ACSL4_HUMAN - dbPTM
ACSL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACSL4_HUMAN
UniProt AC O60488
Protein Name Long-chain-fatty-acid--CoA ligase 4
Gene Name ACSL4
Organism Homo sapiens (Human).
Sequence Length 711
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 Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates..
Protein Sequence MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPEGFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK
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
23PhosphorylationHLLITIYSALIFIPW
HHHHHHHHHHHHHHH		16.8546158055
31PhosphorylationALIFIPWYFLTNAKK
HHHHHHHHHHHCHHH		5.3746158097
34PhosphorylationFIPWYFLTNAKKKNA
HHHHHHHHCHHHHCH		24.1946158079
47UbiquitinationNAMAKRIKAKPTSDK
CHHHHHHCCCCCCCC		55.16-
48AcetylationAMAKRIKAKPTSDKP
HHHHHHCCCCCCCCC		22.2319608861
48 (in isoform 2)Ubiquitination-22.23-
49UbiquitinationMAKRIKAKPTSDKPG
HHHHHCCCCCCCCCC		43.77-
51PhosphorylationKRIKAKPTSDKPGSP
HHHCCCCCCCCCCCC		49.1823403867
52PhosphorylationRIKAKPTSDKPGSPY
HHCCCCCCCCCCCCC		52.7623403867
54UbiquitinationKAKPTSDKPGSPYRS
CCCCCCCCCCCCCCC		51.55-
57PhosphorylationPTSDKPGSPYRSVTH
CCCCCCCCCCCCCCC		27.5625159151
59PhosphorylationSDKPGSPYRSVTHFD
CCCCCCCCCCCCCCC		19.7423403867
61PhosphorylationKPGSPYRSVTHFDSL
CCCCCCCCCCCCCCE		26.0627080861
63PhosphorylationGSPYRSVTHFDSLAV
CCCCCCCCCCCCEEE		20.3346158085
67PhosphorylationRSVTHFDSLAVIDIP
CCCCCCCCEEEEECC		19.7927080861
72 (in isoform 2)Ubiquitination-34.1421890473
72UbiquitinationFDSLAVIDIPGADTL
CCCEEEEECCCCHHH		34.1421890473
83 (in isoform 2)Ubiquitination-8.78-
89AcetylationLFDHAVSKFGKKDSL
HHHHHHHHHCCCCCC		52.0819608861
89UbiquitinationLFDHAVSKFGKKDSL
HHHHHHHHHCCCCCC		52.0821890473
92AcetylationHAVSKFGKKDSLGTR
HHHHHHCCCCCCCHH		57.447684447
95PhosphorylationSKFGKKDSLGTREIL
HHHCCCCCCCHHHHC		37.2630576142
107 (in isoform 2)Ubiquitination-42.3421890473
108SulfoxidationILSEENEMQPNGKVF
HCCCCCCCCCCCHHH		13.9721406390
113UbiquitinationNEMQPNGKVFKKLIL
CCCCCCCHHHHHHHH		51.6521890473
113 (in isoform 1)Ubiquitination-51.6521890473
117UbiquitinationPNGKVFKKLILGNYK
CCCHHHHHHHHCCCC		29.33-
140PhosphorylationRRVNNFGSGLTALGL
HHHHCCCCCCHHCCC		26.8820068231
143PhosphorylationNNFGSGLTALGLKPK
HCCCCCCHHCCCCCC		24.3020068231
148UbiquitinationGLTALGLKPKNTIAI
CCHHCCCCCCCEEEE		52.7421906983
148 (in isoform 1)Ubiquitination-52.7421890473
150UbiquitinationTALGLKPKNTIAIFC
HHCCCCCCCEEEEEE		66.20-
190 (in isoform 2)Ubiquitination-3.69-
211UbiquitinationSVELLESKLKTALLD
HHHHHHHHHHHHHHH		44.63-
223UbiquitinationLLDISCVKHIIYVDN
HHHHHHCEEEEEECC		33.15-
227PhosphorylationSCVKHIIYVDNKAIN
HHCEEEEEECCCCCC		10.9328102081
231UbiquitinationHIIYVDNKAINKAEY
EEEEECCCCCCHHCC		46.29-
312UbiquitinationRIPGLGPKDTYIGYL
ECCCCCCCCCEEECC		61.99-
313 (in isoform 2)Ubiquitination-48.1221890473
342PhosphorylationTYGCRIGYSSPLTLS
ECCCCCCCCCCCCCC		12.0130206219
342 (in isoform 2)Ubiquitination-12.01-
343PhosphorylationYGCRIGYSSPLTLSD
CCCCCCCCCCCCCCC		21.9230206219
344PhosphorylationGCRIGYSSPLTLSDQ
CCCCCCCCCCCCCCC		18.5527067055
347PhosphorylationIGYSSPLTLSDQSSK
CCCCCCCCCCCCCCC		27.8330206219
347 (in isoform 2)Ubiquitination-27.8321890473
347UbiquitinationIGYSSPLTLSDQSSK
CCCCCCCCCCCCCCC		27.8321890473
349PhosphorylationYSSPLTLSDQSSKIK
CCCCCCCCCCCCCCC		28.5030206219
352PhosphorylationPLTLSDQSSKIKKGS
CCCCCCCCCCCCCCC		38.2963768293
353PhosphorylationLTLSDQSSKIKKGSK
CCCCCCCCCCCCCCC		32.5421712546
354UbiquitinationTLSDQSSKIKKGSKG
CCCCCCCCCCCCCCC		64.8921906983
354 (in isoform 1)Ubiquitination-64.8921890473
356UbiquitinationSDQSSKIKKGSKGDC
CCCCCCCCCCCCCCC		55.61-
356 (in isoform 2)Ubiquitination-55.6121890473
356UbiquitinationSDQSSKIKKGSKGDC
CCCCCCCCCCCCCCC		55.6121890473
360UbiquitinationSKIKKGSKGDCTVLK
CCCCCCCCCCCEECC		68.39-
360 (in isoform 2)Ubiquitination-68.3921890473
360UbiquitinationSKIKKGSKGDCTVLK
CCCCCCCCCCCEECC		68.3921890473
367UbiquitinationKGDCTVLKPTLMAAV
CCCCEECCHHHHHHH		31.46-
383UbiquitinationEIMDRIYKNVMSKVQ
HHHHHHHHHHHHHHH		40.47-
388MalonylationIYKNVMSKVQEMNYI
HHHHHHHHHHHHHHH		29.8226320211
388UbiquitinationIYKNVMSKVQEMNYI
HHHHHHHHHHHHHHH		29.8221890473
388 (in isoform 1)Ubiquitination-29.8221890473
397AcetylationQEMNYIQKTLFKIGY
HHHHHHHHHHHHHCC		37.3220167786
397UbiquitinationQEMNYIQKTLFKIGY
HHHHHHHHHHHHHCC		37.3221890473
397 (in isoform 1)Ubiquitination-37.3221890473
401AcetylationYIQKTLFKIGYDYKL
HHHHHHHHHCCCCCH		38.0320167786
401UbiquitinationYIQKTLFKIGYDYKL
HHHHHHHHHCCCCCH		38.0321890473
401 (in isoform 1)Ubiquitination-38.0321890473
404PhosphorylationKTLFKIGYDYKLEQI
HHHHHHCCCCCHHHH		21.4169212545
407UbiquitinationFKIGYDYKLEQIKKG
HHHCCCCCHHHHHCC		42.52-
413UbiquitinationYKLEQIKKGYDAPLC
CCHHHHHCCCCCCHH		65.42-
415PhosphorylationLEQIKKGYDAPLCNL
HHHHHCCCCCCHHHH		20.1520090780
420GlutathionylationKGYDAPLCNLLLFKK
CCCCCCHHHHHHHHH		3.0822555962
426UbiquitinationLCNLLLFKKVKALLG
HHHHHHHHHHHHHHC		57.54-
427UbiquitinationCNLLLFKKVKALLGG
HHHHHHHHHHHHHCC		41.45-
441PhosphorylationGNVRMMLSGGAPLSP
CCEEEEEECCCCCCC		19.7925219547
447PhosphorylationLSGGAPLSPQTHRFM
EECCCCCCCCCCCCE		17.5729255136
450PhosphorylationGAPLSPQTHRFMNVC
CCCCCCCCCCCEEEE		20.5729255136
459 (in isoform 2)Ubiquitination-1.9721890473
459UbiquitinationRFMNVCFCCPIGQGY
CCEEEEEECCCCCCC		1.9721890473
483PhosphorylationTVTEVTDYTTGRVGA
CEEEEEECCCCCCCC		9.2422817900
485PhosphorylationTEVTDYTTGRVGAPL
EEEEECCCCCCCCCE		19.4350563231
495 (in isoform 2)Ubiquitination-4.8621890473
498UbiquitinationPLICCEIKLKDWQEG
CEEEEEEECCCHHHC		27.4722053931
498 (in isoform 1)Ubiquitination-27.4721890473
500UbiquitinationICCEIKLKDWQEGGY
EEEEEECCCHHHCCE		52.5021890473
500 (in isoform 1)Ubiquitination-52.5021890473
507PhosphorylationKDWQEGGYTINDKPN
CCHHHCCEECCCCCC		18.4627642862
508PhosphorylationDWQEGGYTINDKPNP
CHHHCCEECCCCCCC		19.31175011
512UbiquitinationGGYTINDKPNPRGEI
CCEECCCCCCCCCEE		42.05-
527PhosphorylationVIGGQNISMGYFKNE
EECCEEEEEEEECCC		17.4420068231
530PhosphorylationGQNISMGYFKNEEKT
CEEEEEEEECCCCCC		11.6220068231
536UbiquitinationGYFKNEEKTAEDYSV
EEECCCCCCCCCCEE		47.0221906983
536 (in isoform 1)Ubiquitination-47.0221890473
541PhosphorylationEEKTAEDYSVDENGQ
CCCCCCCCEECCCCC		11.3320561311
542PhosphorylationEKTAEDYSVDENGQR
CCCCCCCEECCCCCE		35.1027067055
546 (in isoform 2)Ubiquitination-47.6521890473
580 (in isoform 2)Ubiquitination-17.5121890473
580UbiquitinationDLVKLQAGEYVSLGK
CEEEECCCCEEEHHH		17.5121890473
582PhosphorylationVKLQAGEYVSLGKVE
EEECCCCEEEHHHHH		8.4025884760
584PhosphorylationLQAGEYVSLGKVEAA
ECCCCEEEHHHHHHH		30.4228796482
587UbiquitinationGEYVSLGKVEAALKN
CCEEEHHHHHHHHHC		42.04-
587 (in isoform 1)Ubiquitination-42.0421890473
593UbiquitinationGKVEAALKNCPLIDN
HHHHHHHHCCCCCCC		52.34-
607PhosphorylationNICAFAKSDQSYVIS
CEEEEECCCCEEEEE		37.1446158067
610 (in isoform 2)Ubiquitination-26.76-
620 (in isoform 2)Ubiquitination-26.6121890473
621MalonylationSFVVPNQKRLTLLAQ
EEEECCHHHEEEHHH		56.8926320211
621UbiquitinationSFVVPNQKRLTLLAQ
EEEECCHHHEEEHHH		56.8921890473
621 (in isoform 1)Ubiquitination-56.8921890473
624PhosphorylationVPNQKRLTLLAQQKG
ECCHHHEEEHHHHCC		24.6120068231
629 (in isoform 2)Ubiquitination-38.5721890473
629UbiquitinationRLTLLAQQKGVEGTW
HEEEHHHHCCCCCEE		38.5721890473
640GlutathionylationEGTWVDICNNPAMEA
CCEEEECCCCHHHHH		3.3122555962
649 (in isoform 2)Ubiquitination-9.5621890473
651UbiquitinationAMEAEILKEIREAAN
HHHHHHHHHHHHHHH		57.67-
661UbiquitinationREAANAMKLERFEIP
HHHHHHCCCEEEECC		44.8021906983
661 (in isoform 1)Ubiquitination-44.8021890473
661 (in isoform 2)Ubiquitination-44.8021890473
661UbiquitinationREAANAMKLERFEIP
HHHHHHCCCEEEECC		44.8021890473
670UbiquitinationERFEIPIKVRLSPEP
EEEECCEEEEECCCC		18.8921890473
670 (in isoform 1)Ubiquitination-18.8921890473
674PhosphorylationIPIKVRLSPEPWTPE
CCEEEEECCCCCCCC		19.3625159151
679PhosphorylationRLSPEPWTPETGLVT
EECCCCCCCCCCCCC		23.2022617229
682PhosphorylationPEPWTPETGLVTDAF
CCCCCCCCCCCCCHH		36.7028102081
686PhosphorylationTPETGLVTDAFKLKR
CCCCCCCCCHHHHCH		27.0123403867
690AcetylationGLVTDAFKLKRKELR
CCCCCHHHHCHHHHH		55.6124431051
690UbiquitinationGLVTDAFKLKRKELR
CCCCCHHHHCHHHHH		55.61-
690 (in isoform 1)Ubiquitination-55.6121890473
692UbiquitinationVTDAFKLKRKELRNH
CCCHHHHCHHHHHHH		63.11-
702UbiquitinationELRNHYLKDIERMYG
HHHHHHHHHHHHHHC		49.8721890473
702 (in isoform 1)Ubiquitination-49.8721890473
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 ACSL4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACSL4_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 ACSL4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
DSE_HUMANDSEphysical
21988832
ACSL3_HUMANACSL3physical
26496610
TF3B_HUMANBRF1physical
26496610
AAAT_HUMANSLC1A5physical
26496610
ABCG1_HUMANABCG1physical
26496610
EDEM1_HUMANEDEM1physical
26496610
RT15_HUMANMRPS15physical
26496610
TJAP1_HUMANTJAP1physical
26496610
HTAI2_HUMANHTATIP2physical
21252234
RAB5A_HUMANRAB5Aphysical
21252234
Drug and Disease Associations
Kegg Disease
H00480 Non-syndromic X-linked mental retardation
OMIM Disease
300387Mental retardation, X-linked 63 (MRX63)
300194Alport syndrome with mental retardation, midface hypoplasia and elliptocytosis (ATS-MR)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00159Icosapent
DB00412Rosiglitazone
Regulatory Network of ACSL4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, AND MASS SPECTROMETRY.

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