ACSF2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ACSF2_MOUSE
• UniProt AC: Q8VCW8
• Protein Name: Acyl-CoA synthetase family member 2, mitochondrial
• Gene Name: Acsf2
• Organism: Mus musculus (Mouse).
• Sequence Length: 615
• Subcellular Localization: Mitochondrion .
• Protein Description: Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation..
• Protein Sequence: MAVYHGMLRFGRLCIASLGARGPRTLLSRPRPNSKLQSVRALSSGMVNCTNPLPIGGLSYIQGHTDSHLVNTTVGECLDATAQRFPDREALVILHENIRLNFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLIQLATAQAGIILVSVNPAYQSSELEYVLRKVGCKGIVFPKQFKTQQYYDILKQVCPELEKAQPGALKSERLPDLTTVISVDAPLPGTLLLDDIVAAGGKEQNLAQLRYNQRFLSCYDPINIQFTSGTTGNPKGATLSHHNIVNNSMLIGQRLKMPTKTAEELRLVLPSPLYHCLGSVGGTMVSMMHGATLLLSSPSFNGKKALEAISREKGTLLYGTPTMFVDILNQPDFSSYDFTSIRGGVIAGSPAPPELIRAIINKMNMKELVVVYGTTENSPVTFMNFPEDTLEQKAGSVGRIMPHTEAQIVNVETGELTNLNVPGELYIRGYCVMQGYWGEPQKTFETVGQDKWYRTGDIALMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFLKHPQVQEAQVVGVKDERMGEEICACIRLKSGETTTAEEIKAFCKGKISHFKIPRYIVFVEGYPLTISGKIQKFKLREQMEQHLKL

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
106	Acetylation	RLNFAQLKEEVDKAA HHCHHHHHHHHHHHH	39.48	23954790
106	Succinylation	RLNFAQLKEEVDKAA HHCHHHHHHHHHHHH	39.48	23954790
111	Acetylation	QLKEEVDKAASGLLS HHHHHHHHHHHHHHH	51.53	23864654
179	Acetylation	CKGIVFPKQFKTQQY CCCEECCHHHCHHHH	57.83	23576753
179	Succinylation	CKGIVFPKQFKTQQY CCCEECCHHHCHHHH	57.83	23806337
179	Ubiquitination	CKGIVFPKQFKTQQY CCCEECCHHHCHHHH	57.83	-
182	Succinylation	IVFPKQFKTQQYYDI EECCHHHCHHHHHHH	42.82	-
182	Acetylation	IVFPKQFKTQQYYDI EECCHHHCHHHHHHH	42.82	23806337
182	Malonylation	IVFPKQFKTQQYYDI EECCHHHCHHHHHHH	42.82	26073543
182	Glutarylation	IVFPKQFKTQQYYDI EECCHHHCHHHHHHH	42.82	24703693
182	Succinylation	IVFPKQFKTQQYYDI EECCHHHCHHHHHHH	42.82	23806337
182	Ubiquitination	IVFPKQFKTQQYYDI EECCHHHCHHHHHHH	42.82	-
183	Phosphorylation	VFPKQFKTQQYYDIL ECCHHHCHHHHHHHH	23.38	29472430
191	Acetylation	QQYYDILKQVCPELE HHHHHHHHHHCHHHH	40.81	23864654
194	S-palmitoylation	YDILKQVCPELEKAQ HHHHHHHCHHHHHHC	1.69	28526873
199	Malonylation	QVCPELEKAQPGALK HHCHHHHHHCCCCCC	66.02	26320211
199	Succinylation	QVCPELEKAQPGALK HHCHHHHHHCCCCCC	66.02	24315375
199	Glutarylation	QVCPELEKAQPGALK HHCHHHHHHCCCCCC	66.02	24703693
199	Acetylation	QVCPELEKAQPGALK HHCHHHHHHCCCCCC	66.02	23576753
206	Succinylation	KAQPGALKSERLPDL HHCCCCCCCCCCCCC	50.14	23806337
206	Acetylation	KAQPGALKSERLPDL HHCCCCCCCCCCCCC	50.14	23864654
206	Glutarylation	KAQPGALKSERLPDL HHCCCCCCCCCCCCC	50.14	24703693
207	Phosphorylation	AQPGALKSERLPDLT HCCCCCCCCCCCCCC	28.88	51457959
254	S-palmitoylation	YNQRFLSCYDPINIQ HCHHHHHCCCCEEEE	4.93	28526873
267	Phosphorylation	IQFTSGTTGNPKGAT EEEECCCCCCCCCCE	38.19	30352176
296	Acetylation	QRLKMPTKTAEELRL CCCCCCCCCHHHHHH	39.61	23201123
340	Acetylation	SPSFNGKKALEAISR CCCCCCHHHHHHHHH	60.65	23576753
340	Succinylation	SPSFNGKKALEAISR CCCCCCHHHHHHHHH	60.65	-
340	Glutarylation	SPSFNGKKALEAISR CCCCCCHHHHHHHHH	60.65	24703693
340	Ubiquitination	SPSFNGKKALEAISR CCCCCCHHHHHHHHH	60.65	-
340	Malonylation	SPSFNGKKALEAISR CCCCCCHHHHHHHHH	60.65	26320211
385	Phosphorylation	RGGVIAGSPAPPELI ECCEECCCCCCHHHH	14.63	27180971
398	Acetylation	LIRAIINKMNMKELV HHHHHHHHCCCCEEE	22.65	23576753
398	Ubiquitination	LIRAIINKMNMKELV HHHHHHHHCCCCEEE	22.65	27667366
398	Succinylation	LIRAIINKMNMKELV HHHHHHHHCCCCEEE	22.65	24315375
398	Malonylation	LIRAIINKMNMKELV HHHHHHHHCCCCEEE	22.65	26320211
402	Succinylation	IINKMNMKELVVVYG HHHHCCCCEEEEEEE	42.78	23954790
467	S-nitrosylation	ELYIRGYCVMQGYWG EEEEEEEEEECCCCC	1.98	21278135
467	S-palmitoylation	ELYIRGYCVMQGYWG EEEEEEEEEECCCCC	1.98	28526873
467	S-nitrosocysteine	ELYIRGYCVMQGYWG EEEEEEEEEECCCCC	1.98	-
478	Succinylation	GYWGEPQKTFETVGQ CCCCCCCCEEEECCC	66.93	-
478	Succinylation	GYWGEPQKTFETVGQ CCCCCCCCEEEECCC	66.93	23806337
478	Acetylation	GYWGEPQKTFETVGQ CCCCCCCCEEEECCC	66.93	23806337
487	Acetylation	FETVGQDKWYRTGDI EEECCCCCCEEECCE	37.93	23576753
503	S-palmitoylation	LMDEQGFCKIVGRSK EECCCCCEEEEECCC	3.63	28526873
503	S-nitrosocysteine	LMDEQGFCKIVGRSK EECCCCCEEEEECCC	3.63	-
503	S-nitrosylation	LMDEQGFCKIVGRSK EECCCCCEEEEECCC	3.63	21278135
504	Acetylation	MDEQGFCKIVGRSKD ECCCCCEEEEECCCC	37.86	23201123
510	Acetylation	CKIVGRSKDMIIRGG EEEEECCCCEEEECC	50.37	23576753
531	Ubiquitination	ELEDFFLKHPQVQEA HHHHHHHHCCCCCEE	48.35	-
531	Acetylation	ELEDFFLKHPQVQEA HHHHHHHHCCCCCEE	48.35	23864654
531	Succinylation	ELEDFFLKHPQVQEA HHHHHHHHCCCCCEE	48.35	23806337
544	Succinylation	EAQVVGVKDERMGEE EEEEECCCCCCCCCE	48.20	-
544	Acetylation	EAQVVGVKDERMGEE EEEEECCCCCCCCCE	48.20	23576753
544	Succinylation	EAQVVGVKDERMGEE EEEEECCCCCCCCCE	48.20	23806337
553	S-palmitoylation	ERMGEEICACIRLKS CCCCCEEEEEEEECC	2.60	28526873
555	S-palmitoylation	MGEEICACIRLKSGE CCCEEEEEEEECCCC	1.29	28526873
559	Acetylation	ICACIRLKSGETTTA EEEEEEECCCCCCCH	46.71	23576753
570	Succinylation	TTTAEEIKAFCKGKI CCCHHHHHHHHCCCC	38.39	-
570	Succinylation	TTTAEEIKAFCKGKI CCCHHHHHHHHCCCC	38.39	23806337
570	Acetylation	TTTAEEIKAFCKGKI CCCHHHHHHHHCCCC	38.39	23576753
570	Glutarylation	TTTAEEIKAFCKGKI CCCHHHHHHHHCCCC	38.39	24703693
574	Acetylation	EEIKAFCKGKISHFK HHHHHHHCCCCCCCC	57.70	23864654
576	Acetylation	IKAFCKGKISHFKIP HHHHHCCCCCCCCCC	26.91	23201123
581	Acetylation	KGKISHFKIPRYIVF CCCCCCCCCCEEEEE	46.51	23864654
592	Phosphorylation	YIVFVEGYPLTISGK EEEEEECCEEEEECE	4.99	23140645
595	Phosphorylation	FVEGYPLTISGKIQK EEECCEEEEECEEHH	14.48	23984901
597	Phosphorylation	EGYPLTISGKIQKFK ECCEEEEECEEHHHH	28.88	26643407
599	Succinylation	YPLTISGKIQKFKLR CEEEEECEEHHHHHH	34.86	-
599	Succinylation	YPLTISGKIQKFKLR CEEEEECEEHHHHHH	34.86	23806337
599	Ubiquitination	YPLTISGKIQKFKLR CEEEEECEEHHHHHH	34.86	-
599	Acetylation	YPLTISGKIQKFKLR CEEEEECEEHHHHHH	34.86	23806337
614	Acetylation	EQMEQHLKL------ HHHHHHHCC------	50.45	23576753

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

Oops, there are no upstream regulatory protein records of ACSF2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ACSF2_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 ACSF2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ACSF2_MOUSE !!

Drug and Disease Associations

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