| UniProt ID | MGN2_HUMAN | |
|---|---|---|
| UniProt AC | Q96A72 | |
| Protein Name | Protein mago nashi homolog 2 | |
| Gene Name | MAGOHB | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 148 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Involved in mRNA splicing and in the nonsense-mediated decay (NMD) pathway.. | |
| Protein Sequence | MAVASDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI | |
| 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 | ------MAVASDFYL ------CCCCCCEEE | 12.94 | 22223895 | |
| 16 | Ubiquitination | LRYYVGHKGKFGHEF EEEECCCCCCCCCEE | 58.84 | - | |
| 18 | Acetylation | YYVGHKGKFGHEFLE EECCCCCCCCCEEEE | 53.64 | - | |
| 18 | Ubiquitination | YYVGHKGKFGHEFLE EECCCCCCCCCEEEE | 53.64 | 21890473 | |
| 33 | Ubiquitination | FEFRPDGKLRYANNS EEECCCCCEEECCCC | 36.85 | 21890473 | |
| 36 | Phosphorylation | RPDGKLRYANNSNYK CCCCCEEECCCCCCC | 24.90 | - | |
| 40 | Phosphorylation | KLRYANNSNYKNDVM CEEECCCCCCCCCEE | 41.15 | 27273156 | |
| 42 | Phosphorylation | RYANNSNYKNDVMIR EECCCCCCCCCEEEE | 15.81 | 27155012 | |
| 43 | Ubiquitination | YANNSNYKNDVMIRK ECCCCCCCCCEEEEH | 51.42 | 21890473 | |
| 53 | Phosphorylation | VMIRKEAYVHKSVME EEEEHHHHHCHHHHH | 12.27 | 20049867 | |
| 56 | Ubiquitination | RKEAYVHKSVMEELK EHHHHHCHHHHHHHH | 34.40 | - | |
| 63 | Ubiquitination | KSVMEELKRIIDDSE HHHHHHHHHHCCHHH | 44.84 | - | |
| 73 | Ubiquitination | IDDSEITKEDDALWP CCHHHCCCCCCCCCC | 65.88 | 21890473 | |
| 100 | Phosphorylation | VIGDEHISFTTSKIG EECCCCCEEECCCCC | 20.60 | 21406692 | |
| 102 | Phosphorylation | GDEHISFTTSKIGSL CCCCCEEECCCCCCE | 24.30 | 21406692 | |
| 103 | Phosphorylation | DEHISFTTSKIGSLI CCCCEEECCCCCCEE | 26.47 | 21406692 | |
| 104 | Phosphorylation | EHISFTTSKIGSLID CCCEEECCCCCCEEE | 21.15 | 21406692 | |
| 108 | Phosphorylation | FTTSKIGSLIDVNQS EECCCCCCEEECCCC | 26.14 | 23401153 | |
| 115 | Phosphorylation | SLIDVNQSKDPEGLR CEEECCCCCCCCHHH | 33.55 | 26074081 | |
| 116 | Ubiquitination | LIDVNQSKDPEGLRV EEECCCCCCCCHHHH | 68.49 | 21906983 | |
| 116 | Acetylation | LIDVNQSKDPEGLRV EEECCCCCCCCHHHH | 68.49 | 37092765 | |
| 125 | Phosphorylation | PEGLRVFYYLVQDLK CCHHHHHHHHHHHHH | 7.95 | - | |
| 132 | Ubiquitination | YYLVQDLKCLVFSLI HHHHHHHHHHHHHHH | 33.54 | - |
| 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 MGN2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MGN2_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 MGN2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RBM8A_HUMAN | RBM8A | physical | 22939629 | |
| DX39B_HUMAN | DDX39B | physical | 22939629 | |
| ZN398_HUMAN | ZNF398 | physical | 25416956 | |
| ZN250_HUMAN | ZNF250 | physical | 25416956 | |
| C102B_HUMAN | CCDC102B | physical | 25416956 | |
| K1C40_HUMAN | KRT40 | physical | 25416956 | |
| TRI42_HUMAN | TRIM42 | physical | 25416956 | |
| RBM8A_HUMAN | RBM8A | physical | 26496610 | |
| PYM1_HUMAN | WIBG | physical | 26496610 | |
| EFGM_HUMAN | GFM1 | physical | 26496610 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| 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. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY. | |