ACOX2_HUMAN - dbPTM
ACOX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACOX2_HUMAN
UniProt AC Q99424
Protein Name Peroxisomal acyl-coenzyme A oxidase 2 {ECO:0000303|PubMed:14702039}
Gene Name ACOX2 {ECO:0000312|HGNC:HGNC:120}
Organism Homo sapiens (Human).
Sequence Length 681
Subcellular Localization Peroxisome .
Protein Description Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids..
Protein Sequence MGSPVHRVSLGDTWSRQMHPDIESERYMQSFDVERLTNILDGGAQNTALRRKVESIIHSYPEFSCKDNYFMTQNERYKAAMRRAFHIRLIARRLGWLEDGRELGYAYRALSGDVALNIHRVFVRALRSLGSEEQIAKWDPLCKNIQIIATYAQTELGHGTYLQGLETEATYDAATQEFVIHSPTLTATKWWPGDLGRSATHALVQAQLICSGARRGMHAFIVPIRSLQDHTPLPGIIIGDIGPKMDFDQTDNGFLQLNHVRVPRENMLSRFAQVLPDGTYVKLGTAQSNYLPMVVVRVELLSGEILPILQKACVIAMRYSVIRRQSRLRPSDPEAKVLDYQTQQQKLFPQLAISYAFHFLAVSLLEFFQHSYTAILNQDFSFLPELHALSTGMKAMMSEFCTQGAEMCRRACGGHGYSKLSGLPSLVTKLSASCTYEGENTVLYLQVARFLVKSYLQTQMSPGSTPQRSLSPSVAYLTAPDLARCPAQRAADFLCPELYTTAWAHVAVRLIKDSVQHLQTLTQSGADQHEAWNQTTVIHLQAAKVHCYYVTVKGFTEALEKLENEPAIQQVLKRLCDLHAIHGILTNSGDFLHDAFLSGAQVDMARTAYLDLLRLIRKDAILLTDAFDFTDQCLNSALGCYDGNVYERLFQWAQKSPTNTQENPAYEEYIRPLLQSWRSKL
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
3Phosphorylation-----MGSPVHRVSL
-----CCCCCEEEEC		23.58-
9PhosphorylationGSPVHRVSLGDTWSR
CCCCEEEECCCHHHH		26.9622798277
13PhosphorylationHRVSLGDTWSRQMHP
EEEECCCHHHHCCCC		24.4428450419
15PhosphorylationVSLGDTWSRQMHPDI
EECCCHHHHCCCCCC		18.0922210691
24PhosphorylationQMHPDIESERYMQSF
CCCCCCCCHHHHHHC		27.9222210691
55PhosphorylationALRRKVESIIHSYPE
HHHHHHHHHHHHCCC		29.8159148725
66SuccinylationSYPEFSCKDNYFMTQ
HCCCCCCCCCCCCCH		48.05-
66SuccinylationSYPEFSCKDNYFMTQ
HCCCCCCCCCCCCCH		48.05-
137SuccinylationGSEEQIAKWDPLCKN
CCHHHHHCCCHHHCH		54.48-
137SuccinylationGSEEQIAKWDPLCKN
CCHHHHHCCCHHHCH		54.48-
290PhosphorylationLGTAQSNYLPMVVVR
ECCCCCCCCCEEEEE		19.897108255
390PhosphorylationLPELHALSTGMKAMM
HHHHHHHHHHHHHHH		24.5723879269
398PhosphorylationTGMKAMMSEFCTQGA
HHHHHHHHHHHHHHH		17.9023879269
417PhosphorylationRACGGHGYSKLSGLP
HHHCCCCCHHCCCCC		9.2822817900
425PhosphorylationSKLSGLPSLVTKLSA
HHCCCCCHHHHHEEE		40.2823612710
431PhosphorylationPSLVTKLSASCTYEG
CHHHHHEEECCEECC		21.4924043423
433PhosphorylationLVTKLSASCTYEGEN
HHHHEEECCEECCCC		12.0124043423
435PhosphorylationTKLSASCTYEGENTV
HHEEECCEECCCCHH		23.3224043423
436PhosphorylationKLSASCTYEGENTVL
HEEECCEECCCCHHH		26.6824043423
441PhosphorylationCTYEGENTVLYLQVA
CEECCCCHHHHHHHH		13.9524043423
444PhosphorylationEGENTVLYLQVARFL
CCCCHHHHHHHHHHH		7.2524043423
453SuccinylationQVARFLVKSYLQTQM
HHHHHHHHHHHHHCC		35.21-
453SuccinylationQVARFLVKSYLQTQM
HHHHHHHHHHHHHCC		35.21-
453MalonylationQVARFLVKSYLQTQM
HHHHHHHHHHHHHCC		35.2126320211
454PhosphorylationVARFLVKSYLQTQMS
HHHHHHHHHHHHCCC		24.4824043423
455PhosphorylationARFLVKSYLQTQMSP
HHHHHHHHHHHCCCC		9.3424043423
458PhosphorylationLVKSYLQTQMSPGST
HHHHHHHHCCCCCCC		24.5224043423
461PhosphorylationSYLQTQMSPGSTPQR
HHHHHCCCCCCCCCC		19.1124043423
464PhosphorylationQTQMSPGSTPQRSLS
HHCCCCCCCCCCCCC		40.0528857561
465PhosphorylationTQMSPGSTPQRSLSP
HCCCCCCCCCCCCCC		29.3828857561
556O-linked_GlycosylationYVTVKGFTEALEKLE
EEEECCHHHHHHHHC		29.0830379171
561SuccinylationGFTEALEKLENEPAI
CHHHHHHHHCCCHHH		63.05-
561SuccinylationGFTEALEKLENEPAI
CHHHHHHHHCCCHHH		63.05-
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 ACOX2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACOX2_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 ACOX2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLMAP_HUMANSLMAPphysical
28514442
STRN3_HUMANSTRN3physical
28514442
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
There are no disease associations of PTM sites.
Regulatory Network of ACOX2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-417, AND MASSSPECTROMETRY.

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