GDPD3_HUMAN - dbPTM
GDPD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSLLLYYAL
------CCHHHHHHH
27.9424043423
6Phosphorylation--MSLLLYYALPALG
--CCHHHHHHHHHHH
6.1524043423
7Phosphorylation-MSLLLYYALPALGS
-CCHHHHHHHHHHHH
11.1324043423
14PhosphorylationYALPALGSYAMLSIF
HHHHHHHHHHHHHHH
15.5724043423
15PhosphorylationALPALGSYAMLSIFF
HHHHHHHHHHHHHHH
8.3324043423
19PhosphorylationLGSYAMLSIFFLRRP
HHHHHHHHHHHHHCC
12.3124043423
31PhosphorylationRRPHLLHTPRAPTFR
HCCCHHCCCCCCEEE
17.9124043423
102PhosphorylationGLNRDVGSLDFEDLP
CCCCCCCCCCCCCCC
25.3121406692
111PhosphorylationDFEDLPLYKEKLEVY
CCCCCCCHHHEEEEE
18.3721406692
128PhosphorylationPGHFAHGSDRRMVRL
CCCCCCCCCCCEEEH
20.34-
145PhosphorylationLFQRFPRTPMSVEIK
HHHHCCCCCCEEEEC
24.4720071362
154UbiquitinationMSVEIKGKNEELIRE
CEEEECCCCHHHHHH
57.0733845483
169PhosphorylationIAGLVRRYDRNEITI
HHHHHHHHCCCCEEE
14.5319702290
175PhosphorylationRYDRNEITIWASEKS
HHCCCCEEEEECCCC
12.3219702290
179PhosphorylationNEITIWASEKSSVMK
CCEEEEECCCCHHHH
30.4719702290
200PhosphorylationPEMPLSFTISRGFWV
CCCCEEEEEHHHHHH
18.0522210691
262PhosphorylationKWLIMRKSLIRHLEE
HHHHHHHHHHHHHHH
20.7524719451
300PhosphorylationATGVITDYPTALRHY
CCEEECCHHHHHHHH
8.2022210691
302PhosphorylationGVITDYPTALRHYLD
EEECCHHHHHHHHHH
31.9022210691

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDPD3_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GDPD3_HUMAN !!

Drug and Disease Associations
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.
Regulatory Network of GDPD3_HUMAN

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Related Literatures of Post-Translational Modification

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