ACSL5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ACSL5_MOUSE
• UniProt AC: Q8JZR0
• Protein Name: Long-chain-fatty-acid--CoA ligase 5
• Gene Name: Acsl5
• Organism: Mus musculus (Mouse).
• Sequence Length: 683
• Subcellular Localization: Mitochondrion. Endoplasmic reticulum. Mitochondrion outer membrane; Single-pass type III membrane protein. Endoplasmic reticulum membrane; Single-pass type III membrane protein.
• Protein Description: Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity). It was suggested that it may also stimulate fatty acid oxidation (By similarity). At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL (By similarity). May have a role in the survival of glioma cells (By similarity). Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity)..
• Protein Sequence: MLFIFNFLFSPLPTPALICLLTFGTAIFLWLINRPQPVLPLIDLDNQSVGIEGGARRGAFQKNNDLILYYFSDAKTLYENFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDTPQKATMLVENVEKGLTPGLKTIILMDPFDDDLMKRGEKCGVEMLSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIISKFNEVKNGIIRRDSLWDKLVFSKIQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGVKGSFEELCKNQCVKEAILEDLQKIGKEGGLKSFEQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE

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
62	Ubiquitination	ARRGAFQKNNDLILY CCCCCCCCCCCEEEE	51.79	-
69	Phosphorylation	KNNDLILYYFSDAKT CCCCEEEEEECCHHH	8.75	15582521
70	Phosphorylation	NNDLILYYFSDAKTL CCCEEEEEECCHHHH	7.99	23140645
72	Phosphorylation	DLILYYFSDAKTLYE CEEEEEECCHHHHHH	22.12	23140645
93	S-palmitoylation	AVSDNGPCLGYRKPN CCCCCCCCCCCCCCC	4.95	28526873
96	Phosphorylation	DNGPCLGYRKPNQPY CCCCCCCCCCCCCCC	11.52	119479
98	Malonylation	GPCLGYRKPNQPYKW CCCCCCCCCCCCCEE	39.58	26320211
104	Malonylation	RKPNQPYKWISYKQV CCCCCCCEEEEEEEH	44.74	26320211
109	Ubiquitination	PYKWISYKQVSDRAE CCEEEEEEEHHHHHH	37.12	-
109	Acetylation	PYKWISYKQVSDRAE CCEEEEEEEHHHHHH	37.12	23954790
121	S-palmitoylation	RAEYLGSCLLHKGYK HHHHHHHHHHHCCCC	4.44	28526873
185	S-palmitoylation	ADIPVVICDTPQKAT CCCCEEEECCCCCEE	3.01	28526873
200	Ubiquitination	MLVENVEKGLTPGLK EHHHHHHCCCCCCCE	55.74	-
221	Ubiquitination	PFDDDLMKRGEKCGV CCCHHHHHHHHHCCC	65.63	-
225	Ubiquitination	DLMKRGEKCGVEMLS HHHHHHHHCCCEEEE	38.83	-
245	Acetylation	NIGKENFKKPVPPKP HHCCCCCCCCCCCCC	68.68	23864654
259	S-palmitoylation	PEDLSVICFTSGTTG CCCCEEEEEECCCCC	2.59	28526873
322	S-palmitoylation	VQGILFSCGGKIGFF HHHHHHHCCCCCEEC	6.98	28526873
341	Acetylation	RLLPDDMKALKPTVF EECCCHHHHHCCCCC	58.52	23864654
341	Malonylation	RLLPDDMKALKPTVF EECCCHHHHHCCCCC	58.52	26320211
344	Ubiquitination	PDDMKALKPTVFPTV CCHHHHHCCCCCCCH	43.43	-
344	Succinylation	PDDMKALKPTVFPTV CCHHHHHCCCCCCCH	43.43	23954790
344	Acetylation	PDDMKALKPTVFPTV CCHHHHHCCCCCCCH	43.43	23864654
344	Malonylation	PDDMKALKPTVFPTV CCHHHHHCCCCCCCH	43.43	26320211
359	Phosphorylation	PRLLNRVYDKVQNEA HHHHHHHHHHHHHHC	13.55	51457989
361	Acetylation	LLNRVYDKVQNEAKT HHHHHHHHHHHHCCC	28.21	23576753
361	Ubiquitination	LLNRVYDKVQNEAKT HHHHHHHHHHHHCCC	28.21	-
361	Malonylation	LLNRVYDKVQNEAKT HHHHHHHHHHHHCCC	28.21	26320211
367	Malonylation	DKVQNEAKTPLKKFL HHHHHHCCCHHHHHH	44.49	26320211
367	Ubiquitination	DKVQNEAKTPLKKFL HHHHHHCCCHHHHHH	44.49	-
367	Acetylation	DKVQNEAKTPLKKFL HHHHHHCCCHHHHHH	44.49	23201123
368	Phosphorylation	KVQNEAKTPLKKFLL HHHHHCCCHHHHHHH	40.68	51457995
399	Ubiquitination	RRDSLWDKLVFSKIQ CCCCHHHHHHHHHHC	34.66	-
399	Acetylation	RRDSLWDKLVFSKIQ CCCCHHHHHHHHHHC	34.66	23954790
404	Ubiquitination	WDKLVFSKIQGSLGG HHHHHHHHHCCCCCC	27.81	-
404	Malonylation	WDKLVFSKIQGSLGG HHHHHHHHHCCCCCC	27.81	26320211
412	Ubiquitination	IQGSLGGKVRLMITG HCCCCCCEEEEEEEC	23.53	-
412	Malonylation	IQGSLGGKVRLMITG HCCCCCCEEEEEEEC	23.53	26320211
502	Ubiquitination	IKGNNVFKGYLKDPE ECCCCEEEEECCCHH	42.22	-
510	Ubiquitination	GYLKDPEKTQEVLDK EECCCHHHHHHHHCC	61.98	-
517	Ubiquitination	KTQEVLDKDGWLHTG HHHHHHCCCCCEECC	54.72	-
517	Acetylation	KTQEVLDKDGWLHTG HHHHHHCCCCCEECC	54.72	23954790
536	Ubiquitination	WLPNGTLKIVDRKKN CCCCCCEEEEECCCC	40.29	-
536	Malonylation	WLPNGTLKIVDRKKN CCCCCCEEEEECCCC	40.29	26320211
536	Acetylation	WLPNGTLKIVDRKKN CCCCCCEEEEECCCC	40.29	23954790
546	Ubiquitination	DRKKNIFKLAQGEYI ECCCCHHHHHCCCEE	38.83	-
557	Acetylation	GEYIAPEKIENVYSR CCEECHHHHHHHHHC	55.02	23864654
557	Ubiquitination	GEYIAPEKIENVYSR CCEECHHHHHHHHHC	55.02	-
595	Phosphorylation	PDPDSLPSFAAKIGV CCCCCCHHHHHHHCC	32.58	30352176
603	Ubiquitination	FAAKIGVKGSFEELC HHHHHCCCCCHHHHH	43.56	-
610	S-palmitoylation	KGSFEELCKNQCVKE CCCHHHHHHCHHHHH	4.38	28526873
611	Acetylation	GSFEELCKNQCVKEA CCHHHHHHCHHHHHH	63.78	23201123
611	Ubiquitination	GSFEELCKNQCVKEA CCHHHHHHCHHHHHH	63.78	-
616	Ubiquitination	LCKNQCVKEAILEDL HHHCHHHHHHHHHHH	49.40	-
625	Acetylation	AILEDLQKIGKEGGL HHHHHHHHHCHHCCC	61.80	22902405
625	Ubiquitination	AILEDLQKIGKEGGL HHHHHHHHHCHHCCC	61.80	-
628	Malonylation	EDLQKIGKEGGLKSF HHHHHHCHHCCCCCH	57.57	26320211
628	Acetylation	EDLQKIGKEGGLKSF HHHHHHCHHCCCCCH	57.57	23864654
634	Phosphorylation	GKEGGLKSFEQVKSI CHHCCCCCHHHHHEE	38.77	20495213
639	Ubiquitination	LKSFEQVKSIFVHPE CCCHHHHHEEEECCC	37.21	-
668	Ubiquitination	AKRVELAKFFQTQIK HHHHHHHHHHHHHHH	60.37	-
675	Ubiquitination	KFFQTQIKSLYESIE HHHHHHHHHHHHHHC	25.29	-
680	Phosphorylation	QIKSLYESIEE---- HHHHHHHHHCC----	23.03	73245531

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

Oops, there are no upstream regulatory protein records of ACSL5_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ACSL5_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ACSL5_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ACSL5_MOUSE !!

Drug and Disease Associations

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