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Q9NUB1

- ACS2L_HUMAN

UniProt

Q9NUB1 - ACS2L_HUMAN

Protein

Acetyl-coenzyme A synthetase 2-like, mitochondrial

Gene

ACSS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (23 Apr 2003)
      Previous versions | rss
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    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
    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

    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

    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.2 Publications

    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 SIRT3.1 Publication

    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.
    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.
    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.

    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:
    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]
    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 ]
    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

    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: October 1, 2014
    This is version 121 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