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Q9NR19

- ACSA_HUMAN

UniProt

Q9NR19 - ACSA_HUMAN

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Protein

Acetyl-coenzyme A synthetase, cytoplasmic

Gene

ACSS2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. acetate-CoA ligase activity Source: UniProtKB
  2. AMP binding Source: UniProtKB
  3. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. acetate biosynthetic process Source: Ensembl
  2. acetyl-CoA biosynthetic process from acetate Source: InterPro
  3. ethanol oxidation Source: Reactome
  4. lipid biosynthetic process Source: UniProtKB
  5. propionate biosynthetic process Source: Ensembl
  6. small molecule metabolic process Source: Reactome
  7. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05484-MONOMER.
BRENDAi6.2.1.1. 2681.
ReactomeiREACT_34. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:15814. ACSS2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. intracellular membrane-bounded organelle Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24429.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 701701Acetyl-coenzyme A synthetase, cytoplasmicPRO_0000208423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301Phosphoserine1 Publication
Modified residuei263 – 2631PhosphoserineBy similarity
Modified residuei267 – 2671Phosphoserine2 Publications
Modified residuei418 – 4181N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NR19.
PaxDbiQ9NR19.
PRIDEiQ9NR19.

PTM databases

PhosphoSiteiQ9NR19.

Expressioni

Gene expression databases

BgeeiQ9NR19.
CleanExiHS_ACSS2.
ExpressionAtlasiQ9NR19. baseline and differential.
GenevestigatoriQ9NR19.

Organism-specific databases

HPAiHPA004141.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
UPF1Q929001EBI-372879,EBI-373471

Protein-protein interaction databases

BioGridi120989. 2 interactions.
IntActiQ9NR19. 3 interactions.
STRINGi9606.ENSP00000353804.

Structurei

3D structure databases

ProteinModelPortaliQ9NR19.
SMRiQ9NR19. Positions 45-696.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229981.
HOVERGENiHBG014401.
InParanoidiQ9NR19.
KOiK01895.
OMAiAWIWYRD.
OrthoDBiEOG77T140.
PhylomeDBiQ9NR19.
TreeFamiTF300417.

Family and domain databases

InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NR19-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGLPEERVRS GSGSRGQEEA GAGGRARSWS PPPEVSRSAH VPSLQRYREL
60 70 80 90 100
HRRSVEEPRE FWGDIAKEFY WKTPCPGPFL RYNFDVTKGK IFIEWMKGAT
110 120 130 140 150
TNICYNVLDR NVHEKKLGDK VAFYWEGNEP GETTQITYHQ LLVQVCQFSN
160 170 180 190 200
VLRKQGIQKG DRVAIYMPMI PELVVAMLAC ARIGALHSIV FAGFSSESLC
210 220 230 240 250
ERILDSSCSL LITTDAFYRG EKLVNLKELA DEALQKCQEK GFPVRCCIVV
260 270 280 290 300
KHLGRAELGM GDSTSQSPPI KRSCPDVQIS WNQGIDLWWH ELMQEAGDEC
310 320 330 340 350
EPEWCDAEDP LFILYTSGST GKPKGVVHTV GGYMLYVATT FKYVFDFHAE
360 370 380 390 400
DVFWCTADIG WITGHSYVTY GPLANGATSV LFEGIPTYPD VNRLWSIVDK
410 420 430 440 450
YKVTKFYTAP TAIRLLMKFG DEPVTKHSRA SLQVLGTVGE PINPEAWLWY
460 470 480 490 500
HRVVGAQRCP IVDTFWQTET GGHMLTPLPG ATPMKPGSAT FPFFGVAPAI
510 520 530 540 550
LNESGEELEG EAEGYLVFKQ PWPGIMRTVY GNHERFETTY FKKFPGYYVT
560 570 580 590 600
GDGCQRDQDG YYWITGRIDD MLNVSGHLLS TAEVESALVE HEAVAEAAVV
610 620 630 640 650
GHPHPVKGEC LYCFVTLCDG HTFSPKLTEE LKKQIREKIG PIATPDYIQN
660 670 680 690 700
APGLPKTRSG KIMRRVLRKI AQNDHDLGDM STVADPSVIS HLFSHRCLTI

Q
Length:701
Mass (Da):78,580
Last modified:October 1, 2000 - v1
Checksum:i833580B41B73A8B4
GO
Isoform 2 (identifier: Q9NR19-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:714
Mass (Da):80,087
Checksum:i820E84E62A72E214
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791F → L in BAC03849. (PubMed:14702039)Curated
Sequence conflicti615 – 6151V → F in AAH12172. (PubMed:15489334)Curated
Sequence conflicti680 – 6801M → L in BAC03849. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei277 – 2771V → VQGKLKEKSKRVQP in isoform 2. 1 PublicationVSP_046376

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13243.1. [Q9NR19-1]
CCDS42868.2. [Q9NR19-2]
RefSeqiNP_001070020.2. NM_001076552.2. [Q9NR19-2]
NP_061147.1. NM_018677.3. [Q9NR19-1]
UniGeneiHs.517034.

Genome annotation databases

EnsembliENST00000253382; ENSP00000253382; ENSG00000131069. [Q9NR19-2]
ENST00000360596; ENSP00000353804; ENSG00000131069. [Q9NR19-1]
GeneIDi55902.
KEGGihsa:55902.
UCSCiuc002xbc.2. human. [Q9NR19-1]
uc010gey.2. human.

Polymorphism databases

DMDMi20137525.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS13243.1. [Q9NR19-1 ]
CCDS42868.2. [Q9NR19-2 ]
RefSeqi NP_001070020.2. NM_001076552.2. [Q9NR19-2 ]
NP_061147.1. NM_018677.3. [Q9NR19-1 ]
UniGenei Hs.517034.

3D structure databases

ProteinModelPortali Q9NR19.
SMRi Q9NR19. Positions 45-696.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120989. 2 interactions.
IntActi Q9NR19. 3 interactions.
STRINGi 9606.ENSP00000353804.

Chemistry

DrugBanki DB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.

PTM databases

PhosphoSitei Q9NR19.

Polymorphism databases

DMDMi 20137525.

Proteomic databases

MaxQBi Q9NR19.
PaxDbi Q9NR19.
PRIDEi Q9NR19.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253382 ; ENSP00000253382 ; ENSG00000131069 . [Q9NR19-2 ]
ENST00000360596 ; ENSP00000353804 ; ENSG00000131069 . [Q9NR19-1 ]
GeneIDi 55902.
KEGGi hsa:55902.
UCSCi uc002xbc.2. human. [Q9NR19-1 ]
uc010gey.2. human.

Organism-specific databases

CTDi 55902.
GeneCardsi GC20P033459.
HGNCi HGNC:15814. ACSS2.
HPAi HPA004141.
MIMi 605832. gene.
neXtProti NX_Q9NR19.
PharmGKBi PA24429.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0365.
GeneTreei ENSGT00760000119178.
HOGENOMi HOG000229981.
HOVERGENi HBG014401.
InParanoidi Q9NR19.
KOi K01895.
OMAi AWIWYRD.
OrthoDBi EOG77T140.
PhylomeDBi Q9NR19.
TreeFami TF300417.

Enzyme and pathway databases

BioCyci MetaCyc:HS05484-MONOMER.
BRENDAi 6.2.1.1. 2681.
Reactomei REACT_34. Ethanol oxidation.

Miscellaneous databases

ChiTaRSi ACSS2. human.
GeneWikii ACSS2.
GenomeRNAii 55902.
NextBioi 61271.
PROi Q9NR19.
SOURCEi Search...

Gene expression databases

Bgeei Q9NR19.
CleanExi HS_ACSS2.
ExpressionAtlasi Q9NR19. baseline and differential.
Genevestigatori Q9NR19.

Family and domain databases

InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  7. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACSA_HUMAN
AccessioniPrimary (citable) accession number: Q9NR19
Secondary accession number(s): A6NE90
, Q5QPH2, Q5QPH3, Q8N238, Q96EL0, Q9NQP7, Q9UJ15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3