| UniProt ID | MMAD_HUMAN | |
|---|---|---|
| UniProt AC | Q9H3L0 | |
| Protein Name | Methylmalonic aciduria and homocystinuria type D protein, mitochondrial | |
| Gene Name | MMADHC | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 296 | |
| Subcellular Localization | Cytoplasm . Mitochondrion . | |
| Protein Description | Involved in cobalamin metabolism. [PubMed: 18385497] | |
| Protein Sequence | MANVLCNRARLVSYLPGFCSLVKRVVNPKAFSTAGSSGSDESHVAAAPPDICSRTVWPDETMGPFGPQDQRFQLPGNIGFDCHLNGTASQKKSLVHKTLPDVLAEPLSSERHEFVMAQYVNEFQGNDAPVEQEINSAETYFESARVECAIQTCPELLRKDFESLFPEVANGKLMILTVTQKTKNDMTVWSEEVEIEREVLLEKFINGAKEICYALRAEGYWADFIDPSSGLAFFGPYTNNTLFETDERYRHLGFSVDDLGCCKVIRHSLWGTHVVVGSIFTNATPDSHIMKKLSGN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 29 | Ubiquitination | VKRVVNPKAFSTAGS HHHHCCHHHHCCCCC | 57.78 | 29967540 | |
| 89 | Phosphorylation | CHLNGTASQKKSLVH EECCCCCHHCHHHHC | 42.23 | - | |
| 97 | Ubiquitination | QKKSLVHKTLPDVLA HCHHHHCCCHHHHHH | 44.25 | 29967540 | |
| 152 | Phosphorylation | RVECAIQTCPELLRK HHHHHHHHCHHHHHH | 24.74 | 23403867 | |
| 159 | Ubiquitination | TCPELLRKDFESLFP HCHHHHHHHHHHHCH | 67.73 | 29967540 | |
| 163 | Phosphorylation | LLRKDFESLFPEVAN HHHHHHHHHCHHHHC | 34.99 | 26074081 | |
| 177 | Phosphorylation | NGKLMILTVTQKTKN CCEEEEEEEEECCCC | 15.58 | 26074081 | |
| 179 | Phosphorylation | KLMILTVTQKTKNDM EEEEEEEEECCCCCC | 21.07 | 26074081 | |
| 182 | Phosphorylation | ILTVTQKTKNDMTVW EEEEEECCCCCCEEE | 25.84 | 26074081 | |
| 187 | Phosphorylation | QKTKNDMTVWSEEVE ECCCCCCEEEECCEE | 22.99 | 26074081 | |
| 190 | Phosphorylation | KNDMTVWSEEVEIER CCCCEEEECCEEEHH | 21.39 | 26074081 | |
| 203 | Acetylation | EREVLLEKFINGAKE HHHHHHHHHHHHHHH | 52.06 | 19608861 | |
| 203 | Ubiquitination | EREVLLEKFINGAKE HHHHHHHHHHHHHHH | 52.06 | 19608861 | |
| 203 | Malonylation | EREVLLEKFINGAKE HHHHHHHHHHHHHHH | 52.06 | 26320211 |
| 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 MMAD_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MMAD_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 MMAD_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MMAD_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 277410 | Methylmalonic aciduria and homocystinuria type cblD (MMAHCD) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Acetylation | |
| Reference | PubMed |
| "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-203, AND MASS SPECTROMETRY. | |
