GPAT1_HUMAN - dbPTM
GPAT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPAT1_HUMAN
UniProt AC Q9HCL2
Protein Name Glycerol-3-phosphate acyltransferase 1, mitochondrial
Gene Name GPAM
Organism Homo sapiens (Human).
Sequence Length 828
Subcellular Localization Mitochondrion outer 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..
Protein Sequence MDESALTLGTIDVSYLPHSSEYSVGRCKHTSEEWGECGFRPTIFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKRILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDVLYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNVIPDILIIPVGISYDRIIEGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSALLSLEQALLPAILPSRPSDAADEGRDTSINESRNATDESLRRRLIANLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCVTITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLNKRGLGGPTSTPPNLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQVCHETVGKFIQYGILTVAEHDDQEDISPSLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAIFVHNFSGPVPEPEYLQKLHKYLITRTERNVAVYAESATYCLVKNAVKMFKDIGVFKETKQKRVSVLELSSTFLPQCNRQKLLEYILSFVVL
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
54PhosphorylationATLKWKESLMSRKRP
CCHHHHHHHHHCCCC		26.1628555341
57PhosphorylationKWKESLMSRKRPFVG
HHHHHHHHCCCCCCC		39.69-
111PhosphorylationWLARRLSYVLFIQER
HHHHHHHEEEEEEHH		13.0317924679
136PhosphorylationVTENVLNSSRVQEAI
CCHHHHCCHHHHHHH		18.5027251275
161UbiquitinationGSAQQQSKAVNKVKK
CCHHHHHHHHHHHHH		52.6021906983
292PhosphorylationDGRKDVLYRALLHGH
CCCHHHHHHHHHCHH		8.1622468782
333PhosphorylationCARAGLLSVVVDTLS
HHHHHHHHHHHHHCC		20.22-
338PhosphorylationLLSVVVDTLSTNVIP
HHHHHHHHCCCCCCC		15.82-
340PhosphorylationSVVVDTLSTNVIPDI
HHHHHHCCCCCCCCE		21.74-
377PhosphorylationGKPKKNESLWSVARG
CCCCCCHHHHHHHHH		44.5223403867
380PhosphorylationKKNESLWSVARGVIR
CCCHHHHHHHHHHHH		15.9323403867
391AcetylationGVIRMLRKNYGCVRV
HHHHHHHHHCCEEEE		51.037481533
409PhosphorylationQPFSLKEYLESQSQK
CCCCHHHHHHHCCCC		17.74-
438PhosphorylationAILPSRPSDAADEGR
HHCCCCCCCCCCCCC		38.4824275569
447PhosphorylationAADEGRDTSINESRN
CCCCCCCCCCHHHCC		30.1021815630
448PhosphorylationADEGRDTSINESRNA
CCCCCCCCCHHHCCC		27.9225072903
603PhosphorylationKRGLGGPTSTPPNLI
HCCCCCCCCCCCCCC		48.8125072903
604PhosphorylationRGLGGPTSTPPNLIS
CCCCCCCCCCCCCCC		41.8925072903
605PhosphorylationGLGGPTSTPPNLISQ
CCCCCCCCCCCCCCH		45.2925072903
668PhosphorylationHDDQEDISPSLAEQQ
CCCCCCCCHHHHHHH		22.2828192239
670PhosphorylationDQEDISPSLAEQQWD
CCCCCCHHHHHHHHH		33.1628348404
685PhosphorylationKKLPEPLSWRSDEED
HCCCCCCCCCCCCCC		31.0330266825
688PhosphorylationPEPLSWRSDEEDEDS
CCCCCCCCCCCCCCC		43.0230266825
695PhosphorylationSDEEDEDSDFGEEQR
CCCCCCCCCCCHHHH		32.5630266825
705PhosphorylationGEEQRDCYLKVSQSK
CHHHHHEEEEECCCH		17.5323312004
780AcetylationSATYCLVKNAVKMFK
HHHHHHHHHHHHHHH		26.6626051181
784AcetylationCLVKNAVKMFKDIGV
HHHHHHHHHHHHHCC		35.8926051181
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 GPAT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPAT1_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 GPAT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
GPAT1_HUMANGPAMphysical
27499296
IDE_HUMANIDEphysical
27499296
ECH1_HUMANECH1physical
27499296
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 GPAT1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND MASSSPECTROMETRY.
"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-111, AND MASSSPECTROMETRY.

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