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Acetyl-coenzyme A synthetase, cytoplasmic (EC 6.2.1.1) (Acetate--CoA ligase) (Acetyl-CoA synthetase) (ACS) (AceCS) (Acyl-CoA synthetase short-chain family member 2) (Acyl-activating enzyme)

 ACSA_HUMAN              Reviewed;         701 AA.
Q9NR19; A6NE90; Q5QPH2; Q5QPH3; Q8N238; Q96EL0; Q9NQP7; Q9UJ15;
03-APR-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 149.
RecName: Full=Acetyl-coenzyme A synthetase, cytoplasmic;
EC=6.2.1.1;
AltName: Full=Acetate--CoA ligase;
AltName: Full=Acetyl-CoA synthetase;
Short=ACS;
Short=AceCS;
AltName: Full=Acyl-CoA synthetase short-chain family member 2;
AltName: Full=Acyl-activating enzyme;
Name=ACSS2; Synonyms=ACAS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
PubMed=10843999; DOI=10.1074/jbc.M004160200;
Luong A., Hannah V.C., Brown M.S., Goldstein J.L.;
"Molecular characterization of human acetyl-CoA synthetase, an enzyme
regulated by sterol regulatory element-binding proteins.";
J. Biol. Chem. 275:26458-26466(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
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.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-267, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-30 AND SER-267,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-30; SER-36 AND
SER-267, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- 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: Monomer.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NR19-1; Sequence=Displayed;
Name=2;
IsoId=Q9NR19-2; Sequence=VSP_046376;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
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EMBL; AF263614; AAF75064.1; -; mRNA.
EMBL; AK092281; BAC03849.1; -; mRNA.
EMBL; AL133324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL049709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW76248.1; -; Genomic_DNA.
EMBL; BC012172; AAH12172.1; -; mRNA.
CCDS; CCDS13243.1; -. [Q9NR19-1]
CCDS; CCDS42868.2; -. [Q9NR19-2]
RefSeq; NP_001070020.2; NM_001076552.2. [Q9NR19-2]
RefSeq; NP_061147.1; NM_018677.3. [Q9NR19-1]
UniGene; Hs.517034; -.
ProteinModelPortal; Q9NR19; -.
SMR; Q9NR19; -.
BioGrid; 120989; 6.
IntAct; Q9NR19; 5.
STRING; 9606.ENSP00000253382; -.
DrugBank; DB00131; Adenosine monophosphate.
DrugBank; DB00171; Adenosine triphosphate.
DrugBank; DB09395; Sodium acetate.
SwissLipids; SLP:000001167; -.
iPTMnet; Q9NR19; -.
PhosphoSitePlus; Q9NR19; -.
BioMuta; ACSS2; -.
DMDM; 20137525; -.
EPD; Q9NR19; -.
MaxQB; Q9NR19; -.
PaxDb; Q9NR19; -.
PeptideAtlas; Q9NR19; -.
PRIDE; Q9NR19; -.
Ensembl; ENST00000253382; ENSP00000253382; ENSG00000131069. [Q9NR19-2]
Ensembl; ENST00000360596; ENSP00000353804; ENSG00000131069. [Q9NR19-1]
GeneID; 55902; -.
KEGG; hsa:55902; -.
UCSC; uc002xbd.3; human. [Q9NR19-1]
CTD; 55902; -.
DisGeNET; 55902; -.
EuPathDB; HostDB:ENSG00000131069.19; -.
GeneCards; ACSS2; -.
HGNC; HGNC:15814; ACSS2.
HPA; HPA004141; -.
MIM; 605832; gene.
neXtProt; NX_Q9NR19; -.
OpenTargets; ENSG00000131069; -.
PharmGKB; PA24429; -.
eggNOG; KOG1175; Eukaryota.
eggNOG; COG0365; LUCA.
GeneTree; ENSGT00760000119178; -.
HOGENOM; HOG000229981; -.
HOVERGEN; HBG014401; -.
InParanoid; Q9NR19; -.
KO; K01895; -.
OMA; DHWWHDL; -.
OrthoDB; EOG091G039C; -.
PhylomeDB; Q9NR19; -.
TreeFam; TF300417; -.
BioCyc; MetaCyc:HS05484-MONOMER; -.
BRENDA; 6.2.1.1; 2681.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-71384; Ethanol oxidation.
ChiTaRS; ACSS2; human.
GeneWiki; ACSS2; -.
GenomeRNAi; 55902; -.
PRO; PR:Q9NR19; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000131069; -.
CleanEx; HS_ACSS2; -.
ExpressionAtlas; Q9NR19; baseline and differential.
Genevisible; Q9NR19; HS.
GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003987; F:acetate-CoA ligase activity; IDA:UniProtKB.
GO; GO:0016208; F:AMP binding; IC:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019413; P:acetate biosynthetic process; IEA:Ensembl.
GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
GO; GO:0006069; P:ethanol oxidation; TAS:Reactome.
GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:0019542; P:propionate biosynthetic process; IEA:Ensembl.
CDD; cd05966; ACS; 1.
InterPro; IPR011904; Ac_CoA_lig.
InterPro; IPR032387; ACAS_N.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
Pfam; PF16177; ACAS_N; 1.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Ligase; Nucleotide-binding; Phosphoprotein;
Reference proteome.
CHAIN 1 701 Acetyl-coenzyme A synthetase,
cytoplasmic.
/FTId=PRO_0000208423.
NP_BIND 439 441 ATP. {ECO:0000250}.
NP_BIND 463 468 ATP. {ECO:0000250}.
REGION 219 222 Coenzyme A binding. {ECO:0000250}.
BINDING 363 363 Coenzyme A. {ECO:0000250}.
BINDING 552 552 ATP. {ECO:0000250}.
BINDING 567 567 ATP. {ECO:0000250}.
BINDING 575 575 Coenzyme A; via carbonyl oxygen.
{ECO:0000250}.
BINDING 636 636 Coenzyme A. {ECO:0000250}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 263 263 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QXG4}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QXG4}.
MOD_RES 267 267 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 418 418 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 277 277 V -> VQGKLKEKSKRVQP (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046376.
CONFLICT 79 79 F -> L (in Ref. 2; BAC03849).
{ECO:0000305}.
CONFLICT 615 615 V -> F (in Ref. 5; AAH12172).
{ECO:0000305}.
CONFLICT 680 680 M -> L (in Ref. 2; BAC03849).
{ECO:0000305}.
SEQUENCE 701 AA; 78580 MW; 833580B41B73A8B4 CRC64;
MGLPEERVRS GSGSRGQEEA GAGGRARSWS PPPEVSRSAH VPSLQRYREL HRRSVEEPRE
FWGDIAKEFY WKTPCPGPFL RYNFDVTKGK IFIEWMKGAT TNICYNVLDR NVHEKKLGDK
VAFYWEGNEP GETTQITYHQ LLVQVCQFSN VLRKQGIQKG DRVAIYMPMI PELVVAMLAC
ARIGALHSIV FAGFSSESLC ERILDSSCSL LITTDAFYRG EKLVNLKELA DEALQKCQEK
GFPVRCCIVV KHLGRAELGM GDSTSQSPPI KRSCPDVQIS WNQGIDLWWH ELMQEAGDEC
EPEWCDAEDP LFILYTSGST GKPKGVVHTV GGYMLYVATT FKYVFDFHAE DVFWCTADIG
WITGHSYVTY GPLANGATSV LFEGIPTYPD VNRLWSIVDK YKVTKFYTAP TAIRLLMKFG
DEPVTKHSRA SLQVLGTVGE PINPEAWLWY HRVVGAQRCP IVDTFWQTET GGHMLTPLPG
ATPMKPGSAT FPFFGVAPAI LNESGEELEG EAEGYLVFKQ PWPGIMRTVY GNHERFETTY
FKKFPGYYVT GDGCQRDQDG YYWITGRIDD MLNVSGHLLS TAEVESALVE HEAVAEAAVV
GHPHPVKGEC LYCFVTLCDG HTFSPKLTEE LKKQIREKIG PIATPDYIQN APGLPKTRSG
KIMRRVLRKI AQNDHDLGDM STVADPSVIS HLFSHRCLTI Q


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