| UniProt ID | MARC2_HUMAN | |
|---|---|---|
| UniProt AC | Q969Z3 | |
| Protein Name | Mitochondrial amidoxime reducing component 2 | |
| Gene Name | 2-Mar | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 335 | |
| Subcellular Localization |
Mitochondrion outer membrane Peripheral membrane protein. Peroxisome. |
|
| Protein Description | As a component of the benzamidoxime prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively.. | |
| Protein Sequence | MGASSSSALARLGLPARPWPRWLGVAALGLAAVALGTVAWRRAWPRRRRRLQQVGTVAKLWIYPVKSCKGVPVSEAECTAMGLRSGNLRDRFWLVIKEDGHMVTARQEPRLVLISIIYENNCLIFRAPDMDQLVLPSKQPSSNKLHNCRIFGLDIKGRDCGNEAAKWFTNFLKTEAYRLVQFETNMKGRTSRKLLPTLDQNFQVAYPDYCPLLIMTDASLVDLNTRMEKKMKMENFRPNIVVTGCDAFEEDTWDELLIGSVEVKKVMACPRCILTTVDPDTGVIDRKQPLDTLKSYRLCDPSERELYKLSPLFGIYYSVEKIGSLRVGDPVYRMV | |
| 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 | ---MGASSSSALARL ---CCCCHHHHHHHC | - | ||
| 56 | Phosphorylation | RRLQQVGTVAKLWIY HHHHHHCCEEEEEEE | 25072903 | ||
| 59 | Ubiquitination | QQVGTVAKLWIYPVK HHHCCEEEEEEEECC | 21890473 | ||
| 59 | Ubiquitination | QQVGTVAKLWIYPVK HHHCCEEEEEEEECC | 21890473 | ||
| 59 (in isoform 1) | Ubiquitination | - | 21890473 | ||
| 59 (in isoform 2) | Ubiquitination | - | 21890473 | ||
| 66 | Malonylation | KLWIYPVKSCKGVPV EEEEEECCCCCCCCC | 26320211 | ||
| 66 | Ubiquitination | KLWIYPVKSCKGVPV EEEEEECCCCCCCCC | 21890473 | ||
| 69 | Ubiquitination | IYPVKSCKGVPVSEA EEECCCCCCCCCCHH | 21963094 | ||
| 76 | Ubiquitination | KGVPVSEAECTAMGL CCCCCCHHHHHHCCC | 21890473 | ||
| 83 | Ubiquitination | AECTAMGLRSGNLRD HHHHHCCCCCCCCCC | 21890473 | ||
| 137 | Phosphorylation | MDQLVLPSKQPSSNK HHHEECCCCCCCCCC | 24719451 | ||
| 138 | Ubiquitination | DQLVLPSKQPSSNKL HHEECCCCCCCCCCC | 25621951 | ||
| 144 | Ubiquitination | SKQPSSNKLHNCRIF CCCCCCCCCCCCEEE | 25621951 | ||
| 156 | Malonylation | RIFGLDIKGRDCGNE EEEEEEECCCCCCHH | 26320211 | ||
| 156 | Ubiquitination | RIFGLDIKGRDCGNE EEEEEEECCCCCCHH | 21890473 | ||
| 156 | Acetylation | RIFGLDIKGRDCGNE EEEEEEECCCCCCHH | 26051181 | ||
| 156 (in isoform 1) | Ubiquitination | - | 21890473 | ||
| 156 | Ubiquitination | RIFGLDIKGRDCGNE EEEEEEECCCCCCHH | 21963094 | ||
| 156 (in isoform 2) | Ubiquitination | - | 21890473 | ||
| 166 (in isoform 1) | Ubiquitination | - | 21890473 | ||
| 166 | Ubiquitination | DCGNEAAKWFTNFLK CCCHHHHHHHHHHHH | 21890473 | ||
| 166 | Ubiquitination | DCGNEAAKWFTNFLK CCCHHHHHHHHHHHH | 21963094 | ||
| 166 (in isoform 2) | Ubiquitination | - | 21890473 | ||
| 173 | Ubiquitination | KWFTNFLKTEAYRLV HHHHHHHHHHHHHHH | 21890473 | ||
| 173 (in isoform 1) | Ubiquitination | - | 21890473 | ||
| 173 (in isoform 2) | Ubiquitination | - | 21890473 | ||
| 173 | Ubiquitination | KWFTNFLKTEAYRLV HHHHHHHHHHHHHHH | 22817900 | ||
| 184 | Phosphorylation | YRLVQFETNMKGRTS HHHHHHHHCCCCCCC | 28857561 | ||
| 187 | Ubiquitination | VQFETNMKGRTSRKL HHHHHCCCCCCCCCC | 25621951 | ||
| 190 | Phosphorylation | ETNMKGRTSRKLLPT HHCCCCCCCCCCCCC | 22210691 | ||
| 197 | Phosphorylation | TSRKLLPTLDQNFQV CCCCCCCCCCCCCCC | 22210691 | ||
| 225 | Phosphorylation | ASLVDLNTRMEKKMK HHHCCCHHHHHHHHC | 22210691 | ||
| 287 | Ubiquitination | DTGVIDRKQPLDTLK CCCCCCCCCCCCHHH | 25621951 | ||
| 294 | Ubiquitination | KQPLDTLKSYRLCDP CCCCCHHHHCCCCCH | 25621951 | ||
| 295 | Phosphorylation | QPLDTLKSYRLCDPS CCCCHHHHCCCCCHH | 28857561 | ||
| 302 | Phosphorylation | SYRLCDPSERELYKL HCCCCCHHHHHHHHH | 22798277 | ||
| 307 | Phosphorylation | DPSERELYKLSPLFG CHHHHHHHHHHHHHE | - | ||
| 310 | Phosphorylation | ERELYKLSPLFGIYY HHHHHHHHHHHEEEE | 28348404 | ||
| 317 | Phosphorylation | SPLFGIYYSVEKIGS HHHHEEEEEHHHCCC | - | ||
| 324 | Phosphorylation | YSVEKIGSLRVGDPV EEHHHCCCEECCCCE | 24719451 | ||
| 332 | Phosphorylation | LRVGDPVYRMV---- EECCCCEEECC---- | - |
| 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 MARC2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MARC2_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 MARC2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MARC2_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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