ACBG1_HUMAN - dbPTM
ACBG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACBG1_HUMAN
UniProt AC Q96GR2
Protein Name Long-chain-fatty-acid--CoA ligase ACSBG1
Gene Name ACSBG1
Organism Homo sapiens (Human).
Sequence Length 724
Subcellular Localization Cytoplasm . Cytoplasmic vesicle. Microsome. Endoplasmic reticulum.
Protein Description Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids..
Protein Sequence MPRNSGAGYGCPHGDPSMLDSRETPQESRQDMIVRTTQEKLKTSSLTDRQPLSKESLNHALELSVPEKVNNAQWDAPEEALWTTRADGRVRLRIDPSCPQLPYTVHRMFYEALDKYGDLIALGFKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDLKPFTTRLADYLVLAKVRQALGFAKCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISNAMLIGDQRKFLSMLLTLKCTLDPDTSDQTDNLTEQAMEFCQRVGSRATTVSEIIEKKDEAVYQAIEEGIRRVNMNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQKM
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---MPRNSGAGYGCP
---CCCCCCCCCCCC
31.1622210691
17PhosphorylationGCPHGDPSMLDSRET
CCCCCCHHHCCCCCC
36.4022210691
24PhosphorylationSMLDSRETPQESRQD
HHCCCCCCCHHHHHC
29.2125690035
53PhosphorylationLTDRQPLSKESLNHA
CCCCCCCCHHHHHHH
40.85-
56PhosphorylationRQPLSKESLNHALEL
CCCCCHHHHHHHHHH
37.9027732954
64PhosphorylationLNHALELSVPEKVNN
HHHHHHHCCCHHHCC
26.6727732954
134PhosphorylationQDKWEHISYSQYYLL
CCCCCCCCHHHHHHH
22.1919690332
135PhosphorylationDKWEHISYSQYYLLA
CCCCCCCHHHHHHHH
10.132074991
136PhosphorylationKWEHISYSQYYLLAR
CCCCCCHHHHHHHHH
12.6219690332
138PhosphorylationEHISYSQYYLLARRA
CCCCHHHHHHHHHHH
7.0822817900
139PhosphorylationHISYSQYYLLARRAA
CCCHHHHHHHHHHHH
6.392075207
236AcetylationLKAVVIYKEPPPNKM
CEEEEEECCCCCCCC
53.2530586703
295PhosphorylationNPKGVMLSQDNITWT
CCCCEEEECCCEEEE
19.8622496350
300PhosphorylationMLSQDNITWTARYGS
EEECCCEEEEEECCC
24.0267054361
359PhosphorylationEPDALKGSLVNTLRE
CCHHHCCCHHHHHCC
27.7946158013
370PhosphorylationTLREVEPTSHMGVPR
HHCCCCCCCCCCCHH
20.1230206219
371PhosphorylationLREVEPTSHMGVPRV
HCCCCCCCCCCCHHH
23.3830206219
595PhosphorylationKMELPIISNAMLIGD
HCCCCEECCCEECCC
21.1846158019
641PhosphorylationEFCQRVGSRATTVSE
HHHHHHHCCCCCHHH
18.8428258704
644PhosphorylationQRVGSRATTVSEIIE
HHHHCCCCCHHHHHH
26.9828258704
647PhosphorylationGSRATTVSEIIEKKD
HCCCCCHHHHHHHHC
22.4528258704
658PhosphorylationEKKDEAVYQAIEEGI
HHHCHHHHHHHHHHH
10.16-
690PhosphorylationAILERDFSISGGELG
HEEEEECCCCCCCCC
21.8226074081
692PhosphorylationLERDFSISGGELGPT
EEEECCCCCCCCCCC
39.2826074081
699PhosphorylationSGGELGPTMKLKRLT
CCCCCCCCEEEEEHH
25.7426074081

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 ACBG1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACBG1_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 ACBG1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 ACBG1_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-135; TYR-138 ANDTYR-139, AND MASS SPECTROMETRY.

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