ABCD1_HUMAN - dbPTM
ABCD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCD1_HUMAN
UniProt AC P33897
Protein Name ATP-binding cassette sub-family D member 1
Gene Name ABCD1
Organism Homo sapiens (Human).
Sequence Length 745
Subcellular Localization Peroxisome membrane
Multi-pass membrane protein.
Protein Description Probable transporter. The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity..
Protein Sequence MPVLSRPRPWRGNTLKRTAVLLALAAYGAHKVYPLVRQCLAPARGLQAPAGEPTQEASGVAAAKAGMNRVFLQRLLWLLRLLFPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAGTAWPSAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATGYSESDAEAVKKAALEKKEEELVSERTEAFTIARNLLTAAADAIERIMSSYKEVTELAGYTARVHEMFQVFEDVQRCHFKRPRELEDAQAGSGTIGRSGVRVEGPLKIRGQVVDVEQGIICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAARLSLTEEKQRLEQQLAGIPKMQRRLQELCQILGEAVAPAHVPAPSPQGPGGLQGAST
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
58PhosphorylationGEPTQEASGVAAAKA
CCCCCCHHHHHHHHH		32.8021815630
64UbiquitinationASGVAAAKAGMNRVF
HHHHHHHHHCCCHHH		40.5221963094
105PhosphorylationSAALVSRTFLSVYVA
HHHHHHHHHHHHHHH		22.7920860994
110PhosphorylationSRTFLSVYVARLDGR
HHHHHHHHHHHCCCC		5.7520860994
214N-linked_GlycosylationSVAHLYSNLTKPLLD
HHHHHHHCCCHHHHH		37.87UniProtKB CARBOHYD
262PhosphorylationANVLRAFSPKFGELV
HHHHHHHCHHHHHHH		26.6224719451
264UbiquitinationVLRAFSPKFGELVAE
HHHHHCHHHHHHHHH		65.8821963094
337PhosphorylationLEQFLMKYVWSASGL
HHHHHHHHHHHHCCH		8.0057474621
357PhosphorylationPIITATGYSESDAEA
EEEECCCCCHHHHHH		12.6246156823
358PhosphorylationIITATGYSESDAEAV
EEECCCCCHHHHHHH		31.7850558655
360PhosphorylationTATGYSESDAEAVKK
ECCCCCHHHHHHHHH		35.8650558661
367UbiquitinationSDAEAVKKAALEKKE
HHHHHHHHHHHHHHH		32.0927667366
393PhosphorylationTIARNLLTAAADAIE
HHHHHHHHHHHHHHH		19.8822210691
404PhosphorylationDAIERIMSSYKEVTE
HHHHHHHHHCHHHHH		28.3025003641
406PhosphorylationIERIMSSYKEVTELA
HHHHHHHCHHHHHHH		12.1272550291
407UbiquitinationERIMSSYKEVTELAG
HHHHHHCHHHHHHHC		47.8929901268
410PhosphorylationMSSYKEVTELAGYTA
HHHCHHHHHHHCHHH		26.7720068231
415PhosphorylationEVTELAGYTARVHEM
HHHHHHCHHHHHHHH		7.5120068231
416PhosphorylationVTELAGYTARVHEMF
HHHHHCHHHHHHHHH		13.6820068231
447PhosphorylationLEDAQAGSGTIGRSG
HCCCCCCCCCCCCCC		35.4625072903
449PhosphorylationDAQAGSGTIGRSGVR
CCCCCCCCCCCCCCE		23.1925072903
453PhosphorylationGSGTIGRSGVRVEGP
CCCCCCCCCCEEECC		36.1159151727
462UbiquitinationVRVEGPLKIRGQVVD
CEEECCEEEECEEEE		33.2332142685
513UbiquitinationTGPNGCGKSSLFRIL
ECCCCCCHHHHHHHH		40.7322817900
515PhosphorylationPNGCGKSSLFRILGG
CCCCCHHHHHHHHCC		34.7124719451
533UbiquitinationTYGGVLYKPPPQRMF
CCCEEEECCCCCCEE		47.0621963094
569UbiquitinationSVEDMQRKGYSEQDL
CHHHHHHCCCCHHHH		45.3621963094
602UbiquitinationWEAMCDWKDVLSGGE
HHHCCCHHHHCCCCC		25.3829967540
610UbiquitinationDVLSGGEKQRIGMAR
HHCCCCCCCCCEEHH		48.4229901268
6102-HydroxyisobutyrylationDVLSGGEKQRIGMAR
HHCCCCCCCCCEEHH		48.42-
648UbiquitinationGKIFQAAKDAGIALL
CHHHHHHHHHCEEEE		51.6421963094
656PhosphorylationDAGIALLSITHRPSL
HHCEEEEEECCCCCH		26.7020873877
658PhosphorylationGIALLSITHRPSLWK
CEEEEEECCCCCHHH		14.4120873877
662PhosphorylationLSITHRPSLWKYHTH
EEECCCCCHHHEEEE		46.9820873877
666PhosphorylationHRPSLWKYHTHLLQF
CCCCHHHEEEEEEEE		10.607331161
680UbiquitinationFDGEGGWKFEKLDSA
ECCCCCEEEEECCHH		47.0929967540
683UbiquitinationEGGWKFEKLDSAARL
CCCEEEEECCHHHHH		61.8129901268
696AcetylationRLSLTEEKQRLEQQL
HHCCHHHHHHHHHHH		34.1926051181
696UbiquitinationRLSLTEEKQRLEQQL
HHCCHHHHHHHHHHH		34.1929967540
708UbiquitinationQQLAGIPKMQRRLQE
HHHCCHHHHHHHHHH		45.8322817900
733PhosphorylationPAHVPAPSPQGPGGL
CCCCCCCCCCCCCCC		31.7721889498
744PhosphorylationPGGLQGAST------
CCCCCCCCC------		41.2824719451
745PhosphorylationGGLQGAST-------
CCCCCCCC-------		41.9420873877
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 ABCD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABCD1_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 ABCD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABCD2_HUMANABCD2physical
10551832
ABCD3_HUMANABCD3physical
22939629
PEX3_HUMANPEX3physical
22939629
NDUAC_HUMANNDUFA12physical
22939629
NDUB4_HUMANNDUFB4physical
22939629
ADAS_HUMANAGPSphysical
22939629
ITPR3_HUMANITPR3physical
22939629
ELAV1_HUMANELAVL1physical
22939629
S27A2_HUMANSLC27A2physical
16781659
RSSA_HUMANRPSAphysical
21988832
Drug and Disease Associations
Kegg Disease
H00176 Adrenoleukodystrophy (ALD), including: Schilder-Addison Complex; Childhood cerebral adrenoleukodystr
OMIM Disease
300100Adrenoleukodystrophy (ALD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABCD1_HUMAN

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Related Literatures of Post-Translational Modification
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-733, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND MASSSPECTROMETRY.

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