Q9NR19 (ACSA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-coenzyme A synthetase, cytoplasmic
EC=6.2.1.1

Alternative name(s):
Acetate--CoA ligase
Acetyl-CoA synthetase
Short name=ACS
Short name=AceCS
Acyl-CoA synthetase short-chain family member 2
Acyl-activating enzyme

Gene names

Name:	ACSS2
Synonyms:	ACAS2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	701 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Activates acetate so that it can be used for lipid synthesis or for energy generation.
Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ethanol oxidation Traceable author statement. Source: Reactome lipid biosynthetic process Inferred from mutant phenotype Ref.1. Source: UniProtKB xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA
Molecular function	AMP binding Inferred by curator Ref.1. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
UPF1	Q92900	1	EBI-372879,EBI-373471

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 701	701	Acetyl-coenzyme A synthetase, cytoplasmic		PRO_0000208423
Amino acid modifications
	Modified residue	30	1	Phosphoserine Ref.4 Ref.5 Ref.6
	Modified residue	263	1	Phosphoserine By similarity
	Modified residue	267	1	Phosphoserine Ref.5
	Modified residue	418	1	N6-acetyllysine Ref.7
Experimental info
	Sequence conflict	615	1	V → F in AAH12172. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9NR19 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 833580B41B73A8B4	FASTA	701	78,580
	10 20 30 40 50 60 MGLPEERVRS GSGSRGQEEA GAGGRARSWS PPPEVSRSAH VPSLQRYREL HRRSVEEPRE 70 80 90 100 110 120 FWGDIAKEFY WKTPCPGPFL RYNFDVTKGK IFIEWMKGAT TNICYNVLDR NVHEKKLGDK 130 140 150 160 170 180 VAFYWEGNEP GETTQITYHQ LLVQVCQFSN VLRKQGIQKG DRVAIYMPMI PELVVAMLAC 190 200 210 220 230 240 ARIGALHSIV FAGFSSESLC ERILDSSCSL LITTDAFYRG EKLVNLKELA DEALQKCQEK 250 260 270 280 290 300 GFPVRCCIVV KHLGRAELGM GDSTSQSPPI KRSCPDVQIS WNQGIDLWWH ELMQEAGDEC 310 320 330 340 350 360 EPEWCDAEDP LFILYTSGST GKPKGVVHTV GGYMLYVATT FKYVFDFHAE DVFWCTADIG 370 380 390 400 410 420 WITGHSYVTY GPLANGATSV LFEGIPTYPD VNRLWSIVDK YKVTKFYTAP TAIRLLMKFG 430 440 450 460 470 480 DEPVTKHSRA SLQVLGTVGE PINPEAWLWY HRVVGAQRCP IVDTFWQTET GGHMLTPLPG 490 500 510 520 530 540 ATPMKPGSAT FPFFGVAPAI LNESGEELEG EAEGYLVFKQ PWPGIMRTVY GNHERFETTY 550 560 570 580 590 600 FKKFPGYYVT GDGCQRDQDG YYWITGRIDD MLNVSGHLLS TAEVESALVE HEAVAEAAVV 610 620 630 640 650 660 GHPHPVKGEC LYCFVTLCDG HTFSPKLTEE LKKQIREKIG PIATPDYIQN APGLPKTRSG 670 680 690 700 KIMRRVLRKI AQNDHDLGDM STVADPSVIS HLFSHRCLTI Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins." Luong A., Hannah V.C., Brown M.S., Goldstein J.L. J. Biol. Chem. 275:26458-26466(2000) [PubMed: 10843999] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[4]	"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) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, MASS SPECTROMETRY. Tissue: Platelet.
[5]	"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) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-267, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-418, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF263614 mRNA. Translation: AAF75064.1. AL049709, AL133324 Genomic DNA. Translation: CAI19726.1. AL133324, AL049709 Genomic DNA. Translation: CAI19312.1. BC012172 mRNA. Translation: AAH12172.1.
IPI	IPI00413730.
RefSeq	NP_061147.1. NM_018677.3.
UniGene	Hs.517034.
3D structure databases
ProteinModelPortal	Q9NR19.
SMR	Q9NR19. Positions 31-697.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NR19. 3 interactions.
STRING	Q9NR19.
PTM databases
PhosphoSite	Q9NR19.
Polymorphism databases
DMDM	20137525.
Proteomic databases
PRIDE	Q9NR19.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000360596; ENSP00000353804; ENSG00000131069.
GeneID	55902.
KEGG	hsa:55902.
UCSC	uc002xbd.1. human.
Organism-specific databases
CTD	55902.
GeneCards	GC20P033459.
H-InvDB	HIX0015754.
HGNC	HGNC:15814. ACSS2.
HPA	HPA004141.
MIM	605832. gene.
neXtProt	NX_Q9NR19.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00550000074278.
HOVERGEN	HBG014401.
OrthoDB	EOG4VHK61.
PhylomeDB	Q9NR19.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000131069-MONOMER.
BRENDA	6.2.1.1. 2681.
Pathway_Interaction_DB	hdac_classiii_pathway. Signaling events mediated by HDAC Class III.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q9NR19.
Bgee	Q9NR19.
CleanEx	HS_ACSS2.
Genevestigator	Q9NR19.
GermOnline	ENSG00000131069. Homo sapiens.
Family and domain databases
InterPro	IPR011904. Ac_CoA_lig. IPR024597. Acyl-CoA_synth_DUF3448. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
KO	K01895.
PANTHER	PTHR24095:SF42. PTHR24095:SF42. 1 hit.
Pfam	PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 1 hit. [Graphical view]
TIGRFAMs	TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00131. Adenosine monophosphate. DB00171. Adenosine triphosphate.
NextBio	61271.
SOURCE	Search...

Entry information

Entry name

ACSA_HUMAN

Accession

Primary (citable) accession number: Q9NR19
Secondary accession number(s): Q5QPH2 , Q96EL0, Q9NQP7, Q9UJ15

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.