ACO13_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ACO13_HUMAN
• UniProt AC: Q9NPJ3
• Protein Name: Acyl-coenzyme A thioesterase 13
• Gene Name: ACOT13
• Organism: Homo sapiens (Human).
• Sequence Length: 140
• Subcellular Localization: Cytoplasm, cytosol . Mitochondrion . Nucleus . Cytoplasm, cytoskeleton, spindle . During interphase, found both in the nucleus and in the cytoplasm. At mitosis, localizes to the spindle. Colocalizes with tubulin.
• 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. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis (By similarity)..
• Protein Sequence: MTSMTQSLREVIKAMTKARNFERVLGKITLVSAAPGKVICEMKVEEEHTNAIGTLHGGLTATLVDNISTMALLCTERGAPGVSVDMNITYMSPAKLGEDIVITAHVLKQGKTLAFTSVDLTNKATGKLIAQGRHTKHLGN

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
1	Acetylation	-------MTSMTQSL -------CCHHHHHH	5.89	22223895
2	Phosphorylation	------MTSMTQSLR ------CCHHHHHHH	27.49	20068231
2	Acetylation	------MTSMTQSLR ------CCHHHHHHH	27.49	19413330
3	Phosphorylation	-----MTSMTQSLRE -----CCHHHHHHHH	20.66	20068231
5	Phosphorylation	---MTSMTQSLREVI ---CCHHHHHHHHHH	18.12	20068231
7	Phosphorylation	-MTSMTQSLREVIKA -CCHHHHHHHHHHHH	21.89	20068231
9 (in isoform 2)	Phosphorylation	-	41.19	24275569
13	Malonylation	QSLREVIKAMTKARN HHHHHHHHHHHHHCC	36.96	26320211
13	Ubiquitination	QSLREVIKAMTKARN HHHHHHHHHHHHHCC	36.96	32015554
17	Ubiquitination	EVIKAMTKARNFERV HHHHHHHHHCCHHHH	32.06	24816145
27	Malonylation	NFERVLGKITLVSAA CHHHHHCEEEEEEEC	28.49	26320211
27	2-Hydroxyisobutyrylation	NFERVLGKITLVSAA CHHHHHCEEEEEEEC	28.49	-
27	Succinylation	NFERVLGKITLVSAA CHHHHHCEEEEEEEC	28.49	23954790
27	Ubiquitination	NFERVLGKITLVSAA CHHHHHCEEEEEEEC	28.49	-
27	Acetylation	NFERVLGKITLVSAA CHHHHHCEEEEEEEC	28.49	25038526
29	Phosphorylation	ERVLGKITLVSAAPG HHHHCEEEEEEECCC	25.29	21406692
32	Phosphorylation	LGKITLVSAAPGKVI HCEEEEEEECCCCEE	23.09	21406692
37	Acetylation	LVSAAPGKVICEMKV EEEECCCCEEEEEEE	27.63	25038526
37	Malonylation	LVSAAPGKVICEMKV EEEECCCCEEEEEEE	27.63	26320211
37	2-Hydroxyisobutyrylation	LVSAAPGKVICEMKV EEEECCCCEEEEEEE	27.63	-
43	Acetylation	GKVICEMKVEEEHTN CCEEEEEEECCCCCC	24.97	-
83	Phosphorylation	ERGAPGVSVDMNITY CCCCCCEEEEEEEEE	20.51	25072903
85	Ubiquitination	GAPGVSVDMNITYMS CCCCEEEEEEEEECC	19.53	32015554
88	Ubiquitination	GVSVDMNITYMSPAK CEEEEEEEEECCHHH	2.04	27667366
89	Phosphorylation	VSVDMNITYMSPAKL EEEEEEEEECCHHHC	14.25	25072903
90	Phosphorylation	SVDMNITYMSPAKLG EEEEEEEECCHHHCC	7.56	25072903
92	Phosphorylation	DMNITYMSPAKLGED EEEEEECCHHHCCCC	15.99	25159151
100	Ubiquitination	PAKLGEDIVITAHVL HHHCCCCEEEEEEEE	1.78	29967540
104	Ubiquitination	GEDIVITAHVLKQGK CCCEEEEEEEECCCC	4.62	27667366
108	Acetylation	VITAHVLKQGKTLAF EEEEEEECCCCEEEE	56.78	25953088
108	Succinylation	VITAHVLKQGKTLAF EEEEEEECCCCEEEE	56.78	23954790
108	Malonylation	VITAHVLKQGKTLAF EEEEEEECCCCEEEE	56.78	26320211
108	Ubiquitination	VITAHVLKQGKTLAF EEEEEEECCCCEEEE	56.78	32015554
111	Methylation	AHVLKQGKTLAFTSV EEEECCCCEEEEEEE	37.56	24129315
111	Succinylation	AHVLKQGKTLAFTSV EEEECCCCEEEEEEE	37.56	23954790
111	Malonylation	AHVLKQGKTLAFTSV EEEECCCCEEEEEEE	37.56	26320211
111	Ubiquitination	AHVLKQGKTLAFTSV EEEECCCCEEEEEEE	37.56	27667366
116	Phosphorylation	QGKTLAFTSVDLTNK CCCEEEEEEEECCCH	23.41	-
123	2-Hydroxyisobutyrylation	TSVDLTNKATGKLIA EEEECCCHHHCCEEE	41.93	-
123	Ubiquitination	TSVDLTNKATGKLIA EEEECCCHHHCCEEE	41.93	29967540
123	Malonylation	TSVDLTNKATGKLIA EEEECCCHHHCCEEE	41.93	26320211
127	Ubiquitination	LTNKATGKLIAQGRH CCCHHHCCEEEECCC	32.16	27667366
127	Acetylation	LTNKATGKLIAQGRH CCCHHHCCEEEECCC	32.16	23749302
127	2-Hydroxyisobutyrylation	LTNKATGKLIAQGRH CCCHHHCCEEEECCC	32.16	-
127	Malonylation	LTNKATGKLIAQGRH CCCHHHCCEEEECCC	32.16	26320211
136	2-Hydroxyisobutyrylation	IAQGRHTKHLGN--- EEECCCCCCCCC---	30.61	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ACO13_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ACO13_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ACO13_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NU214_HUMAN	NUP214	physical	22939629
EFTS_HUMAN	TSFM	physical	22939629
KLC2_HUMAN	KLC2	physical	22939629
NDUF2_HUMAN	NDUFAF2	physical	22939629
ECI2_HUMAN	ECI2	physical	22939629
RAB31_HUMAN	RAB31	physical	22939629
SBDS_HUMAN	SBDS	physical	22939629
ACO13_HUMAN	ACOT13	physical	16934754
ACO13_HUMAN	ACOT13	physical	19170545
PUR9_HUMAN	ATIC	physical	26344197
KCY_HUMAN	CMPK1	physical	26344197
LMA2L_HUMAN	LMAN2L	physical	26344197
NH2L1_HUMAN	NHP2L1	physical	26344197
PTPA_HUMAN	PPP2R4	physical	26344197
TENN_HUMAN	TNN	physical	26344197
TRNT1_HUMAN	TRNT1	physical	26344197
UBE2N_HUMAN	UBE2N	physical	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.