dbPTM

ACS2L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACS2L_HUMAN
UniProt AC	Q9NUB1
Protein Name	Acetyl-coenzyme A synthetase 2-like, mitochondrial
Gene Name	ACSS1
Organism	Homo sapiens (Human).
Sequence Length	689
Subcellular Localization	Mitochondrion matrix .
Protein Description	Important for maintaining normal body temperature during fasting and for energy homeostasis. Essential for energy expenditure under ketogenic conditions (By similarity). Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2)..
Protein Sequence	MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPALSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILSVYQKCKDKQAAAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Phosphorylation	GVGRLLGSLRGLSGQ HHHHHHHHHCCCCCC	18.18	62150437
32	Phosphorylation	ARPPCGVSAPRRAAS CCCCCCCCCCCCHHC	20.17	62150443
39	Phosphorylation	SAPRRAASGPSGSAP CCCCCHHCCCCCCHH	50.69	22210691
58	Phosphorylation	AAAQPGSYPALSAQA HHCCCCCCHHCCHHH	9.84	22210691
158	Acetylation	CRLANTLKRHGVHRG HHHHHHHHHCCCCCC	40.07	25953088
275	Acetylation	EQEMAKEDPVCAPES HHHHHHHCCCCCCHH	39.98	19608861
285	Phosphorylation	CAPESMGSEDMLFML CCCHHCCCCCEEEEE	23.06	68696455
396	Acetylation	TAVRLLLKYGDAWVK HHHHHHHHHCCHHHH	47.35	19608861
396	Malonylation	TAVRLLLKYGDAWVK HHHHHHHHHCCHHHH	47.35	26320211
481	Sulfoxidation	FGIVPVLMDEKGSVV CCEEEEEECCCCCEE	6.78	21406390
521	Phosphorylation	HQRFVDAYFKAYPGY HHHHHHHHHHHCCCE	10.93	59304851
523	Ubiquitination	RFVDAYFKAYPGYYF HHHHHHHHHCCCEEE	34.04	-
525	Phosphorylation	VDAYFKAYPGYYFTG HHHHHHHCCCEEEEC	9.59	26503514
528	Phosphorylation	YFKAYPGYYFTGDGA HHHHCCCEEEECCCC	7.30	26503514
531	Phosphorylation	AYPGYYFTGDGAYRT HCCCEEEECCCCEEC	20.45	26503514
542	Phosphorylation	AYRTEGGYYQITGRM CEECCCEEEEEEECC	11.76	75127
549	Sulfoxidation	YYQITGRMDDVINIS EEEEEECCCCEEEEC	5.66	21406390
622	Acetylation	MVATKIAKYAVPDEI HHHHHHHHHCCCCEE	36.90	25953088
633	Ubiquitination	PDEILVVKRLPKTRS CCEEEEEEECCCCCC	40.51	-
642	Acetylation	LPKTRSGKVMRRLLR CCCCCCHHHHHHHHH	33.82	16788062
678	Phosphorylation	IAEILSVYQKCKDKQ HHHHHHHHHHHHHHH	10.01	7331867

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of ACS2L_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
642	K	Acetylation		16788062
Reversibly acetylated on Lys-642.

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ACS2L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ACS2L_HUMAN !!

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
DB00131	Adenosine monophosphate
DB00171	Adenosine triphosphate

Regulatory Network of ACS2L_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-396, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Reversible lysine acetylation controls the activity of themitochondrial enzyme acetyl-CoA synthetase 2."; Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., Verdin E.; Proc. Natl. Acad. Sci. U.S.A. 103:10224-10229(2006). Cited for: ACETYLATION AT LYS-642, MUTAGENESIS OF LYS-642, FUNCTION, ENZYMEREGULATION, PROTEIN SEQUENCE OF N-TERMINUS, MASS SPECTROMETRY, ANDSUBCELLULAR LOCATION.	16788062 [Abstract]