UniProt ID | GDPD3_HUMAN | |
---|---|---|
UniProt AC | Q7L5L3 | |
Protein Name | Lysophospholipase D GDPD3 {ECO:0000305} | |
Gene Name | GDPD3 {ECO:0000312|HGNC:HGNC:28638} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 318 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . Cytoplasm, perinuclear region . Endoplasmic reticulum . Partially co-localized with CANX. |
|
Protein Description | Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines. Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) and lysophosphatidylcholine (lyso-PC), and to a lesser extent for lysophosphatidylethanolamine (lyso-PE). Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine.. | |
Protein Sequence | MSLLLYYALPALGSYAMLSIFFLRRPHLLHTPRAPTFRIRLGAHRGGSGELLENTMEAMENSMAQRSDLLELDCQLTRDRVVVVSHDENLCRQSGLNRDVGSLDFEDLPLYKEKLEVYFSPGHFAHGSDRRMVRLEDLFQRFPRTPMSVEIKGKNEELIREIAGLVRRYDRNEITIWASEKSSVMKKCKAANPEMPLSFTISRGFWVLLSYYLGLLPFIPIPEKFFFCFLPNIINRTYFPFSCSCLNQLLAVVSKWLIMRKSLIRHLEERGVQVVFWCLNEESDFEAAFSVGATGVITDYPTALRHYLDNHGPAARTS | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSLLLYYAL ------CCHHHHHHH | 27.94 | 24043423 | |
6 | Phosphorylation | --MSLLLYYALPALG --CCHHHHHHHHHHH | 6.15 | 24043423 | |
7 | Phosphorylation | -MSLLLYYALPALGS -CCHHHHHHHHHHHH | 11.13 | 24043423 | |
14 | Phosphorylation | YALPALGSYAMLSIF HHHHHHHHHHHHHHH | 15.57 | 24043423 | |
15 | Phosphorylation | ALPALGSYAMLSIFF HHHHHHHHHHHHHHH | 8.33 | 24043423 | |
19 | Phosphorylation | LGSYAMLSIFFLRRP HHHHHHHHHHHHHCC | 12.31 | 24043423 | |
31 | Phosphorylation | RRPHLLHTPRAPTFR HCCCHHCCCCCCEEE | 17.91 | 24043423 | |
102 | Phosphorylation | GLNRDVGSLDFEDLP CCCCCCCCCCCCCCC | 25.31 | 21406692 | |
111 | Phosphorylation | DFEDLPLYKEKLEVY CCCCCCCHHHEEEEE | 18.37 | 21406692 | |
128 | Phosphorylation | PGHFAHGSDRRMVRL CCCCCCCCCCCEEEH | 20.34 | - | |
145 | Phosphorylation | LFQRFPRTPMSVEIK HHHHCCCCCCEEEEC | 24.47 | 20071362 | |
154 | Ubiquitination | MSVEIKGKNEELIRE CEEEECCCCHHHHHH | 57.07 | 33845483 | |
169 | Phosphorylation | IAGLVRRYDRNEITI HHHHHHHHCCCCEEE | 14.53 | 19702290 | |
175 | Phosphorylation | RYDRNEITIWASEKS HHCCCCEEEEECCCC | 12.32 | 19702290 | |
179 | Phosphorylation | NEITIWASEKSSVMK CCEEEEECCCCHHHH | 30.47 | 19702290 | |
200 | Phosphorylation | PEMPLSFTISRGFWV CCCCEEEEEHHHHHH | 18.05 | 22210691 | |
262 | Phosphorylation | KWLIMRKSLIRHLEE HHHHHHHHHHHHHHH | 20.75 | 24719451 | |
300 | Phosphorylation | ATGVITDYPTALRHY CCEEECCHHHHHHHH | 8.20 | 22210691 | |
302 | Phosphorylation | GVITDYPTALRHYLD EEECCHHHHHHHHHH | 31.90 | 22210691 |
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 GDPD3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GDPD3_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 GDPD3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of GDPD3_HUMAN !! |
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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