ABCD3_MOUSE - dbPTM
ABCD3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCD3_MOUSE
UniProt AC P55096
Protein Name ATP-binding cassette sub-family D member 3
Gene Name Abcd3
Organism Mus musculus (Mouse).
Sequence Length 659
Subcellular Localization Peroxisome membrane
Multi-pass membrane protein.
Protein Description Probable transporter involved in the transport of branched-chain fatty acids and C27 bile acids into the peroxisome; the latter function is a crucial step in bile acid biosynthesis. The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity..
Protein Sequence MAAFSKYLTARNTSLAGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVDKVFLSRLSQILKIMVPRTFCKETGYLLLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSSKDFKRYLFNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTRYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHNFIFFRFSMGFIDSIIAKYVATVVGYLVVSRPFLDLAHPRHLHSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFTARITELMQVLKDLNHGRYERTMVSQQEKGIEGAQASPLVPGAGEIINTDNIIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKKRGISDQVLKEYLDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKKITEDTVEFGS
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
6Succinylation--MAAFSKYLTARNT
--CCHHHHHHHHCCC		37.5124315375
12N-linked_GlycosylationSKYLTARNTSLAGAA
HHHHHHCCCHHHHHH		31.39-
24S-nitrosylationGAAFLLLCLLHKRRR
HHHHHHHHHHHHHHH		3.7122178444
38MalonylationRALGLHGKKSGKPPL
HHHCCCCCCCCCCCC		32.7726320211
38UbiquitinationRALGLHGKKSGKPPL
HHHCCCCCCCCCCCC		32.7727667366
39UbiquitinationALGLHGKKSGKPPLQ
HHCCCCCCCCCCCCC		69.8722790023
40PhosphorylationLGLHGKKSGKPPLQN
HCCCCCCCCCCCCCC		56.3872273821
42UbiquitinationLHGKKSGKPPLQNNE
CCCCCCCCCCCCCCC		51.0227667366
42AcetylationLHGKKSGKPPLQNNE
CCCCCCCCCCCCCCC		51.0223864654
42MalonylationLHGKKSGKPPLQNNE
CCCCCCCCCCCCCCC		51.0226320211
53AcetylationQNNEKEGKKERAVVD
CCCCCCCHHHHHHHH		53.182389921
54AcetylationNNEKEGKKERAVVDK
CCCCCCHHHHHHHHH		64.396569323
61SuccinylationKERAVVDKVFLSRLS
HHHHHHHHHHHHHHH		24.2324315375
61AcetylationKERAVVDKVFLSRLS
HHHHHHHHHHHHHHH		24.2323576753
61UbiquitinationKERAVVDKVFLSRLS
HHHHHHHHHHHHHHH		24.23-
72UbiquitinationSRLSQILKIMVPRTF
HHHHHHHHHHCCHHH		30.3122790023
106N-linked_GlycosylationCDVWMIQNGTLIESG
CCEEEEECCEEEECC		34.20-
123AcetylationGRSSKDFKRYLFNFI
CCCCHHHHHHHHHHH		50.716566943
180UbiquitinationYKMGNLDNRIANPDQ
HHCCCCCCCCCCHHH		40.1927667366
187UbiquitinationNRIANPDQLLTQDVE
CCCCCHHHHHHHHHH		39.3627667366
206N-linked_GlycosylationSVVDLYSNLSKPFLD
HHHHHHHCCCHHHHH		34.47-
213UbiquitinationNLSKPFLDIVLYIFK
CCCHHHHHHHHHHHH		29.3627667366
253UbiquitinationRLRRPIGKMTIMEQK
HHCCCCCCCEEEEEE		33.3227667366
253MalonylationRLRRPIGKMTIMEQK
HHCCCCCCCEEEEEE		33.3226320211
260AcetylationKMTIMEQKYEGEYRY
CCEEEEEECCCCEEE		31.7823576753
260MalonylationKMTIMEQKYEGEYRY
CCEEEEEECCCCEEE		31.7826320211
260UbiquitinationKMTIMEQKYEGEYRY
CCEEEEEECCCCEEE		31.7827667366
261PhosphorylationMTIMEQKYEGEYRYV
CEEEEEECCCCEEEE		28.9417242355
265PhosphorylationEQKYEGEYRYVNSRL
EEECCCCEEEECCEE		20.3525521595
286MalonylationIAFYNGNKREKQTIH
EEEECCCHHHHHHHH		64.4326320211
286AcetylationIAFYNGNKREKQTIH
EEEECCCHHHHHHHH		64.4323864654
286UbiquitinationIAFYNGNKREKQTIH
EEEECCCHHHHHHHH		64.4327667366
289SuccinylationYNGNKREKQTIHSVF
ECCCHHHHHHHHHHH		57.6924315375
289AcetylationYNGNKREKQTIHSVF
ECCCHHHHHHHHHHH		57.6923864654
289MalonylationYNGNKREKQTIHSVF
ECCCHHHHHHHHHHH		57.6926320211
294PhosphorylationREKQTIHSVFRKLVE
HHHHHHHHHHHHHHH		21.0759155015
298MalonylationTIHSVFRKLVEHLHN
HHHHHHHHHHHHHHH		45.4825418362
343UbiquitinationPFLDLAHPRHLHSTH
CCHHCCCCCCCCCCH		21.5627667366
366DimethylationQSGRMLLRMSQALGR
HHHHHHHHHHHHHHH		20.81-
368PhosphorylationGRMLLRMSQALGRIV
HHHHHHHHHHHHHHH		13.0822817900
373DimethylationRMSQALGRIVLAGRE
HHHHHHHHHHHCHHH		19.38-
379DimethylationGRIVLAGREMTRLAG
HHHHHCHHHHHHHHH		25.55-
382PhosphorylationVLAGREMTRLAGFTA
HHCHHHHHHHHHHHH		20.1351500365
399AcetylationTELMQVLKDLNHGRY
HHHHHHHHHCCCCCC		62.4023576753
399UbiquitinationTELMQVLKDLNHGRY
HHHHHHHHHCCCCCC		62.40-
399SuccinylationTELMQVLKDLNHGRY
HHHHHHHHHCCCCCC		62.4024315375
406PhosphorylationKDLNHGRYERTMVSQ
HHCCCCCCCCCCCCH		17.8522345495
416UbiquitinationTMVSQQEKGIEGAQA
CCCCHHHHCCCCCCC		61.9322790023
424PhosphorylationGIEGAQASPLVPGAG
CCCCCCCCCCCCCCC		13.4925521595
436PhosphorylationGAGEIINTDNIIKFD
CCCCCCCCCCCEEEC		21.7323140645
456UbiquitinationTPNGDILIQDLSFEV
CCCCCEEEEECCEEE		2.8227667366
479UbiquitinationCGPNGCGKSSLFRVL
ECCCCCCHHHHHHHH		40.7322790023
529AcetylationQVIYPDGKEDQKKRG
CEECCCCCHHHHHCC		66.5523864654
529MalonylationQVIYPDGKEDQKKRG
CEECCCCCHHHHHCC		66.5526320211
529UbiquitinationQVIYPDGKEDQKKRG
CEECCCCCHHHHHCC		66.5527667366
533SuccinylationPDGKEDQKKRGISDQ
CCCCHHHHHCCCCHH		57.6823954790
533AcetylationPDGKEDQKKRGISDQ
CCCCHHHHHCCCCHH		57.6823576753
533MalonylationPDGKEDQKKRGISDQ
CCCCHHHHHCCCCHH		57.6826320211
534UbiquitinationDGKEDQKKRGISDQV
CCCHHHHHCCCCHHH		50.6622790023
534MalonylationDGKEDQKKRGISDQV
CCCHHHHHCCCCHHH		50.6625418362
534AcetylationDGKEDQKKRGISDQV
CCCHHHHHCCCCHHH		50.662373131
538PhosphorylationDQKKRGISDQVLKEY
HHHHCCCCHHHHHHH		25.4728066266
543UbiquitinationGISDQVLKEYLDNVQ
CCCHHHHHHHHHHCC		45.5222790023
543AcetylationGISDQVLKEYLDNVQ
CCCHHHHHHHHHHCC		45.5223864654
576UbiquitinationDVLSGGEKQRMAMAR
HHHCCHHHHHHHHHH		46.62-
576AcetylationDVLSGGEKQRMAMAR
HHHCCHHHHHHHHHH		46.6223954790
576SuccinylationDVLSGGEKQRMAMAR
HHHCCHHHHHHHHHH		46.6224315375
615UbiquitinationYIYSHCRKVGITLFT
HHHHHHHHCCEEEEE		50.6522790023
648AcetylationGRGNYEFKKITEDTV
CCCCEEEEECCCCCC		31.1823864654
659PhosphorylationEDTVEFGS-------
CCCCCCCC-------		42.2325521595
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 ABCD3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABCD3_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 ABCD3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ABCD3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABCD3_MOUSE

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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-260, AND MASS SPECTROMETRY.
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-424, AND MASSSPECTROMETRY.

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