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Q9NUB1

- ACS2L_HUMAN

UniProt

Q9NUB1 - ACS2L_HUMAN

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Protein

Acetyl-coenzyme A synthetase 2-like, mitochondrial

Gene
ACSS1, ACAS2L, KIAA1846
Organism
Homo sapiens (Human)
Status
Reviewed - 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 CO2.1 Publication

Catalytic activityi

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

Enzyme regulationi

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

GO - Molecular functioni

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

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: Chromosome 20

Organism-specific databases

HGNCiHGNC:16091. ACSS1.

Subcellular locationi

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.

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

ArrayExpressiQ9NUB1.
BgeeiQ9NUB1.
CleanExiHS_ACSS1.
GenevestigatoriQ9NUB1.

Organism-specific databases

HPAiHPA041014.
HPA043228.

Interactioni

Subunit structurei

Interacts with SIRT3.

Protein-protein interaction databases

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:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ9NUB1.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0365.
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. Align

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

MAARTLGRGV GRLLGSLRGL SGQPARPPCG VSAPRRAASG PSGSAPAVAA    50
AAAQPGSYPA LSAQAAREPA AFWGPLARDT LVWDTPYHTV WDCDFSTGKI 100
GWFLGGQLNV SVNCLDQHVR KSPESVALIW ERDEPGTEVR ITYRELLETT 150
CRLANTLKRH GVHRGDRVAI YMPVSPLAVA AMLACARIGA VHTVIFAGFS 200
AESLAGRIND AKCKVVITFN QGLRGGRVVE LKKIVDEAVK HCPTVQHVLV 250
AHRTDNKVHM GDLDVPLEQE MAKEDPVCAP ESMGSEDMLF MLYTSGSTGM 300
PKGIVHTQAG YLLYAALTHK LVFDHQPGDI FGCVADIGWI TGHSYVVYGP 350
LCNGATSVLF ESTPVYPNAG RYWETVERLK INQFYGAPTA VRLLLKYGDA 400
WVKKYDRSSL RTLGSVGEPI NCEAWEWLHR VVGDSRCTLV DTWWQTETGG 450
ICIAPRPSEE GAEILPAMAM RPFFGIVPVL MDEKGSVVEG SNVSGALCIS 500
QAWPGMARTI YGDHQRFVDA YFKAYPGYYF TGDGAYRTEG GYYQITGRMD 550
DVINISGHRL GTAEIEDAIA DHPAVPESAV IGYPHDIKGE AAFAFIVVKD 600
SAGDSDVVVQ ELKSMVATKI AKYAVPDEIL VVKRLPKTRS GKVMRRLLRK 650
IITSEAQELG DTTTLEDPSI IAEILSVYQK CKDKQAAAK 689
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 BAC03853.1 differs from that shown. Reason: Sequencing errors.
The sequence BAC03853.1 differs from that shown. Reason: Frameshift at position 250.
The sequence BAB55390.1 differs from that shown. Reason: Erroneous initiation.

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. VSP_044693Add
BLAST
Alternative sequencei23 – 143121Missing in isoform 3. VSP_044694Add
BLAST
Alternative sequencei446 – 4472Missing in isoform 2. VSP_007249
Alternative sequencei556 – 57520SGHRL…DHPAV → LQIVGFFREAIRNSGDLLEH in isoform 4. VSP_045546Add
BLAST
Alternative sequencei576 – 689114Missing in isoform 4. VSP_045547Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2331K → I in BAG54524. 1 Publication
Sequence conflicti277 – 2771V → M in AAH39261. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000542618; ENSP00000437657; ENSG00000154930. [Q9NUB1-3]
GeneIDi84532.
KEGGihsa:84532.
UCSCiuc002wub.3. human. [Q9NUB1-1]
uc002wuc.3. human. [Q9NUB1-2]

Polymorphism databases

DMDMi30172968.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS13167.1. [Q9NUB1-1 ]
CCDS58764.1. [Q9NUB1-3 ]
CCDS58765.1. [Q9NUB1-4 ]
RefSeqi NP_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 ]
UniGenei Hs.529353.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GLR X-ray 1.80 B 638-649 [» ]
3GLT X-ray 2.10 B 638-649 [» ]
3GLU X-ray 2.50 B 638-649 [» ]
4BVE X-ray 2.05 B 638-647 [» ]
4BVF X-ray 2.70 B 638-647 [» ]
4BVG X-ray 2.50 B 638-647 [» ]
4C78 X-ray 2.00 C 638-647 [» ]
ProteinModelPortali Q9NUB1.
SMRi Q9NUB1. Positions 55-679.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000316924.

Chemistry

DrugBanki DB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.

PTM databases

PhosphoSitei Q9NUB1.

Polymorphism databases

DMDMi 30172968.

Proteomic databases

MaxQBi Q9NUB1.
PaxDbi Q9NUB1.
PRIDEi Q9NUB1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000323482 ; ENSP00000316924 ; ENSG00000154930 . [Q9NUB1-1 ]
ENST00000432802 ; ENSP00000388793 ; ENSG00000154930 . [Q9NUB1-4 ]
ENST00000542618 ; ENSP00000437657 ; ENSG00000154930 . [Q9NUB1-3 ]
GeneIDi 84532.
KEGGi hsa:84532.
UCSCi uc002wub.3. human. [Q9NUB1-1 ]
uc002wuc.3. human. [Q9NUB1-2 ]

Organism-specific databases

CTDi 84532.
GeneCardsi GC20M024986.
H-InvDB HIX0015699.
HGNCi HGNC:16091. ACSS1.
HPAi HPA041014.
HPA043228.
MIMi 614355. gene.
neXtProti NX_Q9NUB1.
PharmGKBi PA24430.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0365.
HOVERGENi HBG014401.
InParanoidi Q9NUB1.
KOi K01895.
OMAi TEGGYYQ.
OrthoDBi EOG77T140.
PhylomeDBi Q9NUB1.
TreeFami TF354241.

Enzyme and pathway databases

BRENDAi 6.2.1.1. 2681.
Reactomei REACT_34. Ethanol oxidation.

Miscellaneous databases

ChiTaRSi ACSS1. human.
EvolutionaryTracei Q9NUB1.
GenomeRNAii 84532.
NextBioi 74375.
PROi Q9NUB1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NUB1.
Bgeei Q9NUB1.
CleanExi HS_ACSS1.
Genevestigatori Q9NUB1.

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. "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: September 3, 2014
This is version 120 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

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