GDPD1_HUMAN - dbPTM
GDPD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDPD1_HUMAN
UniProt AC Q8N9F7
Protein Name Lysophospholipase D GDPD1 {ECO:0000305}
Gene Name GDPD1 {ECO:0000312|HGNC:HGNC:20883}
Organism Homo sapiens (Human).
Sequence Length 314
Subcellular Localization Cytoplasm . Membrane
Multi-pass membrane protein . Cytoplasm, perinuclear region . Concentrated at the perinuclear region and the cell periphery (PubMed:18991142).
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), lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine (lyso-PC). May be involved in bioactive N-acylethanolamine biosynthesis. Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine..
Protein Sequence MSSTAAFYLLSTLGGYLVTSFLLLKYPTLLHQRKKQRFLSKHISHRGGAGENLENTMAAFQHAVKIGTDMLELDCHITKDEQVVVSHDENLKRATGVNVNISDLKYCELPPYLGKLDVSFQRACQCEGKDNRIPLLKEVFEAFPNTPINIDIKVNNNVLIKKVSELVKRYNREHLTVWGNANYEIVEKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHTMSRSQKFLIWLSDLLLMRKALFDHLTARGIQVYIWVLNEEQEYKRAFDLGATGVMTDYPTKLRDFLHNFSA
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
41UbiquitinationKKQRFLSKHISHRGG
HHHHHHHHHCCCCCC		47.2922817900
41 (in isoform 3)Ubiquitination-47.2921890473
41 (in isoform 2)Ubiquitination-47.2921890473
41 (in isoform 1)Ubiquitination-47.2921890473
65UbiquitinationAAFQHAVKIGTDMLE
HHHHHHHHHCCCCEE		35.8832015554
79UbiquitinationELDCHITKDEQVVVS
EEEEECCCCCCEEEC		59.6832015554
92 (in isoform 3)Ubiquitination-52.1221890473
92 (in isoform 2)Ubiquitination-52.1221890473
92 (in isoform 1)Ubiquitination-52.1221890473
92UbiquitinationVSHDENLKRATGVNV
ECCCCCCHHHCCCCC		52.1221906983
105AcetylationNVNISDLKYCELPPY
CCCHHHCCCCCCCCC		53.5025038526
105UbiquitinationNVNISDLKYCELPPY
CCCHHHCCCCCCCCC		53.5032015554
129UbiquitinationRACQCEGKDNRIPLL
HHHCCCCCCCCCHHH		29.54-
211UbiquitinationRVLLILGLFFTGLLP
HHHHHHHHHHHCCCC		2.6022817900
243PhosphorylationLKLKEPHTMSRSQKF
EEECCCCCCCHHHHH		27.7924719451
295PhosphorylationRAFDLGATGVMTDYP
HHHCCCCCCCCCCCC		28.6323663014
299PhosphorylationLGATGVMTDYPTKLR
CCCCCCCCCCCHHHH		29.9423663014
301PhosphorylationATGVMTDYPTKLRDF
CCCCCCCCCHHHHHH		12.0223663014
303PhosphorylationGVMTDYPTKLRDFLH
CCCCCCCHHHHHHHH		36.1623663014
304UbiquitinationVMTDYPTKLRDFLHN
CCCCCCHHHHHHHHH		36.7022817900
304 (in isoform 1)Ubiquitination-36.7021890473
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 GDPD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDPD1_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 GDPD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRFE_HUMANTFphysical
26186194
CO3_HUMANC3physical
26186194
ALBU_HUMANALBphysical
26186194
AACT_HUMANSERPINA3physical
26186194
ITIH2_HUMANITIH2physical
26186194
APOA1_HUMANAPOA1physical
26186194
A2MG_HUMANA2Mphysical
26186194
CERU_HUMANCPphysical
26186194
HPT_HUMANHPphysical
26186194
A1AT_HUMANSERPINA1physical
26186194
CFAB_HUMANCFBphysical
26186194
HBD_HUMANHBDphysical
26186194
HBB_HUMANHBBphysical
26186194
APOA2_HUMANAPOA2physical
26186194
FETUA_HUMANAHSGphysical
26186194
HEMO_HUMANHPXphysical
26186194
A1BG_HUMANA1BGphysical
26186194
CO4A_HUMANC4Aphysical
26186194
A1AG2_HUMANORM2physical
26186194
A1AG1_HUMANORM1physical
26186194
KNG1_HUMANKNG1physical
26186194
APOA1_HUMANAPOA1physical
28514442
HBB_HUMANHBBphysical
28514442
CERU_HUMANCPphysical
28514442
CO3_HUMANC3physical
28514442
HPT_HUMANHPphysical
28514442
A1BG_HUMANA1BGphysical
28514442
A1AG1_HUMANORM1physical
28514442
HEMO_HUMANHPXphysical
28514442
A1AG2_HUMANORM2physical
28514442
ITIH2_HUMANITIH2physical
28514442
HBD_HUMANHBDphysical
28514442
FETUA_HUMANAHSGphysical
28514442
TRFE_HUMANTFphysical
28514442
CO4A_HUMANC4Aphysical
28514442
KNG1_HUMANKNG1physical
28514442
A2MG_HUMANA2Mphysical
28514442
A1AT_HUMANSERPINA1physical
28514442
CFAB_HUMANCFBphysical
28514442
AACT_HUMANSERPINA3physical
28514442
ALBU_HUMANALBphysical
28514442
APOA2_HUMANAPOA2physical
28514442
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 GDPD1_HUMAN

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Related Literatures of Post-Translational Modification

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