ACSL3_HUMAN - dbPTM
ACSL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACSL3_HUMAN
UniProt AC O95573
Protein Name Long-chain-fatty-acid--CoA ligase 3
Gene Name ACSL3
Organism Homo sapiens (Human).
Sequence Length 720
Subcellular Localization Mitochondrion outer membrane
Single-pass type III membrane protein. Peroxisome membrane
Single-pass type III membrane protein. Microsome membrane
Single-pass type III membrane protein. Endoplasmic reticulum membrane
Single-pass type III membrane prote
Protein Description Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis (By similarity). Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates (By similarity). Has mainly an anabolic role in energy metabolism. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins)..
Protein Sequence MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPVNSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPNGKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGKPPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQSSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQISKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLKVLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK
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
6Phosphorylation--MNNHVSSKPSTMK
--CCCCCCCCCCHHH		25.7025599653
7Phosphorylation-MNNHVSSKPSTMKL
-CCCCCCCCCCHHHH		47.7121406692
10PhosphorylationNHVSSKPSTMKLKHT
CCCCCCCCHHHHHHH		44.8925599653
11PhosphorylationHVSSKPSTMKLKHTI
CCCCCCCHHHHHHHH		27.1825599653
13UbiquitinationSSKPSTMKLKHTINP
CCCCCHHHHHHHHHH		55.24-
56UbiquitinationQEKSNRIKAKPVNSK
HHHHHCCCCCCCCCC		47.31-
58UbiquitinationKSNRIKAKPVNSKPD
HHHCCCCCCCCCCCC		44.49-
62PhosphorylationIKAKPVNSKPDSAYR
CCCCCCCCCCCHHHH		45.8823898821
63UbiquitinationKAKPVNSKPDSAYRS
CCCCCCCCCCHHHHC		47.87-
70PhosphorylationKPDSAYRSVNSLDGL
CCCHHHHCCCCHHHH		16.9928348404
73PhosphorylationSAYRSVNSLDGLASV
HHHHCCCCHHHHHHH		26.1928348404
90UbiquitinationPGCDTLDKVFTYAKN
CCCCHHHHHHHHHHH		42.22-
962-HydroxyisobutyrylationDKVFTYAKNKFKNKR
HHHHHHHHHHHCCCE		50.70-
96UbiquitinationDKVFTYAKNKFKNKR
HHHHHHHHHHHCCCE		50.70-
96MalonylationDKVFTYAKNKFKNKR
HHHHHHHHHHHCCCE		50.7026320211
107PhosphorylationKNKRLLGTREVLNEE
CCCEECCCHHHCCCC		24.5120068231
122AcetylationDEVQPNGKIFKKVIL
CCCCCCCCEEEEHHH		52.1623954790
122UbiquitinationDEVQPNGKIFKKVIL
CCCCCCCCEEEEHHH		52.1621890473
157UbiquitinationGLQMLGQKPKTNIAI
HHHHCCCCCCCCEEE		46.8421890473
1592-HydroxyisobutyrylationQMLGQKPKTNIAIFC
HHCCCCCCCCEEEEE		62.33-
220UbiquitinationSKELLQTKLKDIVSL
CHHHHHHHHHHHHHH		40.3521890473
220AcetylationSKELLQTKLKDIVSL
CHHHHHHHHHHHHHH		40.3523236377
2222-HydroxyisobutyrylationELLQTKLKDIVSLVP
HHHHHHHHHHHHHHH		47.14-
222UbiquitinationELLQTKLKDIVSLVP
HHHHHHHHHHHHHHH		47.14-
240UbiquitinationHIITVDGKPPTWSEF
EEEEECCCCCCHHHC		43.28-
274PhosphorylationSMENQPHSKPLPSDI
HHCCCCCCCCCCCCE		42.5224719451
351PhosphorylationSHGCRIGYSSPQTLA
HCCCCCCCCCCHHHH		12.0128152594
352PhosphorylationHGCRIGYSSPQTLAD
CCCCCCCCCCHHHHH		30.2628152594
353PhosphorylationGCRIGYSSPQTLADQ
CCCCCCCCCHHHHHC		16.7325850435
356PhosphorylationIGYSSPQTLADQSSK
CCCCCCHHHHHCCCC		27.5726471730
362PhosphorylationQTLADQSSKIKKGSK
HHHHHCCCCCCCCCC		32.5426437602
363MalonylationTLADQSSKIKKGSKG
HHHHCCCCCCCCCCC		64.8926320211
363UbiquitinationTLADQSSKIKKGSKG
HHHHCCCCCCCCCCC		64.8921906983
372PhosphorylationKKGSKGDTSMLKPTL
CCCCCCCCHHHHHHH		25.3830576142
373PhosphorylationKGSKGDTSMLKPTLM
CCCCCCCHHHHHHHH		27.1930576142
376UbiquitinationKGDTSMLKPTLMAAV
CCCCHHHHHHHHHHH		27.58-
392MalonylationEIMDRIYKNVMNKVS
HHHHHHHHHHHHHHH		40.4726320211
392UbiquitinationEIMDRIYKNVMNKVS
HHHHHHHHHHHHHHH		40.47-
392AcetylationEIMDRIYKNVMNKVS
HHHHHHHHHHHHHHH		40.4725953088
397MalonylationIYKNVMNKVSEMSSF
HHHHHHHHHHHHHHH		29.1026320211
3972-HydroxyisobutyrylationIYKNVMNKVSEMSSF
HHHHHHHHHHHHHHH		29.10-
397UbiquitinationIYKNVMNKVSEMSSF
HHHHHHHHHHHHHHH		29.10-
401SulfoxidationVMNKVSEMSSFQRNL
HHHHHHHHHHHHHHH		2.9521406390
403PhosphorylationNKVSEMSSFQRNLFI
HHHHHHHHHHHHHHH		24.8826437602
421PhosphorylationNYKMEQISKGRNTPL
HHHHHHHHCCCCCCC		28.8426437602
422UbiquitinationYKMEQISKGRNTPLC
HHHHHHHCCCCCCCC		64.62-
450S-nitrosylationGNIRLLLCGGAPLSA
CCEEEEEECCCCCCH		4.8222178444
450S-nitrosocysteineGNIRLLLCGGAPLSA
CCEEEEEECCCCCCH		4.82-
507UbiquitinationPLVCCEIKLKNWEEG
CEEEEEEECCCCHHC		30.99-
507AcetylationPLVCCEIKLKNWEEG
CEEEEEEECCCCHHC		30.9925953088
509UbiquitinationVCCEIKLKNWEEGGY
EEEEEECCCCHHCCC		55.82-
516PhosphorylationKNWEEGGYFNTDKPH
CCCHHCCCCCCCCCC		12.43110738355
521UbiquitinationGGYFNTDKPHPRGEI
CCCCCCCCCCCCCEE		43.09-
521AcetylationGGYFNTDKPHPRGEI
CCCCCCCCCCCCCEE		43.0926051181
536O-linked_GlycosylationLIGGQSVTMGYYKNE
EECCEEEECCEECCC		15.32OGP
547UbiquitinationYKNEAKTKADFFEDE
ECCCCCCCCCEEECC		45.3021906983
547MalonylationYKNEAKTKADFFEDE
ECCCCCCCCCEEECC		45.3026320211
5472-HydroxyisobutyrylationYKNEAKTKADFFEDE
ECCCCCCCCCEEECC		45.30-
561S-nitrosocysteineENGQRWLCTGDIGEF
CCCCEEEEEECCCEE		2.95-
561S-nitrosylationENGQRWLCTGDIGEF
CCCCEEEEEECCCEE		2.9519483679
573S-nitrosylationGEFEPDGCLKIIDRK
CEECCCCCEEEEECC		4.5719483679
573S-nitrosocysteineGEFEPDGCLKIIDRK
CEECCCCCEEEEECC		4.57-
575UbiquitinationFEPDGCLKIIDRKKD
ECCCCCEEEEECCCC		41.51-
591PhosphorylationVKLQAGEYVSLGKVE
EEECCCCEEEHHHHH		8.4025884760
593PhosphorylationLQAGEYVSLGKVEAA
ECCCCEEEHHHHHHH		30.4228152594
596UbiquitinationGEYVSLGKVEAALKN
CCEEEHHHHHHHHHC		42.0421890473
642UbiquitinationLARKKGLKGTWEELC
HHHHHCCCCHHHHHH		64.06-
673UbiquitinationAISASLEKFEIPVKI
HHHHCHHHCCCCEEE		54.30-
6732-HydroxyisobutyrylationAISASLEKFEIPVKI
HHHHCHHHCCCCEEE		54.30-
673AcetylationAISASLEKFEIPVKI
HHHHCHHHCCCCEEE		54.3023236377
679UbiquitinationEKFEIPVKIRLSPEP
HHCCCCEEEEECCCC		19.4321890473
679AcetylationEKFEIPVKIRLSPEP
HHCCCCEEEEECCCC		19.4325953088
679MalonylationEKFEIPVKIRLSPEP
HHCCCCEEEEECCCC		19.4326320211
683PhosphorylationIPVKIRLSPEPWTPE
CCEEEEECCCCCCCC		19.8525159151
688PhosphorylationRLSPEPWTPETGLVT
EECCCCCCCCCCCCC		23.2023927012
691PhosphorylationPEPWTPETGLVTDAF
CCCCCCCCCCCCHHH		36.7023927012
695PhosphorylationTPETGLVTDAFKLKR
CCCCCCCCHHHHHCH		27.0123927012
699UbiquitinationGLVTDAFKLKRKELK
CCCCHHHHHCHHHHH		55.6121890473
6992-HydroxyisobutyrylationGLVTDAFKLKRKELK
CCCCHHHHHCHHHHH		55.61-
699AcetylationGLVTDAFKLKRKELK
CCCCHHHHHCHHHHH		55.6124431075
7062-HydroxyisobutyrylationKLKRKELKTHYQADI
HHCHHHHHHHHHHHH		34.06-
706MalonylationKLKRKELKTHYQADI
HHCHHHHHHHHHHHH		34.0626320211
706AcetylationKLKRKELKTHYQADI
HHCHHHHHHHHHHHH		34.0623954790
706UbiquitinationKLKRKELKTHYQADI
HHCHHHHHHHHHHHH		34.06-
707PhosphorylationLKRKELKTHYQADIE
HCHHHHHHHHHHHHH		38.1428796482
709PhosphorylationRKELKTHYQADIERM
HHHHHHHHHHHHHHH		15.6128796482
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 ACSL3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACSL3_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 ACSL3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ACSL4_HUMANACSL4physical
22939629
C1TC_HUMANMTHFD1physical
22939629
LYN_HUMANLYNphysical
20605918
YES_HUMANYES1physical
20605918
WDR19_HUMANWDR19physical
27173435
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
DB00159Icosapent
Regulatory Network of ACSL3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683 AND THR-688, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593, AND MASSSPECTROMETRY.

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