PGS2_HUMAN - dbPTM
PGS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGS2_HUMAN
UniProt AC P07585
Protein Name Decorin
Gene Name DCN
Organism Homo sapiens (Human).
Sequence Length 359
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description May affect the rate of fibrils formation..
Protein Sequence MKATIILLLLAQVSWAGPFQQRGLFDFMLEDEASGIGPEVPDDRDFEPSLGPVCPFRCQCHLRVVQCSDLGLDKVPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKVSPGAFTPLVKLERLYLSKNQLKELPEKMPKTLQELRAHENEITKVRKVTFNGLNQMIVIELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITSIPQGLPPSLTELHLDGNKISRVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLDNNKLTRVPGGLAEHKYIQVVYLHNNNISVVGSSDFCPPGHNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRSAIQLGNYK
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
4O-linked_Glycosylation----MKATIILLLLA
----CCHHHHHHHHH
11.752108171
34O-linked_GlycosylationFMLEDEASGIGPEVP
EEECCCCCCCCCCCC
28.973484330
67S-nitrosylationCHLRVVQCSDLGLDK
EEEEEEECHHHCCCC
2.0025040305
92UbiquitinationLLDLQNNKITEIKDG
EEECCCCCEEECCCC
59.56-
102AcetylationEIKDGDFKNLKNLHA
ECCCCCCCCCCCCEE
67.1430585717
126PhosphorylationKVSPGAFTPLVKLER
CCCCCCCCHHHHHHH
18.38-
138AcetylationLERLYLSKNQLKELP
HHHHHCCHHHHHHCH
46.2387831
147AcetylationQLKELPEKMPKTLQE
HHHHCHHHCCHHHHH
59.5787835
200AcetylationNGAFQGMKKLSYIRI
CCCCCCCCCCEEEEE
58.347669741
201AcetylationGAFQGMKKLSYIRIA
CCCCCCCCCEEEEEE
33.5030585723
211N-linked_GlycosylationYIRIADTNITSIPQG
EEEEECCCCCCCCCC
35.7719159218
214PhosphorylationIADTNITSIPQGLPP
EECCCCCCCCCCCCC
28.6022210691
234PhosphorylationHLDGNKISRVDAASL
EECCCCCCCCHHHHH
28.0622210691
262N-linked_GlycosylationNSISAVDNGSLANTP
CCEEEECCCCCCCCC
35.0419159218
280UbiquitinationELHLDNNKLTRVPGG
EEECCCCCCCCCCCC
58.45-
303N-linked_GlycosylationVVYLHNNNISVVGSS
EEEEECCCEEEEECC
32.98UniProtKB CARBOHYD
328PhosphorylationKASYSGVSLFSNPVQ
CCEECCEECCCCCEE
27.50-
331PhosphorylationYSGVSLFSNPVQYWE
ECCEECCCCCEEEEE
45.5826657352

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 PGS2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGS2_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 PGS2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EGFR_HUMANEGFRphysical
12105206
FLNA_HUMANFLNAphysical
12106908
CO6A1_HUMANCOL6A1physical
1544908
TGFB1_HUMANTGFB1physical
9675033
FETUA_HUMANAHSGphysical
12071714
EGFR_HUMANEGFRphysical
9988678
TGFB1_HUMANTGFB1physical
7798269
CHSS1_HUMANCHSY1physical
26186194
KLH17_HUMANKLHL17physical
26186194
KAISO_HUMANZBTB33physical
26186194
LONP2_HUMANLONP2physical
26186194
TPA_HUMANPLATphysical
26186194
CHSS1_HUMANCHSY1physical
28514442
KLH17_HUMANKLHL17physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610048Corneal dystrophy, congenital stromal (CSCD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGS2_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-211 AND ASN-262, AND MASSSPECTROMETRY.
O-linked Glycosylation
ReferencePubMed
"Primary structure of an extracellular matrix proteoglycan coreprotein deduced from cloned cDNA.";
Krusius T., Ruoslahti E.;
Proc. Natl. Acad. Sci. U.S.A. 83:7683-7687(1986).
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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