SDC4_HUMAN - dbPTM
SDC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDC4_HUMAN
UniProt AC P31431
Protein Name Syndecan-4
Gene Name SDC4
Organism Homo sapiens (Human).
Sequence Length 198
Subcellular Localization Isoform 1: Membrane
Single-pass type I membrane protein . Secreted . Shedding of the ectodomain produces a soluble form.
Isoform 2: Secreted.
Protein Description Cell surface proteoglycan that bears heparan sulfate. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP. [PubMed: 22660413]
Protein Sequence MAPARLFALLLFFVGGVAESIRETEVIDPQDLLEGRYFSGALPDDEDVVGPGQESDDFELSGSGDLDDLEDSMIGPEVVHPLVPLDNHIPERAGSGSQVPTEPKKLEENEVIPKRISPVEESEDVSNKVSMSSTVQGSNIFERTEVLAALIVGGIVGILFAVFLILLLMYRMKKKDEGSYDLGKKPIYKKAPTNEFYA
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
24O-linked_GlycosylationVAESIRETEVIDPQD
HHHHHHHCCCCCHHH
26.21OGP
39O-linked_GlycosylationLLEGRYFSGALPDDE
HHCCCCCCCCCCCCC
17.77-
61O-linked_GlycosylationESDDFELSGSGDLDD
CCCCCCCCCCCCHHH
24.58-
63O-linked_GlycosylationDDFELSGSGDLDDLE
CCCCCCCCCCHHHHH
26.26-
97O-linked_GlycosylationPERAGSGSQVPTEPK
CCCCCCCCCCCCCCC
29.6955824389
97PhosphorylationPERAGSGSQVPTEPK
CCCCCCCCCCCCCCC
29.6928348404
101O-linked_GlycosylationGSGSQVPTEPKKLEE
CCCCCCCCCCCCCCC
67.0955824393
101PhosphorylationGSGSQVPTEPKKLEE
CCCCCCCCCCCCCCC
67.0924719451
104UbiquitinationSQVPTEPKKLEENEV
CCCCCCCCCCCCCCC
64.85-
117O-linked_GlycosylationEVIPKRISPVEESED
CCCCCCCCCCCCCCC
27.2555832651
126O-linked_GlycosylationVEESEDVSNKVSMSS
CCCCCCCCCCCCCCC
43.1655832655
134PhosphorylationNKVSMSSTVQGSNIF
CCCCCCCCCCCCCHH
15.00-
174UbiquitinationLLMYRMKKKDEGSYD
HHHHHHHHCCCCCCC
56.99-
179PhosphorylationMKKKDEGSYDLGKKP
HHHCCCCCCCCCCCC
17.2727794612
180PhosphorylationKKKDEGSYDLGKKPI
HHCCCCCCCCCCCCC
26.5027259358
190UbiquitinationGKKPIYKKAPTNEFY
CCCCCCCCCCCCCCC
42.5021906983
193PhosphorylationPIYKKAPTNEFYA--
CCCCCCCCCCCCC--
52.8426356563
197PhosphorylationKAPTNEFYA------
CCCCCCCCC------
12.7727273156

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
180YPhosphorylationKinaseSRCP12931
PSP
197YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SDC4_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 SDC4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GIPC1_HUMANGIPC1physical
10911369
DVL1_HUMANDVL1physical
20639201
TGFB3_HUMANTGFB3physical
21988832
TANK_HUMANTANKphysical
21988832
SGTA_HUMANSGTAphysical
25416956
HRSL4_HUMANRARRES3physical
27279133

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 SDC4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197, AND MASSSPECTROMETRY.

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