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UniProtKB/Swiss-Prot entry Q9NR19


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACSA_HUMAN
Primary accession number Q9NR19
Secondary accession numbers Q5QPH2 Q96EL0 Q9NQP7 Q9UJ15
Integrated into Swiss-Prot on April 3, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 64)
Name and origin of the protein
Protein name Acetyl-coenzyme A synthetase, cytoplasmic
Synonyms EC 6.2.1.1
Acetate--CoA ligase
Acyl-activating enzyme
Acetyl-CoA synthetase
AceCS
ACS
Acyl-CoA synthetase short-chain family member 2
Gene name
Name: ACSS2
Synonyms: ACAS2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
DOI=10.1074/jbc.M004160200; PubMed=10843999 [NCBI, ExPASy, EBI, Israel, Japan]
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 GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-267, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF263614; AAF75064.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049709; CAI19726.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133324; CAI19726.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133324; CAI19312.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049709; CAI19312.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012172; AAH12172.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_061147.1; -.
UniGene Hs.517034
3D structure databases
HSSP Q8ZKF6; 1PG4. [HSSP ENTRY / PDB]
ModBase Q9NR19.
Protein-protein interaction databases
IntAct Q9NR19; -.
PTM databases
PhosphoSite Q9NR19; -.
Enzyme and pathway databases
BioCyc MetaCyc:ENSG00000131069-MON; -.
Reactome REACT_2063; Metabolism of xenobiotics.
Organism-specific databases
H-InvDB HIX0015754; -.
HGNC HGNC:15814; ACSS2.
GenAtlas ACSS2.
HPA HPA004141; -.
MIM 605832; gene. [NCBI / EBI]
PharmGKB PA24429; -.
GeneCards Q9NR19.
Gene expression databases
ArrayExpress Q9NR19; -.
CleanEx HS_ACSS2; -.
GermOnline ENSG00000131069; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0003987; Molecular function: acetate-CoA ligase activity (inferred from direct assay from UniProtKB).
GO:0016208; Molecular function: AMP binding (inferred by curator from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008610; Biological process: lipid biosynthetic process (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011904; Ac_CoA_lig_AcsA.
IPR000873; AMP-dep_Synth/Lig.
Graphical view of domain structure.
Pfam PF00501; AMP-binding; 1.
Pfam graphical view of domain structure.
PRINTS PR00154; AMPBINDING.
TIGRFAMs TIGR02188; Ac_CoA_lig_AcsA; 1.
PROSITE PS00455; AMP_BINDING; 1.
ProtoNet Q9NR19.
Genome annotation databases
Ensembl ENSG00000131069; Homo sapiens. [Contig view]
GeneID 55902; -.
Phylogenomic databases
HOVERGEN Q9NR19; -.
Other
DrugBank DB00131; Adenosine monophosphate.
DB00171; Adenosine triphosphate.
NextBio 61271; -.
SOURCE ACSS2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Ligase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   701  701     Acetyl-coenzyme A synthetase, cytoplasmic. PRO_0000208423
MOD_RES   30    30        Phosphoserine. 
MOD_RES   263   263        Phosphoserine (By similarity). 
MOD_RES   267   267        Phosphoserine. 
CONFLICT   615   615        V -> F (in Ref. 3; AAH12172). 
Sequence information
Length: 701 AA [This is the length of the unprocessed precursor] Molecular weight: 78580 Da [This is the MW of the unprocessed precursor] CRC64: 833580B41B73A8B4 [This is a checksum on the sequence]
        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 

Q9NR19 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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