Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NR19 (ACSA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length701 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UPF1Q929001EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 701701Acetyl-coenzyme A synthetase, cytoplasmic
PRO_0000208423

Amino acid modifications

Modified residue301Phosphoserine Ref.7
Modified residue2631Phosphoserine By similarity
Modified residue2671Phosphoserine Ref.7 Ref.10
Modified residue4181N6-acetyllysine Ref.9

Natural variations

Alternative sequence2771V → VQGKLKEKSKRVQP in isoform 2.
VSP_046376

Experimental info

Sequence conflict791F → L in BAC03849. Ref.2
Sequence conflict6151V → F in AAH12172. Ref.5
Sequence conflict6801M → L in BAC03849. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 833580B41B73A8B4

FASTA70178,580
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 820E84E62A72E214
Show »

FASTA71480,087

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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.
CCDSCCDS13243.1. [Q9NR19-1]
CCDS42868.2. [Q9NR19-2]
RefSeqNP_001070020.2. NM_001076552.2. [Q9NR19-2]
NP_061147.1. NM_018677.3. [Q9NR19-1]
UniGeneHs.517034.

3D structure databases

ProteinModelPortalQ9NR19.
SMRQ9NR19. Positions 45-696.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120989. 2 interactions.
IntActQ9NR19. 3 interactions.
STRING9606.ENSP00000353804.

Chemistry

DrugBankDB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.

PTM databases

PhosphoSiteQ9NR19.

Polymorphism databases

DMDM20137525.

Proteomic databases

MaxQBQ9NR19.
PaxDbQ9NR19.
PRIDEQ9NR19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253382; ENSP00000253382; ENSG00000131069. [Q9NR19-2]
ENST00000360596; ENSP00000353804; ENSG00000131069. [Q9NR19-1]
GeneID55902.
KEGGhsa:55902.
UCSCuc002xbc.2. human. [Q9NR19-1]
uc010gey.2. human.

Organism-specific databases

CTD55902.
GeneCardsGC20P033459.
HGNCHGNC:15814. ACSS2.
HPAHPA004141.
MIM605832. gene.
neXtProtNX_Q9NR19.
PharmGKBPA24429.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
HOVERGENHBG014401.
KOK01895.
OMAAWIWYRD.
OrthoDBEOG77T140.
PhylomeDBQ9NR19.
TreeFamTF300417.

Enzyme and pathway databases

BioCycMetaCyc:HS05484-MONOMER.
BRENDA6.2.1.1. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9NR19.
BgeeQ9NR19.
CleanExHS_ACSS2.
GenevestigatorQ9NR19.

Family and domain databases

InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiACSS2.
GenomeRNAi55902.
NextBio61271.
PROQ9NR19.
SOURCESearch...

Entry information

Entry nameACSA_HUMAN
AccessionPrimary (citable) accession number: Q9NR19
Secondary accession number(s): A6NE90 expand/collapse secondary AC list , Q5QPH2, Q5QPH3, Q8N238, Q96EL0, Q9NQP7, Q9UJ15
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM