| UniProt ID | MINP1_HUMAN | |
|---|---|---|
| UniProt AC | Q9UNW1 | |
| Protein Name | Multiple inositol polyphosphate phosphatase 1 {ECO:0000312|HGNC:HGNC:7102} | |
| Gene Name | MINPP1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 487 | |
| Subcellular Localization | Endoplasmic reticulum lumen . | |
| Protein Description | Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate. May play a role in bone development (endochondral ossification). May play a role in the transition of chondrocytes from proliferation to hypertrophy (By similarity).. | |
| Protein Sequence | MLRAPGCLLRTSVAPAAALAAALLSSLARCSLLEPRDPVASSLSPYFGTKTRYEDVNPVLLSGPEAPWRDPELLEGTCTPVQLVALIRHGTRYPTVKQIRKLRQLHGLLQARGSRDGGASSTGSRDLGAALADWPLWYADWMDGQLVEKGRQDMRQLALRLASLFPALFSRENYGRLRLITSSKHRCMDSSAAFLQGLWQHYHPGLPPPDVADMEFGPPTVNDKLMRFFDHCEKFLTEVEKNATALYHVEAFKTGPEMQNILKKVAATLQVPVNDLNADLIQVAFFTCSFDLAIKGVKSPWCDVFDIDDAKVLEYLNDLKQYWKRGYGYTINSRSSCTLFQDIFQHLDKAVEQKQRSQPISSPVILQFGHAETLLPLLSLMGYFKDKEPLTAYNYKKQMHRKFRSGLIVPYASNLIFVLYHCENAKTPKEQFRVQMLLNEKVLPLAYSQETVSFYEDLKNHYKDILQSCQTSEECELARANSTSDEL | |
| 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 |
|---|---|---|---|---|---|
| 11 | Phosphorylation | APGCLLRTSVAPAAA CCCCCCCCCHHHHHH | 27.76 | - | |
| 41 | O-linked_Glycosylation | EPRDPVASSLSPYFG CCCCCCHHHCCCCCC | 31.85 | OGP | |
| 41 | Phosphorylation | EPRDPVASSLSPYFG CCCCCCHHHCCCCCC | 31.85 | 28152594 | |
| 42 | O-linked_Glycosylation | PRDPVASSLSPYFGT CCCCCHHHCCCCCCC | 24.11 | 55826543 | |
| 42 | Phosphorylation | PRDPVASSLSPYFGT CCCCCHHHCCCCCCC | 24.11 | 28152594 | |
| 44 | Phosphorylation | DPVASSLSPYFGTKT CCCHHHCCCCCCCCC | 21.36 | 28152594 | |
| 46 | Phosphorylation | VASSLSPYFGTKTRY CHHHCCCCCCCCCCC | 15.97 | 28152594 | |
| 49 | Phosphorylation | SLSPYFGTKTRYEDV HCCCCCCCCCCCCCC | 21.24 | 28152594 | |
| 50 (in isoform 3) | Ubiquitination | - | 31.24 | 21906983 | |
| 50 (in isoform 2) | Ubiquitination | - | 31.24 | 21906983 | |
| 50 (in isoform 1) | Ubiquitination | - | 31.24 | 21906983 | |
| 50 | Ubiquitination | LSPYFGTKTRYEDVN CCCCCCCCCCCCCCC | 31.24 | 27667366 | |
| 51 | O-linked_Glycosylation | SPYFGTKTRYEDVNP CCCCCCCCCCCCCCC | 38.02 | OGP | |
| 91 | Phosphorylation | VALIRHGTRYPTVKQ HHHHHCCCCCCHHHH | 22.39 | - | |
| 97 | Ubiquitination | GTRYPTVKQIRKLRQ CCCCCHHHHHHHHHH | 42.35 | 29967540 | |
| 170 | Phosphorylation | SLFPALFSRENYGRL HHHHHHHCCCCCCCE | 39.26 | 24043423 | |
| 174 | Phosphorylation | ALFSRENYGRLRLIT HHHCCCCCCCEEEEE | 10.00 | 24043423 | |
| 184 | 2-Hydroxyisobutyrylation | LRLITSSKHRCMDSS EEEEECCCCCCCCHH | 34.53 | - | |
| 242 | N-linked_Glycosylation | FLTEVEKNATALYHV HHHHHHHHHCEEEEH | 29.08 | 16335952 | |
| 262 | Ubiquitination | GPEMQNILKKVAATL CHHHHHHHHHHHHHC | 6.03 | 29967540 | |
| 298 | Ubiquitination | DLAIKGVKSPWCDVF HHHHCCCCCCCCCEE | 60.51 | 29967540 | |
| 306 (in isoform 2) | Phosphorylation | - | 43.16 | 22210691 | |
| 307 (in isoform 2) | Phosphorylation | - | 3.33 | 22210691 | |
| 309 (in isoform 2) | Phosphorylation | - | 48.93 | 22210691 | |
| 315 | Phosphorylation | DDAKVLEYLNDLKQY CHHHHHHHHHHHHHH | 13.47 | 19664994 | |
| 396 | 2-Hydroxyisobutyrylation | PLTAYNYKKQMHRKF CCCCCCHHHHHHHHH | 32.65 | - | |
| 463 | Ubiquitination | EDLKNHYKDILQSCQ HHHHHHHHHHHHHCC | 30.64 | 29967540 | |
| 471 | Phosphorylation | DILQSCQTSEECELA HHHHHCCCHHHHHHH | 42.29 | 26657352 | |
| 481 | N-linked_Glycosylation | ECELARANSTSDEL- HHHHHHHHCCCCCC- | 40.02 | UniProtKB CARBOHYD | |
| 482 | Phosphorylation | CELARANSTSDEL-- HHHHHHHCCCCCC-- | 28.44 | 24719451 |
| 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 MINP1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MINP1_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 MINP1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| VWA1_HUMAN | VWA1 | physical | 28514442 | |
| CA087_HUMAN | C1orf87 | physical | 28514442 | |
| HNRLL_HUMAN | HNRNPLL | physical | 28514442 | |
| MRS2_HUMAN | MRS2 | physical | 28514442 | |
| GDAP1_HUMAN | GDAP1 | 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. | ||||||
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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-242, AND MASSSPECTROMETRY. | |
