UniProt ID | DCA16_HUMAN | |
---|---|---|
UniProt AC | Q9NXF7 | |
Protein Name | DDB1- and CUL4-associated factor 16 | |
Gene Name | DCAF16 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 216 | |
Subcellular Localization | ||
Protein Description | May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.. | |
Protein Sequence | MGPRNPSPDHLSESESEEEENISYLNESSGEEWDSSEEEDSMVPNLSPLESLAWQVKCLLKYSTTWKPLNPNSWLYHAKLLDPSTPVHILREIGLRLSHCSHCVPKLEPIPEWPPLASCGVPPFQKPLTSPSRLSRDHATLNGALQFATKQLSRTLSRATPIPEYLKQIPNSCVSGCCCGWLTKTVKETTRTEPINTTYSYTDFQKAVNKLLTASL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
61 | Acetylation | WQVKCLLKYSTTWKP HHHHHHHHCCCCCCC | 24.98 | 19608861 | |
79 | Ubiquitination | NSWLYHAKLLDPSTP CCEEEEEECCCCCCC | 35.95 | - | |
79 | Ubiquitination | NSWLYHAKLLDPSTP CCEEEEEECCCCCCC | 35.95 | 23000965 | |
85 | Phosphorylation | AKLLDPSTPVHILRE EECCCCCCCHHHHHH | 34.42 | - | |
129 | Phosphorylation | PPFQKPLTSPSRLSR CCCCCCCCCHHHHCC | 47.31 | 27067055 | |
130 | Phosphorylation | PFQKPLTSPSRLSRD CCCCCCCCHHHHCCC | 28.67 | 27067055 | |
135 | Phosphorylation | LTSPSRLSRDHATLN CCCHHHHCCCCHHHH | 34.25 | 26657352 | |
150 | Ubiquitination | GALQFATKQLSRTLS HHHHHHHHHHHHHHH | 45.90 | 21890473 | |
150 | Ubiquitination | GALQFATKQLSRTLS HHHHHHHHHHHHHHH | 45.90 | 22817900 | |
165 | Phosphorylation | RATPIPEYLKQIPNS HCCCCHHHHHHCCCC | 17.53 | 27642862 | |
167 | Ubiquitination | TPIPEYLKQIPNSCV CCCHHHHHHCCCCCH | 45.33 | 22505724 | |
187 | Ubiquitination | GWLTKTVKETTRTEP HHHHHCCCCCCCCCC | 55.35 | 29967540 | |
192 | Phosphorylation | TVKETTRTEPINTTY CCCCCCCCCCCCCCE | 43.98 | 24043423 | |
197 | Phosphorylation | TRTEPINTTYSYTDF CCCCCCCCCEEHHHH | 28.03 | 24043423 | |
198 | Phosphorylation | RTEPINTTYSYTDFQ CCCCCCCCEEHHHHH | 13.14 | 24043423 | |
199 | Phosphorylation | TEPINTTYSYTDFQK CCCCCCCEEHHHHHH | 9.53 | 27642862 | |
200 | Phosphorylation | EPINTTYSYTDFQKA CCCCCCEEHHHHHHH | 21.33 | 24043423 | |
201 | Phosphorylation | PINTTYSYTDFQKAV CCCCCEEHHHHHHHH | 10.42 | 24043423 | |
202 | Phosphorylation | INTTYSYTDFQKAVN CCCCEEHHHHHHHHH | 25.13 | 24043423 | |
206 | Ubiquitination | YSYTDFQKAVNKLLT EEHHHHHHHHHHHHH | 55.05 | 21906983 | |
210 | Ubiquitination | DFQKAVNKLLTASL- HHHHHHHHHHHHCC- | 37.97 | 22817900 |
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 DCA16_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DCA16_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 DCA16_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ANM1_HUMAN | PRMT1 | physical | 23455924 | |
ANM6_HUMAN | PRMT6 | physical | 23455924 | |
DDB1_HUMAN | DDB1 | physical | 16949367 | |
CUL4A_HUMAN | CUL4A | physical | 16949367 |
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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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND MASS SPECTROMETRY. |