UniProt ID | PLD3_HUMAN | |
---|---|---|
UniProt AC | Q8IV08 | |
Protein Name | Phospholipase D3 | |
Gene Name | PLD3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 490 | |
Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type II membrane protein . |
|
Protein Description | May be involved in APP processing.. | |
Protein Sequence | MKPKLMYQELKVPAEEPANELPMNEIEAWKAAEKKARWVLLVLILAVVGFGALMTQLFLWEYGDLHLFGPNQRPAPCYDPCEAVLVESIPEGLDFPNASTGNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTQEPSAQQGEEVLRQLQTLAPKGVNVRIAVSKPSGPQPQADLQALLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARDLTKIFEAYWFLGQAGSSIPSTWPRFYDTRYNQETPMEICLNGTPALAYLASAPPPLCPSGRTPDLKALLNVVDNARSFIYVAVMNYLPTLEFSHPHRFWPAIDDGLRRATYERGVKVRLLISCWGHSEPSMRAFLLSLAALRDNHTHSDIQVKLFVVPADEAQARIPYARVNHNKYMVTERATYIGTSNWSGNYFTETAGTSLLVTQNGRGGLRSQLEAIFLRDWDSPYSHDLDTSADSVGNACRLL | |
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 |
---|---|---|---|---|---|
4 | Ubiquitination | ----MKPKLMYQELK ----CCCCCCCEECC | 40.13 | - | |
7 | Phosphorylation | -MKPKLMYQELKVPA -CCCCCCCEECCCCC | 14.85 | 21945579 | |
11 | Ubiquitination | KLMYQELKVPAEEPA CCCCEECCCCCCCCC | 45.48 | 21906983 | |
30 | Ubiquitination | MNEIEAWKAAEKKAR HHHHHHHHHHHHHHH | 44.78 | 21906983 | |
97 | N-linked_Glycosylation | PEGLDFPNASTGNPS CCCCCCCCCCCCCCC | 46.66 | 19159218 | |
132 | N-linked_Glycosylation | FYWTLTNNDTHTQEP HEEECCCCCCCCCCC | 50.77 | 19159218 | |
157 | Ubiquitination | QLQTLAPKGVNVRIA HHHHHCCCCCEEEEE | 70.64 | 21906983 | |
167 | Ubiquitination | NVRIAVSKPSGPQPQ EEEEEEECCCCCCCH | 36.28 | 21906983 | |
216 | Phosphorylation | QTHFYLGSANMDWRS CCCEEECCCCCCHHH | 17.55 | - | |
223 | Phosphorylation | SANMDWRSLTQVKEL CCCCCHHHHHHHHHH | 31.36 | 29759185 | |
225 | Phosphorylation | NMDWRSLTQVKELGV CCCHHHHHHHHHHCE | 32.34 | 29759185 | |
235 | Phosphorylation | KELGVVMYNCSCLAR HHHCEEEEEHHHHHH | 11.04 | 29759185 | |
238 | Phosphorylation | GVVMYNCSCLARDLT CEEEEEHHHHHHHHH | 14.45 | 29759185 | |
294 | O-linked_Glycosylation | PALAYLASAPPPLCP HHHHHHHCCCCCCCC | 38.42 | OGP | |
309 | Ubiquitination | SGRTPDLKALLNVVD CCCCCCHHHHHHHHH | 44.35 | 21906983 | |
380 | Phosphorylation | SMRAFLLSLAALRDN HHHHHHHHHHHHHCC | 20.36 | 29116813 | |
389 | Phosphorylation | AALRDNHTHSDIQVK HHHHCCCCCCCCEEE | 29.36 | 29116813 | |
391 | Phosphorylation | LRDNHTHSDIQVKLF HHCCCCCCCCEEEEE | 37.25 | 30206219 | |
426 | Phosphorylation | YMVTERATYIGTSNW EEEEECEEEEECCCC | 23.15 | 24719451 | |
430 | Phosphorylation | ERATYIGTSNWSGNY ECEEEEECCCCCCCC | 14.88 | 24719451 | |
434 | Phosphorylation | YIGTSNWSGNYFTET EEECCCCCCCCEECC | 22.78 | 24719451 |
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 PLD3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PLD3_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 PLD3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
HNRH3_HUMAN | HNRNPH3 | physical | 26344197 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
615711 | Alzheimer disease 19 (AD19) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97 AND ASN-132, AND MASSSPECTROMETRY. |