GPAT4_HUMAN - dbPTM
GPAT4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPAT4_HUMAN
UniProt AC Q86UL3
Protein Name Glycerol-3-phosphate acyltransferase 4 {ECO:0000312|HGNC:HGNC:20880}
Gene Name GPAT4 {ECO:0000312|HGNC:HGNC:20880}
Organism Homo sapiens (Human).
Sequence Length 456
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Active against both saturated and unsaturated long-chain fatty acyl-CoAs..
Protein Sequence MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKSLLKIFAWATLRMERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCRKGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRIALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRNGGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHLVAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAFWNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLLWDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS
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
49PhosphorylationIRKLYMKSLLKIFAW
HHHHHHHHHHHHHHH		23.5424719451
76PhosphorylationNHQLYKPYTNGIIAK
CCCCCCCCCCCCCCC		14.5321214269
77PhosphorylationHQLYKPYTNGIIAKD
CCCCCCCCCCCCCCC		35.1821214269
86PhosphorylationGIIAKDPTSLEEEIK
CCCCCCCCCHHHHHH		56.9529214152
87PhosphorylationIIAKDPTSLEEEIKE
CCCCCCCCHHHHHHH		38.8929214152
93UbiquitinationTSLEEEIKEIRRSGS
CCHHHHHHHHHHHCC		50.8229967540
98PhosphorylationEIKEIRRSGSSKALD
HHHHHHHHCCCCCCC		32.9326074081
100PhosphorylationKEIRRSGSSKALDNT
HHHHHHCCCCCCCCC		29.8826074081
101PhosphorylationEIRRSGSSKALDNTP
HHHHHCCCCCCCCCC		26.0224719451
107PhosphorylationSSKALDNTPEFELSD
CCCCCCCCCCCCHHH		24.7028464451
121UbiquitinationDIFYFCRKGMETIMD
HHHHHHHCCCCHHCC		64.8822817900
133UbiquitinationIMDDEVTKRFSAEEL
HCCHHHHHCCCHHHH		57.5322817900
136PhosphorylationDEVTKRFSAEELESW
HHHHHCCCHHHHHHC		38.5130108239
185PhosphorylationLRIALAFTGISLLVV
HHHHHHHHCCCEEEE		28.1824719451
188PhosphorylationALAFTGISLLVVGTT
HHHHHCCCEEEEECE		19.5924719451
195PhosphorylationSLLVVGTTVVGYLPN
CEEEEECEEEECCCC		13.7824719451
218PhosphorylationKHVHLMCYRICVRAL
HCHHHHHHHHHHHHH		6.7717924679
218UbiquitinationKHVHLMCYRICVRAL
HCHHHHHHHHHHHHH		6.7722817900
221UbiquitinationHLMCYRICVRALTAI
HHHHHHHHHHHHHHH		0.9422817900
223UbiquitinationMCYRICVRALTAIIT
HHHHHHHHHHHHHHH		21.3322817900
247N-linked_GlycosylationNGGICVANHTSPIDV
CCCEEECCCCCCCEE		20.69UniProtKB CARBOHYD
283UbiquitinationVIQRAMVKACPHVWF
HHHHHHHHHCCCEEE		31.05-
303UbiquitinationKDRHLVAKRLTEHVQ
CHHHHHHHHHHHHCC		40.2229967540
306PhosphorylationHLVAKRLTEHVQDKS
HHHHHHHHHHCCCCC		28.2550564005
312UbiquitinationLTEHVQDKSKLPILI
HHHHCCCCCCCCEEE		32.1929967540
3122-HydroxyisobutyrylationLTEHVQDKSKLPILI
HHHHCCCCCCCCEEE		32.19-
313O-linked_GlycosylationTEHVQDKSKLPILIF
HHHCCCCCCCCEEEC		47.9529351928
313PhosphorylationTEHVQDKSKLPILIF
HHHCCCCCCCCEEEC		47.9550564011
327N-linked_GlycosylationFPEGTCINNTSVMMF
CCCCCCCCCCEEEEE		48.12UniProtKB CARBOHYD
328N-linked_GlycosylationPEGTCINNTSVMMFK
CCCCCCCCCEEEEEE		17.51UniProtKB CARBOHYD
335AcetylationNTSVMMFKKGSFEIG
CCEEEEEECCEEECC		38.0330586789
362N-linked_GlycosylationQFGDAFWNSSKYGMV
CCCCCCCCCCHHHHH		29.92UniProtKB CARBOHYD
377PhosphorylationTYLLRMMTSWAIVCS
HHHHHHHHHHHHHHH		16.2722210691
378PhosphorylationYLLRMMTSWAIVCSV
HHHHHHHHHHHHHHH		9.1622210691
387PhosphorylationAIVCSVWYLPPMTRE
HHHHHHHHCCCCCCC		13.7446160547
392PhosphorylationVWYLPPMTREADEDA
HHHCCCCCCCCCHHH		31.0046160541
426UbiquitinationLLWDGGLKREKVKDT
HEECCCCCHHHHHHH		62.8821906983
426AcetylationLLWDGGLKREKVKDT
HEECCCCCHHHHHHH		62.8824471185
429UbiquitinationDGGLKREKVKDTFKE
CCCCCHHHHHHHCHH		59.6322817900
431UbiquitinationGLKREKVKDTFKEEQ
CCCHHHHHHHCHHHH		63.2222817900
440UbiquitinationTFKEEQQKLYSKMIV
HCHHHHHHHHHHHCC		49.4329967540
444UbiquitinationEQQKLYSKMIVGNHK
HHHHHHHHHCCCCCC		21.0629967540
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 GPAT4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPAT4_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 GPAT4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHB7_HUMANHSD17B7physical
21988832
EHD2_HUMANEHD2physical
28514442
DFNA5_HUMANDFNA5physical
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 GPAT4_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-218, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory