| UniProt ID | DPEP1_HUMAN | |
|---|---|---|
| UniProt AC | P16444 | |
| Protein Name | Dipeptidase 1 | |
| Gene Name | DPEP1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 411 | |
| Subcellular Localization |
Apical cell membrane Lipid-anchor, GPI-anchor. Cell projection, microvillus membrane Lipid-anchor, GPI-anchor. Brush border membrane. |
|
| Protein Description | Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity.. | |
| Protein Sequence | MWSGWWLWPLVAVCTADFFRDEAERIMRDSPVIDGHNDLPWQLLDMFNNRLQDERANLTTLAGTHTNIPKLRAGFVGGQFWSVYTPCDTQNKDAVRRTLEQMDVVHRMCRMYPETFLYVTSSAGIRQAFREGKVASLIGVEGGHSIDSSLGVLRALYQLGMRYLTLTHSCNTPWADNWLVDTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVSVATMKATLQLSRAPVIFSHSSAYSVCASRRNVPDDVLRLVKQTDSLVMVNFYNNYISCTNKANLSQVADHLDHIKEVAGARAVGFGGDFDGVPRVPEGLEDVSKYPDLIAELLRRNWTEAEVKGALADNLLRVFEAVEQASNLTQAPEEEPIPLDQLGGSCRTHYGYSSGASSLHRHWGLLLASLAPLVLCLSLL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MWSGWWLWPL -----CCCCCCHHHH | 24.20 | 24043423 | |
| 15 | Phosphorylation | WPLVAVCTADFFRDE HHHHHHHHHHHHHHH | 23.74 | 24043423 | |
| 57 | N-linked_Glycosylation | RLQDERANLTTLAGT HHHHHHHCCHHHCCC | 44.11 | 12144777 | |
| 112 | Phosphorylation | VHRMCRMYPETFLYV HHHHHHHCCCCEEEE | 4.41 | - | |
| 118 | Phosphorylation | MYPETFLYVTSSAGI HCCCCEEEEECCHHH | 9.48 | - | |
| 239 | Phosphorylation | IFSHSSAYSVCASRR EEECCCHHHHHHHCC | 12.00 | - | |
| 240 | Phosphorylation | FSHSSAYSVCASRRN EECCCHHHHHHHCCC | 15.50 | - | |
| 271 | Phosphorylation | MVNFYNNYISCTNKA EEEECCCCEECCCCC | 7.20 | 29759185 | |
| 279 | N-linked_Glycosylation | ISCTNKANLSQVADH EECCCCCCHHHHHHH | 41.66 | 19159218 | |
| 291 | Ubiquitination | ADHLDHIKEVAGARA HHHHHHHHHHHCCCC | 42.59 | - | |
| 320 | Ubiquitination | EGLEDVSKYPDLIAE CCCCCHHHCHHHHHH | 61.73 | - | |
| 332 | N-linked_Glycosylation | IAELLRRNWTEAEVK HHHHHHCCCCHHHHH | 43.52 | 12144777 | |
| 339 | Ubiquitination | NWTEAEVKGALADNL CCCHHHHHHHHHHHH | 29.94 | - | |
| 358 | N-linked_Glycosylation | EAVEQASNLTQAPEE HHHHHHHCCCCCCCC | 50.55 | UniProtKB CARBOHYD | |
| 360 | O-linked_Glycosylation | VEQASNLTQAPEEEP HHHHHCCCCCCCCCC | 27.25 | OGP | |
| 385 | GPI-anchor | RTHYGYSSGASSLHR CCCCCCCCCCCHHHH | 29.87 | 2168407 |
| 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 DPEP1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPEP1_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 DPEP1_HUMAN !! | ||||||
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| GPI-anchor | |
| Reference | PubMed |
| "Identification of membrane anchoring site of human renal dipeptidaseand construction and expression of a cDNA for its secretory form."; Adachi H., Katayama T., Inuzuka C., Oikawa S., Tsujimoto M.,Nakazato H.; J. Biol. Chem. 265:15341-15345(1990). Cited for: GPI-ANCHOR AT SER-385. | |
| 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-57 AND ASN-279, AND MASSSPECTROMETRY. | |
