHLESLHLEDNALKVLHNGTLAELQGLPHIRVFLDNNPWVCDCHMADMVTWLKETEVVQGKDRLTCAYPEKMRNRVLLELNSADLDCDPILPPSLQTSYVFLGIVLALIGAIFLLVLYLNRKGIKKWMHNIRDACRDHMEGYHYRYEINADPRLTNLSSNSDV
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
50O-linked_GlycosylationSSAPFLASAVSAQPP
CCHHHHHHHHCCCCC
31.20OGP
53O-linked_GlycosylationPFLASAVSAQPPLPD
HHHHHHHCCCCCCCC
22.39OGP
81N-linked_GlycosylationTVKCVNRNLTEVPTD
HHHHCCCCCCCCCCC
46.22UniProtKB CARBOHYD
99PhosphorylationYVRNLFLTGNQLAVL
HHHHHHCCCCEEEEE
27.1022817900
124N-linked_GlycosylationLAELAALNLSGSRLD
HHHHHHHCCCCCCHH
27.6819159218
143PhosphorylationGAFEHLPSLRQLDLS
CHHHHCCCHHHCCCC
42.4124719451
192N-linked_GlycosylationPPEDERQNRSFEGMV
CCCHHHCCCCHHHHH
48.02-
192N-linked_GlycosylationPPEDERQNRSFEGMV
CCCHHHCCCCHHHHH
48.0211903056
235PhosphorylationDVLAQLPSLRHLDLS
HHHHCCCCCCCEECC
46.7824719451
275N-linked_GlycosylationNALKVLHNGTLAELQ
CCCHHHHCCHHHHHC
40.77UniProtKB CARBOHYD
318UbiquitinationETEVVQGKDRLTCAY
HCCEECCCCCEEECC
23.6829967540
403PhosphorylationMEGYHYRYEINADPR
HCCCCEEEEECCCCC
17.6227642862
415PhosphorylationDPRLTNLSSNSDV--
CCCCCCCCCCCCC--
29.5523403867
416PhosphorylationPRLTNLSSNSDV---
CCCCCCCCCCCC---
43.4422617229
418PhosphorylationLTNLSSNSDV-----
CCCCCCCCCC-----
41.5228355574

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 TPBG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPBG_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 TPBG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GIPC1_HUMANGIPC1physical
11798178

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

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-124, AND MASSSPECTROMETRY.

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