| UniProt ID | DCTD_HUMAN | |
|---|---|---|
| UniProt AC | P32321 | |
| Protein Name | Deoxycytidylate deaminase | |
| Gene Name | DCTD | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 178 | |
| Subcellular Localization | ||
| Protein Description | Supplies the nucleotide substrate for thymidylate synthetase.. | |
| Protein Sequence | MSEVSCKKRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVNSENKIVGIGYNGMPNGCSDDVLPWRRTAENKLDTKYPYVCHAELNAIMNKNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDSDEATAARLLFNMAGVTFRKFIPKCSKIVIDFDSINSRPSQKLQ | |
| 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 |
|---|---|---|---|---|---|
| 7 | Ubiquitination | -MSEVSCKKRDDYLE -CCCCCCCCCCCCCC | 43.25 | 33845483 | |
| 12 | Phosphorylation | SCKKRDDYLEWPEYF CCCCCCCCCCCHHHH | 15.71 | 20736484 | |
| 16 (in isoform 2) | Phosphorylation | - | 19.62 | 29507054 | |
| 18 | Ubiquitination | DYLEWPEYFMAVAFL CCCCCHHHHHHHHHH | 8.45 | 33845483 | |
| 31 | Ubiquitination | FLSAQRSKDPNSQVG HHHHHHCCCCCCCCE | 78.41 | 33845483 | |
| 35 | Phosphorylation | QRSKDPNSQVGACIV HHCCCCCCCCEEEEE | 31.47 | 27282143 | |
| 42 (in isoform 2) | Ubiquitination | - | 6.93 | - | |
| 42 | Ubiquitination | SQVGACIVNSENKIV CCCEEEEECCCCCEE | 6.93 | 33845483 | |
| 74 | Acetylation | WRRTAENKLDTKYPY CHHHHCCCCCCCCCE | 38.96 | 22424773 | |
| 77 | Phosphorylation | TAENKLDTKYPYVCH HHCCCCCCCCCEEEH | 42.80 | - | |
| 79 | Phosphorylation | ENKLDTKYPYVCHAE CCCCCCCCCEEEHHH | 11.24 | 19060867 | |
| 91 | Sulfoxidation | HAELNAIMNKNSTDV HHHHHHHHCCCCCCC | 5.62 | 30846556 | |
| 131 | Malonylation | EVIFMSDKYHDSDEA EEEEECCCCCCCCHH | 36.86 | 26320211 | |
| 131 | Acetylation | EVIFMSDKYHDSDEA EEEEECCCCCCCCHH | 36.86 | 23236377 | |
| 168 | Phosphorylation | KIVIDFDSINSRPSQ EEEEEHHHHCCCCCC | 24.54 | 23186163 | |
| 171 | Phosphorylation | IDFDSINSRPSQKLQ EEHHHHCCCCCCCCC | 43.85 | 23186163 | |
| 174 | Phosphorylation | DSINSRPSQKLQ--- HHHCCCCCCCCC--- | 38.55 | 23186163 |
| 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 DCTD_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DCTD_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 DCTD_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| LNX1_HUMAN | LNX1 | physical | 16189514 | |
| CEP76_HUMAN | CEP76 | physical | 16189514 | |
| NUD18_HUMAN | NUDT18 | physical | 16189514 | |
| NIF3L_HUMAN | NIF3L1 | physical | 16189514 | |
| DCTD_HUMAN | DCTD | physical | 16189514 | |
| DCTD_HUMAN | DCTD | physical | 21988832 | |
| FGF12_HUMAN | FGF12 | physical | 25416956 | |
| SDCB1_HUMAN | SDCBP | physical | 25416956 | |
| THIOM_HUMAN | TXN2 | physical | 25416956 | |
| GORS2_HUMAN | GORASP2 | physical | 25416956 | |
| MASU1_HUMAN | MALSU1 | physical | 25416956 | |
| NGRN_HUMAN | NGRN | physical | 26496610 |
| 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 | |
| DB00987 | Cytarabine |
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| Phosphorylation | |
| Reference | PubMed |
| "Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-79, AND MASSSPECTROMETRY. | |