SDC3_HUMAN - dbPTM
SDC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDC3_HUMAN
UniProt AC O75056
Protein Name Syndecan-3
Gene Name SDC3
Organism Homo sapiens (Human).
Sequence Length 442
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Cell surface proteoglycan that may bear heparan sulfate (By similarity). May have a role in the organization of cell shape by affecting the actin cytoskeleton, possibly by transferring signals from the cell surface in a sugar-dependent mechanism..
Protein Sequence MKPGPPHRAGAAHGAGAGAGAAAGPGARGLLLPPLLLLLLAGRAAGAQRWRSENFERPVDLEGSGDDDSFPDDELDDLYSGSGSGYFEQESGIETAMRFSPDVALAVSTTPAVLPTTNIQPVGTPFEELPSERPTLEPATSPLVVTEVPEEPSQRATTVSTTMATTAATSTGDPTVATVPATVATATPSTPAAPPFTATTAVIRTTGVRRLLPLPLTTVATARATTPEAPSPPTTAAVLDTEAPTPRLVSTATSRPRALPRPATTQEPDIPERSTLPLGTTAPGPTEVAQTPTPETFLTTIRDEPEVPVSGGPSGDFELPEEETTQPDTANEVVAVGGAAAKASSPPGTLPKGARPGPGLLDNAIDSGSSAAQLPQKSILERKEVLVAVIVGGVVGALFAAFLVTLLIYRMKKKDEGSYTLEEPKQASVTYQKPDKQEEFYA
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
80O-linked_GlycosylationDELDDLYSGSGSGYF
HHHHHHHCCCCCCCE		33.51-
82O-linked_GlycosylationLDDLYSGSGSGYFEQ
HHHHHCCCCCCCEEE		24.68-
84O-linked_GlycosylationDLYSGSGSGYFEQES
HHHCCCCCCCEEECC		31.83-
91O-linked_GlycosylationSGYFEQESGIETAMR
CCCEEECCCCCHHHH		44.77-
131PhosphorylationTPFEELPSERPTLEP
CCHHHCCCCCCCCCC		59.8824719451
146PhosphorylationATSPLVVTEVPEEPS
CCCCEEEEECCCCHH		24.64-
225O-linked_GlycosylationTVATARATTPEAPSP
EEEEEECCCCCCCCC		37.01OGP
234PhosphorylationPEAPSPPTTAAVLDT
CCCCCCCCEEEEECC		32.24-
245PhosphorylationVLDTEAPTPRLVSTA
EECCCCCCCCEEECC		28.26-
250O-linked_GlycosylationAPTPRLVSTATSRPR
CCCCCEEECCCCCCC		19.5455835901
250PhosphorylationAPTPRLVSTATSRPR
CCCCCEEECCCCCCC		19.54-
251O-linked_GlycosylationPTPRLVSTATSRPRA
CCCCEEECCCCCCCC		26.8655835905
251PhosphorylationPTPRLVSTATSRPRA
CCCCEEECCCCCCCC		26.86-
253O-linked_GlycosylationPRLVSTATSRPRALP
CCEEECCCCCCCCCC		25.9255835911
254O-linked_GlycosylationRLVSTATSRPRALPR
CEEECCCCCCCCCCC		37.51OGP
264O-linked_GlycosylationRALPRPATTQEPDIP
CCCCCCCCCCCCCCC		31.5255832437
265O-linked_GlycosylationALPRPATTQEPDIPE
CCCCCCCCCCCCCCC		32.8055832443
314O-linked_GlycosylationVPVSGGPSGDFELPE
CCCCCCCCCCCCCCC		55.03-
324O-linked_GlycosylationFELPEEETTQPDTAN
CCCCCCCCCCCCCCC		33.73OGP
344PhosphorylationGGAAAKASSPPGTLP
CHHHHHCCCCCCCCC		42.54-
344O-linked_GlycosylationGGAAAKASSPPGTLP
CHHHHHCCCCCCCCC		42.5455833131
345O-linked_GlycosylationGAAAKASSPPGTLPK
HHHHHCCCCCCCCCC		39.72OGP
349O-linked_GlycosylationKASSPPGTLPKGARP
HCCCCCCCCCCCCCC		45.7446300053
349PhosphorylationKASSPPGTLPKGARP
HCCCCCCCCCCCCCC		45.74-
367O-linked_GlycosylationLLDNAIDSGSSAAQL
HHHCCHHCCCCHHHC		34.17-
369PhosphorylationDNAIDSGSSAAQLPQ
HCCHHCCCCHHHCCC		22.2828258704
370PhosphorylationNAIDSGSSAAQLPQK
CCHHCCCCHHHCCCC		31.0228258704
378PhosphorylationAAQLPQKSILERKEV
HHHCCCCHHHHCHHH		27.4528258704
409PhosphorylationFLVTLLIYRMKKKDE
HHHHHHHHHHHHCCC		12.489388509
414UbiquitinationLIYRMKKKDEGSYTL
HHHHHHHCCCCCCCC		56.33-
418PhosphorylationMKKKDEGSYTLEEPK
HHHCCCCCCCCCCCC		16.9422210691
419PhosphorylationKKKDEGSYTLEEPKQ
HHCCCCCCCCCCCCC		26.639388509
420PhosphorylationKKDEGSYTLEEPKQA
HCCCCCCCCCCCCCC		29.4123312004
428PhosphorylationLEEPKQASVTYQKPD
CCCCCCCEEEEECCC		16.7026657352
430PhosphorylationEPKQASVTYQKPDKQ
CCCCCEEEEECCCCC		20.1023312004
431PhosphorylationPKQASVTYQKPDKQE
CCCCEEEEECCCCCC		16.639388509
433UbiquitinationQASVTYQKPDKQEEF
CCEEEEECCCCCCCC		44.7832142685
436UbiquitinationVTYQKPDKQEEFYA-
EEEECCCCCCCCCC-		69.0432142685
441PhosphorylationPDKQEEFYA------
CCCCCCCCC------		18.0619534553
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 SDC3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SDC3_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 SDC3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBA1A_HUMANTUBA1Aphysical
9553134
SRC8_HUMANCTTNphysical
9553134
FYN_HUMANFYNphysical
9553134
CSK_HUMANCSKphysical
9553134
TBB5_HUMANTUBBphysical
9553134
TBB2A_HUMANTUBB2Aphysical
9553134
FGF2_HUMANFGF2physical
8344959
KR103_HUMANKRTAP10-3physical
25416956
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 SDC3_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-441, AND MASSSPECTROMETRY.

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