ACOX1_MOUSE - dbPTM
ACOX1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACOX1_MOUSE
UniProt AC Q9R0H0
Protein Name Peroxisomal acyl-coenzyme A oxidase 1 {ECO:0000250|UniProtKB:Q15067}
Gene Name Acox1 {ECO:0000312|MGI:MGI:1330812}
Organism Mus musculus (Mouse).
Sequence Length 661
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 (By similarity)..
Protein Sequence MNPDLRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQHEDYNFLTRSQRYEVAVKKSATMVKKMREFGIADPEEIMWFKKLHMVNFVEPVGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRSEPEPQILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQVQSGKLVGGMVSYLNDLPSQRIQPQQVAVWPTLVDINSLDSLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQAVLRNLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFEWAKKSPLNKTEVHESYYKHLKPLQSKL
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
20PhosphorylationTFNPELITHILDGSP
HCCHHHHHHHHCCCC
18.5821183079
26PhosphorylationITHILDGSPENTRRR
HHHHHCCCCCHHHHH
28.8021082442
30PhosphorylationLDGSPENTRRRREIE
HCCCCCHHHHHHHHH
24.7219060867
51PhosphorylationPDFQHEDYNFLTRSQ
CCCCCCCCCHHCHHH
12.588234233
57PhosphorylationDYNFLTRSQRYEVAV
CCCHHCHHHHHEEEE
17.4930352176
60PhosphorylationFLTRSQRYEVAVKKS
HHCHHHHHEEEEHHH
13.7129472430
65AcetylationQRYEVAVKKSATMVK
HHHEEEEHHHHHHHH
31.1323576753
65GlutarylationQRYEVAVKKSATMVK
HHHEEEEHHHHHHHH
31.1324703693
65UbiquitinationQRYEVAVKKSATMVK
HHHEEEEHHHHHHHH
31.1327667366
69PhosphorylationVAVKKSATMVKKMRE
EEEHHHHHHHHHHHH
29.5959149931
72AcetylationKKSATMVKKMREFGI
HHHHHHHHHHHHHCC
29.9923864654
89AcetylationPEEIMWFKKLHMVNF
HHHHHHHEECCCCCC
38.6223806337
89SuccinylationPEEIMWFKKLHMVNF
HHHHHHHEECCCCCC
38.62-
89SuccinylationPEEIMWFKKLHMVNF
HHHHHHHEECCCCCC
38.6223806337
89UbiquitinationPEEIMWFKKLHMVNF
HHHHHHHEECCCCCC
38.62-
89 (in isoform 2)Ubiquitination-38.62-
90AcetylationEEIMWFKKLHMVNFV
HHHHHHEECCCCCCC
33.8623806337
90SuccinylationEEIMWFKKLHMVNFV
HHHHHHEECCCCCCC
33.86-
90SuccinylationEEIMWFKKLHMVNFV
HHHHHHEECCCCCCC
33.8623806337
90UbiquitinationEEIMWFKKLHMVNFV
HHHHHHEECCCCCCC
33.86-
148UbiquitinationMGHGTHLRGLETTAT
CCCCCEECCCEEEEE
39.7927667366
159AcetylationTTATYDPKTQEFILN
EEEEECCCCCEEECC
61.0023864654
159SuccinylationTTATYDPKTQEFILN
EEEEECCCCCEEECC
61.00-
159SuccinylationTTATYDPKTQEFILN
EEEEECCCCCEEECC
61.0023806337
159UbiquitinationTTATYDPKTQEFILN
EEEEECCCCCEEECC
61.00-
174AcetylationSPTVTSIKWWPGGLG
CCCEEEEEECCCCCC
42.8623954790
174UbiquitinationSPTVTSIKWWPGGLG
CCCEEEEEECCCCCC
42.8622790023
182AcetylationWWPGGLGKTSNHAIV
ECCCCCCCCCCHHHH
54.5523864654
187UbiquitinationLGKTSNHAIVLAQLI
CCCCCCHHHHHHHHH
9.6127667366
192UbiquitinationNHAIVLAQLITRGEC
CHHHHHHHHHHCCCC
29.2727667366
199S-nitrosocysteineQLITRGECYGLHAFV
HHHHCCCCCCEEEEE
3.48-
199S-nitrosylationQLITRGECYGLHAFV
HHHHCCCCCCEEEEE
3.4821278135
199S-palmitoylationQLITRGECYGLHAFV
HHHHCCCCCCEEEEE
3.4826165157
199UbiquitinationQLITRGECYGLHAFV
HHHHCCCCCCEEEEE
3.4827667366
200PhosphorylationLITRGECYGLHAFVV
HHHCCCCCCEEEEEE
20.5825195567
216AcetylationIREIGTHKPLPGITV
HHHCCCCCCCCCCEE
48.3523576753
216SuccinylationIREIGTHKPLPGITV
HHHCCCCCCCCCCEE
48.3524315375
216UbiquitinationIREIGTHKPLPGITV
HHHCCCCCCCCCCEE
48.3527667366
229AcetylationTVGDIGPKFGYEEMD
EEECCCHHCCCCCCC
46.3223864654
229UbiquitinationTVGDIGPKFGYEEMD
EEECCCHHCCCCCCC
46.3222790023
232PhosphorylationDIGPKFGYEEMDNGY
CCCHHCCCCCCCCCE
16.3217242355
241AcetylationEMDNGYLKMDNYRIP
CCCCCEECCCCCCCC
35.4123806337
241SuccinylationEMDNGYLKMDNYRIP
CCCCCEECCCCCCCC
35.41-
241SuccinylationEMDNGYLKMDNYRIP
CCCCCEECCCCCCCC
35.4123806337
241UbiquitinationEMDNGYLKMDNYRIP
CCCCCEECCCCCCCC
35.41-
246DimethylationYLKMDNYRIPRENML
EECCCCCCCCCHHHC
38.39-
255AcetylationPRENMLMKYAQVKPD
CCHHHCHHHEEECCC
33.2123201123
255UbiquitinationPRENMLMKYAQVKPD
CCHHHCHHHEEECCC
33.2127667366
256PhosphorylationRENMLMKYAQVKPDG
CHHHCHHHEEECCCC
6.5725195567
260AcetylationLMKYAQVKPDGTYVK
CHHHEEECCCCCEEE
25.8823864654
260MalonylationLMKYAQVKPDGTYVK
CHHHEEECCCCCEEE
25.8826320211
260UbiquitinationLMKYAQVKPDGTYVK
CHHHEEECCCCCEEE
25.8827667366
267AcetylationKPDGTYVKPLSNKLT
CCCCCEEEECCCCCC
29.8123576753
267MalonylationKPDGTYVKPLSNKLT
CCCCCEEEECCCCCC
29.8126320211
267UbiquitinationKPDGTYVKPLSNKLT
CCCCCEEEECCCCCC
29.8127667366
272AcetylationYVKPLSNKLTYGTMV
EEEECCCCCCHHCCH
38.5423576753
272UbiquitinationYVKPLSNKLTYGTMV
EEEECCCCCCHHCCH
38.5422790023
275PhosphorylationPLSNKLTYGTMVFVR
ECCCCCCHHCCHHHH
22.4917242355
281UbiquitinationTYGTMVFVRSFLVGS
CHHCCHHHHHHHHHH
3.2227667366
288PhosphorylationVRSFLVGSAAQSLSK
HHHHHHHHHHHHHHH
16.9829472430
292PhosphorylationLVGSAAQSLSKACTI
HHHHHHHHHHHHHHH
29.8629472430
294PhosphorylationGSAAQSLSKACTIAI
HHHHHHHHHHHHHHH
24.3729472430
295SuccinylationSAAQSLSKACTIAIR
HHHHHHHHHHHHHHH
53.4224315375
297S-palmitoylationAQSLSKACTIAIRYS
HHHHHHHHHHHHHHH
3.0426165157
310PhosphorylationYSAVRRQSEIKRSEP
HHHHHCHHHHCCCCC
39.204317759
313AcetylationVRRQSEIKRSEPEPQ
HHCHHHHCCCCCCCC
45.9123864654
315PhosphorylationRQSEIKRSEPEPQIL
CHHHHCCCCCCCCCC
53.1259149993
330AcetylationDFQTQQYKLFPLLAT
CCCCHHHHHHHHHHH
39.0423864654
349AcetylationHFLGRYIKETYMRIN
HHHHHHHHHHHHHHH
34.7623864654
349SuccinylationHFLGRYIKETYMRIN
HHHHHHHHHHHHHHH
34.76-
349SuccinylationHFLGRYIKETYMRIN
HHHHHHHHHHHHHHH
34.7623806337
349UbiquitinationHFLGRYIKETYMRIN
HHHHHHHHHHHHHHH
34.7627667366
358PhosphorylationTYMRINESIGQGDLS
HHHHHHHCCCCCCHH
27.7735096103
365PhosphorylationSIGQGDLSELPELHA
CCCCCCHHHCHHHHH
41.6559150187
392S-nitrosocysteineANAGIEECRMACGGH
CCCCHHHHHHHHCCC
2.03-
392S-nitrosylationANAGIEECRMACGGH
CCCCHHHHHHHHCCC
2.0321278135
392S-palmitoylationANAGIEECRMACGGH
CCCCHHHHHHHHCCC
2.0328526873
437AcetylationQTARFLMKIYDQVQS
HHHHHHHHHHHHHHC
40.0223576753
437MalonylationQTARFLMKIYDQVQS
HHHHHHHHHHHHHHC
40.0226320211
437SuccinylationQTARFLMKIYDQVQS
HHHHHHHHHHHHHHC
40.02-
437SuccinylationQTARFLMKIYDQVQS
HHHHHHHHHHHHHHC
40.0223806337
437UbiquitinationQTARFLMKIYDQVQS
HHHHHHHHHHHHHHC
40.02-
444PhosphorylationKIYDQVQSGKLVGGM
HHHHHHHCCCCCCHH
38.7525195567
444UbiquitinationKIYDQVQSGKLVGGM
HHHHHHHCCCCCCHH
38.7527667366
446AcetylationYDQVQSGKLVGGMVS
HHHHHCCCCCCHHHH
45.2923576753
446SuccinylationYDQVQSGKLVGGMVS
HHHHHCCCCCCHHHH
45.29-
446SuccinylationYDQVQSGKLVGGMVS
HHHHHCCCCCCHHHH
45.2923806337
446UbiquitinationYDQVQSGKLVGGMVS
HHHHHCCCCCCHHHH
45.29-
453PhosphorylationKLVGGMVSYLNDLPS
CCCCHHHHHHHCCCC
18.2723140645
488AcetylationDSLTEAYKLRAARLV
HHHHHHHHHHHHHHH
38.2523954790
488SuccinylationDSLTEAYKLRAARLV
HHHHHHHHHHHHHHH
38.2524315375
488UbiquitinationDSLTEAYKLRAARLV
HHHHHHHHHHHHHHH
38.25-
500AcetylationRLVEIAAKNLQAQVS
HHHHHHHHHHHHHHC
49.5223954790
500SuccinylationRLVEIAAKNLQAQVS
HHHHHHHHHHHHHHC
49.5224315375
500UbiquitinationRLVEIAAKNLQAQVS
HHHHHHHHHHHHHHC
49.52-
507PhosphorylationKNLQAQVSHRKSKEV
HHHHHHHCCCCCCHH
12.9059151943
511PhosphorylationAQVSHRKSKEVAWNL
HHHCCCCCCHHHCCC
33.72108430779
512AcetylationQVSHRKSKEVAWNLT
HHCCCCCCHHHCCCC
60.2823576753
512SuccinylationQVSHRKSKEVAWNLT
HHCCCCCCHHHCCCC
60.28-
512SuccinylationQVSHRKSKEVAWNLT
HHCCCCCCHHHCCCC
60.2823806337
512UbiquitinationQVSHRKSKEVAWNLT
HHCCCCCCHHHCCCC
60.2827667366
527PhosphorylationSVDLVRASEAHCHYV
HHHHHHHHHCCCEEE
25.4222807455
531S-nitrosocysteineVRASEAHCHYVTVKV
HHHHHCCCEEEEEEH
2.97-
531S-nitrosylationVRASEAHCHYVTVKV
HHHHHCCCEEEEEEH
2.9721278135
537AcetylationHCHYVTVKVFADKLP
CCEEEEEEHHHHCCC
23.4423864654
537SuccinylationHCHYVTVKVFADKLP
CCEEEEEEHHHHCCC
23.4424315375
542AcetylationTVKVFADKLPKIQDR
EEEHHHHCCCHHHHH
64.3623864654
542GlutarylationTVKVFADKLPKIQDR
EEEHHHHCCCHHHHH
64.3624703693
542SuccinylationTVKVFADKLPKIQDR
EEEHHHHCCCHHHHH
64.36-
542SuccinylationTVKVFADKLPKIQDR
EEEHHHHCCCHHHHH
64.3623806337
542UbiquitinationTVKVFADKLPKIQDR
EEEHHHHCCCHHHHH
64.36-
545AcetylationVFADKLPKIQDRAVQ
HHHHCCCHHHHHHHH
64.5323864654
545GlutarylationVFADKLPKIQDRAVQ
HHHHCCCHHHHHHHH
64.5324703693
559S-nitrosocysteineQAVLRNLCLLYSLYG
HHHHHHHHHHHHHHC
2.55-
559S-nitrosylationQAVLRNLCLLYSLYG
HHHHHHHHHHHHHHC
2.5521278135
559S-palmitoylationQAVLRNLCLLYSLYG
HHHHHHHHHHHHHHC
2.5526165157
624PhosphorylationLGSVLGRYDGNVYEN
HHHHHEECCCCHHHH
26.8025195567
629PhosphorylationGRYDGNVYENLFEWA
EECCCCHHHHHHHHH
11.7817242355
637AcetylationENLFEWAKKSPLNKT
HHHHHHHHHCCCCCH
55.6523576753
637SuccinylationENLFEWAKKSPLNKT
HHHHHHHHHCCCCCH
55.65-
637SuccinylationENLFEWAKKSPLNKT
HHHHHHHHHCCCCCH
55.6523806337
638AcetylationNLFEWAKKSPLNKTE
HHHHHHHHCCCCCHH
49.942374599
638SuccinylationNLFEWAKKSPLNKTE
HHHHHHHHCCCCCHH
49.9424315375
643AcetylationAKKSPLNKTEVHESY
HHHCCCCCHHHHHHH
54.4623864654
643MalonylationAKKSPLNKTEVHESY
HHHCCCCCHHHHHHH
54.4626320211
643SuccinylationAKKSPLNKTEVHESY
HHHCCCCCHHHHHHH
54.46-
643SuccinylationAKKSPLNKTEVHESY
HHHCCCCCHHHHHHH
54.4623806337
643UbiquitinationAKKSPLNKTEVHESY
HHHCCCCCHHHHHHH
54.46-
644PhosphorylationKKSPLNKTEVHESYY
HHCCCCCHHHHHHHH
42.0155992781
649PhosphorylationNKTEVHESYYKHLKP
CCHHHHHHHHHHHHH
20.9117208939
650PhosphorylationKTEVHESYYKHLKPL
CHHHHHHHHHHHHHH
17.3573245799
651PhosphorylationTEVHESYYKHLKPLQ
HHHHHHHHHHHHHHH
10.9523140645
652AcetylationEVHESYYKHLKPLQS
HHHHHHHHHHHHHHH
33.9423576753
652SuccinylationEVHESYYKHLKPLQS
HHHHHHHHHHHHHHH
33.9424315375
652UbiquitinationEVHESYYKHLKPLQS
HHHHHHHHHHHHHHH
33.94-
655AcetylationESYYKHLKPLQSKL-
HHHHHHHHHHHHCC-
43.3223864654
655GlutarylationESYYKHLKPLQSKL-
HHHHHHHHHHHHCC-
43.3224703693
655SuccinylationESYYKHLKPLQSKL-
HHHHHHHHHHHHCC-
43.32-
655SuccinylationESYYKHLKPLQSKL-
HHHHHHHHHHHHCC-
43.3223806337
660AcetylationHLKPLQSKL------
HHHHHHHCC------
45.302374607
660SuccinylationHLKPLQSKL------
HHHHHHHCC------
45.3024315375

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACOX1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACOX1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACOX1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267 AND LYS-643, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-649, ANDMASS SPECTROMETRY.

TOP