| UniProt ID | MGLL_MOUSE | |
|---|---|---|
| UniProt AC | O35678 | |
| Protein Name | Monoglyceride lipase {ECO:0000312|MGI:MGI:1346042} | |
| Gene Name | Mgll {ECO:0000312|MGI:MGI:1346042} | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 303 | |
| Subcellular Localization |
Cytoplasm, cytosol . Membrane Peripheral membrane protein . |
|
| Protein Description | Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain. [PubMed: 9341166] | |
| Protein Sequence | MPEASSPRRTPQNVPYQDLPHLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRIAAAGAGCPP | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MPEASSPRRTPQ ---CCCCCCCCCCCC | 38.93 | 29899451 | |
| 6 | Phosphorylation | --MPEASSPRRTPQN --CCCCCCCCCCCCC | 29.49 | 29899451 | |
| 10 | Phosphorylation | EASSPRRTPQNVPYQ CCCCCCCCCCCCCHH | 30.42 | 19060867 | |
| 32 | S-nitrosocysteine | ADGQYLFCRYWKPSG CCCCEEEEEEECCCC | 2.77 | - | |
| 32 | S-palmitoylation | ADGQYLFCRYWKPSG CCCCEEEEEEECCCC | 2.77 | 28526873 | |
| 32 | S-nitrosylation | ADGQYLFCRYWKPSG CCCCEEEEEEECCCC | 2.77 | 21278135 | |
| 36 | Ubiquitination | YLFCRYWKPSGTPKA EEEEEEECCCCCCCE | 21.99 | - | |
| 38 | Phosphorylation | FCRYWKPSGTPKALI EEEEECCCCCCCEEE | 52.12 | - | |
| 40 | Phosphorylation | RYWKPSGTPKALIFV EEECCCCCCCEEEEE | 26.42 | 21183079 | |
| 48 | Phosphorylation | PKALIFVSHGAGEHC CCEEEEEECCCHHCC | 12.88 | - | |
| 54 | Phosphorylation | VSHGAGEHCGRYDEL EECCCHHCCCCHHHH | 20.58 | 24719451 | |
| 55 | S-palmitoylation | SHGAGEHCGRYDELA ECCCHHCCCCHHHHH | 2.63 | 28526873 | |
| 56 | Phosphorylation | HGAGEHCGRYDELAH CCCHHCCCCHHHHHH | 32.84 | 24719451 | |
| 58 | Nitration | AGEHCGRYDELAHML CHHCCCCHHHHHHHH | 10.07 | 16800626 | |
| 58 | Nitration | AGEHCGRYDELAHML CHHCCCCHHHHHHHH | 10.07 | 16800626 | |
| 58 | Nitrated tyrosine | AGEHCGRYDELAHML CHHCCCCHHHHHHHH | 10.07 | - | |
| 64 | Phosphorylation | RYDELAHMLKGLDML CHHHHHHHHHCCCEE | 3.26 | 24719451 | |
| 137 | Phosphorylation | LVAAERPTYFSGMVL HHHCCCCCCCCCCEE | 43.34 | 25777480 | |
| 138 | Phosphorylation | VAAERPTYFSGMVLI HHCCCCCCCCCCEEE | 9.83 | 25777480 | |
| 140 | Phosphorylation | AERPTYFSGMVLISP CCCCCCCCCCEEECC | 18.63 | 25777480 | |
| 146 | Phosphorylation | FSGMVLISPLVLANP CCCCEEECCHHHCCC | 14.18 | 25777480 | |
| 155 | Phosphorylation | LVLANPESASTLKVL HHHCCCCCHHHHHHH | 28.86 | 25777480 | |
| 157 | Phosphorylation | LANPESASTLKVLAA HCCCCCHHHHHHHHH | 43.48 | 25777480 | |
| 158 | Phosphorylation | ANPESASTLKVLAAK CCCCCHHHHHHHHHH | 30.25 | 25777480 | |
| 182 | Phosphorylation | TLGRIDSSVLSRNKS CCCCCCHHHHCCCHH | 24.27 | - | |
| 188 | Ubiquitination | SSVLSRNKSEVDLYN HHHHCCCHHHHCCCC | 47.05 | - | |
| 189 | Phosphorylation | SVLSRNKSEVDLYNS HHHCCCHHHHCCCCC | 46.53 | 25521595 | |
| 194 | Phosphorylation | NKSEVDLYNSDPLVC CHHHHCCCCCCCCHH | 14.25 | 29472430 | |
| 196 | Phosphorylation | SEVDLYNSDPLVCRA HHHCCCCCCCCHHHH | 27.35 | 19367708 | |
| 201 | S-palmitoylation | YNSDPLVCRAGLKVC CCCCCCHHHHCHHHH | 3.04 | 28526873 | |
| 205 | Phosphorylation | PLVCRAGLKVCFGIQ CCHHHHCHHHHHHHH | 3.52 | 24719451 | |
| 208 | S-palmitoylation | CRAGLKVCFGIQLLN HHHCHHHHHHHHHHH | 2.18 | 28526873 | |
| 228 | Phosphorylation | ERAMPRLTLPFLLLQ HHHCHHCCHHHHHHH | 33.39 | 27180971 | |
| 245 | Ubiquitination | ADRLCDSKGAYLLME HHHHHCCCCCEEEEE | 34.02 | - |
| 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 MGLL_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MGLL_MOUSE !! | ||||||
* 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 MGLL_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MGLL_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Nitration | |
| Reference | PubMed |
| "Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease."; Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.; Biochemistry 45:8009-8022(2006). Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-58, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASSSPECTROMETRY. | |