| UniProt ID | CCNA2_HUMAN | |
|---|---|---|
| UniProt AC | P20248 | |
| Protein Name | Cyclin-A2 {ECO:0000312|HGNC:HGNC:1578} | |
| Gene Name | CCNA2 {ECO:0000312|HGNC:HGNC:1578} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 432 | |
| Subcellular Localization | Nucleus . Cytoplasm . Exclusively nuclear during interphase (PubMed:1312467). Detected in the nucleus and the cytoplasm at prophase (PubMed:1312467). Cytoplasmic when associated with SCAPER (PubMed:17698606). | |
| Protein Description | Cyclin which controls both the G1/S and the G2/M transition phases of the cell cycle. Functions through the formation of specific serine/threonine protein kinase holoenzyme complexes with the cyclin-dependent protein kinases CDK1 or CDK2. The cyclin subunit confers the substrate specificity of these complexes and differentially interacts with and activates CDK1 and CDK2 throughout the cell cycle.. | |
| Protein Sequence | MLGNSAPGPATREAGSALLALQQTALQEDQENINPEKAAPVQQPRTRAALAVLKSGNPRGLAQQQRPKTRRVAPLKDLPVNDEHVTVPPWKANSKQPAFTIHVDEAEKEAQKKPAESQKIEREDALAFNSAISLPGPRKPLVPLDYPMDGSFESPHTMDMSIILEDEKPVSVNEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNSKYHGVSLLNPPETLNL | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MLGNSAPG -------CCCCCCCC | 11.03 | 19369195 | |
| 1 | Sulfoxidation | -------MLGNSAPG -------CCCCCCCC | 11.03 | 21406390 | |
| 5 | Phosphorylation | ---MLGNSAPGPATR ---CCCCCCCCHHHH | 33.76 | 18691976 | |
| 37 | Ubiquitination | QENINPEKAAPVQQP HHCCCHHHCCCCCCC | 51.62 | 21906983 | |
| 54 | Acetylation | RAALAVLKSGNPRGL HHHHHHHHCCCCCCH | 50.12 | 19483727 | |
| 54 | Ubiquitination | RAALAVLKSGNPRGL HHHHHHHHCCCCCCH | 50.12 | 27667366 | |
| 55 | Phosphorylation | AALAVLKSGNPRGLA HHHHHHHCCCCCCHH | 39.37 | 18691976 | |
| 68 | Acetylation | LAQQQRPKTRRVAPL HHHHCCCCCCCCCCC | 57.78 | 19483727 | |
| 76 | Acetylation | TRRVAPLKDLPVNDE CCCCCCCCCCCCCCC | 57.04 | 25953088 | |
| 95 | Acetylation | PPWKANSKQPAFTIH CCCCCCCCCCCEEEE | 61.17 | 19483727 | |
| 95 | Ubiquitination | PPWKANSKQPAFTIH CCCCCCCCCCCEEEE | 61.17 | 33845483 | |
| 112 | Acetylation | EAEKEAQKKPAESQK HHHHHHHHCHHHHHC | 68.70 | 20074040 | |
| 146 | Phosphorylation | KPLVPLDYPMDGSFE CCCCCCCCCCCCCCC | 14.24 | 18691976 | |
| 151 | Phosphorylation | LDYPMDGSFESPHTM CCCCCCCCCCCCCEE | 22.90 | 18691976 | |
| 154 | Phosphorylation | PMDGSFESPHTMDMS CCCCCCCCCCEEEEE | 21.70 | 26074081 | |
| 157 | Phosphorylation | GSFESPHTMDMSIIL CCCCCCCEEEEEEEE | 20.46 | 26074081 | |
| 192 | Ubiquitination | YLREMEVKCKPKVGY HHHHCHHCCCCCCCC | 24.20 | 29967540 | |
| 209 | Phosphorylation | KQPDITNSMRAILVD CCCCCCHHHHHHHHH | 10.86 | - | |
| 225 | Phosphorylation | LVEVGEEYKLQNETL HHHCCHHHCCCCCHH | 16.82 | - | |
| 244 | Phosphorylation | NYIDRFLSSMSVLRG HHHHHHHHHHHHHHH | 22.68 | - | |
| 271 | Phosphorylation | ASKFEEIYPPEVAEF HHHCHHHCCHHHEEE | 18.93 | 23401153 | |
| 280 | Phosphorylation | PEVAEFVYITDDTYT HHHEEEEEEECCCCC | 11.92 | 23401153 | |
| 282 | Phosphorylation | VAEFVYITDDTYTKK HEEEEEEECCCCCHH | 15.33 | 23401153 | |
| 285 | Phosphorylation | FVYITDDTYTKKQVL EEEEECCCCCHHHHH | 35.58 | 23401153 | |
| 286 | Phosphorylation | VYITDDTYTKKQVLR EEEECCCCCHHHHHH | 24.45 | 23401153 | |
| 287 | Phosphorylation | YITDDTYTKKQVLRM EEECCCCCHHHHHHH | 33.58 | 23401153 | |
| 331 | Phosphorylation | PANCKVESLAMFLGE CCCCCHHHHHHHHHH | 25.15 | 23607784 | |
| 340 | Phosphorylation | AMFLGELSLIDADPY HHHHHHHHCCCCCHH | 20.98 | 23607784 | |
| 347 | Phosphorylation | SLIDADPYLKYLPSV HCCCCCHHHHHHHHH | 19.17 | 23607784 | |
| 375 | Phosphorylation | TGQSWPESLIRKTGY HCCCCCHHHHHHHCC | 25.64 | 24719451 | |
| 388 | Ubiquitination | GYTLESLKPCLMDLH CCCHHHHHHHHHHHH | 42.86 | 29967540 | |
| 400 | Ubiquitination | DLHQTYLKAPQHAQQ HHHHHHHHCHHHHHH | 47.83 | 29967540 | |
| 413 | Phosphorylation | QQSIREKYKNSKYHG HHHHHHHHHCCCCCC | 15.62 | 25690035 | |
| 416 | Phosphorylation | IREKYKNSKYHGVSL HHHHHHCCCCCCCCC | 30.36 | 25690035 | |
| 417 | Ubiquitination | REKYKNSKYHGVSLL HHHHHCCCCCCCCCC | 51.14 | 29967540 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 154 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | FZR1 | Q9UM11 | PMID:18485873 |
| - | K | Ubiquitination | E3 ubiquitin ligase | CDC20 | Q12834 | PMID:19826003 |
| - | K | Ubiquitination | E3 ubiquitin ligase | SKP2 | Q13309 | PMID:24658274 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CCNA2_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 CCNA2_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 |
| "Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-55, AND MASSSPECTROMETRY. | |
