ACSF3_HUMAN - dbPTM
ACSF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACSF3_HUMAN
UniProt AC Q4G176
Protein Name Acyl-CoA synthetase family member 3, mitochondrial
Gene Name ACSF3
Organism Homo sapiens (Human).
Sequence Length 576
Subcellular Localization Mitochondrion .
Protein Description Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates..
Protein Sequence MLPHVVLTFRRLGCALASCRLAPARHRGSGLLHTAPVARSDRSAPVFTRALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLCGCVGGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGWRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFLSSETPRINVFMAVPTIYTKLMEYYDRHFTQPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSENPQREACSYTIHAEGDERGTKVTPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHFHPS
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
56MethylationRALAFGDRIALVDQH
HHHHCCCEEEEEECC		19.23-
72PhosphorylationRHTYRELYSRSLRLS
HHHHHHHHHHHHHHH		9.40-
73PhosphorylationHTYRELYSRSLRLSQ
HHHHHHHHHHHHHHH		28.1924719451
99PhosphorylationDLREERVSFLCANDA
CCCHHHHHEEECCCH		20.7922210691
118PhosphorylationAQWASWMSGGVAVPL
HHHHHHHCCCEEEEE		26.5722210691
162UbiquitinationLLSPVVRKLGVPLLP
HHHHHHHHHCCCCCC		37.67-
171PhosphorylationGVPLLPLTPAIYTGA
CCCCCCCCCCEECCC		14.56110752325
205PhosphorylationMIIYTSGTTGRPKGV
EEEEECCCCCCCCCC		26.3368723083
214PhosphorylationGRPKGVLSTHQNIRA
CCCCCCCCHHHHHHH		22.8020068231
215PhosphorylationRPKGVLSTHQNIRAV
CCCCCCCHHHHHHHH		24.2620068231
271PhosphorylationCVMMPEFSPQQVWEK
EEECCCCCHHHHHHH		21.8222985185
297PhosphorylationFMAVPTIYTKLMEYY
EEEHHHHHHHHHHHH		10.57139201
303PhosphorylationIYTKLMEYYDRHFTQ
HHHHHHHHHHHHCCC		9.19139205
304PhosphorylationYTKLMEYYDRHFTQP
HHHHHHHHHHHCCCH		8.00139209
306MethylationKLMEYYDRHFTQPHA
HHHHHHHHHCCCHHH		15.65-
3242-HydroxyisobutyrylationLRAVCEEKIRLMVSG
HHHHHHHHHHEEEEC		15.72-
324UbiquitinationLRAVCEEKIRLMVSG
HHHHHHHHHHEEEEC		15.72-
324AcetylationLRAVCEEKIRLMVSG
HHHHHHHHHHEEEEC		15.7225953088
342UbiquitinationLPLPVLEKWKNITGH
CCHHHHHHHCCCCCC		60.34-
344UbiquitinationLPVLEKWKNITGHTL
HHHHHHHCCCCCCHH		49.92-
355PhosphorylationGHTLLERYGMTEIGM
CCHHHHHHCCCHHHH		11.2422817900
358PhosphorylationLLERYGMTEIGMALS
HHHHHCCCHHHHCCC		21.7925262027
365PhosphorylationTEIGMALSGPLTTAV
CHHHHCCCCCCEEEE		28.9125262027
369PhosphorylationMALSGPLTTAVRLPG
HCCCCCCEEEEECCC		18.8225262027
370PhosphorylationALSGPLTTAVRLPGS
CCCCCCEEEEECCCC		30.7325262027
380PhosphorylationRLPGSVGTPLPGVQV
ECCCCCCCCCCCCEE		21.3530624053
413AcetylationEGDERGTKVTPGFEE
CCCCCCCEECCCCEE		47.1125953088
413UbiquitinationEGDERGTKVTPGFEE
CCCCCCCEECCCCEE		47.11-
421AcetylationVTPGFEEKEGELLVR
ECCCCEECCCEEEEE		64.9125953088
421UbiquitinationVTPGFEEKEGELLVR
ECCCCEECCCEEEEE		64.91-
439UbiquitinationVFREYWNKPEETKSA
HHHHHCCCHHHCCCC		39.3919608861
439AcetylationVFREYWNKPEETKSA
HHHHHCCCHHHCCCC		39.3919608861
444UbiquitinationWNKPEETKSAFTLDG
CCCHHHCCCCEEEEE		42.96-
462UbiquitinationTGDTVVFKDGQYWIR
CCCEEEEECCEEEEE		49.71-
466PhosphorylationVVFKDGQYWIRGRTS
EEEECCEEEEECCEE		14.3446158037
472PhosphorylationQYWIRGRTSVDIIKT
EEEEECCEEEEEEEC		35.6123312004
473PhosphorylationYWIRGRTSVDIIKTG
EEEECCEEEEEEECC		19.2127282143
478UbiquitinationRTSVDIIKTGGYKVS
CEEEEEEECCCEEEE		41.26-
478AcetylationRTSVDIIKTGGYKVS
CEEEEEEECCCEEEE		41.2625953088
521PhosphorylationQRVTAVVTLREGHSL
CEEEEEEEECCCCCC		17.3118785766
534UbiquitinationSLSHRELKEWARNVL
CCCHHHHHHHHHHCH		46.59-
534MalonylationSLSHRELKEWARNVL
CCCHHHHHHHHHHCH		46.5926320211
534AcetylationSLSHRELKEWARNVL
CCCHHHHHHHHHHCH		46.5925953088
534SuccinylationSLSHRELKEWARNVL
CCCHHHHHHHHHHCH		46.5923954790
544PhosphorylationARNVLAPYAVPSELV
HHHCHHCCCCCHHEE		18.0211309835
566UbiquitinationNQMGKIDKKALIRHF
HCCCCCCHHHHHHHC		43.34-
567UbiquitinationQMGKIDKKALIRHFH
CCCCCCHHHHHHHCC		44.68-
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 ACSF3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACSF3_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 ACSF3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACSF3_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614265Combined malonic and methylmalonic aciduria (CMAMMA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACSF3_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-439, AND MASS SPECTROMETRY.

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