UniProt ID | PDCL3_HUMAN | |
---|---|---|
UniProt AC | Q9H2J4 | |
Protein Name | Phosducin-like protein 3 | |
Gene Name | PDCL3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 239 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, controlling its abundance and inhibiting its ubiquitination and degradation. Modulates the activation of caspases during apoptosis. Is a substrate for Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV) IAP-mediated ubiquitination.. | |
Protein Sequence | MQDPNADTEWNDILRKKGILPPKESLKELEEEAEEEQRILQQSVVKTYEDMTLEELEDHEDEFNEEDERAIEMYRRRRLAEWKATKLKNKFGEVLEISGKDYVQEVTKAGEGLWVILHLYKQGIPLCALINQHLSGLARKFPDVKFIKAISTTCIPNYPDRNLPTIFVYLEGDIKAQFIGPLVFGGMNLTRDELEWKLSESGAIMTDLEENPKKPIEDVLLSSVRRSVLMKRDSDSEGD | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MQDPNADT -------CCCCCCCC | 10.33 | 26059764 | |
17 | Ubiquitination | WNDILRKKGILPPKE HHHHHHHCCCCCCHH | 44.76 | 24816145 | |
25 | Phosphorylation | GILPPKESLKELEEE CCCCCHHHHHHHHHH | 51.36 | 24719451 | |
27 | Ubiquitination | LPPKESLKELEEEAE CCCHHHHHHHHHHHH | 70.32 | 32015554 | |
33 | Phosphorylation | LKELEEEAEEEQRIL HHHHHHHHHHHHHHH | 32.55 | 32645325 | |
40 | Ubiquitination | AEEEQRILQQSVVKT HHHHHHHHHHHHHHH | 4.06 | 21890473 | |
43 | Phosphorylation | EQRILQQSVVKTYED HHHHHHHHHHHHHHC | 18.86 | 25159151 | |
47 | Phosphorylation | LQQSVVKTYEDMTLE HHHHHHHHHHCCCHH | 22.12 | 28796482 | |
48 | Phosphorylation | QQSVVKTYEDMTLEE HHHHHHHHHCCCHHH | 12.29 | 28796482 | |
52 | Phosphorylation | VKTYEDMTLEELEDH HHHHHCCCHHHHHHC | 43.25 | 29978859 | |
83 | Ubiquitination | RRRLAEWKATKLKNK HHHHHHHHHHHHHHH | 37.37 | 32015554 | |
90 | Acetylation | KATKLKNKFGEVLEI HHHHHHHHHCCEEEE | 53.83 | 27452117 | |
90 | Ubiquitination | KATKLKNKFGEVLEI HHHHHHHHHCCEEEE | 53.83 | 21890473 | |
205 | Sulfoxidation | LSESGAIMTDLEENP HCCCCCCCCCCHHCC | 2.06 | 21406390 | |
206 | Phosphorylation | SESGAIMTDLEENPK CCCCCCCCCCHHCCC | 31.18 | - | |
222 | Phosphorylation | PIEDVLLSSVRRSVL CHHHHHHHHHHHHHH | 23.72 | 24719451 | |
223 | Phosphorylation | IEDVLLSSVRRSVLM HHHHHHHHHHHHHHH | 21.44 | 28857561 | |
227 | Phosphorylation | LLSSVRRSVLMKRDS HHHHHHHHHHHCCCC | 14.72 | 23403867 | |
231 | Acetylation | VRRSVLMKRDSDSEG HHHHHHHCCCCCCCC | 49.22 | 30591189 | |
234 | Phosphorylation | SVLMKRDSDSEGD-- HHHHCCCCCCCCC-- | 47.25 | 28355574 | |
236 | Phosphorylation | LMKRDSDSEGD---- HHCCCCCCCCC---- | 47.64 | 23927012 |
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 PDCL3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PDCL3_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 PDCL3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TCPG_HUMAN | CCT3 | physical | 26344197 | |
TCPZ_HUMAN | CCT6A | physical | 26344197 | |
TCPH_HUMAN | CCT7 | physical | 26344197 | |
TCPQ_HUMAN | CCT8 | physical | 26344197 |
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 |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-234 AND SER-236,AND MASS SPECTROMETRY. | |
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, ANDMASS SPECTROMETRY. |