dbPTM

ACSA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACSA_HUMAN
UniProt AC	Q9NR19
Protein Name	Acetyl-coenzyme A synthetase, cytoplasmic
Gene Name	ACSS2
Organism	Homo sapiens (Human).
Sequence Length	701
Subcellular Localization	Cytoplasm.
Protein Description	Activates acetate so that it can be used for lipid synthesis or for energy generation..
Protein Sequence	MGLPEERVRSGSGSRGQEEAGAGGRARSWSPPPEVSRSAHVPSLQRYRELHRRSVEEPREFWGDIAKEFYWKTPCPGPFLRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVADPSVISHLFSHRCLTIQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	LPEERVRSGSGSRGQ CCHHHHCCCCCCCCC	34.16	23090842
12	Phosphorylation	EERVRSGSGSRGQEE HHHHCCCCCCCCCCC	34.54	25262027
14	Phosphorylation	RVRSGSGSRGQEEAG HHCCCCCCCCCCCCC	34.63	23090842
28	Phosphorylation	GAGGRARSWSPPPEV CCCCCCCCCCCCCCC	30.81	30266825
30	Phosphorylation	GGRARSWSPPPEVSR CCCCCCCCCCCCCCC	28.86	22167270
36	Phosphorylation	WSPPPEVSRSAHVPS CCCCCCCCCCCCCCH	20.89	23927012
38	Phosphorylation	PPPEVSRSAHVPSLQ CCCCCCCCCCCCHHH	18.41	29978859
43	Phosphorylation	SRSAHVPSLQRYREL CCCCCCCHHHHHHHH	35.73	26091039
47	Phosphorylation	HVPSLQRYRELHRRS CCCHHHHHHHHHHCC	8.76	29978859
54	Phosphorylation	YRELHRRSVEEPREF HHHHHHCCCCCHHHH	33.56	101545065
88	Ubiquitination	RYNFDVTKGKIFIEW EEEEEECCCEEEEEE	59.04	-
100	Phosphorylation	IEWMKGATTNICYNV EEECCCCCCCHHHHH	29.10	46158209
101	Phosphorylation	EWMKGATTNICYNVL EECCCCCCCHHHHHH	23.27	46158215
222	Malonylation	DAFYRGEKLVNLKEL CCCCCCCCEECHHHH	61.63	26320211
222 (in isoform 2)	Malonylation	-	61.63	26320211
227	Ubiquitination	GEKLVNLKELADEAL CCCEECHHHHHHHHH	45.54	21890473
236	Ubiquitination	LADEALQKCQEKGFP HHHHHHHHHHHCCCC	38.44	-
263	Phosphorylation	AELGMGDSTSQSPPI EECCCCCCCCCCCCC	24.99	29255136
264	Phosphorylation	ELGMGDSTSQSPPIK ECCCCCCCCCCCCCC	35.21	29255136
265	Phosphorylation	LGMGDSTSQSPPIKR CCCCCCCCCCCCCCC	32.39	23401153
267	Phosphorylation	MGDSTSQSPPIKRSC CCCCCCCCCCCCCCC	32.20	29255136
271	Ubiquitination	TSQSPPIKRSCPDVQ CCCCCCCCCCCCCCE	43.99	21890473
273 (in isoform 2)	Phosphorylation	-	25.62	26657352
411	Phosphorylation	TKFYTAPTAIRLLMK CEEECHHHHHHHHHH	32.05	51458037
418	Ubiquitination	TAIRLLMKFGDEPVT HHHHHHHHHCCCCCC	46.28	21890473
418	Acetylation	TAIRLLMKFGDEPVT HHHHHHHHHCCCCCC	46.28	19608861
426	Ubiquitination	FGDEPVTKHSRASLQ HCCCCCCCCCHHHEE	39.56	21890473
431	Ubiquitination	VTKHSRASLQVLGTV CCCCCHHHEEEECCC	20.44	21890473
431	Ubiquitination	VTKHSRASLQVLGTV CCCCCHHHEEEECCC	20.44	21890473
431 (in isoform 2)	Malonylation	-	20.44	26320211
464	Phosphorylation	QRCPIVDTFWQTETG CCCCEEEEEEECCCC	18.84	27050516
476	Phosphorylation	ETGGHMLTPLPGATP CCCCCCEECCCCCCC	18.40	27050516
561	Phosphorylation	CQRDQDGYYWITGRI CCCCCCCEEEEEEEC	12.15	75131
622	Phosphorylation	VTLCDGHTFSPKLTE EEECCCCCCCHHHHH	31.19	25627689
624	Phosphorylation	LCDGHTFSPKLTEEL ECCCCCCCHHHHHHH	23.45	24719451
632	Acetylation	PKLTEELKKQIREKI HHHHHHHHHHHHHHH	46.00	21339330
638	Ubiquitination	LKKQIREKIGPIATP HHHHHHHHHCCCCCC	43.01	-
644	Phosphorylation	EKIGPIATPDYIQNA HHHCCCCCCHHHHCC	19.88	25159151
659	Phosphorylation	PGLPKTRSGKIMRRV CCCCCCCCHHHHHHH	50.06	23532336
661	Acetylation	LPKTRSGKIMRRVLR CCCCCCHHHHHHHHH	34.28	-

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
659	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
661	K	Acetylation		-
Reversibly acetylated at Lys-661 (By similarity).

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 ACSA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
PYR1_HUMAN	CAD	physical	26344197
SYWC_HUMAN	WARS	physical	26344197

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 ACSA_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-418, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-267, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY.	18088087 [Abstract]

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