ACADL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ACADL_MOUSE
• UniProt AC: P51174
• Protein Name: Long-chain specific acyl-CoA dehydrogenase, mitochondrial
• Gene Name: Acadl
• Organism: Mus musculus (Mouse).
• Sequence Length: 430
• Subcellular Localization: Mitochondrion matrix.
• Protein Sequence: MAARLLLRSLRVLKARSAPRPPPSARCSHSGAEARLETPSAKKLTDVGIRRIFSSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIVVAVTNREARSPAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSASMAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSDS

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
42	Succinylation	RLETPSAKKLTDVGI CCCCCCCCCCCHHHH	53.29	23806337
42	Acetylation	RLETPSAKKLTDVGI CCCCCCCCCCCHHHH	53.29	23576753
42	Malonylation	RLETPSAKKLTDVGI CCCCCCCCCCCHHHH	53.29	26320211
43	Glutarylation	LETPSAKKLTDVGIR CCCCCCCCCCHHHHH	57.23	24703693
43	Acetylation	LETPSAKKLTDVGIR CCCCCCCCCCHHHHH	57.23	24062335
54	Phosphorylation	VGIRRIFSSEHDIFR HHHHHHHCCCHHHHH	32.23	27742792
55	Phosphorylation	GIRRIFSSEHDIFRE HHHHHHCCCHHHHHH	28.35	26824392
63	Phosphorylation	EHDIFRESVRKFFQE CHHHHHHHHHHHHHH	23.98	27742792
66	Succinylation	IFRESVRKFFQEEVI HHHHHHHHHHHHCCC	48.66	23806337
66	Acetylation	IFRESVRKFFQEEVI HHHHHHHHHHHHCCC	48.66	23576753
66	Succinylation	IFRESVRKFFQEEVI HHHHHHHHHHHHCCC	48.66	-
81	Succinylation	PHHTEWEKAGEVSRE CCCCHHHHHCHHHHH	63.87	23806337
81	Ubiquitination	PHHTEWEKAGEVSRE CCCCHHHHHCHHHHH	63.87	-
81	Succinylation	PHHTEWEKAGEVSRE CCCCHHHHHCHHHHH	63.87	-
81	Acetylation	PHHTEWEKAGEVSRE CCCCHHHHHCHHHHH	63.87	23576753
81	Glutarylation	PHHTEWEKAGEVSRE CCCCHHHHHCHHHHH	63.87	24703693
92	Acetylation	VSREVWEKAGKQGLL HHHHHHHHHHHCCCE	46.88	23576753
92	Succinylation	VSREVWEKAGKQGLL HHHHHHHHHHHCCCE	46.88	23806337
95	Malonylation	EVWEKAGKQGLLGIN HHHHHHHHCCCEEEE	46.16	32601280
95	Succinylation	EVWEKAGKQGLLGIN HHHHHHHHCCCEEEE	46.16	23806337
95	Acetylation	EVWEKAGKQGLLGIN HHHHHHHHCCCEEEE	46.16	23576753
151	Acetylation	YIANYGTKEQIEKFI HHHCCCCHHHHHHHH	43.17	22733758
156	Acetylation	GTKEQIEKFIPQMTA CCHHHHHHHHHHCCC	50.66	23864654
156	Succinylation	GTKEQIEKFIPQMTA CCHHHHHHHHHHCCC	50.66	23806337
165	Acetylation	IPQMTAGKCIGAIAM HHHCCCCCEEEEEEE	21.88	23806337
165	Succinylation	IPQMTAGKCIGAIAM HHHCCCCCEEEEEEE	21.88	23806337
165	Succinylation	IPQMTAGKCIGAIAM HHHCCCCCEEEEEEE	21.88	-
166	S-nitrosylation	PQMTAGKCIGAIAMT HHCCCCCEEEEEEEC	3.20	22178444
166	S-nitrosocysteine	PQMTAGKCIGAIAMT HHCCCCCEEEEEEEC	3.20	-
173	Phosphorylation	CIGAIAMTEPGAGSD EEEEEEECCCCCCCC	29.97	23737553
179	Phosphorylation	MTEPGAGSDLQGVRT ECCCCCCCCCCCCCC	34.31	26525534
189	Acetylation	QGVRTNAKRSGSDWI CCCCCCCCCCCCCEE	49.52	6269747
191	Phosphorylation	VRTNAKRSGSDWILN CCCCCCCCCCCEEEC	41.78	25521595
193	Phosphorylation	TNAKRSGSDWILNGS CCCCCCCCCEEECCC	30.90	9416615
200	Phosphorylation	SDWILNGSKVFITNG CCEEECCCEEEEECC	25.27	22817900
225	Phosphorylation	VTNREARSPAHGISL ECCCCCCCCCCCEEE	33.22	21082442
240	Acetylation	FLVENGMKGFIKGRK EEEECCCCCEECCCH	52.66	23806337
240	Succinylation	FLVENGMKGFIKGRK EEEECCCCCEECCCH	52.66	23806337
240	Succinylation	FLVENGMKGFIKGRK EEEECCCCCEECCCH	52.66	-
254	Succinylation	KLHKMGMKAQDTAEL HHHHCCCCHHHHHHH	36.85	23806337
254	Acetylation	KLHKMGMKAQDTAEL HHHHCCCCHHHHHHH	36.85	23576753
254	Glutarylation	KLHKMGMKAQDTAEL HHHHCCCCHHHHHHH	36.85	24703693
254	Succinylation	KLHKMGMKAQDTAEL HHHHCCCCHHHHHHH	36.85	-
279	Succinylation	ALLGEENKGFYYLMQ HHCCCCCCHHHHHHH	54.39	23806337
279	Succinylation	ALLGEENKGFYYLMQ HHCCCCCCHHHHHHH	54.39	-
279	Acetylation	ALLGEENKGFYYLMQ HHCCCCCCHHHHHHH	54.39	23576753
315	Acetylation	EETRNYVKQRKAFGK HHHHHHHHHHHHHCC	33.74	23576753
318	Acetylation	RNYVKQRKAFGKTVA HHHHHHHHHHCCHHH	45.64	24121500
322	Succinylation	KQRKAFGKTVAHIQT HHHHHHCCHHHHHHH	33.11	23806337
322	Glutarylation	KQRKAFGKTVAHIQT HHHHHHCCHHHHHHH	33.11	24703693
322	Succinylation	KQRKAFGKTVAHIQT HHHHHHCCHHHHHHH	33.11	-
322	Acetylation	KQRKAFGKTVAHIQT HHHHHHCCHHHHHHH	33.11	23576753
322	Malonylation	KQRKAFGKTVAHIQT HHHHHHCCHHHHHHH	33.11	26320211
338	Acetylation	QHKLAELKTHICVTR HHHHHHHHHCHHHHH	29.57	24062335
342	S-nitrosylation	AELKTHICVTRAFVD HHHHHCHHHHHHHHH	1.66	22178444
342	S-palmitoylation	AELKTHICVTRAFVD HHHHHCHHHHHHHHH	1.66	26165157
342	S-nitrosocysteine	AELKTHICVTRAFVD HHHHHCHHHHHHHHH	1.66	-
351	S-nitrosocysteine	TRAFVDSCLQLHETK HHHHHHHHHHHHHCC	2.13	-
351	S-nitrosylation	TRAFVDSCLQLHETK HHHHHHHHHHHHHCC	2.13	21278135
351	S-palmitoylation	TRAFVDSCLQLHETK HHHHHHHHHHHHHCC	2.13	28526873
358	Acetylation	CLQLHETKRLDSGSA HHHHHHCCCCCCCCH	48.23	23576753
362	Phosphorylation	HETKRLDSGSASMAK HHCCCCCCCCHHHHH	38.96	22817900
364	Phosphorylation	TKRLDSGSASMAKYW CCCCCCCCHHHHHHH	22.56	23140645
396	Phosphorylation	GWGYMWEYPIAKAYV CCEEEEECCCHHHHH	5.61	51457633
419	Acetylation	GGTNEIMKELIARQI CCHHHHHHHHHHHHH	55.84	23954790
428	Phosphorylation	LIARQIVSDS----- HHHHHHHCCC-----	33.49	22210690
430	Phosphorylation	ARQIVSDS------- HHHHHCCC-------	34.32	22210690

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

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
318	K	Acetylation	Acetylation at Lys-318 and Lys-322 in proximity of the cofactor-binding sites strongly reduces catalytic activity.	24121500
322	K	Acetylation	Acetylation at Lys-318 and Lys-322 in proximity of the cofactor-binding sites strongly reduces catalytic activity.	24121500

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of ACADL_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.