| UniProt ID | CMBL_HUMAN | |
|---|---|---|
| UniProt AC | Q96DG6 | |
| Protein Name | Carboxymethylenebutenolidase homolog | |
| Gene Name | CMBL | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 245 | |
| Subcellular Localization | Cytoplasm, cytosol . | |
| Protein Description | Cysteine hydrolase. Can convert the prodrug olmesartan medoxomil into its pharmacologically active metabolite olmerstatan, an angiotensin receptor blocker, in liver and intestine. May also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin.. | |
| Protein Sequence | MANEAYPCPCDIGHRLEYGGLGREVQVEHIKAYVTKSPVDAGKAVIVIQDIFGWQLPNTRYIADMISGNGYTTIVPDFFVGQEPWDPSGDWSIFPEWLKTRNAQKIDREISAILKYLKQQCHAQKIGIVGFCWGGTAVHHLMMKYSEFRAGVSVYGIVKDSEDIYNLKNPTLFIFAENDVVIPLKDVSLLTQKLKEHCKVEYQIKTFSGQTHGFVHRKREDCSPADKPYIDEARRNLIEWLNKYM | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MANEAYPCP ------CCCCCCCCC | 23.67 | - | |
| 6 | Phosphorylation | --MANEAYPCPCDIG --CCCCCCCCCCCCC | 10.13 | 25159151 | |
| 18 | Phosphorylation | DIGHRLEYGGLGREV CCCCCCCCCCCCCEE | 22.53 | 29496907 | |
| 31 | Ubiquitination | EVQVEHIKAYVTKSP EEEEEEEEEEEECCC | 35.26 | 22817900 | |
| 31 | Acetylation | EVQVEHIKAYVTKSP EEEEEEEEEEEECCC | 35.26 | 26051181 | |
| 33 | Phosphorylation | QVEHIKAYVTKSPVD EEEEEEEEEECCCCC | 12.03 | 29496907 | |
| 35 | Phosphorylation | EHIKAYVTKSPVDAG EEEEEEEECCCCCCC | 17.09 | 26270265 | |
| 36 | Acetylation | HIKAYVTKSPVDAGK EEEEEEECCCCCCCC | 42.59 | 19608861 | |
| 36 | Ubiquitination | HIKAYVTKSPVDAGK EEEEEEECCCCCCCC | 42.59 | 27667366 | |
| 37 | Phosphorylation | IKAYVTKSPVDAGKA EEEEEECCCCCCCCE | 22.31 | 26270265 | |
| 111 | Phosphorylation | QKIDREISAILKYLK HHHHHHHHHHHHHHH | 12.42 | 26437602 | |
| 115 | Acetylation | REISAILKYLKQQCH HHHHHHHHHHHHHHH | 42.28 | 26051181 | |
| 115 | Ubiquitination | REISAILKYLKQQCH HHHHHHHHHHHHHHH | 42.28 | 29967540 | |
| 116 | Phosphorylation | EISAILKYLKQQCHA HHHHHHHHHHHHHHH | 18.71 | - | |
| 118 | Acetylation | SAILKYLKQQCHAQK HHHHHHHHHHHHHCC | 34.92 | 26051181 | |
| 118 | Ubiquitination | SAILKYLKQQCHAQK HHHHHHHHHHHHHCC | 34.92 | 29967540 | |
| 146 | Phosphorylation | HHLMMKYSEFRAGVS HHHHHHHHHHCCCEE | 25.41 | 27642862 | |
| 155 | Phosphorylation | FRAGVSVYGIVKDSE HCCCEEEEEEECCHH | 8.14 | 27642862 | |
| 165 | Phosphorylation | VKDSEDIYNLKNPTL ECCHHHHHCCCCCEE | 27.11 | 25159151 | |
| 188 | Phosphorylation | VIPLKDVSLLTQKLK EEEHHHHHHHHHHHH | 28.00 | 26437602 | |
| 191 | Phosphorylation | LKDVSLLTQKLKEHC HHHHHHHHHHHHHHC | 29.02 | 20860994 | |
| 193 | Ubiquitination | DVSLLTQKLKEHCKV HHHHHHHHHHHHCCE | 57.18 | 27667366 | |
| 193 | Acetylation | DVSLLTQKLKEHCKV HHHHHHHHHHHHCCE | 57.18 | 27452117 | |
| 195 | Ubiquitination | SLLTQKLKEHCKVEY HHHHHHHHHHCCEEE | 53.07 | 27667366 | |
| 199 | Ubiquitination | QKLKEHCKVEYQIKT HHHHHHCCEEEEEEE | 39.75 | 29967540 | |
| 199 | Methylation | QKLKEHCKVEYQIKT HHHHHHCCEEEEEEE | 39.75 | - | |
| 199 | Acetylation | QKLKEHCKVEYQIKT HHHHHHCCEEEEEEE | 39.75 | 26051181 | |
| 202 | Phosphorylation | KEHCKVEYQIKTFSG HHHCCEEEEEEECCC | 20.65 | 26437602 | |
| 206 | Phosphorylation | KVEYQIKTFSGQTHG CEEEEEEECCCCCCE | 25.35 | 28857561 | |
| 208 | Phosphorylation | EYQIKTFSGQTHGFV EEEEEECCCCCCEEE | 34.91 | 25159151 | |
| 211 | Phosphorylation | IKTFSGQTHGFVHRK EEECCCCCCEEEEEC | 27.73 | 23186163 | |
| 218 | Ubiquitination | THGFVHRKREDCSPA CCEEEEECCCCCCCC | 45.31 | 29967540 | |
| 223 | Phosphorylation | HRKREDCSPADKPYI EECCCCCCCCCCCCH | 35.13 | 26657352 | |
| 227 | Ubiquitination | EDCSPADKPYIDEAR CCCCCCCCCCHHHHH | 41.65 | 29967540 | |
| 227 | Acetylation | EDCSPADKPYIDEAR CCCCCCCCCCHHHHH | 41.65 | 26051181 |
| 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 CMBL_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CMBL_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 CMBL_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CMBL_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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| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND MASS SPECTROMETRY. | |