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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
4 | O-linked_Glycosylation | ----MKATIILLLLA ----CCHHHHHHHHH | 11.75 | 2108171 | |
34 | O-linked_Glycosylation | FMLEDEASGIGPEVP EEECCCCCCCCCCCC | 28.97 | 3484330 | |
67 | S-nitrosylation | CHLRVVQCSDLGLDK EEEEEEECHHHCCCC | 2.00 | 25040305 | |
92 | Ubiquitination | LLDLQNNKITEIKDG EEECCCCCEEECCCC | 59.56 | - | |
102 | Acetylation | EIKDGDFKNLKNLHA ECCCCCCCCCCCCEE | 67.14 | 30585717 | |
126 | Phosphorylation | KVSPGAFTPLVKLER CCCCCCCCHHHHHHH | 18.38 | - | |
138 | Acetylation | LERLYLSKNQLKELP HHHHHCCHHHHHHCH | 46.23 | 87831 | |
147 | Acetylation | QLKELPEKMPKTLQE HHHHCHHHCCHHHHH | 59.57 | 87835 | |
200 | Acetylation | NGAFQGMKKLSYIRI CCCCCCCCCCEEEEE | 58.34 | 7669741 | |
201 | Acetylation | GAFQGMKKLSYIRIA CCCCCCCCCEEEEEE | 33.50 | 30585723 | |
211 | N-linked_Glycosylation | YIRIADTNITSIPQG EEEEECCCCCCCCCC | 35.77 | 19159218 | |
214 | Phosphorylation | IADTNITSIPQGLPP EECCCCCCCCCCCCC | 28.60 | 22210691 | |
234 | Phosphorylation | HLDGNKISRVDAASL EECCCCCCCCHHHHH | 28.06 | 22210691 | |
262 | N-linked_Glycosylation | NSISAVDNGSLANTP CCEEEECCCCCCCCC | 35.04 | 19159218 | |
280 | Ubiquitination | ELHLDNNKLTRVPGG EEECCCCCCCCCCCC | 58.45 | - | |
303 | N-linked_Glycosylation | VVYLHNNNISVVGSS EEEEECCCEEEEECC | 32.98 | UniProtKB CARBOHYD | |
328 | Phosphorylation | KASYSGVSLFSNPVQ CCEECCEECCCCCEE | 27.50 | - | |
331 | Phosphorylation | YSGVSLFSNPVQYWE ECCEECCCCCEEEEE | 45.58 | 26657352 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PGS2_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
EGFR_HUMAN | EGFR | physical | 12105206 | |
FLNA_HUMAN | FLNA | physical | 12106908 | |
CO6A1_HUMAN | COL6A1 | physical | 1544908 | |
TGFB1_HUMAN | TGFB1 | physical | 9675033 | |
FETUA_HUMAN | AHSG | physical | 12071714 | |
EGFR_HUMAN | EGFR | physical | 9988678 | |
TGFB1_HUMAN | TGFB1 | physical | 7798269 | |
CHSS1_HUMAN | CHSY1 | physical | 26186194 | |
KLH17_HUMAN | KLHL17 | physical | 26186194 | |
KAISO_HUMAN | ZBTB33 | physical | 26186194 | |
LONP2_HUMAN | LONP2 | physical | 26186194 | |
TPA_HUMAN | PLAT | physical | 26186194 | |
CHSS1_HUMAN | CHSY1 | physical | 28514442 | |
KLH17_HUMAN | KLHL17 | physical | 28514442 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
610048 | Corneal dystrophy, congenital stromal (CSCD) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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]. |