ACSF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ACSF2_HUMAN
• UniProt AC: Q96CM8
• Protein Name: Acyl-CoA synthetase family member 2, mitochondrial
• Gene Name: ACSF2
• Organism: Homo sapiens (Human).
• 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: MAVYVGMLRLGRLCAGSSGVLGARAALSRSWQEARLQGVRFLSSREVDRMVSTPIGGLSYVQGCTKKHLNSKTVGQCLETTAQRVPEREALVVLHEDVRLTFAQLKEEVDKAASGLLSIGLCKGDRLGMWGPNSYAWVLMQLATAQAGIILVSVNPAYQAMELEYVLKKVGCKALVFPKQFKTQQYYNVLKQICPEVENAQPGALKSQRLPDLTTVISVDAPLPGTLLLDEVVAAGSTRQHLDQLQYNQQFLSCHDPINIQFTSGTTGSPKGATLSHYNIVNNSNILGERLKLHEKTPEQLRMILPNPLYHCLGSVAGTMMCLMYGATLILASPIFNGKKALEAISRERGTFLYGTPTMFVDILNQPDFSSYDISTMCGGVIAGSPAPPELIRAIINKINMKDLVVAYGTTENSPVTFAHFPEDTVEQKAESVGRIMPHTEARIMNMEAGTLAKLNTPGELCIRGYCVMLGYWGEPQKTEEAVDQDKWYWTGDVATMNEQGFCKIVGRSKDMIIRGGENIYPAELEDFFHTHPKVQEVQVVGVKDDRMGEEICACIRLKDGEETTVEEIKAFCKGKISHFKIPKYIVFVTNYPLTISGKIQKFKLREQMERHLNL

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
17	Phosphorylation	LGRLCAGSSGVLGAR HHHHCCCCCCHHHHH	12.85	68717059
18	Phosphorylation	GRLCAGSSGVLGARA HHHCCCCCCHHHHHH	31.81	68717065
52	Phosphorylation	REVDRMVSTPIGGLS HHHHHHCCCCCCCHH	21.08	22964224
53	Phosphorylation	EVDRMVSTPIGGLSY HHHHHCCCCCCCHHH	13.91	100646223
59	Phosphorylation	STPIGGLSYVQGCTK CCCCCCHHHHCCCCH	26.91	100646215
60	Phosphorylation	TPIGGLSYVQGCTKK CCCCCHHHHCCCCHH	11.22	100646231
65	Phosphorylation	LSYVQGCTKKHLNSK HHHHCCCCHHHCCCC	50.37	46158031
66	Malonylation	SYVQGCTKKHLNSKT HHHCCCCHHHCCCCC	42.12	26320211
66	Acetylation	SYVQGCTKKHLNSKT HHHCCCCHHHCCCCC	42.12	25953088
71	Phosphorylation	CTKKHLNSKTVGQCL CCHHHCCCCCHHHHH	35.74	50563217
72	Malonylation	TKKHLNSKTVGQCLE CHHHCCCCCHHHHHH	46.27	26320211
106	2-Hydroxyisobutyrylation	RLTFAQLKEEVDKAA HHHHHHHHHHHHHHH	39.48	-
136	Acetylation	MWGPNSYAWVLMQLA CCCCCHHHHHHHHHH	6.96	19608861
179	Succinylation	CKALVFPKQFKTQQY CCEEECCHHHCHHHH	57.83	27452117
179	Acetylation	CKALVFPKQFKTQQY CCEEECCHHHCHHHH	57.83	27178108
182	Succinylation	LVFPKQFKTQQYYNV EECCHHHCHHHHHHH	42.82	-
182	Succinylation	LVFPKQFKTQQYYNV EECCHHHCHHHHHHH	42.82	27452117
182	Acetylation	LVFPKQFKTQQYYNV EECCHHHCHHHHHHH	42.82	25953088
182	Malonylation	LVFPKQFKTQQYYNV EECCHHHCHHHHHHH	42.82	26320211
274	Phosphorylation	TGSPKGATLSHYNIV CCCCCCCEEEEEEEC	37.15	22468782
276	Phosphorylation	SPKGATLSHYNIVNN CCCCCEEEEEEECCC	21.41	22468782
278	Phosphorylation	KGATLSHYNIVNNSN CCCEEEEEEECCCCC	11.83	22468782
283	Acetylation	SHYNIVNNSNILGER EEEEECCCCCCCCHH	26.07	19608861
296	Acetylation	ERLKLHEKTPEQLRM HHHHHCCCCHHHHHH	59.64	19608861
321	Acetylation	GSVAGTMMCLMYGAT HHHHHHHHHHHHHHH	1.27	19608861
340	Succinylation	SPIFNGKKALEAISR CHHHCCHHHHHHHHH	60.65	27452117
340	Malonylation	SPIFNGKKALEAISR CHHHCCHHHHHHHHH	60.65	26320211
340	Acetylation	SPIFNGKKALEAISR CHHHCCHHHHHHHHH	60.65	-
398	Acetylation	LIRAIINKINMKDLV HHHHHHHHCCHHHEE	25.67	-
417	O-linked_Glycosylation	TTENSPVTFAHFPED CCCCCCCEEECCCCC	20.63	29351928
466	Phosphorylation	GELCIRGYCVMLGYW CCEEEEEEEEECCCC	3.36	24719451
472	Phosphorylation	GYCVMLGYWGEPQKT EEEEECCCCCCCCCC	13.28	25147952
478	Succinylation	GYWGEPQKTEEAVDQ CCCCCCCCCCCCHHC	69.49	-
478	Succinylation	GYWGEPQKTEEAVDQ CCCCCCCCCCCCHHC	69.49	-
510	Malonylation	CKIVGRSKDMIIRGG EEEEECCCCEEEECC	50.37	26320211
510	Acetylation	CKIVGRSKDMIIRGG EEEEECCCCEEEECC	50.37	-
531	Phosphorylation	ELEDFFHTHPKVQEV HHHHHHCCCCCEEEE	34.42	25159151
544	Succinylation	EVQVVGVKDDRMGEE EEEEEEECCCCCCCE	48.24	-
544	Succinylation	EVQVVGVKDDRMGEE EEEEEEECCCCCCCE	48.24	-
544	Acetylation	EVQVVGVKDDRMGEE EEEEEEECCCCCCCE	48.24	-
564	Phosphorylation	RLKDGEETTVEEIKA ECCCCCCCCHHHHHH	31.66	110756093
570	Acetylation	ETTVEEIKAFCKGKI CCCHHHHHHHHCCCC	38.39	-
570	Succinylation	ETTVEEIKAFCKGKI CCCHHHHHHHHCCCC	38.39	-
570	Succinylation	ETTVEEIKAFCKGKI CCCHHHHHHHHCCCC	38.39	-
585	Phosphorylation	SHFKIPKYIVFVTNY CCCCCCCEEEEEECC	9.28	25690035
592	Phosphorylation	YIVFVTNYPLTISGK EEEEEECCCEEECCH	7.11	18491316
595	Phosphorylation	FVTNYPLTISGKIQK EEECCCEEECCHHHH	14.48	50563209
597	Phosphorylation	TNYPLTISGKIQKFK ECCCEEECCHHHHHH	28.88	18491316
599	Succinylation	YPLTISGKIQKFKLR CCEEECCHHHHHHHH	34.86	-
599	Succinylation	YPLTISGKIQKFKLR CCEEECCHHHHHHHH	34.86	-
609	Ubiquitination	KFKLREQMERHLNL- HHHHHHHHHHHHCC-	4.13	-

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

Oops, there are no upstream regulatory protein records of ACSF2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ACSF2_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 ACSF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CKLF5_HUMAN	CMTM5	physical	25416956
GBB2_HUMAN	GNB2	physical	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.

Related Literatures of Post-Translational Modification

Acetylation

"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-296, AND MASS SPECTROMETRY.
PubMed: 19608861