ABCD3_HUMAN - dbPTM
ABCD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCD3_HUMAN
UniProt AC P28288
Protein Name ATP-binding cassette sub-family D member 3
Gene Name ABCD3
Organism Homo sapiens (Human).
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. [PubMed: 25168382 The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity]
Protein Sequence MAAFSKYLTARNSSLAGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVDKVFFSRLIQILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTKYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLVVSGLFLTRLRRPIGKMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFILFRFSMGFIDSIIAKYLATVVGYLVVSRPFLDLSHPRHLKSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFTARITELMQVLKDLNHGKYERTMVSQQEKGIEGVQVIPLIPGAGEIIIADNIIKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKGISDLVLKEYLDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKQITEDTVEFGS
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
5Phosphorylation---MAAFSKYLTARN
---CCHHHHHHHHCC
18.7020068231
62-Hydroxyisobutyrylation--MAAFSKYLTARNS
--CCHHHHHHHHCCC
37.51-
6Acetylation--MAAFSKYLTARNS
--CCHHHHHHHHCCC
37.5125825284
6Ubiquitination--MAAFSKYLTARNS
--CCHHHHHHHHCCC
37.5124816145
7Phosphorylation-MAAFSKYLTARNSS
-CCHHHHHHHHCCCH
14.2120068231
9PhosphorylationAAFSKYLTARNSSLA
CHHHHHHHHCCCHHH
22.0820068231
12N-linked_GlycosylationSKYLTARNSSLAGAA
HHHHHHCCCHHHHHH
33.22UniProtKB CARBOHYD
35UbiquitinationKRRRALGLHGKKSGK
HHHHHHCCCCCCCCC
5.1121890473
382-HydroxyisobutyrylationRALGLHGKKSGKPPL
HHHCCCCCCCCCCCC
32.77-
38UbiquitinationRALGLHGKKSGKPPL
HHHCCCCCCCCCCCC
32.7722817900
39UbiquitinationALGLHGKKSGKPPLQ
HHCCCCCCCCCCCCC
69.8721906983
39 (in isoform 1)Ubiquitination-69.8721890473
39 (in isoform 2)Ubiquitination-69.8721890473
39 (in isoform 3)Ubiquitination-69.8721890473
40PhosphorylationLGLHGKKSGKPPLQN
HCCCCCCCCCCCCCC
56.3830266825
42UbiquitinationLHGKKSGKPPLQNNE
CCCCCCCCCCCCCCC
51.0229967540
50UbiquitinationPPLQNNEKEGKKERA
CCCCCCCCCCHHHHH
74.1032142685
612-HydroxyisobutyrylationKERAVVDKVFFSRLI
HHHHHHHHHHHHHHH
29.36-
61AcetylationKERAVVDKVFFSRLI
HHHHHHHHHHHHHHH
29.3627452117
61UbiquitinationKERAVVDKVFFSRLI
HHHHHHHHHHHHHHH
29.3622817900
61 (in isoform 1)Ubiquitination-29.3621890473
61 (in isoform 2)Ubiquitination-29.3621890473
61 (in isoform 3)Ubiquitination-29.3621890473
65PhosphorylationVVDKVFFSRLIQILK
HHHHHHHHHHHHHHH
18.0846267013
72UbiquitinationSRLIQILKIMVPRTF
HHHHHHHHHHCCHHH
30.3121963094
78UbiquitinationLKIMVPRTFCKETGY
HHHHCCHHHCHHHCH
27.5821963094
85PhosphorylationTFCKETGYLVLIAVM
HHCHHHCHHHHHHHH
10.8920068231
85UbiquitinationTFCKETGYLVLIAVM
HHCHHHCHHHHHHHH
10.8921890473
87UbiquitinationCKETGYLVLIAVMLV
CHHHCHHHHHHHHHH
2.4721963094
93UbiquitinationLVLIAVMLVSRTYCD
HHHHHHHHHCCCCCC
2.2521963094
95PhosphorylationLIAVMLVSRTYCDVW
HHHHHHHCCCCCCEE
18.2346267019
96UbiquitinationIAVMLVSRTYCDVWM
HHHHHHCCCCCCEEE
23.4121963094
101UbiquitinationVSRTYCDVWMIQNGT
HCCCCCCEEEEECCE
3.1421963094
106N-linked_GlycosylationCDVWMIQNGTLIESG
CCEEEEECCEEEECC
34.20UniProtKB CARBOHYD
145PhosphorylationLVNNFLKYGLNELKL
HHHHHHHHCCHHHHH
29.065051317
151AcetylationKYGLNELKLCFRVRL
HHCCHHHHHHHHHHH
36.7126051181
151UbiquitinationKYGLNELKLCFRVRL
HHCCHHHHHHHHHHH
36.7121963094
160UbiquitinationCFRVRLTKYLYEEYL
HHHHHHHHHHHHHHH
37.5421963094
163PhosphorylationVRLTKYLYEEYLQAF
HHHHHHHHHHHHHHH
12.018273949
167UbiquitinationKYLYEEYLQAFTYYK
HHHHHHHHHHHHHHH
3.1521963094
173PhosphorylationYLQAFTYYKMGNLDN
HHHHHHHHHCCCCCC
7.468273961
174UbiquitinationLQAFTYYKMGNLDNR
HHHHHHHHCCCCCCC
29.8921963094
175UbiquitinationQAFTYYKMGNLDNRI
HHHHHHHCCCCCCCC
2.1921963094
180UbiquitinationYKMGNLDNRIANPDQ
HHCCCCCCCCCCHHH
40.1921963094
184UbiquitinationNLDNRIANPDQLLTQ
CCCCCCCCHHHHHHH
38.0121963094
187UbiquitinationNRIANPDQLLTQDVE
CCCCCHHHHHHHHHH
39.3623000965
192UbiquitinationPDQLLTQDVEKFCNS
HHHHHHHHHHHHHHH
45.3623000965
198UbiquitinationQDVEKFCNSVVDLYS
HHHHHHHHHHHHHHH
40.7621963094
206N-linked_GlycosylationSVVDLYSNLSKPFLD
HHHHHHHCCCHHHHH
34.47UniProtKB CARBOHYD
213UbiquitinationNLSKPFLDIVLYIFK
CCCHHHHHHHHHHHH
29.3623000965
216UbiquitinationKPFLDIVLYIFKLTS
HHHHHHHHHHHHHHH
2.5123000965
221UbiquitinationIVLYIFKLTSAIGAQ
HHHHHHHHHHHHCCC
2.9722817900
223UbiquitinationLYIFKLTSAIGAQGP
HHHHHHHHHHCCCCC
28.4622817900
231UbiquitinationAIGAQGPASMMAYLV
HHCCCCCHHHHHHHH
19.5121963094
253MalonylationRLRRPIGKMTITEQK
CCCCCCCCCEEEEEE
33.3226320211
253UbiquitinationRLRRPIGKMTITEQK
CCCCCCCCCEEEEEE
33.3222817900
253 (in isoform 1)Ubiquitination-33.3221890473
253 (in isoform 2)Ubiquitination-33.3221890473
2602-HydroxyisobutyrylationKMTITEQKYEGEYRY
CCEEEEEEECCEEEE
38.75-
260AcetylationKMTITEQKYEGEYRY
CCEEEEEEECCEEEE
38.7519608861
260MalonylationKMTITEQKYEGEYRY
CCEEEEEEECCEEEE
38.7526320211
260UbiquitinationKMTITEQKYEGEYRY
CCEEEEEEECCEEEE
38.7532142685
260 (in isoform 1)Ubiquitination-38.7521890473
260 (in isoform 2)Ubiquitination-38.7521890473
264UbiquitinationTEQKYEGEYRYVNSR
EEEEECCEEEEECCE
18.2021963094
274UbiquitinationYVNSRLITNSEEIAF
EECCEEECCCCCEEE
36.9721890473
277UbiquitinationSRLITNSEEIAFYNG
CEEECCCCCEEEECC
56.3321963094
284UbiquitinationEEIAFYNGNKREKQT
CCEEEECCCHHHHHH
29.6521963094
286AcetylationIAFYNGNKREKQTVH
EEEECCCHHHHHHHH
64.4326051181
286UbiquitinationIAFYNGNKREKQTVH
EEEECCCHHHHHHHH
64.4323000965
286 (in isoform 1)Ubiquitination-64.4321890473
289MalonylationYNGNKREKQTVHSVF
ECCCHHHHHHHHHHH
56.1326320211
289UbiquitinationYNGNKREKQTVHSVF
ECCCHHHHHHHHHHH
56.1323000965
289 (in isoform 2)Ubiquitination-56.1321890473
295 (in isoform 2)Ubiquitination-3.0421890473
310UbiquitinationLHNFILFRFSMGFID
HHHHHHHHHHHHHHH
21.2023000965
313UbiquitinationFILFRFSMGFIDSII
HHHHHHHHHHHHHHH
4.7023000965
326UbiquitinationIIAKYLATVVGYLVV
HHHHHHHHHHHHHHH
17.0921963094
332UbiquitinationATVVGYLVVSRPFLD
HHHHHHHHHCCCCCC
2.5021963094
334PhosphorylationVVGYLVVSRPFLDLS
HHHHHHHCCCCCCCC
27.1024719451
3472-HydroxyisobutyrylationLSHPRHLKSTHSELL
CCCCCHHHHHHHHHH
47.38-
347AcetylationLSHPRHLKSTHSELL
CCCCCHHHHHHHHHH
47.3826051181
347UbiquitinationLSHPRHLKSTHSELL
CCCCCHHHHHHHHHH
47.3821963094
347 (in isoform 1)Ubiquitination-47.3821890473
357PhosphorylationHSELLEDYYQSGRML
HHHHHHHHHHHHHHH
8.27110743123
358PhosphorylationSELLEDYYQSGRMLL
HHHHHHHHHHHHHHH
14.44110743131
360PhosphorylationLLEDYYQSGRMLLRM
HHHHHHHHHHHHHHH
16.55110743139
368PhosphorylationGRMLLRMSQALGRIV
HHHHHHHHHHHHHHH
13.0829978859
371UbiquitinationLLRMSQALGRIVLAG
HHHHHHHHHHHHHCH
3.5221890473
388PhosphorylationMTRLAGFTARITELM
HHHHHHHHHHHHHHH
17.7046267025
392PhosphorylationAGFTARITELMQVLK
HHHHHHHHHHHHHHH
19.9525599653
395SulfoxidationTARITELMQVLKDLN
HHHHHHHHHHHHHCC
1.7921406390
399AcetylationTELMQVLKDLNHGKY
HHHHHHHHHCCCCCC
62.4019608861
399UbiquitinationTELMQVLKDLNHGKY
HHHHHHHHHCCCCCC
62.4021963094
399 (in isoform 1)Ubiquitination-62.4021890473
4052-HydroxyisobutyrylationLKDLNHGKYERTMVS
HHHCCCCCCCCCCCC
36.07-
405AcetylationLKDLNHGKYERTMVS
HHHCCCCCCCCCCCC
36.0726051181
405UbiquitinationLKDLNHGKYERTMVS
HHHCCCCCCCCCCCC
36.0721906983
405 (in isoform 1)Ubiquitination-36.0721890473
406UbiquitinationKDLNHGKYERTMVSQ
HHCCCCCCCCCCCCC
18.4221963094
416UbiquitinationTMVSQQEKGIEGVQV
CCCCCCCCCCCCEEE
61.93-
423UbiquitinationKGIEGVQVIPLIPGA
CCCCCEEEEECCCCC
4.5221963094
425 (in isoform 2)Ubiquitination-25.9421890473
426UbiquitinationEGVQVIPLIPGAGEI
CCEEEEECCCCCCEE
5.1923000965
429UbiquitinationQVIPLIPGAGEIIIA
EEEECCCCCCEEEEE
38.9421963094
431UbiquitinationIPLIPGAGEIIIADN
EECCCCCCEEEEECC
32.3323000965
433 (in isoform 2)Ubiquitination-2.4321890473
449PhosphorylationFDHVPLATPNGDVLI
ECCCCCCCCCCCEEE
25.6027050516
460UbiquitinationDVLIRDLNFEVRSGA
CEEEEECCEEEECCC
35.0122817900
462UbiquitinationLIRDLNFEVRSGANV
EEEECCEEEECCCEE
35.6322817900
466 (in isoform 2)Ubiquitination-15.5921890473
470UbiquitinationVRSGANVLICGPNGC
EECCCEEEEECCCCC
2.4121963094
472S-nitrosylationSGANVLICGPNGCGK
CCCEEEEECCCCCCH
6.922212679
479UbiquitinationCGPNGCGKSSLFRVL
ECCCCCCHHHHHHHH
40.7321963094
481PhosphorylationPNGCGKSSLFRVLGE
CCCCCHHHHHHHHHH
34.7124719451
499UbiquitinationLFGGRLTKPERGKLF
HHCCCCCCCCCCCCE
49.8523000965
503UbiquitinationRLTKPERGKLFYVPQ
CCCCCCCCCCEEECC
29.3821963094
504UbiquitinationLTKPERGKLFYVPQR
CCCCCCCCCEEECCC
41.4623000965
523UbiquitinationLGTLRDQVIYPDGRE
CCCCCCEEECCCCCH
5.4723000965
525PhosphorylationTLRDQVIYPDGREDQ
CCCCEEECCCCCHHH
9.0920068231
528UbiquitinationDQVIYPDGREDQKRK
CEEECCCCCHHHHHC
30.3023000965
533AcetylationPDGREDQKRKGISDL
CCCCHHHHHCCHHHH
69.2925953088
533UbiquitinationPDGREDQKRKGISDL
CCCCHHHHHCCHHHH
69.2922817900
535UbiquitinationGREDQKRKGISDLVL
CCHHHHHCCHHHHHH
68.5721906983
535 (in isoform 1)Ubiquitination-68.5721890473
543UbiquitinationGISDLVLKEYLDNVQ
CHHHHHHHHHHHCCC
36.5121906983
543 (in isoform 1)Ubiquitination-36.5121890473
545PhosphorylationSDLVLKEYLDNVQLG
HHHHHHHHHHCCCHH
20.12110743155
557UbiquitinationQLGHILEREGGWDSV
CHHHHHHCCCCCHHH
44.4022817900
559UbiquitinationGHILEREGGWDSVQD
HHHHHCCCCCHHHHH
49.0322817900
567UbiquitinationGWDSVQDWMDVLSGG
CCHHHHHHHHHHCCH
2.8121963094
572PhosphorylationQDWMDVLSGGEKQRM
HHHHHHHCCHHHHHH
44.60110743163
576AcetylationDVLSGGEKQRMAMAR
HHHCCHHHHHHHHHH
46.6226051181
576UbiquitinationDVLSGGEKQRMAMAR
HHHCCHHHHHHHHHH
46.6221963094
576 (in isoform 1)Ubiquitination-46.6221890473
600UbiquitinationILDECTSAVSVDVEG
EHHCCCCCEEEECCH
4.5821963094
619PhosphorylationHCRKVGITLFTVSHR
HHCCEEEEEEEECCC
15.1930108239
622PhosphorylationKVGITLFTVSHRKSL
CEEEEEEEECCCHHH
24.9830108239
624PhosphorylationGITLFTVSHRKSLWK
EEEEEEECCCHHHHH
17.9530108239
631AcetylationSHRKSLWKHHEYYLH
CCCHHHHHCCEEEEC
40.1425825284
635PhosphorylationSLWKHHEYYLHMDGR
HHHHCCEEEECCCCC
13.637601317
636PhosphorylationLWKHHEYYLHMDGRG
HHHCCEEEECCCCCC
6.277601329
645PhosphorylationHMDGRGNYEFKQITE
CCCCCCCEEEEECCC
26.107601341
651PhosphorylationNYEFKQITEDTVEFG
CEEEEECCCCCCCCC
25.8929759185
654PhosphorylationFKQITEDTVEFGS--
EEECCCCCCCCCC--
18.72113307785
659PhosphorylationEDTVEFGS-------
CCCCCCCC-------
42.2329759185

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABCD3_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 ABCD3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABCD1_HUMANABCD1physical
10551832
PEX19_HUMANPEX19physical
11453642
PEX3_HUMANPEX3physical
22939629
NDUV1_HUMANNDUFV1physical
22939629
MPV17_HUMANMPV17physical
22939629
TAP1_HUMANTAP1physical
22939629
VATC1_HUMANATP6V1C1physical
22939629
ADAS_HUMANAGPSphysical
22939629
NNTM_HUMANNNTphysical
22939629
SURF1_HUMANSURF1physical
22939629
SYJ2B_HUMANSYNJ2BPphysical
22939629
RM41_HUMANMRPL41physical
22939629
ZN454_HUMANZNF454physical
22939629
TIDC1_HUMANTIMMDC1physical
22939629
NDUBB_HUMANNDUFB11physical
22939629
NDUS4_HUMANNDUFS4physical
22939629
TOM40_HUMANTOMM40physical
22939629
TUFT1_HUMANTUFT1physical
21988832
PSA1_HUMANPSMA1physical
21988832
EF2_HUMANEEF2physical
26344197
STOM_HUMANSTOMphysical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616278Congenital bile acid synthesis defect 5 (CBAS5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABCD3_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-260 AND LYS-399, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND MASSSPECTROMETRY.

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