| UniProt ID | MA2C1_HUMAN | |
|---|---|---|
| UniProt AC | Q9NTJ4 | |
| Protein Name | Alpha-mannosidase 2C1 | |
| Gene Name | MAN2C1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 1040 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Cleaves alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues from glycoproteins. Involved in the degradation of free oligosaccharides in the cytoplasm.. | |
| Protein Sequence | MAAAPALKHWRTTLERVEKFVSPLYFTDCNLRGRLFGASCPVAVLSSFLTPERLPYQEAVQRDFRPAQVGDSFGPTWWTCWFRVELTIPEAWVGQEVHLCWESDGEGLVWRDGEPVQGLTKEGEKTSYVLTDRLGERDPRSLTLYVEVACNGLLGAGKGSMIAAPDPEKMFQLSRAELAVFHRDVHMLLVDLELLLGIAKGLGKDNQRSFQALYTANQMVNVCDPAQPETFPVAQALASRFFGQHGGESQHTIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVPVGGTWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFPHHTFFWEGLDGSRVLVHFPPGDSYGMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRLSNTDGLPRVQLSSPRQLFSALESDSEQLCTWVGELFLELHNGTYTTHAQIKKGNRECERILHDVELLSSLALARSAQFLYPAAQLQHLWRLLLLNQFHDVVTGSCIQMVAEEAMCHYEDIRSHGNTLLSAAAAALCAGEPGPEGLLIVNTLPWKRIEVMALPKPGGAHSLALVTVPSMGYAPVPPPTSLQPLLPQQPVFVVQETDGSVTLDNGIIRVKLDPTGRLTSLVLVASGREAIAEGAVGNQFVLFDDVPLYWDAWDVMDYHLETRKPVLGQAGTLAVGTEGGLRGSAWFLLQISPNSRLSQEVVLDVGCPYVRFHTEVHWHEAHKFLKVEFPARVRSSQATYEIQFGHLQRPTHYNTSWDWARFEVWAHRWMDLSEHGFGLALLNDCKYGASVRGSILSLSLLRAPKAPDATADTGRHEFTYALMPHKGSFQDAGVIQAAYSLNFPLLALPAPSPAPATSWSAFSVSSPAVVLETVKQAESSPQRRSLVLRLYEAHGSHVDCWLHLSLPVQEAILCDLLERPDPAGHLTLRDNRLKLTFSPFQVLSLLLVLQPPPH | |
| 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 |
|---|---|---|---|---|---|
| 8 | Ubiquitination | MAAAPALKHWRTTLE CCCHHHHHHHHHHHH | 43.13 | - | |
| 19 | Ubiquitination | TTLERVEKFVSPLYF HHHHHHHHHHCCCEE | 48.48 | - | |
| 25 | Phosphorylation | EKFVSPLYFTDCNLR HHHHCCCEEECCCCC | 14.07 | - | |
| 125 | Ubiquitination | GLTKEGEKTSYVLTD CCCCCCCEEEEEEEC | 54.34 | - | |
| 126 | Phosphorylation | LTKEGEKTSYVLTDR CCCCCCEEEEEEECC | 22.46 | 29083192 | |
| 127 | Phosphorylation | TKEGEKTSYVLTDRL CCCCCEEEEEEECCC | 25.06 | 29083192 | |
| 128 | Phosphorylation | KEGEKTSYVLTDRLG CCCCEEEEEEECCCC | 12.52 | 29083192 | |
| 214 | Phosphorylation | QRSFQALYTANQMVN HHHHHHHHHHHHHHC | 13.56 | - | |
| 279 | Phosphorylation | TVRKCARSWVTALQL HHHHHHHHHHHHHHH | 13.84 | - | |
| 315 | Phosphorylation | SRYPGLYSRIQEFAC HHCCCHHHHHHHHHH | 28.13 | 24719451 | |
| 342 | Phosphorylation | EMDGNLPSGEAMVRQ EECCCCCCHHHHHHH | 53.05 | 30576142 | |
| 480 | Phosphorylation | LDRLKRLSNTDGLPR HHHHHHHCCCCCCCC | 41.54 | 28176443 | |
| 482 | Phosphorylation | RLKRLSNTDGLPRVQ HHHHHCCCCCCCCEE | 28.24 | 26055452 | |
| 491 | Phosphorylation | GLPRVQLSSPRQLFS CCCCEECCCHHHHHH | 22.62 | 24719451 | |
| 492 | Phosphorylation | LPRVQLSSPRQLFSA CCCEECCCHHHHHHH | 32.47 | 17081983 | |
| 701 | Phosphorylation | IRVKLDPTGRLTSLV EEEEECCCCCEEEEE | 34.30 | - | |
| 712 | Phosphorylation | TSLVLVASGREAIAE EEEEEEEECCHHHHC | 30.79 | - | |
| 750 | Ubiquitination | DYHLETRKPVLGQAG HHHHHCCCCCCCCCE | 47.07 | 21890473 | |
| 750 | Ubiquitination | DYHLETRKPVLGQAG HHHHHCCCCCCCCCE | 47.07 | 21890473 | |
| 809 | Ubiquitination | VHWHEAHKFLKVEFP EEHHHHHHEEEEEEC | 60.48 | - | |
| 812 | Ubiquitination | HEAHKFLKVEFPARV HHHHHEEEEEECCEE | 42.74 | 21890473 | |
| 859 | Phosphorylation | AHRWMDLSEHGFGLA HHHCCCHHHCCCEEH | 24.23 | - | |
| 914 | Phosphorylation | ALMPHKGSFQDAGVI EECCCCCCCCCHHHH | 25.25 | 22210691 | |
| 949 | Phosphorylation | ATSWSAFSVSSPAVV CCCCCCEECCCCCHH | 22.32 | 22210691 | |
| 959 | Phosphorylation | SPAVVLETVKQAESS CCCHHHHHHHHHCCC | 28.92 | 22210691 | |
| 965 | Phosphorylation | ETVKQAESSPQRRSL HHHHHHCCCHHHHHH | 50.78 | 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 MA2C1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MA2C1_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 MA2C1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MA2C1_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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| Phosphorylation | |
| Reference | PubMed |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND THR-482, ANDMASS SPECTROMETRY. | |
