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Protein

Acetyl-coenzyme A synthetase 2-like, mitochondrial

Gene

ACSS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important for maintaining normal body temperature during fasting and for energy homeostasis. Essential for energy expenditure under ketogenic conditions (By similarity). Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO2.By similarity1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by acetylation at Lys-642 and activated by deacetylation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei341 – 3411Coenzyme ABy similarity
Binding sitei533 – 5331ATPBy similarity
Binding sitei548 – 5481ATPBy similarity
Binding sitei556 – 5561Coenzyme A; via carbonyl oxygenBy similarity
Binding sitei559 – 5591ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi417 – 4193ATPBy similarity
Nucleotide bindingi441 – 4466ATPBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. acetate biosynthetic process Source: Ensembl
  2. acetyl-CoA biosynthetic process Source: UniProtKB
  3. acetyl-CoA biosynthetic process from acetate Source: InterPro
  4. ethanol oxidation Source: Reactome
  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

BRENDAi6.2.1.1. 2681.
ReactomeiREACT_34. Ethanol oxidation.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase 2-like, mitochondrial (EC:6.2.1.1)
Alternative name(s):
Acetate--CoA ligase 2
Acetyl-CoA synthetase 2
Short name:
AceCS2
Acyl-CoA synthetase short-chain family member 1
Gene namesi
Name:ACSS1
Synonyms:ACAS2L, KIAA1846
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16091. ACSS1.

Subcellular locationi

  1. Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi642 – 6421K → Q: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA24430.

Chemistry

DrugBankiDB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.

Polymorphism and mutation databases

BioMutaiACSS1.
DMDMi30172968.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737Mitochondrion1 PublicationAdd
BLAST
Chaini38 – 689652Acetyl-coenzyme A synthetase 2-like, mitochondrialPRO_0000000596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei396 – 3961N6-acetyllysine1 Publication
Modified residuei642 – 6421N6-acetyllysine1 Publication

Post-translational modificationi

Reversibly acetylated on Lys-642. The acetyl-CoA synthase activity is inhibited by acetylation and activated by deacetylation.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NUB1.
PaxDbiQ9NUB1.
PRIDEiQ9NUB1.

PTM databases

PhosphoSiteiQ9NUB1.

Expressioni

Gene expression databases

BgeeiQ9NUB1.
CleanExiHS_ACSS1.
ExpressionAtlasiQ9NUB1. baseline and differential.
GenevestigatoriQ9NUB1.

Organism-specific databases

HPAiHPA041014.
HPA043228.

Interactioni

Subunit structurei

Interacts with SIRT3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
VAC14Q08AM63EBI-10313831,EBI-2107455

Protein-protein interaction databases

BioGridi124122. 3 interactions.
DIPiDIP-61208N.
IntActiQ9NUB1. 1 interaction.
STRINGi9606.ENSP00000316924.

Structurei

Secondary structure

1
689
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi643 – 6453

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GLRX-ray1.80B638-649[»]
3GLTX-ray2.10B638-649[»]
3GLUX-ray2.50B638-649[»]
4BVEX-ray2.05B638-647[»]
4BVFX-ray2.70B638-647[»]
4BVGX-ray2.50B638-647[»]
4C78X-ray2.00C638-647[»]
ProteinModelPortaliQ9NUB1.
SMRiQ9NUB1. Positions 55-679.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NUB1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni224 – 2274Coenzyme A bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi45 – 539Poly-Ala

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOVERGENiHBG014401.
InParanoidiQ9NUB1.
KOiK01895.
OMAiTEGGYYQ.
OrthoDBiEOG77T140.
PhylomeDBiQ9NUB1.
TreeFamiTF354241.

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 (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NUB1-1) [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
MAARTLGRGV GRLLGSLRGL SGQPARPPCG VSAPRRAASG PSGSAPAVAA
60 70 80 90 100
AAAQPGSYPA LSAQAAREPA AFWGPLARDT LVWDTPYHTV WDCDFSTGKI
110 120 130 140 150
GWFLGGQLNV SVNCLDQHVR KSPESVALIW ERDEPGTEVR ITYRELLETT
160 170 180 190 200
CRLANTLKRH GVHRGDRVAI YMPVSPLAVA AMLACARIGA VHTVIFAGFS
210 220 230 240 250
AESLAGRIND AKCKVVITFN QGLRGGRVVE LKKIVDEAVK HCPTVQHVLV
260 270 280 290 300
AHRTDNKVHM GDLDVPLEQE MAKEDPVCAP ESMGSEDMLF MLYTSGSTGM
310 320 330 340 350
PKGIVHTQAG YLLYAALTHK LVFDHQPGDI FGCVADIGWI TGHSYVVYGP
360 370 380 390 400
LCNGATSVLF ESTPVYPNAG RYWETVERLK INQFYGAPTA VRLLLKYGDA
410 420 430 440 450
WVKKYDRSSL RTLGSVGEPI NCEAWEWLHR VVGDSRCTLV DTWWQTETGG
460 470 480 490 500
ICIAPRPSEE GAEILPAMAM RPFFGIVPVL MDEKGSVVEG SNVSGALCIS
510 520 530 540 550
QAWPGMARTI YGDHQRFVDA YFKAYPGYYF TGDGAYRTEG GYYQITGRMD
560 570 580 590 600
DVINISGHRL GTAEIEDAIA DHPAVPESAV IGYPHDIKGE AAFAFIVVKD
610 620 630 640 650
SAGDSDVVVQ ELKSMVATKI AKYAVPDEIL VVKRLPKTRS GKVMRRLLRK
660 670 680
IITSEAQELG DTTTLEDPSI IAEILSVYQK CKDKQAAAK
Length:689
Mass (Da):74,857
Last modified:April 23, 2003 - v2
Checksum:i66E84E39302AD08B
GO
Isoform 2 (identifier: Q9NUB1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     446-447: Missing.

Note: No experimental confirmation available.

Show »
Length:687
Mass (Da):74,627
Checksum:i99888770D7E10BA4
GO
Isoform 3 (identifier: Q9NUB1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MAARTLGRGVGRLLGSLRGLSG → MRRRKERQPWDRFHFLHFAPHG
     23-143: Missing.

Note: No experimental confirmation available.

Show »
Length:568
Mass (Da):62,722
Checksum:i061B9CF91C387B3F
GO
Isoform 4 (identifier: Q9NUB1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     556-575: SGHRLGTAEIEDAIADHPAV → LQIVGFFREAIRNSGDLLEH
     576-689: Missing.

Note: No experimental confirmation available.

Show »
Length:575
Mass (Da):62,688
Checksum:i4D419E89EB8DF015
GO

Sequence cautioni

The sequence BAB55390.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC03853.1 differs from that shown.Sequencing errors.Curated
The sequence BAC03853.1 differs from that shown. Reason: Frameshift at position 250. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2331K → I in BAG54524 (PubMed:14702039).Curated
Sequence conflicti277 – 2771V → M in AAH39261 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti488 – 4881V → M.2 Publications
Corresponds to variant rs6050249 [ dbSNP | Ensembl ].
VAR_048184

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2222MAART…RGLSG → MRRRKERQPWDRFHFLHFAP HG in isoform 3. 1 PublicationVSP_044693Add
BLAST
Alternative sequencei23 – 143121Missing in isoform 3. 1 PublicationVSP_044694Add
BLAST
Alternative sequencei446 – 4472Missing in isoform 2. 1 PublicationVSP_007249
Alternative sequencei556 – 57520SGHRL…DHPAV → LQIVGFFREAIRNSGDLLEH in isoform 4. 1 PublicationVSP_045546Add
BLAST
Alternative sequencei576 – 689114Missing in isoform 4. 1 PublicationVSP_045547Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027817 mRNA. Translation: BAB55390.1. Different initiation.
AK092295 mRNA. Translation: BAC03853.1. Sequence problems.
AK127566 mRNA. Translation: BAG54524.1.
AK296306 mRNA. Translation: BAG59005.1.
AL035661, AL080312 Genomic DNA. Translation: CAI21828.1.
AL080312, AL035661 Genomic DNA. Translation: CAI18917.1.
CH471133 Genomic DNA. Translation: EAX10106.1.
CH471133 Genomic DNA. Translation: EAX10109.1.
BC039261 mRNA. Translation: AAH39261.1.
BC044588 mRNA. Translation: AAH44588.1.
AB058749 mRNA. Translation: BAB47475.1.
CCDSiCCDS13167.1. [Q9NUB1-1]
CCDS58764.1. [Q9NUB1-3]
CCDS58765.1. [Q9NUB1-4]
RefSeqiNP_001239604.1. NM_001252675.1. [Q9NUB1-2]
NP_001239605.1. NM_001252676.1. [Q9NUB1-3]
NP_001239606.1. NM_001252677.1. [Q9NUB1-4]
NP_115890.2. NM_032501.3. [Q9NUB1-1]
UniGeneiHs.529353.

Genome annotation databases

EnsembliENST00000323482; ENSP00000316924; ENSG00000154930. [Q9NUB1-1]
ENST00000432802; ENSP00000388793; ENSG00000154930. [Q9NUB1-4]
ENST00000537502; ENSP00000439304; ENSG00000154930. [Q9NUB1-3]
GeneIDi84532.
KEGGihsa:84532.
UCSCiuc002wub.3. human. [Q9NUB1-1]
uc002wuc.3. human. [Q9NUB1-2]

Polymorphism and mutation databases

BioMutaiACSS1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027817 mRNA. Translation: BAB55390.1. Different initiation.
AK092295 mRNA. Translation: BAC03853.1. Sequence problems.
AK127566 mRNA. Translation: BAG54524.1.
AK296306 mRNA. Translation: BAG59005.1.
AL035661, AL080312 Genomic DNA. Translation: CAI21828.1.
AL080312, AL035661 Genomic DNA. Translation: CAI18917.1.
CH471133 Genomic DNA. Translation: EAX10106.1.
CH471133 Genomic DNA. Translation: EAX10109.1.
BC039261 mRNA. Translation: AAH39261.1.
BC044588 mRNA. Translation: AAH44588.1.
AB058749 mRNA. Translation: BAB47475.1.
CCDSiCCDS13167.1. [Q9NUB1-1]
CCDS58764.1. [Q9NUB1-3]
CCDS58765.1. [Q9NUB1-4]
RefSeqiNP_001239604.1. NM_001252675.1. [Q9NUB1-2]
NP_001239605.1. NM_001252676.1. [Q9NUB1-3]
NP_001239606.1. NM_001252677.1. [Q9NUB1-4]
NP_115890.2. NM_032501.3. [Q9NUB1-1]
UniGeneiHs.529353.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GLRX-ray1.80B638-649[»]
3GLTX-ray2.10B638-649[»]
3GLUX-ray2.50B638-649[»]
4BVEX-ray2.05B638-647[»]
4BVFX-ray2.70B638-647[»]
4BVGX-ray2.50B638-647[»]
4C78X-ray2.00C638-647[»]
ProteinModelPortaliQ9NUB1.
SMRiQ9NUB1. Positions 55-679.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124122. 3 interactions.
DIPiDIP-61208N.
IntActiQ9NUB1. 1 interaction.
STRINGi9606.ENSP00000316924.

Chemistry

DrugBankiDB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.

PTM databases

PhosphoSiteiQ9NUB1.

Polymorphism and mutation databases

BioMutaiACSS1.
DMDMi30172968.

Proteomic databases

MaxQBiQ9NUB1.
PaxDbiQ9NUB1.
PRIDEiQ9NUB1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323482; ENSP00000316924; ENSG00000154930. [Q9NUB1-1]
ENST00000432802; ENSP00000388793; ENSG00000154930. [Q9NUB1-4]
ENST00000537502; ENSP00000439304; ENSG00000154930. [Q9NUB1-3]
GeneIDi84532.
KEGGihsa:84532.
UCSCiuc002wub.3. human. [Q9NUB1-1]
uc002wuc.3. human. [Q9NUB1-2]

Organism-specific databases

CTDi84532.
GeneCardsiGC20M024986.
H-InvDBHIX0015699.
HGNCiHGNC:16091. ACSS1.
HPAiHPA041014.
HPA043228.
MIMi614355. gene.
neXtProtiNX_Q9NUB1.
PharmGKBiPA24430.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOVERGENiHBG014401.
InParanoidiQ9NUB1.
KOiK01895.
OMAiTEGGYYQ.
OrthoDBiEOG77T140.
PhylomeDBiQ9NUB1.
TreeFamiTF354241.

Enzyme and pathway databases

BRENDAi6.2.1.1. 2681.
ReactomeiREACT_34. Ethanol oxidation.

Miscellaneous databases

ChiTaRSiACSS1. human.
EvolutionaryTraceiQ9NUB1.
GenomeRNAii84532.
NextBioi74375.
PROiQ9NUB1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NUB1.
CleanExiHS_ACSS1.
ExpressionAtlasiQ9NUB1. baseline and differential.
GenevestigatoriQ9NUB1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-689 (ISOFORM 1), VARIANT MET-488.
    Tissue: Placenta, Thalamus and Tongue.
  2. "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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 2), VARIANT MET-488.
    Tissue: Brain and Testis.
  5. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 336-689 (ISOFORM 1).
    Tissue: Brain.
  6. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  7. "Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2."
    Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., Verdin E.
    Proc. Natl. Acad. Sci. U.S.A. 103:10224-10229(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-642, MUTAGENESIS OF LYS-642, FUNCTION, ENZYME REGULATION, PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  8. "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-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structures of human SIRT3 displaying substrate-induced conformational changes."
    Jin L., Wei W., Jiang Y., Peng H., Cai J., Mao C., Dai H., Choy W., Bemis J.E., Jirousek M.R., Milne J.C., Westphal C.H., Perni R.B.
    J. Biol. Chem. 284:24394-24405(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 638-649 IN COMPLEX WITH SIRT3.

Entry informationi

Entry nameiACS2L_HUMAN
AccessioniPrimary (citable) accession number: Q9NUB1
Secondary accession number(s): B3KXL2
, B4DJZ3, D3DW48, F5H6F4, F8W7Y1, Q5TF42, Q8IV99, Q8N234, Q96JI1, Q96JX6, Q9NU28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: April 29, 2015
This is version 126 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.