| UniProt ID | RISC_HUMAN | |
|---|---|---|
| UniProt AC | Q9HB40 | |
| Protein Name | Retinoid-inducible serine carboxypeptidase | |
| Gene Name | SCPEP1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 452 | |
| Subcellular Localization | Secreted . | |
| Protein Description | May be involved in vascular wall and kidney homeostasis.. | |
| Protein Sequence | MELALRRSPVPRWLLLLPLLLGLNAGAVIDWPTEEGKEVWDYVTVRKDAYMFWWLYYATNSCKNFSELPLVMWLQGGPGGSSTGFGNFEEIGPLDSDLKPRKTTWLQAASLLFVDNPVGTGFSYVNGSGAYAKDLAMVASDMMVLLKTFFSCHKEFQTVPFYIFSESYGGKMAAGIGLELYKAIQRGTIKCNFAGVALGDSWISPVDSVLSWGPYLYSMSLLEDKGLAEVSKVAEQVLNAVNKGLYREATELWGKAEMIIEQNTDGVNFYNILTKSTPTSTMESSLEFTQSHLVCLCQRHVRHLQRDALSQLMNGPIRKKLKIIPEDQSWGGQATNVFVNMEEDFMKPVISIVDELLEAGINVTVYNGQLDLIVDTMGQEAWVRKLKWPELPKFSQLKWKALYSDPKSLETSAFVKSYKNLAFYWILKAGHMVPSDQGDMALKMMRLVTQQE | |
| 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 |
|---|---|---|---|---|---|
| 42 | Phosphorylation | EGKEVWDYVTVRKDA CCCCEEEEEEEECHH | 5.15 | - | |
| 64 | N-linked_Glycosylation | YATNSCKNFSELPLV HHHCCCCCHHHCCEE | 50.43 | UniProtKB CARBOHYD | |
| 126 | N-linked_Glycosylation | GTGFSYVNGSGAYAK CCCCCEECCCCCHHH | 30.58 | 12754519 | |
| 126 | N-linked_Glycosylation | GTGFSYVNGSGAYAK CCCCCEECCCCCHHH | 30.58 | 12754519 | |
| 243 | Ubiquitination | QVLNAVNKGLYREAT HHHHHHHHCHHHHHH | 43.63 | 21890473 | |
| 243 (in isoform 1) | Ubiquitination | - | 43.63 | 21890473 | |
| 243 (in isoform 2) | Ubiquitination | - | 43.63 | 21890473 | |
| 280 | O-linked_Glycosylation | LTKSTPTSTMESSLE EECCCCCCCCHHHHH | 27.28 | 29351928 | |
| 281 | O-linked_Glycosylation | TKSTPTSTMESSLEF ECCCCCCCCHHHHHH | 27.69 | 29351928 | |
| 362 | N-linked_Glycosylation | ELLEAGINVTVYNGQ HHHHCCCCEEEECCE | 23.61 | UniProtKB CARBOHYD | |
| 400 | Ubiquitination | KFSQLKWKALYSDPK CCCHHCHHHHHCCCC | 27.25 | - | |
| 404 | Phosphorylation | LKWKALYSDPKSLET HCHHHHHCCCCCCCH | 48.57 | - | |
| 407 | Ubiquitination | KALYSDPKSLETSAF HHHHCCCCCCCHHHH | 73.07 | - | |
| 407 | 2-Hydroxyisobutyrylation | KALYSDPKSLETSAF HHHHCCCCCCCHHHH | 73.07 | - | |
| 408 | Phosphorylation | ALYSDPKSLETSAFV HHHCCCCCCCHHHHH | 36.50 | - | |
| 411 | Phosphorylation | SDPKSLETSAFVKSY CCCCCCCHHHHHHHH | 30.56 | - | |
| 416 | Ubiquitination | LETSAFVKSYKNLAF CCHHHHHHHHHHHHH | 41.43 | - |
| 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 RISC_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RISC_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 RISC_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| TBA1A_HUMAN | TUBA1A | physical | 22863883 | |
| TBB5_HUMAN | TUBB | physical | 22863883 | |
| XPO1_HUMAN | XPO1 | physical | 22863883 | |
| 1433E_HUMAN | YWHAE | physical | 22863883 | |
| CD2AP_HUMAN | CD2AP | physical | 26344197 | |
| PRDX6_HUMAN | PRDX6 | physical | 26344197 | |
| ZN507_HUMAN | ZNF507 | physical | 28514442 |
| 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. | ||||||
loading...
| N-linked Glycosylation | |
| Reference | PubMed |
| "Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-126. | |