BACH_HUMAN - dbPTM
BACH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BACH_HUMAN
UniProt AC O00154
Protein Name Cytosolic acyl coenzyme A thioester hydrolase
Gene Name ACOT7
Organism Homo sapiens (Human).
Sequence Length 380
Subcellular Localization Isoform 4: Cytoplasm.
Isoform 6: Cytoplasm.
Isoform 1: Mitochondrion.
Isoform 5: Mitochondrion.
Protein Description Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA..
Protein Sequence MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVVYSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHAEPQP
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
2 (in isoform 2)Phosphorylation-52.8125159151
2 (in isoform 4)Phosphorylation-52.8125159151
2Ubiquitination------MKLLARALR
------CHHHHHHHH		52.81-
2 (in isoform 3)Phosphorylation-52.8125159151
8 (in isoform 2)Phosphorylation-3.4226270265
8 (in isoform 3)Phosphorylation-3.4226270265
8 (in isoform 4)Phosphorylation-3.4226270265
10 (in isoform 2)Phosphorylation-3.2325693802
10 (in isoform 3)Phosphorylation-3.2325693802
10 (in isoform 4)Phosphorylation-3.2325693802
27AcetylationRRLVAGQGCVGPRRG
CCEECCCCCCCCCCC		13.7319608861
34 (in isoform 7)Phosphorylation-16.4922617229
40 (in isoform 7)Phosphorylation-24.1026270265
42 (in isoform 7)Phosphorylation-4.9625693802
48AcetylationVVGPRADLPPCGACI
EECCCCCCCCCCCEE		5.0719608861
68AcetylationRPDDANVAGNVHGGT
CCCCCCCCCCCCCHH		12.0319608861
78AcetylationVHGGTILKMIEEAGA
CCCHHHHHHHHHHCC		33.7019608861
101UbiquitinationSQNGERCVAALARVE
CCCHHHHHHHHHCCC		4.3522817900
102UbiquitinationQNGERCVAALARVER
CCHHHHHHHHHCCCC		10.6122817900
106UbiquitinationRCVAALARVERTDFL
HHHHHHHCCCCCCCC		31.5121890473
106 (in isoform 6)Ubiquitination-31.5121890473
115 (in isoform 2)Ubiquitination-24.6621890473
115 (in isoform 3)Ubiquitination-24.6621890473
117UbiquitinationTDFLSPMCIGEVAHV
CCCCCCHHHHEEEEE		4.0323000965
117AcetylationTDFLSPMCIGEVAHV
CCCCCCHHHHEEEEE		4.0319608861
117 (in isoform 6)Ubiquitination-4.0321890473
121UbiquitinationSPMCIGEVAHVSAEI
CCHHHHEEEEEEEEE		3.6323000965
122UbiquitinationPMCIGEVAHVSAEIT
CHHHHEEEEEEEEEE		7.9622817900
123UbiquitinationMCIGEVAHVSAEITY
HHHHEEEEEEEEEEE		21.1722817900
126 (in isoform 2)Ubiquitination-15.8921890473
126 (in isoform 3)Ubiquitination-15.8921890473
127UbiquitinationEVAHVSAEITYTSKH
EEEEEEEEEEEECCC		28.4921890473
127 (in isoform 5)Ubiquitination-28.4921890473
138UbiquitinationTSKHSVEVQVNVMSE
ECCCEEEEEEEECCC		7.8423000965
138AcetylationTSKHSVEVQVNVMSE
ECCCEEEEEEEECCC		7.8419608861
138 (in isoform 5)Ubiquitination-7.8421890473
142UbiquitinationSVEVQVNVMSENILT
EEEEEEEECCCCCCC		4.7323000965
143UbiquitinationVEVQVNVMSENILTG
EEEEEEECCCCCCCC		3.3322817900
147UbiquitinationVNVMSENILTGAKKL
EEECCCCCCCCCHHH		2.9822817900
147UbiquitinationVNVMSENILTGAKKL
EEECCCCCCCCCHHH		2.9821890473
147 (in isoform 4)Ubiquitination-2.9821890473
152UbiquitinationENILTGAKKLTNKAT
CCCCCCCHHHCCCCE		50.0522817900
153UbiquitinationNILTGAKKLTNKATL
CCCCCCHHHCCCCEE		61.0722817900
153AcetylationNILTGAKKLTNKATL
CCCCCCHHHCCCCEE		61.0725953088
154UbiquitinationILTGAKKLTNKATLW
CCCCCHHHCCCCEEE		6.6832015554
157AcetylationGAKKLTNKATLWYVP
CCHHHCCCCEEEEEE		37.2023954790
157UbiquitinationGAKKLTNKATLWYVP
CCHHHCCCCEEEEEE		37.2021890473
157 (in isoform 1)Ubiquitination-37.2021890473
158UbiquitinationAKKLTNKATLWYVPL
CHHHCCCCEEEEEEC		15.2523000965
158UbiquitinationAKKLTNKATLWYVPL
CHHHCCCCEEEEEEC		15.2521890473
158AcetylationAKKLTNKATLWYVPL
CHHHCCCCEEEEEEC		15.2519608861
158 (in isoform 4)Ubiquitination-15.2521890473
159PhosphorylationKKLTNKATLWYVPLS
HHHCCCCEEEEEECC		21.3168724543
162PhosphorylationTNKATLWYVPLSLKN
CCCCEEEEEECCCCC		8.7068710517
162UbiquitinationTNKATLWYVPLSLKN
CCCCEEEEEECCCCC		8.7023000965
166PhosphorylationTLWYVPLSLKNVDKV
EEEEEECCCCCCCCE		31.0920068231
168AcetylationWYVPLSLKNVDKVLE
EEEECCCCCCCCEEE		52.1019608861
168UbiquitinationWYVPLSLKNVDKVLE
EEEECCCCCCCCEEE		52.1023000965
168 (in isoform 1)Ubiquitination-52.1021890473
172AcetylationLSLKNVDKVLEVPPV
CCCCCCCCEEECCCE		44.4223954790
172UbiquitinationLSLKNVDKVLEVPPV
CCCCCCCCEEECCCE		44.4223000965
172MalonylationLSLKNVDKVLEVPPV
CCCCCCCCEEECCCE		44.4226320211
175UbiquitinationKNVDKVLEVPPVVYS
CCCCCEEECCCEEEC		56.8432015554
181PhosphorylationLEVPPVVYSRQEQEE
EECCCEEECHHHHHH		9.81142163
182PhosphorylationEVPPVVYSRQEQEEE
ECCCEEECHHHHHHH		18.8425394399
188UbiquitinationYSRQEQEEEGRKRYE
ECHHHHHHHHHHHHH		66.5032015554
188AcetylationYSRQEQEEEGRKRYE
ECHHHHHHHHHHHHH		66.5019608861
194PhosphorylationEEEGRKRYEAQKLER
HHHHHHHHHHHHHHH		20.7428152594
195UbiquitinationEEGRKRYEAQKLERM
HHHHHHHHHHHHHHH		48.9732015554
198AcetylationRKRYEAQKLERMETK
HHHHHHHHHHHHHHH		60.4019608861
198UbiquitinationRKRYEAQKLERMETK
HHHHHHHHHHHHHHH		60.4019608861
205UbiquitinationKLERMETKWRNGDIV
HHHHHHHHCCCCCCC		30.7432015554
232UbiquitinationYSQSSLIHLVGPSDC
EECCCCEEEECCCCC		21.5421890473
232AcetylationYSQSSLIHLVGPSDC
EECCCCEEEECCCCC		21.5419608861
232 (in isoform 6)Ubiquitination-21.5421890473
235UbiquitinationSSLIHLVGPSDCTLH
CCCEEEECCCCCEEE		23.5022817900
253UbiquitinationHGGVTMKLMDEVAGI
CCCCHHHHHHHHHHH		3.4821890473
253AcetylationHGGVTMKLMDEVAGI
CCCCHHHHHHHHHHH		3.4819608861
253 (in isoform 5)Ubiquitination-3.4821890473
254SulfoxidationGGVTMKLMDEVAGIV
CCCHHHHHHHHHHHH		3.2621406390
256UbiquitinationVTMKLMDEVAGIVAA
CHHHHHHHHHHHHHH		21.9422817900
267UbiquitinationIVAARHCKTNIVTAS
HHHHHCCCCCEEEEE		38.18-
268PhosphorylationVAARHCKTNIVTASV
HHHHCCCCCEEEEEC		35.2620068231
270UbiquitinationARHCKTNIVTASVDA
HHCCCCCEEEEECCE		3.3522053931
272PhosphorylationHCKTNIVTASVDAIN
CCCCCEEEEECCEEE		14.9320068231
273UbiquitinationCKTNIVTASVDAINF
CCCCEEEEECCEEEC		9.1721890473
273UbiquitinationCKTNIVTASVDAINF
CCCCEEEEECCEEEC		9.1721890473
273AcetylationCKTNIVTASVDAINF
CCCCEEEEECCEEEC		9.1719608861
273 (in isoform 4)Ubiquitination-9.1721890473
274PhosphorylationKTNIVTASVDAINFH
CCCEEEEECCEEECC		15.9120068231
276UbiquitinationNIVTASVDAINFHDK
CEEEEECCEEECCHH		38.9522817900
283AcetylationDAINFHDKIRKGCVI
CEEECCHHHCCCCEE		35.5219608861
283UbiquitinationDAINFHDKIRKGCVI
CEEECCHHHCCCCEE		35.5222817900
2832-HydroxyisobutyrylationDAINFHDKIRKGCVI
CEEECCHHHCCCCEE		35.52-
283 (in isoform 1)Ubiquitination-35.5221890473
286UbiquitinationNFHDKIRKGCVITIS
ECCHHHCCCCEEEEC		61.2022817900
286MalonylationNFHDKIRKGCVITIS
ECCHHHCCCCEEEEC		61.2026320211
286AcetylationNFHDKIRKGCVITIS
ECCHHHCCCCEEEEC		61.2026051181
291UbiquitinationIRKGCVITISGRMTF
HCCCCEEEECCEEEE		6.6822053931
300PhosphorylationSGRMTFTSNKSMEIE
CCEEEECCCCCEEEE		37.7630624053
303PhosphorylationMTFTSNKSMEIEVLV
EEECCCCCEEEEEEE		26.3730624053
304SulfoxidationTFTSNKSMEIEVLVD
EECCCCCEEEEEEEE		6.8530846556
304UbiquitinationTFTSNKSMEIEVLVD
EECCCCCEEEEEEEE		6.8524816145
305UbiquitinationFTSNKSMEIEVLVDA
ECCCCCEEEEEEEEC		42.9924816145
311UbiquitinationMEIEVLVDADPVVDS
EEEEEEEECCCCCCC		40.8822053931
318UbiquitinationDADPVVDSSQKRYRA
ECCCCCCCHHHHHHH		24.0633845483
319PhosphorylationADPVVDSSQKRYRAA
CCCCCCCHHHHHHHH		34.9524719451
321AcetylationPVVDSSQKRYRAASA
CCCCCHHHHHHHHHH		54.037350191
321UbiquitinationPVVDSSQKRYRAASA
CCCCCHHHHHHHHHH		54.0322053931
321 (in isoform 1)Ubiquitination-54.0321890473
325UbiquitinationSSQKRYRAASAFFTY
CHHHHHHHHHHHHEE		9.2424816145
326UbiquitinationSQKRYRAASAFFTYV
HHHHHHHHHHHHEEE		7.7524816145
327PhosphorylationQKRYRAASAFFTYVS
HHHHHHHHHHHEEEE		25.32102778137
336PhosphorylationFFTYVSLSQEGRSLP
HHEEEEECCCCCCCC		20.7630624053
339UbiquitinationYVSLSQEGRSLPVPQ
EEEECCCCCCCCCCC		19.4833845483
345UbiquitinationEGRSLPVPQLVPETE
CCCCCCCCCCCCCCH		21.6124816145
346UbiquitinationGRSLPVPQLVPETED
CCCCCCCCCCCCCHH		56.1624816145
351PhosphorylationVPQLVPETEDEKKRF
CCCCCCCCHHHHHHH		42.54110734971
355UbiquitinationVPETEDEKKRFEEGK
CCCCHHHHHHHHCCC		62.6624816145
3552-HydroxyisobutyrylationVPETEDEKKRFEEGK
CCCCHHHHHHHHCCC		62.66-
355AcetylationVPETEDEKKRFEEGK
CCCCHHHHHHHHCCC		62.6625953088
356UbiquitinationPETEDEKKRFEEGKG
CCCHHHHHHHHCCCC		61.3424816145
359UbiquitinationEDEKKRFEEGKGRYL
HHHHHHHHCCCCHHH		70.6333845483
365PhosphorylationFEEGKGRYLQMKAKR
HHCCCCHHHHHHHHH		15.2328102081
369UbiquitinationKGRYLQMKAKRQGHA
CCHHHHHHHHHCCCC		37.4833845483
369AcetylationKGRYLQMKAKRQGHA
CCHHHHHHHHHCCCC		37.4825953088
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 BACH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BACH_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 BACH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AL9A1_HUMANALDH9A1physical
22863883
G3P_HUMANGAPDHphysical
22863883
PDIA3_HUMANPDIA3physical
22863883
RCC2_HUMANRCC2physical
22863883
DHSO_HUMANSORDphysical
22863883
UBQL1_HUMANUBQLN1physical
25416956
THAP1_HUMANTHAP1physical
25416956
PCBP1_HUMANPCBP1physical
26344197
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 BACH_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-78; LYS-168; LYS-198 ANDLYS-283, AND MASS SPECTROMETRY.

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