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Protein

Acetyl-coenzyme A synthetase, cytoplasmic

Gene

Acss2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activates acetate so that it can be used for lipid synthesis or for energy generation.

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei363 – 3631Coenzyme ABy similarity
Binding sitei552 – 5521ATPBy similarity
Binding sitei567 – 5671ATPBy similarity
Binding sitei575 – 5751Coenzyme A; via carbonyl oxygenBy similarity
Binding sitei636 – 6361Coenzyme ABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi439 – 4413ATPBy similarity
Nucleotide bindingi463 – 4686ATPBy similarity

GO - Molecular functioni

  • acetate-CoA ligase activity Source: MGI
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-71384. Ethanol oxidation.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Acss2
Synonyms:Acas2, Acecs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1890410. Acss2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2924.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 701701Acetyl-coenzyme A synthetase, cytoplasmicPRO_0000208424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301PhosphoserineCombined sources
Modified residuei263 – 2631PhosphoserineCombined sources
Modified residuei265 – 2651PhosphoserineCombined sources
Modified residuei267 – 2671PhosphoserineCombined sources
Modified residuei418 – 4181N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9QXG4.
MaxQBiQ9QXG4.
PaxDbiQ9QXG4.
PRIDEiQ9QXG4.

PTM databases

iPTMnetiQ9QXG4.
PhosphoSiteiQ9QXG4.

Expressioni

Gene expression databases

BgeeiQ9QXG4.
CleanExiMM_ACSS2.
ExpressionAtlasiQ9QXG4. baseline and differential.
GenevisibleiQ9QXG4. MM.

Interactioni

Protein-protein interaction databases

DIPiDIP-61210N.
STRINGi10090.ENSMUSP00000029135.

Structurei

3D structure databases

ProteinModelPortaliQ9QXG4.
SMRiQ9QXG4. Positions 45-696.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni219 – 2224Coenzyme A bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229981.
HOVERGENiHBG014401.
InParanoidiQ9QXG4.
KOiK01895.
OrthoDBiEOG77T140.
TreeFamiTF300417.

Family and domain databases

InterProiIPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QXG4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLPEERRKS GSGSRAREET GAEGRVRGWS PPPEVRRSAH VPSLQRYREL
60 70 80 90 100
HRRSVEEPRE FWGNIAKEFY WKTACPGPFL QYNFDVTKGK IFTEWMKGAT
110 120 130 140 150
TNICYNVLDR NVHEKKLGDK VAFYWEGNEP GETTKITYRE LLVQVCQFSN
160 170 180 190 200
VLRKQGIQKG DRVAIYMPMI LELVVAMLAC ARLGALHSIV FAGFSAESLC
210 220 230 240 250
ERILDSSCCL LITTDAFYRG EKLVNLKELA DESLEKCREK GFPVRCCIVV
260 270 280 290 300
KHLGRAELGM NDSPSQSPPV KRPCPDVQIC WNEGVDLWWH ELMQQAGDEC
310 320 330 340 350
EPEWCDAEDP LFILYTSGST GKPKGVVHTI GGYMLYVATT FKYVFDFHPE
360 370 380 390 400
DVFWCTADIG WITGHSYVTY GPLANGATSV LFEGIPTYPD EGRLWSIVDK
410 420 430 440 450
YKVTKFYTAP TAIRMLMKFG DDPVTKHSRA SLQVLGTVGE PINPEAWLWY
460 470 480 490 500
HRVVGSQRCP IVDTFWQTET GGHMLTPLPG ATPMKPGSAS FPFFGVAPAI
510 520 530 540 550
LNESGEELEG EAEGYLVFKQ PWPGIMRTVY GNHTRFETTY FKKFPGYYVT
560 570 580 590 600
GDGCRRDQDG YYWITGRIDD MLNVSGHLLS TAEVESALVE HEAVAEAAVV
610 620 630 640 650
GHPHPVKGEC LYCFVTLCDG HTFSPTLTEE LKKQIREKIG PIATPDYIQN
660 670 680 690 700
APGLPKTRSG KIMRRVLRKI AQNDHDLGDT STVADPSVIN HLFSHRCLTT

Q
Length:701
Mass (Da):78,862
Last modified:July 27, 2011 - v2
Checksum:iD1EA6312CD4527D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti498 – 5003PAI → LQS in AAF24510 (PubMed:12049778).Curated
Sequence conflicti655 – 6573PKT → LKP in AAF24510 (PubMed:12049778).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216873 mRNA. Translation: AAF24510.1.
AK053877 mRNA. Translation: BAC35571.1.
AL844852 Genomic DNA. Translation: CAM18931.1.
BC051432 mRNA. Translation: AAH51432.1.
CCDSiCCDS16950.1.
RefSeqiNP_062785.2. NM_019811.3.
UniGeneiMm.255026.

Genome annotation databases

EnsembliENSMUST00000029135; ENSMUSP00000029135; ENSMUSG00000027605.
GeneIDi60525.
KEGGimmu:60525.
UCSCiuc008nku.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216873 mRNA. Translation: AAF24510.1.
AK053877 mRNA. Translation: BAC35571.1.
AL844852 Genomic DNA. Translation: CAM18931.1.
BC051432 mRNA. Translation: AAH51432.1.
CCDSiCCDS16950.1.
RefSeqiNP_062785.2. NM_019811.3.
UniGeneiMm.255026.

3D structure databases

ProteinModelPortaliQ9QXG4.
SMRiQ9QXG4. Positions 45-696.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61210N.
STRINGi10090.ENSMUSP00000029135.

Chemistry

ChEMBLiCHEMBL2924.

PTM databases

iPTMnetiQ9QXG4.
PhosphoSiteiQ9QXG4.

Proteomic databases

EPDiQ9QXG4.
MaxQBiQ9QXG4.
PaxDbiQ9QXG4.
PRIDEiQ9QXG4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029135; ENSMUSP00000029135; ENSMUSG00000027605.
GeneIDi60525.
KEGGimmu:60525.
UCSCiuc008nku.1. mouse.

Organism-specific databases

CTDi55902.
MGIiMGI:1890410. Acss2.

Phylogenomic databases

eggNOGiKOG1175. Eukaryota.
COG0365. LUCA.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229981.
HOVERGENiHBG014401.
InParanoidiQ9QXG4.
KOiK01895.
OrthoDBiEOG77T140.
TreeFamiTF300417.

Enzyme and pathway databases

ReactomeiR-MMU-71384. Ethanol oxidation.

Miscellaneous databases

ChiTaRSiAcss2. mouse.
NextBioi314949.
PROiQ9QXG4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXG4.
CleanExiMM_ACSS2.
ExpressionAtlasiQ9QXG4. baseline and differential.
GenevisibleiQ9QXG4. MM.

Family and domain databases

InterProiIPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of cytosolic acetyl-CoA synthetase gene is developmentally regulated."
    Loikkanen I., Haghighi S., Vainio S., Pajunen A.
    Mech. Dev. 115:139-141(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  5. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-263; SER-265 AND SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiACSA_MOUSE
AccessioniPrimary (citable) accession number: Q9QXG4
Secondary accession number(s): Q8BK97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: July 27, 2011
Last modified: March 16, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.