THIC_HUMAN - dbPTM
THIC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THIC_HUMAN
UniProt AC Q9BWD1
Protein Name Acetyl-CoA acetyltransferase, cytosolic
Gene Name ACAT2
Organism Homo sapiens (Human).
Sequence Length 397
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE
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
1Acetylation-------MNAGSDPV
-------CCCCCCCE		7.5722223895
3 (in isoform 2)Phosphorylation-19.9822617229
19 (in isoform 2)Phosphorylation-23.4924706070
23 (in isoform 2)Phosphorylation-21.6922210691
35PhosphorylationVPVQDLGSTVIKEVL
CCHHHHCHHHHHHHH		27.1421712546
36PhosphorylationPVQDLGSTVIKEVLK
CHHHHCHHHHHHHHH		25.1821712546
39UbiquitinationDLGSTVIKEVLKRAT
HHCHHHHHHHHHHCC		37.12-
65S-palmitoylationGHVLAAGCGQNPVRQ
HHHHHCCCCCCCCHH		4.3129575903
81PhosphorylationSVGAGIPYSVPAWSC
CCCCCCCCCCCHHHC		22.0075093
105PhosphorylationAVCLAVQSIGIGDSS
HHHHHHHHHCCCCCE		19.04101544943
124UbiquitinationGGMENMSKAPHLAYL
CCCCCCCCCCCCHHH		55.9925015289
130PhosphorylationSKAPHLAYLRTGVKI
CCCCCCHHHHCCCEE		11.7745562259
136UbiquitinationAYLRTGVKIGEMPLT
HHHHCCCEECCCCCC		46.4629967540
136AcetylationAYLRTGVKIGEMPLT
HHHHCCCEECCCCCC		46.4625953088
153UbiquitinationILCDGLTDAFHNCHM
CCCCCCCHHCHHCCC		52.8925015289
165UbiquitinationCHMGITAENVAKKWQ
CCCCCCHHHHHHHCC		43.52-
165UbiquitinationCHMGITAENVAKKWQ
CCCCCCHHHHHHHCC		43.5229967540
169AcetylationITAENVAKKWQVSRE
CCHHHHHHHCCCCHH		50.7125953088
169UbiquitinationITAENVAKKWQVSRE
CCHHHHHHHCCCCHH		50.7132015554
170AcetylationTAENVAKKWQVSRED
CHHHHHHHCCCCHHH		32.8726051181
170UbiquitinationTAENVAKKWQVSRED
CHHHHHHHCCCCHHH		32.8729967540
180AcetylationVSREDQDKVAVLSQN
CCHHHHHHEEEEECC		26.8523236377
180UbiquitinationVSREDQDKVAVLSQN
CCHHHHHHEEEEECC		26.8524816145
185PhosphorylationQDKVAVLSQNRTENA
HHHEEEEECCHHHHH		20.8621406692
188MethylationVAVLSQNRTENAQKA
EEEEECCHHHHHHHC		35.46-
189PhosphorylationAVLSQNRTENAQKAG
EEEECCHHHHHHHCC		40.9321406692
194UbiquitinationNRTENAQKAGHFDKE
CHHHHHHHCCCCCHH		54.6624816145
194AcetylationNRTENAQKAGHFDKE
CHHHHHHHCCCCCHH		54.6625953088
198UbiquitinationNAQKAGHFDKEIVPV
HHHHCCCCCHHHHHE		16.3632015554
199UbiquitinationAQKAGHFDKEIVPVL
HHHCCCCCHHHHHEE		41.8429967540
199UbiquitinationAQKAGHFDKEIVPVL
HHHCCCCCHHHHHEE		41.84-
200UbiquitinationQKAGHFDKEIVPVLV
HHCCCCCHHHHHEEE		48.6919608861
200AcetylationQKAGHFDKEIVPVLV
HHCCCCCHHHHHEEE		48.6919608861
209UbiquitinationIVPVLVSTRKGLIEV
HHHEEEECCCCEEEE		28.99-
209AcetylationIVPVLVSTRKGLIEV
HHHEEEECCCCEEEE		28.99-
209UbiquitinationIVPVLVSTRKGLIEV
HHHEEEECCCCEEEE		28.9924816145
211AcetylationPVLVSTRKGLIEVKT
HEEEECCCCEEEEEC		59.1526051181
211MalonylationPVLVSTRKGLIEVKT
HEEEECCCCEEEEEC		59.1526320211
211UbiquitinationPVLVSTRKGLIEVKT
HEEEECCCCEEEEEC		59.1529967540
217AcetylationRKGLIEVKTDEFPRH
CCCEEEEECCCCCCC		37.1525953088
217UbiquitinationRKGLIEVKTDEFPRH
CCCEEEEECCCCCCC		37.1532015554
223UbiquitinationVKTDEFPRHGSNIEA
EECCCCCCCCCCHHH		52.7124816145
226PhosphorylationDEFPRHGSNIEAMSK
CCCCCCCCCHHHHHH		28.6322210691
229UbiquitinationPRHGSNIEAMSKLKP
CCCCCCHHHHHHCCC		42.44-
229AcetylationPRHGSNIEAMSKLKP
CCCCCCHHHHHHCCC		42.44-
229UbiquitinationPRHGSNIEAMSKLKP
CCCCCCHHHHHHCCC		42.4419608861
229AcetylationPRHGSNIEAMSKLKP
CCCCCCHHHHHHCCC		42.4419608861
232PhosphorylationGSNIEAMSKLKPYFL
CCCHHHHHHCCCEEE		41.7122210691
233AcetylationSNIEAMSKLKPYFLT
CCHHHHHHCCCEEEC		47.6619608861
233UbiquitinationSNIEAMSKLKPYFLT
CCHHHHHHCCCEEEC		47.6633845483
235AcetylationIEAMSKLKPYFLTDG
HHHHHHCCCEEECCC		41.2119608861
235UbiquitinationIEAMSKLKPYFLTDG
HHHHHHCCCEEECCC		41.2119608861
240UbiquitinationKLKPYFLTDGTGTVT
HCCCEEECCCCCCCC		23.60-
240O-linked_GlycosylationKLKPYFLTDGTGTVT
HCCCEEECCCCCCCC		23.6028510447
240UbiquitinationKLKPYFLTDGTGTVT
HCCCEEECCCCCCCC		23.6029967540
246UbiquitinationLTDGTGTVTPANASG
ECCCCCCCCCCCCCC		6.80-
246UbiquitinationLTDGTGTVTPANASG
ECCCCCCCCCCCCCC		6.8032015554
262UbiquitinationNDGAAAVVLMKKSEA
CCCCEEEEEEEHHHH		3.5633845483
262UbiquitinationNDGAAAVVLMKKSEA
CCCCEEEEEEEHHHH		3.56-
262AcetylationNDGAAAVVLMKKSEA
CCCCEEEEEEEHHHH		3.56-
262AcetylationNDGAAAVVLMKKSEA
CCCCEEEEEEEHHHH		3.5619608861
264AcetylationGAAAVVLMKKSEADK
CCEEEEEEEHHHHHH		3.29-
264AcetylationGAAAVVLMKKSEADK
CCEEEEEEEHHHHHH		3.2919608861
264UbiquitinationGAAAVVLMKKSEADK
CCEEEEEEEHHHHHH		3.2921890473
264UbiquitinationGAAAVVLMKKSEADK
CCEEEEEEEHHHHHH		3.2921890473
265UbiquitinationAAAVVLMKKSEADKR
CEEEEEEEHHHHHHC		49.3232015554
265AcetylationAAAVVLMKKSEADKR
CEEEEEEEHHHHHHC		49.3226051181
266UbiquitinationAAVVLMKKSEADKRG
EEEEEEEHHHHHHCC		39.29-
267PhosphorylationAVVLMKKSEADKRGL
EEEEEEHHHHHHCCC		32.2828258704
294UbiquitinationGVEPSIMGIGPIPAI
CCCCHHCCCCCHHHH		21.74-
294UbiquitinationGVEPSIMGIGPIPAI
CCCCHHCCCCCHHHH		21.7432015554
295UbiquitinationVEPSIMGIGPIPAIK
CCCHHCCCCCHHHHH		3.08-
302UbiquitinationIGPIPAIKQAVTKAG
CCCHHHHHHHHHHCC		34.0222053931
331UbiquitinationFAAVSAAIVKELGLN
HHHHHHHHHHHHCCC		4.5621890473
331UbiquitinationFAAVSAAIVKELGLN
HHHHHHHHHHHHCCC		4.56-
341UbiquitinationELGLNPEKVNIEGGA
HHCCCHHHEEECCCH		41.67-
341AcetylationELGLNPEKVNIEGGA
HHCCCHHHEEECCCH		41.6726051181
358PhosphorylationLGHPLGASGCRILVT
HCCCCCHHHHHHHHH		36.3126091039
365PhosphorylationSGCRILVTLLHTLER
HHHHHHHHHHHHHHH		21.8428258704
370UbiquitinationLVTLLHTLERMGRSR
HHHHHHHHHHCCCCC		2.46-
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 THIC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THIC_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 THIC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VASP_HUMANVASPphysical
22939629
TT39C_HUMANTTC39Cphysical
22939629
THIC_HUMANACAT2physical
21988832
SAHH_HUMANAHCYphysical
22863883
PAPS1_HUMANPAPSS1physical
22863883
THIC_HUMANACAT2physical
25416956
LNX1_HUMANLNX1physical
25416956
THIL_HUMANACAT1physical
26186194
TPPC8_HUMANTRAPPC8physical
26186194
HCDH_HUMANHADHphysical
26344197
CH10_HUMANHSPE1physical
26344197
PCBP1_HUMANPCBP1physical
26344197
PCBP2_HUMANPCBP2physical
26344197
PFD4_HUMANPFDN4physical
26344197
PRRC1_HUMANPRRC1physical
26344197
UB2L3_HUMANUBE2L3physical
26344197
UBXN1_HUMANUBXN1physical
26344197
THIL_HUMANACAT1physical
28514442
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 THIC_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"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-200; LYS-233 AND LYS-235,AND MASS SPECTROMETRY.

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