UniProt ID | DPEP2_HUMAN | |
---|---|---|
UniProt AC | Q9H4A9 | |
Protein Name | Dipeptidase 2 | |
Gene Name | DPEP2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 486 | |
Subcellular Localization |
Membrane Lipid-anchor, GPI-anchor. |
|
Protein Description | Probable metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4).. | |
Protein Sequence | MQPSGLEGPGTFGRWPLLSLLLLLLLLQPVTCAYTTPGPPRALTTLGAPRAHTMPGTYAPSTTLSSPSTQGLQEQARALMRDFPLVDGHNDLPLVLRQVYQKGLQDVNLRNFSYGQTSLDRLRDGLVGAQFWSAYVPCQTQDRDALRLTLEQIDLIRRMCASYSELELVTSAKALNDTQKLACLIGVEGGHSLDNSLSILRTFYMLGVRYLTLTHTCNTPWAESSAKGVHSFYNNISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSLSMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKFPQGLEDVSTYPVLIEELLSRGWSEEELQGVLRGNLLRVFRQVEKVQEENKWQSPLEDKFPDEQLSSSCHSDLSRLRQRQSLTSGQELTEIPIHWTAKLPAKWSVSESSPHMAPVLAVVATFPVLILWL | |
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 |
---|---|---|---|---|---|
11 | Phosphorylation | SGLEGPGTFGRWPLL CCCCCCCCCCHHHHH | 26.50 | 22798277 | |
36 | Phosphorylation | PVTCAYTTPGPPRAL HHCCCCCCCCCCCHH | 17.36 | 24719451 | |
53 | Phosphorylation | LGAPRAHTMPGTYAP CCCCCCCCCCCCCCC | 24.87 | - | |
69 | O-linked_Glycosylation | TTLSSPSTQGLQEQA CCCCCCCCHHHHHHH | 30.00 | OGP | |
100 | Phosphorylation | PLVLRQVYQKGLQDV HHHHHHHHHHCCCCC | 9.00 | 27067055 | |
111 | N-linked_Glycosylation | LQDVNLRNFSYGQTS CCCCCCCCCCCCCCH | 33.12 | 16335952 | |
162 | Phosphorylation | LIRRMCASYSELELV HHHHHHCCCHHHHHH | 25.02 | 30631047 | |
170 | Phosphorylation | YSELELVTSAKALND CHHHHHHHCHHHCCC | 35.27 | 30631047 | |
171 | Phosphorylation | SELELVTSAKALNDT HHHHHHHCHHHCCCH | 21.94 | 30631047 | |
176 | N-linked_Glycosylation | VTSAKALNDTQKLAC HHCHHHCCCHHHEEH | 55.96 | UniProtKB CARBOHYD | |
235 | N-linked_Glycosylation | GVHSFYNNISGLTDF CHHHHHHCCCCCCHH | 20.58 | 16335952 | |
377 | Phosphorylation | VLIEELLSRGWSEEE HHHHHHHHCCCCHHH | 41.18 | 24719451 | |
463 | GPI-anchor | LPAKWSVSESSPHMA CCCCCCCCCCCCCHH | 26.67 | - |
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 DPEP2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPEP2_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 DPEP2_HUMAN !! |
Kegg Disease | ||||||
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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. |
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N-linked Glycosylation | |
Reference | PubMed |
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111 AND ASN-235, AND MASSSPECTROMETRY. |