THIM_HUMAN - dbPTM
THIM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THIM_HUMAN
UniProt AC P42765
Protein Name 3-ketoacyl-CoA thiolase, mitochondrial
Gene Name ACAA2
Organism Homo sapiens (Human).
Sequence Length 397
Subcellular Localization Mitochondrion . Colocalizes with BNIP3 in the mitochondria.
Protein Description Abolishes BNIP3-mediated apoptosis and mitochondrial damage..
Protein Sequence MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
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
13SuccinylationGVFVVAAKRTPFGAY
CEEEEEEECCCCCCC		47.2527452117
13AcetylationGVFVVAAKRTPFGAY
CEEEEEEECCCCCCC		47.2525953088
20PhosphorylationKRTPFGAYGGLLKDF
ECCCCCCCCCCCCCC		16.4720561237
25AcetylationGAYGGLLKDFTATDL
CCCCCCCCCCCCCCH		56.7023954790
25SuccinylationGAYGGLLKDFTATDL
CCCCCCCCCCCCCCH		56.7027452117
25SuccinylationGAYGGLLKDFTATDL
CCCCCCCCCCCCCCH		56.70-
38AcetylationDLSEFAAKAALSAGK
CHHHHHHHHHHHCCC		30.6623236377
38UbiquitinationDLSEFAAKAALSAGK
CHHHHHHHHHHHCCC		30.66-
42PhosphorylationFAAKAALSAGKVSPE
HHHHHHHHCCCCCHH		30.1926437602
45SuccinylationKAALSAGKVSPETVD
HHHHHCCCCCHHHCH		38.98-
45SuccinylationKAALSAGKVSPETVD
HHHHHCCCCCHHHCH		38.98-
68PhosphorylationQSSSDAIYLARHVGL
CCCHHHHHHHHHHCC		8.95110744741
81SuccinylationGLRVGIPKETPALTI
CCCCCCCCCCCCEEH		72.7627452117
81MalonylationGLRVGIPKETPALTI
CCCCCCCCCCCCEEH		72.7626320211
81UbiquitinationGLRVGIPKETPALTI
CCCCCCCCCCCCEEH		72.7619608861
81AcetylationGLRVGIPKETPALTI
CCCCCCCCCCCCEEH		72.7619608861
83PhosphorylationRVGIPKETPALTINR
CCCCCCCCCCEEHHH		21.7121406692
87PhosphorylationPKETPALTINRLCGS
CCCCCCEEHHHHHCC		20.5069007335
92S-palmitoylationALTINRLCGSGFQSI
CEEHHHHHCCCHHHH		3.5329575903
119PhosphorylationEVVLCGGTESMSQAP
EEEEECCCCCCCCCC		15.3518669648
121PhosphorylationVLCGGTESMSQAPYC
EEECCCCCCCCCCCE		24.4618669648
127PhosphorylationESMSQAPYCVRNVRF
CCCCCCCCEEEECCC		13.4418669648
136PhosphorylationVRNVRFGTKLGSDIK
EEECCCCCCCCCCEE		22.00-
137MalonylationRNVRFGTKLGSDIKL
EECCCCCCCCCCEEE		51.7526320211
137SuccinylationRNVRFGTKLGSDIKL
EECCCCCCCCCCEEE		51.75-
137UbiquitinationRNVRFGTKLGSDIKL
EECCCCCCCCCCEEE		51.7519608861
137SuccinylationRNVRFGTKLGSDIKL
EECCCCCCCCCCEEE		51.7523954790
137AcetylationRNVRFGTKLGSDIKL
EECCCCCCCCCCEEE		51.7523954790
140PhosphorylationRFGTKLGSDIKLEDS
CCCCCCCCCEEEECC		46.7424275569
143SuccinylationTKLGSDIKLEDSLWV
CCCCCCEEEECCEEE		51.30-
143SuccinylationTKLGSDIKLEDSLWV
CCCCCCEEEECCEEE		51.30-
143AcetylationTKLGSDIKLEDSLWV
CCCCCCEEEECCEEE		51.3025038526
171SuccinylationTAENLAVKHKISREE
CHHHHHHHHCCCHHH		33.31-
171AcetylationTAENLAVKHKISREE
CHHHHHHHHCCCHHH		33.31-
171SuccinylationTAENLAVKHKISREE
CHHHHHHHHCCCHHH		33.31-
181SuccinylationISREECDKYALQSQQ
CCHHHHHHHHHHHHH		44.0427452117
181UbiquitinationISREECDKYALQSQQ
CCHHHHHHHHHHHHH		44.0419608861
181AcetylationISREECDKYALQSQQ
CCHHHHHHHHHHHHH		44.0425825284
181MalonylationISREECDKYALQSQQ
CCHHHHHHHHHHHHH		44.0426320211
182PhosphorylationSREECDKYALQSQQR
CHHHHHHHHHHHHHH		10.1720561243
191AcetylationLQSQQRWKAANDAGY
HHHHHHHHHHHCCCC		39.55-
191SuccinylationLQSQQRWKAANDAGY
HHHHHHHHHHHCCCC		39.55-
191UbiquitinationLQSQQRWKAANDAGY
HHHHHHHHHHHCCCC		39.55-
191SuccinylationLQSQQRWKAANDAGY
HHHHHHHHHHHCCCC		39.55-
198PhosphorylationKAANDAGYFNDEMAP
HHHHCCCCCCCCCCC		10.8321253578
209AcetylationEMAPIEVKTKKGKQT
CCCCEEEEECCCCCE		41.6625953088
209SuccinylationEMAPIEVKTKKGKQT
CCCCEEEEECCCCCE		41.6627452117
209SuccinylationEMAPIEVKTKKGKQT
CCCCEEEEECCCCCE		41.66-
209MalonylationEMAPIEVKTKKGKQT
CCCCEEEEECCCCCE		41.6626320211
211SuccinylationAPIEVKTKKGKQTMQ
CCEEEEECCCCCEEC		54.53-
211SuccinylationAPIEVKTKKGKQTMQ
CCEEEEECCCCCEEC		54.53-
212SuccinylationPIEVKTKKGKQTMQV
CEEEEECCCCCEECC		76.27-
212SuccinylationPIEVKTKKGKQTMQV
CEEEEECCCCCEECC		76.27-
214MalonylationEVKTKKGKQTMQVDE
EEEECCCCCEECCCC		52.0226320211
214SuccinylationEVKTKKGKQTMQVDE
EEEECCCCCEECCCC		52.0227452117
214SuccinylationEVKTKKGKQTMQVDE
EEEECCCCCEECCCC		52.02-
234MalonylationTTLEQLQKLPPVFKK
CCHHHHHCCCCCCCC		72.1126320211
234UbiquitinationTTLEQLQKLPPVFKK
CCHHHHHCCCCCCCC		72.11-
234SuccinylationTTLEQLQKLPPVFKK
CCHHHHHCCCCCCCC		72.11-
234SuccinylationTTLEQLQKLPPVFKK
CCHHHHHCCCCCCCC		72.1127452117
234AcetylationTTLEQLQKLPPVFKK
CCHHHHHCCCCCCCC		72.1123954790
240AcetylationQKLPPVFKKDGTVTA
HCCCCCCCCCCCEEC		50.63156431
240SuccinylationQKLPPVFKKDGTVTA
HCCCCCCCCCCCEEC		50.63-
240SuccinylationQKLPPVFKKDGTVTA
HCCCCCCCCCCCEEC		50.63-
241UbiquitinationKLPPVFKKDGTVTAG
CCCCCCCCCCCEECC		50.34-
241MalonylationKLPPVFKKDGTVTAG
CCCCCCCCCCCEECC		50.3426320211
241SuccinylationKLPPVFKKDGTVTAG
CCCCCCCCCCCEECC		50.3427452117
241AcetylationKLPPVFKKDGTVTAG
CCCCCCCCCCCEECC		50.34156007
269UbiquitinationIASEDAVKKHNFTPL
EECHHHHHHCCCCHH		50.46-
269AcetylationIASEDAVKKHNFTPL
EECHHHHHHCCCCHH		50.4625038526
270AcetylationASEDAVKKHNFTPLA
ECHHHHHHCCCCHHH		36.8625825284
270MalonylationASEDAVKKHNFTPLA
ECHHHHHHCCCCHHH		36.8626320211
274PhosphorylationAVKKHNFTPLARIVG
HHHHCCCCHHHHHHH		23.789509253
305SuccinylationPAISGALKKAGLSLK
HHHHHHHHHCCCCCC		39.79-
305AcetylationPAISGALKKAGLSLK
HHHHHHHHHCCCCCC		39.7925038526
305SuccinylationPAISGALKKAGLSLK
HHHHHHHHHCCCCCC		39.79-
306AcetylationAISGALKKAGLSLKD
HHHHHHHHCCCCCCC		48.8425038526
310PhosphorylationALKKAGLSLKDMDLV
HHHHCCCCCCCCCEE		32.2424719451
312AcetylationKKAGLSLKDMDLVEV
HHCCCCCCCCCEEEE		47.8625038526
312SuccinylationKKAGLSLKDMDLVEV
HHCCCCCCCCCEEEE		47.86-
312SuccinylationKKAGLSLKDMDLVEV
HHCCCCCCCCCEEEE		47.86-
333PhosphorylationQYLAVERSLDLDISK
HHHEEEEECCCCCCC		16.8424275569
339PhosphorylationRSLDLDISKTNVNGG
EECCCCCCCCCCCCC		32.8521815630
340AcetylationSLDLDISKTNVNGGA
ECCCCCCCCCCCCCE		44.44-
341PhosphorylationLDLDISKTNVNGGAI
CCCCCCCCCCCCCEE		37.2921406692
357PhosphorylationLGHPLGGSGSRITAH
ECCCCCCCCCHHHHH		31.6221406692
359PhosphorylationHPLGGSGSRITAHLV
CCCCCCCCHHHHHHH		23.3921406692
370MethylationAHLVHELRRRGGKYA
HHHHHHHHHCCCCEE		24.22-
375AcetylationELRRRGGKYAVGSAC
HHHHCCCCEEEEEEE		32.62-
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 THIM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THIM_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 THIM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ZFR_HUMANZFRphysical
22939629
TIAR_HUMANTIAL1physical
22939629
TMM65_HUMANTMEM65physical
22939629
TOM40_HUMANTOMM40physical
22939629
VAMP2_HUMANVAMP2physical
22939629
VDAC1_HUMANVDAC1physical
22939629
VDAC2_HUMANVDAC2physical
22939629
TP53B_HUMANTP53BP1physical
22939629
TX1B3_HUMANTAX1BP3physical
22939629
H2AZ_HUMANH2AFZphysical
22863883
PDIA1_HUMANP4HBphysical
22863883
IF2M_HUMANMTIF2physical
26186194
PPCEL_HUMANPREPLphysical
26186194
TR61B_HUMANTRMT61Bphysical
26186194
CSRP1_HUMANCSRP1physical
26344197
ENOA_HUMANENO1physical
26344197
6PGD_HUMANPGDphysical
26344197
PGK1_HUMANPGK1physical
26344197
SPD2B_HUMANSH3PXD2Bphysical
26344197
PPCEL_HUMANPREPLphysical
28514442
SYLM_HUMANLARS2physical
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 THIM_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-25; LYS-81; LYS-137 ANDLYS-181, AND MASS SPECTROMETRY.
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 THR-119; SER-121 ANDTYR-127, AND MASS SPECTROMETRY.

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