ACOX1_HUMAN - dbPTM
ACOX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACOX1_HUMAN
UniProt AC Q15067
Protein Name Peroxisomal acyl-coenzyme A oxidase 1 {ECO:0000303|PubMed:8117268}
Gene Name ACOX1 {ECO:0000312|HGNC:HGNC:119}
Organism Homo sapiens (Human).
Sequence Length 660
Subcellular Localization Peroxisome .
Protein Description Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Isoform 2 is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA..
Protein Sequence MNPDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRYEVAVRKSAIMVKKMREFGIADPDEIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPTMVDINSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKNSPLNKAEVHESYKHLKSLQSKL
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
11PhosphorylationDLRRERDSASFNPEL
HHHHHHHHCCCCHHH		31.8428464451
13PhosphorylationRRERDSASFNPELLT
HHHHHHCCCCHHHHH		29.5223403867
20PhosphorylationSFNPELLTHILDGSP
CCCHHHHHHHHCCCH		21.3528176443
26PhosphorylationLTHILDGSPEKTRRR
HHHHHCCCHHHHHHH		29.5625159151
29UbiquitinationILDGSPEKTRRRREI
HHCCCHHHHHHHHHH		51.2029901268
30PhosphorylationLDGSPEKTRRRREIE
HCCCHHHHHHHHHHH		27.9620873877
35UbiquitinationEKTRRRREIENMILN
HHHHHHHHHHHHHHC		53.4924816145
72AcetylationRKSAIMVKKMREFGI
HHHHHHHHHHHHHCC		24.3825953088
73UbiquitinationKSAIMVKKMREFGIA
HHHHHHHHHHHHCCC		31.6024816145
89AcetylationPDEIMWFKKLHLVNF
HHHHHHHEECCEECC		38.6226051181
89SuccinylationPDEIMWFKKLHLVNF
HHHHHHHEECCEECC		38.62-
89SuccinylationPDEIMWFKKLHLVNF
HHHHHHHEECCEECC		38.62-
90SuccinylationDEIMWFKKLHLVNFV
HHHHHHEECCEECCC		31.50-
90SuccinylationDEIMWFKKLHLVNFV
HHHHHHEECCEECCC		31.50-
122UbiquitinationGTTAQKEKWLLSSKG
CCCHHHHHHHHHCCC		50.61-
124UbiquitinationTAQKEKWLLSSKGLQ
CHHHHHHHHHCCCCE		5.0127667366
127PhosphorylationKEKWLLSSKGLQIIG
HHHHHHHCCCCEEEE		30.6169003047
131UbiquitinationLLSSKGLQIIGTYAQ
HHHCCCCEEEEEEEE		33.6421890473
167PhosphorylationTQEFILNSPTVTSIK
HCEEECCCCCEEEEE		20.64110751293
192UbiquitinationNHAIVLAQLITKGKC
CHHHHHHHHHHCCCC		29.2727667366
196AcetylationVLAQLITKGKCYGLH
HHHHHHHCCCCCEEE		49.7525953088
198AcetylationAQLITKGKCYGLHAF
HHHHHCCCCCEEEEE		26.3223749302
199UbiquitinationQLITKGKCYGLHAFI
HHHHCCCCCEEEEEE		4.4321890473
200PhosphorylationLITKGKCYGLHAFIV
HHHCCCCCEEEEEEE		26.6320090780
216UbiquitinationIREIGTHKPLPGITV
HHHCCCCCCCCCCEE		48.35-
216MalonylationIREIGTHKPLPGITV
HHHCCCCCCCCCCEE		48.3526320211
216AcetylationIREIGTHKPLPGITV
HHHCCCCCCCCCCEE		48.3523236377
217AcetylationREIGTHKPLPGITVG
HHCCCCCCCCCCEEE		35.8619608861
222UbiquitinationHKPLPGITVGDIGPK
CCCCCCCEEECCCCC		25.0927667366
229AcetylationTVGDIGPKFGYDEID
EEECCCCCCCCCCCC		46.3219608861
229UbiquitinationTVGDIGPKFGYDEID
EEECCCCCCCCCCCC		46.3221890473
232PhosphorylationDIGPKFGYDEIDNGY
CCCCCCCCCCCCCCE		17.346854129
241AcetylationEIDNGYLKMDNHRIP
CCCCCEECCCCCCCC		35.4125953088
241SuccinylationEIDNGYLKMDNHRIP
CCCCCEECCCCCCCC		35.41-
241SuccinylationEIDNGYLKMDNHRIP
CCCCCEECCCCCCCC		35.41-
255AcetylationPRENMLMKYAQVKPD
CCHHHCHHHEEECCC		33.2119608861
256PhosphorylationRENMLMKYAQVKPDG
CHHHCHHHEEECCCC		6.5728152594
257UbiquitinationENMLMKYAQVKPDGT
HHHCHHHEEECCCCC		11.3729901268
260MalonylationLMKYAQVKPDGTYVK
CHHHEEECCCCCEEE		25.8826320211
260AcetylationLMKYAQVKPDGTYVK
CHHHEEECCCCCEEE		25.8826051181
260UbiquitinationLMKYAQVKPDGTYVK
CHHHEEECCCCCEEE		25.8827667366
264PhosphorylationAQVKPDGTYVKPLSN
EEECCCCCEEEECCC		32.3026657352
265PhosphorylationQVKPDGTYVKPLSNK
EECCCCCEEEECCCC		16.4126657352
267MalonylationKPDGTYVKPLSNKLT
CCCCCEEEECCCCCC		29.8126320211
267UbiquitinationKPDGTYVKPLSNKLT
CCCCCEEEECCCCCC		29.8121890473
267AcetylationKPDGTYVKPLSNKLT
CCCCCEEEECCCCCC		29.8119608861
270PhosphorylationGTYVKPLSNKLTYGT
CCEEEECCCCCCCCE		40.2128857561
272AcetylationYVKPLSNKLTYGTMV
EEEECCCCCCCCEEH		38.5426051181
274PhosphorylationKPLSNKLTYGTMVFV
EECCCCCCCCEEHHH		22.8630206219
275PhosphorylationPLSNKLTYGTMVFVR
ECCCCCCCCEEHHHH		22.4920090780
277PhosphorylationSNKLTYGTMVFVRSF
CCCCCCCEEHHHHHH		10.3530206219
295UbiquitinationEAARALSKACTIAIR
HHHHHHHHHHHHHHH		48.6229901268
313AcetylationVRHQSEIKPGEPEPQ
HHCCCCCCCCCCCCC		42.8126051181
349SuccinylationQFVGAYMKETYHRIN
HHHHHHHHHHHHHHH		33.94-
349SuccinylationQFVGAYMKETYHRIN
HHHHHHHHHHHHHHH		33.94-
399AcetylationCRMACGGHGYSHCSG
HHHHHCCCCCCCCCC		19.8019608861
437SuccinylationQTARFLMKSYDQVHS
HHHHHHHHHHHHHHC		48.27-
437AcetylationQTARFLMKSYDQVHS
HHHHHHHHHHHHHHC		48.2719608861
437MalonylationQTARFLMKSYDQVHS
HHHHHHHHHHHHHHC		48.2726320211
437SuccinylationQTARFLMKSYDQVHS
HHHHHHHHHHHHHHC		48.27-
446SuccinylationYDQVHSGKLVCGMVS
HHHHHCCCEEHHHHH		40.54-
446SuccinylationYDQVHSGKLVCGMVS
HHHHHCCCEEHHHHH		40.54-
446AcetylationYDQVHSGKLVCGMVS
HHHHHCCCEEHHHHH		40.5425953088
460PhosphorylationSYLNDLPSQRIQPQQ
HHHHCCCCCCCCHHH		39.1124719451
462AcetylationLNDLPSQRIQPQQVA
HHCCCCCCCCHHHEE		33.5719608861
466AcetylationPSQRIQPQQVAVWPT
CCCCCCHHHEEEECE		33.7219608861
487PhosphorylationPESLTEAYKLRAARL
CHHHHHHHHHHHHHH		12.3419835603
500MalonylationRLVEIAAKNLQKEVI
HHHHHHHHHCHHHHH		49.5226320211
500AcetylationRLVEIAAKNLQKEVI
HHHHHHHHHCHHHHH		49.5219608861
504AcetylationIAAKNLQKEVIHRKS
HHHHHCHHHHHHHCC		58.0519608861
512SuccinylationEVIHRKSKEVAWNLT
HHHHHCCCHHHHCCC		60.28-
512AcetylationEVIHRKSKEVAWNLT
HHHHHCCCHHHHCCC		60.2826051181
512SuccinylationEVIHRKSKEVAWNLT
HHHHHCCCHHHHCCC		60.28-
542SuccinylationVVKLFSEKLLKIQDK
EEEHHHHHHHHCCHH		58.90-
542SuccinylationVVKLFSEKLLKIQDK
EEEHHHHHHHHCCHH		58.90-
5422-HydroxyisobutyrylationVVKLFSEKLLKIQDK
EEEHHHHHHHHCCHH		58.90-
549AcetylationKLLKIQDKAIQAVLR
HHHHCCHHHHHHHHH		30.8925953088
5492-HydroxyisobutyrylationKLLKIQDKAIQAVLR
HHHHCCHHHHHHHHH		30.89-
5932-HydroxyisobutyrylationTQVNQRVKELLTLIR
HHHHHHHHHHHHHHH		44.85-
597PhosphorylationQRVKELLTLIRSDAV
HHHHHHHHHHHHHCC		32.5320068231
605UbiquitinationLIRSDAVALVDAFDF
HHHHHCCHHHCCCCC		12.0029967540
613AcetylationLVDAFDFQDVTLGSV
HHCCCCCCCCCHHHH		46.2219608861
629PhosphorylationGRYDGNVYENLFEWA
EECCCCHHHHHHHHH		11.7827259358
637AcetylationENLFEWAKNSPLNKA
HHHHHHHHCCCCCHH		60.06-
637SuccinylationENLFEWAKNSPLNKA
HHHHHHHHCCCCCHH		60.06-
637SuccinylationENLFEWAKNSPLNKA
HHHHHHHHCCCCCHH		60.06-
639PhosphorylationLFEWAKNSPLNKAEV
HHHHHHCCCCCHHHH		30.0229214152
643AcetylationAKNSPLNKAEVHESY
HHCCCCCHHHHHHHH		54.3223749302
643SuccinylationAKNSPLNKAEVHESY
HHCCCCCHHHHHHHH		54.32-
643SuccinylationAKNSPLNKAEVHESY
HHCCCCCHHHHHHHH		54.32-
643UbiquitinationAKNSPLNKAEVHESY
HHCCCCCHHHHHHHH		54.3229967540
649PhosphorylationNKAEVHESYKHLKSL
CHHHHHHHHHHHHHH		25.304318611
651AcetylationAEVHESYKHLKSLQS
HHHHHHHHHHHHHHH		52.3023749302
654SuccinylationHESYKHLKSLQSKL-
HHHHHHHHHHHHCC-		49.17-
654SuccinylationHESYKHLKSLQSKL-
HHHHHHHHHHHHCC-		49.17-
654AcetylationHESYKHLKSLQSKL-
HHHHHHHHHHHHCC-		49.1725953088
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 ACOX1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACOX1_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 ACOX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPRD_HUMANM6PRphysical
22939629
PALLD_HUMANPALLDphysical
22939629
TMED9_HUMANTMED9physical
22939629
RM12_HUMANMRPL12physical
22939629
ECI1_HUMANECI1physical
22939629
CX6B1_HUMANCOX6B1physical
22939629
GRHPR_HUMANGRHPRphysical
22939629
CATA_HUMANCATphysical
26344197
NUP62_HUMANNUP62physical
26344197
PPWD1_HUMANPPWD1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
264470Adrenoleukodystrophy, pseudoneonatal (Pseudo-NALD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB03147Flavin adenine dinucleotide
Regulatory Network of ACOX1_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-255; LYS-267; LYS-437;LYS-500; LYS-504 AND LYS-651, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASSSPECTROMETRY.

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