| UniProt ID | PTTG2_HUMAN | |
|---|---|---|
| UniProt AC | Q9NZH5 | |
| Protein Name | Securin-2 | |
| Gene Name | PTTG2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 202 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | ||
| Protein Sequence | MATLIYVDKEIGEPGTRVAAKDVLKLESRPSIKALDGISQVLTRRFGKTYDAPSALPKATRKALGTVNRATEKSVKTNGPRKQKQPSFSAKKMTEKTVKTKSSVPASDDAYPEIEKFFPFNLLDFESFDLPEERQIAHLPLSGVPLMILDEEGELEKLFQLGPPSPVKMPSPPWECNLLQSPSSILSTLDVELPAVCYDIDI | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MATLIYVDKE -----CCEEEEECCC | 16.64 | 25348772 | |
| 16 | Phosphorylation | KEIGEPGTRVAAKDV CCCCCCCCCEEHHHH | 32.46 | 25348772 | |
| 31 | Phosphorylation | LKLESRPSIKALDGI HHHCCCCCHHHHHHH | 35.29 | - | |
| 54 | Phosphorylation | GKTYDAPSALPKATR CCCCCCCCCCCHHHH | 44.13 | 17192257 | |
| 66 | Phosphorylation | ATRKALGTVNRATEK HHHHHHHCCHHHHHH | 18.56 | - | |
| 87 | Phosphorylation | PRKQKQPSFSAKKMT CCCCCCCCCCCCCCC | 29.37 | 21712546 | |
| 89 | Phosphorylation | KQKQPSFSAKKMTEK CCCCCCCCCCCCCCC | 43.44 | 21815630 | |
| 107 | Phosphorylation | TKSSVPASDDAYPEI CCCCCCCCCCCCHHH | 29.92 | 28842319 | |
| 111 | Phosphorylation | VPASDDAYPEIEKFF CCCCCCCCHHHHHHC | 14.37 | 29978859 | |
| 165 | Phosphorylation | LFQLGPPSPVKMPSP HHCCCCCCCCCCCCC | 45.52 | 19664994 | |
| 165 (in isoform 2) | Phosphorylation | - | 45.52 | 25849741 | |
| 171 | Phosphorylation | PSPVKMPSPPWECNL CCCCCCCCCCCCCCC | 39.84 | 26074081 | |
| 184 | Phosphorylation | NLLQSPSSILSTLDV CCCCCHHHHHHHCCC | 30.82 | 20068231 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 165 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTTG2_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 PTTG2_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 |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY. | |