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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from acetate Inferred from electronic annotation. Source: InterPro 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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NR19-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NR19-2)

The sequence of this isoform differs from the canonical sequence as follows:
     277-277: V → VQGKLKEKSKRVQP

Note: No experimental confirmation available.

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.7
	Modified residue	263	1	Phosphoserine By similarity
	Modified residue	267	1	Phosphoserine Ref.7 Ref.9
	Modified residue	418	1	N6-acetyllysine Ref.8
Natural variations
	Alternative sequence	277	1	V → VQGKLKEKSKRVQP in isoform 2.		VSP_046376
Experimental info
	Sequence conflict	79	1	F → L in BAC03849. Ref.2
	Sequence conflict	615	1	V → F in AAH12172. Ref.5
	Sequence conflict	680	1	M → L in BAC03849. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: 820E84E62A72E214	FASTA	714	80,087
	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 KRSCPDVQGK LKEKSKRVQP QISWNQGIDL 310 320 330 340 350 360 WWHELMQEAG DECEPEWCDA EDPLFILYTS GSTGKPKGVV HTVGGYMLYV ATTFKYVFDF 370 380 390 400 410 420 HAEDVFWCTA DIGWITGHSY VTYGPLANGA TSVLFEGIPT YPDVNRLWSI VDKYKVTKFY 430 440 450 460 470 480 TAPTAIRLLM KFGDEPVTKH SRASLQVLGT VGEPINPEAW LWYHRVVGAQ RCPIVDTFWQ 490 500 510 520 530 540 TETGGHMLTP LPGATPMKPG SATFPFFGVA PAILNESGEE LEGEAEGYLV FKQPWPGIMR 550 560 570 580 590 600 TVYGNHERFE TTYFKKFPGY YVTGDGCQRD QDGYYWITGR IDDMLNVSGH LLSTAEVESA 610 620 630 640 650 660 LVEHEAVAEA AVVGHPHPVK GECLYCFVTL CDGHTFSPKL TEELKKQIRE KIGPIATPDY 670 680 690 700 710 IQNAPGLPKT RSGKIMRRVL RKIAQNDHDL GDMSTVADPS VISHLFSHRC LTIQ

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Tongue.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[6]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-267, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-418, MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF263614 mRNA. Translation: AAF75064.1. AK092281 mRNA. Translation: BAC03849.1. AL133324, AL049709 Genomic DNA. Translation: CAI19311.1. AL133324, AL049709 Genomic DNA. Translation: CAI19312.1. AL049709, AL133324 Genomic DNA. Translation: CAI19725.1. AL049709, AL133324 Genomic DNA. Translation: CAI19726.1. CH471077 Genomic DNA. Translation: EAW76248.1. BC012172 mRNA. Translation: AAH12172.1.
IPI	IPI00413730. IPI00549564.
RefSeq	NP_061147.1. NM_018677.3.
UniGene	Hs.517034.
3D structure databases
ProteinModelPortal	Q9NR19.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NR19. 3 interactions.
STRING	9606.ENSP00000353804.
PTM databases
PhosphoSite	Q9NR19.
Polymorphism databases
DMDM	20137525.
Proteomic databases
PaxDb	Q9NR19.
PRIDE	Q9NR19.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000253382; ENSP00000253382; ENSG00000131069. ENST00000360596; ENSP00000353804; ENSG00000131069.
GeneID	55902.
KEGG	hsa:55902.
UCSC	uc002xbc.2. human.
Organism-specific databases
CTD	55902.
GeneCards	GC20P033459.
HGNC	HGNC:15814. ACSS2.
HPA	HPA004141.
MIM	605832. gene.
neXtProt	NX_Q9NR19.
PharmGKB	PA24429.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0365.
HOGENOM	HOG000229981.
HOVERGEN	HBG014401.
KO	K01895.
OrthoDB	EOG4VHK61.
Enzyme and pathway databases
BioCyc	MetaCyc:HS05484-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. IPR025110. DUF4009. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 1 hit. PF13193. DUF4009. 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.
GenomeRNAi	55902.
NextBio	61271.
SOURCE	Search...

Entry information

Entry name

ACSA_HUMAN

Accession

Primary (citable) accession number: Q9NR19
Secondary accession number(s): A6NE90 , Q5QPH2, Q5QPH3, Q8N238, Q96EL0, Q9NQP7, Q9UJ15

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2002
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 108 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.