ACBD5_HUMAN - dbPTM
ACBD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACBD5_HUMAN
UniProt AC Q5T8D3
Protein Name Acyl-CoA-binding domain-containing protein 5
Gene Name ACBD5
Organism Homo sapiens (Human).
Sequence Length 534
Subcellular Localization Peroxisome membrane
Single-pass membrane protein.
Protein Description Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters..
Protein Sequence MFQFHAGSWESWCCCCLIPADRPWDRGQHWQLEMADTRSVHETRFEAAVKVIQSLPKNGSFQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEMKKIIETMPMTEKVEELLRVIGPFYEIVEDKKSGRSSDITSVRLEKISKCLEDLGNVLTSTPNAKTVNGKAESSDSGAESEEEEAQEEVKGAEQSDNDKKMMKKSADHKNLEVIVTNGYDKDGFVQDIQNDIHASSSLNGRSTEEVKPIDENLGQTGKSAVCIHQDINDDHVEDVTGIQHLTSDSDSEVYCDSMEQFGQEESLDSFTSNNGPFQYYLGGHSSQPMENSGFREDIQVPPGNGNIGNMQVVAVEGKGEVKHGGEDGRNNSGAPHREKRGGETDEFSNVRRGRGHRMQHLSEGTKGRQVGSGGDGERWGSDRGSRGSLNEQIALVLMRLQEDMQNVLQRLQKLETLTALQAKSSTSTLQTAPQPTSQRPSWWPFEMSPGVLTFAIIWPFIAQWLVYLYYQRRRRKLN
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
44 (in isoform 4)Ubiquitination-25.1521890473
46 (in isoform 4)Phosphorylation-32.2118691976
49 (in isoform 4)Phosphorylation-7.0118691976
50 (in isoform 4)Phosphorylation-28.9718669648
53 (in isoform 4)Phosphorylation-41.7318669648
54 (in isoform 4)Phosphorylation-35.2028348404
61 (in isoform 4)Phosphorylation-12.2123663014
62 (in isoform 4)Phosphorylation-45.6825159151
63 (in isoform 4)Phosphorylation-34.8725159151
67 (in isoform 4)Ubiquitination-4.0721890473
70AcetylationPTNEMMLKFYSFYKQ
CCCHHHHHHHHHHHH		25.1026051181
76AcetylationLKFYSFYKQATEGPC
HHHHHHHHHHHCCCC		31.2926051181
118 (in isoform 2)Ubiquitination-3.5721890473
120 (in isoform 2)Phosphorylation-46.3818691976
123 (in isoform 2)Phosphorylation-47.8318691976
124 (in isoform 2)Phosphorylation-2.6118669648
127PhosphorylationEMKKIIETMPMTEKV
HHHHHHHHCCCHHHH		19.0318669648
127 (in isoform 2)Phosphorylation-19.0318669648
128 (in isoform 2)Phosphorylation-1.0728348404
131PhosphorylationIIETMPMTEKVEELL
HHHHCCCHHHHHHHH		27.1226074081
135 (in isoform 2)Phosphorylation-54.7323663014
136 (in isoform 2)Phosphorylation-56.9725159151
137 (in isoform 2)Phosphorylation-2.0425159151
141 (in isoform 2)Ubiquitination-4.7221890473
145PhosphorylationLRVIGPFYEIVEDKK
HHHHHHHHHHHCCCC		14.1028796482
149 (in isoform 4)Ubiquitination-70.5421890473
151UbiquitinationFYEIVEDKKSGRSSD
HHHHHCCCCCCCCCC		35.0221906983
151 (in isoform 1)Ubiquitination-35.0221890473
153PhosphorylationEIVEDKKSGRSSDIT
HHHCCCCCCCCCCCC		45.2218691976
153 (in isoform 3)Ubiquitination-45.2221890473
155PhosphorylationVEDKKSGRSSDITSV
HCCCCCCCCCCCCHH		39.8318691976
155 (in isoform 3)Phosphorylation-39.8318691976
156PhosphorylationEDKKSGRSSDITSVR
CCCCCCCCCCCCHHH		35.5720166139
157PhosphorylationDKKSGRSSDITSVRL
CCCCCCCCCCCHHHH		31.5018669648
158PhosphorylationKKSGRSSDITSVRLE
CCCCCCCCCCHHHHH		49.8118691976
158 (in isoform 3)Phosphorylation-49.8118691976
159PhosphorylationKSGRSSDITSVRLEK
CCCCCCCCCHHHHHH		3.1418669648
159 (in isoform 3)Phosphorylation-3.1418669648
160PhosphorylationSGRSSDITSVRLEKI
CCCCCCCCHHHHHHH		26.5918669648
162PhosphorylationRSSDITSVRLEKISK
CCCCCCHHHHHHHHH		6.4018669648
162 (in isoform 3)Phosphorylation-6.4018669648
163 (in isoform 3)Phosphorylation-36.5828348404
170 (in isoform 3)Phosphorylation-3.9323663014
171 (in isoform 3)Phosphorylation-7.0625159151
172PhosphorylationEKISKCLEDLGNVLT
HHHHHHHHHHHHHHH		61.7419664994
172 (in isoform 3)Phosphorylation-61.7425159151
176 (in isoform 3)Ubiquitination-32.6821890473
179PhosphorylationEDLGNVLTSTPNAKT
HHHHHHHHCCCCCCC		26.6922210691
180PhosphorylationDLGNVLTSTPNAKTV
HHHHHHHCCCCCCCC		37.3923663014
181PhosphorylationLGNVLTSTPNAKTVN
HHHHHHCCCCCCCCC		18.4819664994
184PhosphorylationVLTSTPNAKTVNGKA
HHHCCCCCCCCCCCC		15.3118669648
185PhosphorylationLTSTPNAKTVNGKAE
HHCCCCCCCCCCCCC		60.6918669648
185UbiquitinationLTSTPNAKTVNGKAE
HHCCCCCCCCCCCCC		60.69-
186PhosphorylationTSTPNAKTVNGKAES
HCCCCCCCCCCCCCC		19.4529449344
187PhosphorylationSTPNAKTVNGKAESS
CCCCCCCCCCCCCCC		9.7820166139
191PhosphorylationAKTVNGKAESSDSGA
CCCCCCCCCCCCCCC		24.2520166139
193PhosphorylationTVNGKAESSDSGAES
CCCCCCCCCCCCCCC		44.2822167270
194PhosphorylationVNGKAESSDSGAESE
CCCCCCCCCCCCCCH		27.5722167270
196PhosphorylationGKAESSDSGAESEEE
CCCCCCCCCCCCHHH		41.6822167270
200PhosphorylationSSDSGAESEEEEAQE
CCCCCCCCHHHHHHH		50.1822167270
206PhosphorylationESEEEEAQEEVKGAE
CCHHHHHHHHHHCCC		51.1418691976
215PhosphorylationEVKGAEQSDNDKKMM
HHHCCCCCHHHHHHH		29.8628176443
223 (in isoform 2)Ubiquitination-39.8321890473
247PhosphorylationDKDGFVQDIQNDIHA
CCCCCCHHHHHHHHH		38.8618691976
253PhosphorylationQDIQNDIHASSSLNG
HHHHHHHHHCCCCCC		23.5618691976
255PhosphorylationIQNDIHASSSLNGRS
HHHHHHHCCCCCCCC		13.2928348404
256PhosphorylationQNDIHASSSLNGRST
HHHHHHCCCCCCCCC		39.3617192257
257PhosphorylationNDIHASSSLNGRSTE
HHHHHCCCCCCCCCC		24.2928348404
258 (in isoform 3)Ubiquitination-9.4621890473
260 (in isoform 4)Ubiquitination-30.1521890473
262PhosphorylationSSSLNGRSTEEVKPI
CCCCCCCCCCCCCCC		41.3830266825
263PhosphorylationSSLNGRSTEEVKPID
CCCCCCCCCCCCCCC		34.5023663014
267UbiquitinationGRSTEEVKPIDENLG
CCCCCCCCCCCCCCC		39.2621906983
267 (in isoform 1)Ubiquitination-39.2621890473
276PhosphorylationIDENLGQTGKSAVCI
CCCCCCCCCCEEEEE		44.7923312004
279PhosphorylationNLGQTGKSAVCIHQD
CCCCCCCEEEEEECC		27.5524275569
287PhosphorylationAVCIHQDINDDHVED
EEEEECCCCCCCCEE		4.9819007248
296PhosphorylationDDHVEDVTGIQHLTS
CCCCEECCCCEECCC		40.6719007248
303PhosphorylationTGIQHLTSDSDSEVY
CCCEECCCCCCCCEE		41.2924275569
313PhosphorylationDSEVYCDSMEQFGQE
CCCEEECCHHHHCCH		22.2124275569
334 (in isoform 2)Ubiquitination-29.1521890473
351 (in isoform 4)Ubiquitination-44.1721890473
369 (in isoform 3)Ubiquitination-2.5121890473
378UbiquitinationVEGKGEVKHGGEDGR
EECCEEEECCCCCCC		32.0321906983
378 (in isoform 1)Ubiquitination-32.0321890473
378 (in isoform 2)Ubiquitination-32.03-
379PhosphorylationEGKGEVKHGGEDGRN
ECCEEEECCCCCCCC		55.4518691976
388PhosphorylationGEDGRNNSGAPHREK
CCCCCCCCCCCCCHH		39.6217192257
391PhosphorylationGRNNSGAPHREKRGG
CCCCCCCCCCHHCCC		30.5018691976
400PhosphorylationREKRGGETDEFSNVR
CHHCCCCCCCCCCCC		44.0721082442
404PhosphorylationGGETDEFSNVRRGRG
CCCCCCCCCCCCCCC		32.1621815630
409PhosphorylationEFSNVRRGRGHRMQH
CCCCCCCCCCCCCCC		29.3818691976
418PhosphorylationGHRMQHLSEGTKGRQ
CCCCCCCCCCCCCCC		31.6828355574
419PhosphorylationHRMQHLSEGTKGRQV
CCCCCCCCCCCCCCC		76.7918691976
421PhosphorylationMQHLSEGTKGRQVGS
CCCCCCCCCCCCCCC		26.6930108239
425 (in isoform 2)Ubiquitination-53.2221890473
428PhosphorylationTKGRQVGSGGDGERW
CCCCCCCCCCCCCCC		40.5217192257
437PhosphorylationGDGERWGSDRGSRGS
CCCCCCCCCCCCCCC		19.7117192257
441PhosphorylationRWGSDRGSRGSLNEQ
CCCCCCCCCCCHHHH		34.0730108239
444PhosphorylationSDRGSRGSLNEQIAL
CCCCCCCCHHHHHHH		27.2326657352
460 (in isoform 3)Ubiquitination-2.8421890473
469AcetylationNVLQRLQKLETLTAL
HHHHHHHHHHHHHHH		53.54-
469UbiquitinationNVLQRLQKLETLTAL
HHHHHHHHHHHHHHH		53.5421890473
469 (in isoform 1)Ubiquitination-53.5421890473
472PhosphorylationQRLQKLETLTALQAK
HHHHHHHHHHHHHHH		39.5829083192
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 ACBD5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACBD5_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 ACBD5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACBD5_HUMAN !!
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 ACBD5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 AND SER-200, ANDMASS SPECTROMETRY.
"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-193; SER-194; SER-196AND SER-200, AND MASS SPECTROMETRY.
"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-196; SER-200; SER-215;SER-256; SER-388; THR-400; SER-418; SER-428 AND SER-437, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181, AND MASSSPECTROMETRY.
"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 THR-127 AND THR-131, ANDMASS SPECTROMETRY.
"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 THR-296, AND MASSSPECTROMETRY.

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