| UniProt ID | HMGA2_MOUSE | |
|---|---|---|
| UniProt AC | P52927 | |
| Protein Name | High mobility group protein HMGI-C | |
| Gene Name | Hmga2 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 108 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Functions as a transcriptional regulator. Functions in cell cycle regulation through CCNA2. Plays an important role in chromosome condensation during the meiotic G2/M transition of spermatocytes. Plays a role in postnatal myogenesis, is involved in satellite cell activation. [PubMed: 27446912] | |
| Protein Sequence | MSARGEGAGQPSTSAQGQPAAPVPQKRGRGRPRKQQQEPTCEPSPKRPRGRPKGSKNKSPSKAAQKKAETIGEKRPRGRPRKWPQQVVQKKPAQETEETSSQESAEED | |
| 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 | Phosphorylation | ------MSARGEGAG ------CCCCCCCCC | 27.03 | 26824392 | |
| 2 | Acetylation | ------MSARGEGAG ------CCCCCCCCC | 27.03 | - | |
| 12 | Phosphorylation | GEGAGQPSTSAQGQP CCCCCCCCCCCCCCC | 27.40 | 28059163 | |
| 13 | Phosphorylation | EGAGQPSTSAQGQPA CCCCCCCCCCCCCCC | 34.46 | 29514104 | |
| 14 | Phosphorylation | GAGQPSTSAQGQPAA CCCCCCCCCCCCCCC | 23.96 | 27087446 | |
| 26 | Acetylation | PAAPVPQKRGRGRPR CCCCCCCCCCCCCCC | 51.23 | 129653 | |
| 27 | Methylation | AAPVPQKRGRGRPRK CCCCCCCCCCCCCCC | 34.49 | 18966559 | |
| 40 | Phosphorylation | RKQQQEPTCEPSPKR CCCCCCCCCCCCCCC | 28.84 | 25619855 | |
| 41 | Glutathionylation | KQQQEPTCEPSPKRP CCCCCCCCCCCCCCC | 12.09 | 24333276 | |
| 44 | Phosphorylation | QEPTCEPSPKRPRGR CCCCCCCCCCCCCCC | 22.29 | 25521595 | |
| 59 | Phosphorylation | PKGSKNKSPSKAAQK CCCCCCCCHHHHHHH | 43.74 | 24453211 | |
| 61 | Phosphorylation | GSKNKSPSKAAQKKA CCCCCCHHHHHHHHH | 41.85 | 24453211 | |
| 74 | Acetylation | KAETIGEKRPRGRPR HHHHHHCCCCCCCCC | 63.59 | 23806337 | |
| 96 | Phosphorylation | QKKPAQETEETSSQE HCCCCCCCCHHCCHH | 27.35 | 25619855 | |
| 99 | Phosphorylation | PAQETEETSSQESAE CCCCCCHHCCHHHHH | 27.69 | 25521595 | |
| 100 | Phosphorylation | AQETEETSSQESAEE CCCCCHHCCHHHHHC | 33.05 | 25521595 | |
| 101 | Phosphorylation | QETEETSSQESAEED CCCCHHCCHHHHHCC | 45.44 | 25521595 | |
| 104 | Phosphorylation | EETSSQESAEED--- CHHCCHHHHHCC--- | 33.09 | 25521595 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 44 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
| 59 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
| 99 | T | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 100 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 101 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 104 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HMGA2_MOUSE !! | ||||||
* 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 HMGA2_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| TAF3_MOUSE | Taf3 | physical | 21417337 | |
| CAF1A_MOUSE | Chaf1a | physical | 21417337 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY. | |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY. | |