| UniProt ID | MGDP1_HUMAN | |
|---|---|---|
| UniProt AC | Q86V88 | |
| Protein Name | Magnesium-dependent phosphatase 1 | |
| Gene Name | MDP1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 176 | |
| Subcellular Localization | ||
| Protein Description | Magnesium-dependent phosphatase which may act as a tyrosine phosphatase.. | |
| Protein Sequence | MARLPKLAVFDLDYTLWPFWVDTHVDPPFHKSSDGTVRDRRGQDVRLYPEVPEVLKRLQSLGVPGAAASRTSEIEGANQLLELFDLFRYFVHREIYPGSKITHFERLQQKTGIPFSQMIFFDDERRNIVDVSKLGVTCIHIQNGMNLQTLSQGLETFAKAQTGPLRSSLEESPFEA | |
| 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 |
|---|---|---|---|---|---|
| 46 | Methylation | DRRGQDVRLYPEVPE CCCCCCCEECCCHHH | 36.47 | 115483079 | |
| 56 | Ubiquitination | PEVPEVLKRLQSLGV CCHHHHHHHHHHCCC | 57.13 | 33845483 | |
| 71 | Phosphorylation | PGAAASRTSEIEGAN CCCHHCCCCCCCHHH | 28.37 | 27732954 | |
| 72 | Phosphorylation | GAAASRTSEIEGANQ CCHHCCCCCCCHHHH | 35.15 | 27732954 | |
| 100 | Ubiquitination | REIYPGSKITHFERL HHHCCCCCCCHHHHH | 58.50 | - | |
| 110 | Ubiquitination | HFERLQQKTGIPFSQ HHHHHHHHHCCCHHH | 35.44 | - | |
| 149 | Phosphorylation | QNGMNLQTLSQGLET CCCCCHHHHHHHHHH | 31.38 | 28348404 | |
| 151 | Phosphorylation | GMNLQTLSQGLETFA CCCHHHHHHHHHHHH | 26.11 | 28348404 | |
| 162 | Phosphorylation | ETFAKAQTGPLRSSL HHHHHHCCCCCCHHC | 45.70 | 28348404 | |
| 167 | Phosphorylation | AQTGPLRSSLEESPF HCCCCCCHHCCCCCC | 47.13 | 25159151 | |
| 168 | Phosphorylation | QTGPLRSSLEESPFE CCCCCCHHCCCCCCC | 33.11 | 25159151 | |
| 172 | Phosphorylation | LRSSLEESPFEA--- CCHHCCCCCCCC--- | 26.05 | 25159151 |
| 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 MGDP1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MGDP1_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 MGDP1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MGDP1_HUMAN !! | ||||
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND MASSSPECTROMETRY. | |
