| UniProt ID | PDIP2_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y2S7 | |
| Protein Name | Polymerase delta-interacting protein 2 | |
| Gene Name | POLDIP2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 368 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | ||
| Protein Sequence | MAACTARRALAVGSRWWSRSLTGARWPRPLCAAAGAGAFSPASTTTTRRHLSSRNRPEGKVLETVGVFEVPKQNGKYETGQLFLHSIFGYRGVVLFPWQARLYDRDVASAAPEKAENPAGHGSKEVKGKTHTYYQVLIDARDCPHISQRSQTEAVTFLANHDDSRALYAIPGLDYVSHEDILPYTSTDQVPIQHELFERFLLYDQTKAPPFVARETLRAWQEKNHPWLELSDVHRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLSKEQPAFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLESNKDEKTPPSGLHW | |
| 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 |
|---|---|---|---|---|---|
| 14 | Phosphorylation | RRALAVGSRWWSRSL HHHHHCCCCHHHCCC | 20.37 | 29514088 | |
| 18 | Phosphorylation | AVGSRWWSRSLTGAR HCCCCHHHCCCCCCC | 12.67 | 29514088 | |
| 44 | Phosphorylation | GAFSPASTTTTRRHL CCCCCCCCHHHHHHH | 30.21 | 29116813 | |
| 103 | Phosphorylation | FPWQARLYDRDVASA EEEHHHCCCHHHHHC | 11.90 | - | |
| 123 | Phosphorylation | ENPAGHGSKEVKGKT CCCCCCCCCCCCCCE | 21.70 | - | |
| 129 | Malonylation | GSKEVKGKTHTYYQV CCCCCCCCEEEEEEE | 31.26 | 26320211 | |
| 132 | Phosphorylation | EVKGKTHTYYQVLID CCCCCEEEEEEEEEE | 29.20 | 29496907 | |
| 133 | Phosphorylation | VKGKTHTYYQVLIDA CCCCEEEEEEEEEEC | 5.58 | 29496907 | |
| 143 | S-nitrosylation | VLIDARDCPHISQRS EEEECCCCCCCCCCC | 1.89 | 19483679 | |
| 143 | S-nitrosocysteine | VLIDARDCPHISQRS EEEECCCCCCCCCCC | 1.89 | - | |
| 218 | Methylation | FVARETLRAWQEKNH CHHHHHHHHHHHHCC | 41.00 | 115488063 | |
| 223 | Ubiquitination | TLRAWQEKNHPWLEL HHHHHHHHCCCCEEH | 45.51 | 21890473 | |
| 288 | Phosphorylation | ERHWRIFSLSGTLET HHCEEEEEEECEEEE | 21.18 | 30266825 | |
| 290 | Phosphorylation | HWRIFSLSGTLETVR CEEEEEEECEEEEEC | 28.65 | 30266825 | |
| 292 | Phosphorylation | RIFSLSGTLETVRGR EEEEEECEEEEECCC | 20.32 | 19664994 | |
| 295 | Phosphorylation | SLSGTLETVRGRGVV EEECEEEEECCCCCC | 20.72 | 27794612 | |
| 364 | Phosphorylation | KDEKTPPSGLHW--- CCCCCCCCCCCC--- | 56.01 | 27251275 |
| 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 PDIP2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PDIP2_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 PDIP2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PCNA_HUMAN | PCNA | physical | 12522211 | |
| A4_HUMAN | APP | physical | 21832049 | |
| CLPX_HUMAN | CLPX | physical | 28561026 | |
| NT5D2_HUMAN | NT5DC2 | physical | 28561026 | |
| PDIP2_HUMAN | POLDIP2 | physical | 28561026 |
| 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 |
| "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 THR-292, AND MASSSPECTROMETRY. | |