| UniProt ID | 2ABD_HUMAN | |
|---|---|---|
| UniProt AC | Q66LE6 | |
| Protein Name | Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform | |
| Gene Name | PPP2R2D | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 453 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | B regulatory subunit of protein phosphatase 2A (PP2A) that plays a key role in cell cycle by controlling mitosis entry and exit. The activity of PP2A complexes containing PPP2R2D (PR55-delta) fluctuate during the cell cycle: the activity is high in interphase and low in mitosis. During mitosis, activity of PP2A is inhibited via interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the PP2A complexes, the B regulatory subunits modulate substrate selectivity and catalytic activity, and also may direct the localization of the catalytic enzyme to a particular subcellular compartment (By similarity).. | |
| Protein Sequence | MAGAGGGGCPAGGNDFQWCFSQVKGAIDEDVAEADIISTVEFNYSGDLLATGDKGGRVVIFQREQENKSRPHSRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQNAAHFLLSTNDKTIKLWKISERDKRAEGYNLKDEDGRLRDPFRITALRVPILKPMDLMVEASPRRIFANAHTYHINSISVNSDHETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAEFHPHQCNVFVYSSSKGTIRLCDMRSSALCDRHSKFFEEPEDPSSRSFFSEIISSISDVKFSHSGRYMMTRDYLSVKVWDLNMESRPVETHQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSAIMTGSYNNFFRMFDRDTRRDVTLEASRESSKPRASLKPRKVCTGGKRRKDEISVDSLDFNKKILHTAWHPVDNVIAVAATNNLYIFQDKIN | |
| 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 |
|---|---|---|---|---|---|
| 94 | Ubiquitination | EPEFDYLKSLEIEEK CCCCCCHHHHCHHHH | 46.92 | 21906983 | |
| 101 | Ubiquitination | KSLEIEEKINKIRWL HHHCHHHHHHHCEEC | 38.50 | - | |
| 104 | Ubiquitination | EIEEKINKIRWLPQQ CHHHHHHHCEECCCC | 36.80 | - | |
| 108 | Ubiquitination | KINKIRWLPQQNAAH HHHHCEECCCCCHHH | 1.65 | - | |
| 126 | Ubiquitination | STNDKTIKLWKISER CCCCCEEEEEEECHH | 54.23 | - | |
| 129 | Ubiquitination | DKTIKLWKISERDKR CCEEEEEEECHHHHH | 46.95 | - | |
| 133 | Ubiquitination | KLWKISERDKRAEGY EEEEECHHHHHCCCC | 48.21 | - | |
| 143 | Ubiquitination | RAEGYNLKDEDGRLR HCCCCCCCCCCCCCC | 56.27 | - | |
| 156 | Phosphorylation | LRDPFRITALRVPIL CCCCEEEEEEECCCC | 18.51 | 24719451 | |
| 173 | Phosphorylation | MDLMVEASPRRIFAN HHEEEECCCCEEEEC | 12.87 | 21815630 | |
| 173 | Ubiquitination | MDLMVEASPRRIFAN HHEEEECCCCEEEEC | 12.87 | - | |
| 176 | Phosphorylation | MVEASPRRIFANAHT EEECCCCEEEECCEE | 31.59 | - | |
| 236 | Phosphorylation | EELTEVITAAEFHPH HHHHHHHHHHHCCHH | 25.62 | 23879269 | |
| 246 | Ubiquitination | EFHPHQCNVFVYSSS HCCHHHCEEEEEECC | 24.56 | - | |
| 250 | Phosphorylation | HQCNVFVYSSSKGTI HHCEEEEEECCCCEE | 7.44 | - | |
| 258 | Ubiquitination | SSSKGTIRLCDMRSS ECCCCEEEEECCCCH | 29.15 | - | |
| 272 | Phosphorylation | SALCDRHSKFFEEPE HHHCHHHHHHCCCCC | 31.86 | 23403867 | |
| 273 | Ubiquitination | ALCDRHSKFFEEPED HHCHHHHHHCCCCCC | 48.20 | 21906983 | |
| 282 | Phosphorylation | FEEPEDPSSRSFFSE CCCCCCCCCHHHHHH | 51.18 | 23403867 | |
| 285 | Phosphorylation | PEDPSSRSFFSEIIS CCCCCCHHHHHHHHH | 32.37 | - | |
| 305 | Phosphorylation | KFSHSGRYMMTRDYL EECCCCCEEEECCEE | 8.51 | - | |
| 308 | Phosphorylation | HSGRYMMTRDYLSVK CCCCEEEECCEEEEE | 12.12 | - | |
| 341 | Phosphorylation | YLRSKLCSLYENDCI HHHHHHHHHHCCCCC | 44.41 | 27251275 | |
| 384 | Phosphorylation | RDTRRDVTLEASRES CCCCCCEEHHHHHHC | 24.14 | 29083192 | |
| 388 | Phosphorylation | RDVTLEASRESSKPR CCEEHHHHHHCCCCC | 27.49 | 29083192 | |
| 391 | Phosphorylation | TLEASRESSKPRASL EHHHHHHCCCCCCCC | 42.42 | 29083192 | |
| 392 | Phosphorylation | LEASRESSKPRASLK HHHHHHCCCCCCCCC | 41.76 | 29083192 | |
| 408 | Acetylation | RKVCTGGKRRKDEIS CCCCCCCCCCCCCCE | 50.83 | 22362477 | |
| 415 | Phosphorylation | KRRKDEISVDSLDFN CCCCCCCEEECCCCC | 20.16 | 25159151 | |
| 423 | Ubiquitination | VDSLDFNKKILHTAW EECCCCCHHHHHHHC | 40.98 | 21906983 |
| 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 2ABD_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 2ABD_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 2ABD_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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