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Protein

Long-chain-fatty-acid--CoA ligase 5

Gene

ACSL5

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

Functioni

Acyl-CoA synthetases (ACSL) activate long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity). Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity). It was suggested that it may also stimulate fatty acid oxidation (By similarity). At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL. May have a role in the survival of glioma cells.By similarity3 Publications

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Cofactori

Mg2+By similarity

Kineticsi

  1. KM=0.11 µM for palmitic acid (isoform 1 at pH 7.5)1 Publication
  2. KM=0.38 µM for palmitic acid (isoform 1 at pH 9.5)1 Publication
  3. KM=0.04 µM for palmitic acid (isoform 3 at pH 7.5)1 Publication
  4. KM=0.15 µM for palmitic acid (isoform 3 at pH 8.5)1 Publication

    pH dependencei

    Optimum pH is 9.5 (isoform 1), 7.5-8.5 (isoform 3).1 Publication

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • long-chain fatty acid-CoA ligase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01349-MONOMER.
    ReactomeiREACT_380. Synthesis of very long-chain fatty acyl-CoAs.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase 5 (EC:6.2.1.3)
    Alternative name(s):
    Long-chain acyl-CoA synthetase 5
    Short name:
    LACS 5
    Gene namesi
    Name:ACSL5
    Synonyms:ACS5, FACL5
    ORF Names:UNQ633/PRO1250
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:16526. ACSL5.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei12 – 3221Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
    BLAST
    Topological domaini33 – 683651CytoplasmicSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • endoplasmic reticulum Source: UniProtKB
    • endoplasmic reticulum membrane Source: Reactome
    • integral component of membrane Source: UniProtKB-KW
    • membrane Source: UniProtKB
    • mitochondrial inner membrane Source: Ensembl
    • mitochondrial outer membrane Source: UniProtKB-SubCell
    • mitochondrion Source: UniProtKB
    • nucleolus Source: HPA
    • nucleus Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27969.

    Polymorphism and mutation databases

    BioMutaiACSL5.
    DMDMi13431659.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 683683Long-chain-fatty-acid--CoA ligase 5PRO_0000193112Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei361 – 3611N6-acetyllysineBy similarity
    Isoform 2 (identifier: Q9ULC5-3)
    Modified residuei32 – 321Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9ULC5.
    PaxDbiQ9ULC5.
    PRIDEiQ9ULC5.

    PTM databases

    PhosphoSiteiQ9ULC5.

    Expressioni

    Gene expression databases

    BgeeiQ9ULC5.
    CleanExiHS_ACSL5.
    GenevisibleiQ9ULC5. HS.

    Organism-specific databases

    HPAiCAB062546.
    HPA007162.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9ULC5. 3 interactions.
    STRINGi9606.ENSP00000348429.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ULC5.
    SMRiQ9ULC5. Positions 104-620.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1022.
    GeneTreeiENSGT00690000101725.
    HOGENOMiHOG000159459.
    HOVERGENiHBG050452.
    InParanoidiQ9ULC5.
    KOiK01897.
    OMAiQENKCLT.
    OrthoDBiEOG71CFKN.
    PhylomeDBiQ9ULC5.
    TreeFamiTF313877.

    Family and domain databases

    InterProiIPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9ULC5-1) [UniParc]FASTAAdd to basket

    Also known as: ACSL5b, ACSL5-fl

    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
    MLFIFNFLFS PLPTPALICI LTFGAAIFLW LITRPQPVLP LLDLNNQSVG
    60 70 80 90 100
    IEGGARKGVS QKNNDLTSCC FSDAKTMYEV FQRGLAVSDN GPCLGYRKPN
    110 120 130 140 150
    QPYRWLSYKQ VSDRAEYLGS CLLHKGYKSS PDQFVGIFAQ NRPEWIISEL
    160 170 180 190 200
    ACYTYSMVAV PLYDTLGPEA IVHIVNKADI AMVICDTPQK ALVLIGNVEK
    210 220 230 240 250
    GFTPSLKVII LMDPFDDDLK QRGEKSGIEI LSLYDAENLG KEHFRKPVPP
    260 270 280 290 300
    SPEDLSVICF TSGTTGDPKG AMITHQNIVS NAAAFLKCVE HAYEPTPDDV
    310 320 330 340 350
    AISYLPLAHM FERIVQAVVY SCGARVGFFQ GDIRLLADDM KTLKPTLFPA
    360 370 380 390 400
    VPRLLNRIYD KVQNEAKTPL KKFLLKLAVS SKFKELQKGI IRHDSFWDKL
    410 420 430 440 450
    IFAKIQDSLG GRVRVIVTGA APMSTSVMTF FRAAMGCQVY EAYGQTECTG
    460 470 480 490 500
    GCTFTLPGDW TSGHVGVPLA CNYVKLEDVA DMNYFTVNNE GEVCIKGTNV
    510 520 530 540 550
    FKGYLKDPEK TQEALDSDGW LHTGDIGRWL PNGTLKIIDR KKNIFKLAQG
    560 570 580 590 600
    EYIAPEKIEN IYNRSQPVLQ IFVHGESLRS SLVGVVVPDT DVLPSFAAKL
    610 620 630 640 650
    GVKGSFEELC QNQVVREAIL EDLQKIGKES GLKTFEQVKA IFLHPEPFSI
    660 670 680
    ENGLLTPTLK AKRGELSKYF RTQIDSLYEH IQD
    Note: Localize in mitochondrion and endoplasmic reticulum.
    Length:683
    Mass (Da):75,991
    Last modified:May 1, 2000 - v1
    Checksum:i781AFE1A7A78C286
    GO
    Isoform 2 (identifier: Q9ULC5-3) [UniParc]FASTAAdd to basket

    Also known as: ACSL5a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MDALKPPCLWRNHERGKKDRDSCGRKNSEPGSPHSLEALRDAAPSQGLNFLLLFTKM

    Show »
    Length:739
    Mass (Da):82,263
    Checksum:iC3A1ABCA53717BCE
    GO
    Isoform 3 (identifier: Q9ULC5-4) [UniParc]FASTAAdd to basket

    Also known as: ACSL5delta20

    The sequence of this isoform differs from the canonical sequence as follows:
         614-637: Missing.

    Note: Localize in mitochondrion and endoplasmic reticulum.
    Show »
    Length:659
    Mass (Da):73,278
    Checksum:i8FA678B997F35EF7
    GO

    Sequence cautioni

    The sequence BAA85979.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAA86054.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti182 – 1821M → V.
    Corresponds to variant rs3736946 [ dbSNP | Ensembl ].
    VAR_022117
    Natural varianti388 – 3881K → R in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036377
    Natural varianti466 – 4661G → D in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036378
    Natural varianti486 – 4861T → A.
    Corresponds to variant rs12254915 [ dbSNP | Ensembl ].
    VAR_048240

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MDALKPPCLWRNHERGKKDR DSCGRKNSEPGSPHSLEALR DAAPSQGLNFLLLFTKM in isoform 2. 3 PublicationsVSP_037947
    Alternative sequencei614 – 63724Missing in isoform 3. 1 PublicationVSP_038233Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AM262166 mRNA. Translation: CAK18174.1.
    AY358520 mRNA. Translation: AAQ88884.1.
    AK000339 mRNA. No translation available.
    AK222782 mRNA. No translation available.
    AL157786 Genomic DNA. Translation: CAH72510.1.
    CH471066 Genomic DNA. Translation: EAW49532.1.
    CH471066 Genomic DNA. Translation: EAW49535.1.
    CH471066 Genomic DNA. Translation: EAW49536.1.
    CH471066 Genomic DNA. Translation: EAW49539.1.
    BC007985 mRNA. Translation: AAH07985.2.
    AB033899 mRNA. Translation: BAA85979.1. Different initiation.
    AB033920 Genomic DNA. Translation: BAA86054.1. Sequence problems.
    CCDSiCCDS7572.1. [Q9ULC5-3]
    CCDS7573.1. [Q9ULC5-1]
    RefSeqiNP_057318.2. NM_016234.3. [Q9ULC5-3]
    NP_976313.1. NM_203379.1. [Q9ULC5-1]
    NP_976314.1. NM_203380.1. [Q9ULC5-1]
    UniGeneiHs.11638.

    Genome annotation databases

    EnsembliENST00000354273; ENSP00000346223; ENSG00000197142.
    ENST00000354655; ENSP00000346680; ENSG00000197142.
    ENST00000356116; ENSP00000348429; ENSG00000197142. [Q9ULC5-3]
    ENST00000393081; ENSP00000376796; ENSG00000197142.
    ENST00000433418; ENSP00000403647; ENSG00000197142. [Q9ULC5-4]
    GeneIDi51703.
    KEGGihsa:51703.
    UCSCiuc001kzs.3. human. [Q9ULC5-1]
    uc001kzu.3. human. [Q9ULC5-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AM262166 mRNA. Translation: CAK18174.1.
    AY358520 mRNA. Translation: AAQ88884.1.
    AK000339 mRNA. No translation available.
    AK222782 mRNA. No translation available.
    AL157786 Genomic DNA. Translation: CAH72510.1.
    CH471066 Genomic DNA. Translation: EAW49532.1.
    CH471066 Genomic DNA. Translation: EAW49535.1.
    CH471066 Genomic DNA. Translation: EAW49536.1.
    CH471066 Genomic DNA. Translation: EAW49539.1.
    BC007985 mRNA. Translation: AAH07985.2.
    AB033899 mRNA. Translation: BAA85979.1. Different initiation.
    AB033920 Genomic DNA. Translation: BAA86054.1. Sequence problems.
    CCDSiCCDS7572.1. [Q9ULC5-3]
    CCDS7573.1. [Q9ULC5-1]
    RefSeqiNP_057318.2. NM_016234.3. [Q9ULC5-3]
    NP_976313.1. NM_203379.1. [Q9ULC5-1]
    NP_976314.1. NM_203380.1. [Q9ULC5-1]
    UniGeneiHs.11638.

    3D structure databases

    ProteinModelPortaliQ9ULC5.
    SMRiQ9ULC5. Positions 104-620.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ9ULC5. 3 interactions.
    STRINGi9606.ENSP00000348429.

    PTM databases

    PhosphoSiteiQ9ULC5.

    Polymorphism and mutation databases

    BioMutaiACSL5.
    DMDMi13431659.

    Proteomic databases

    MaxQBiQ9ULC5.
    PaxDbiQ9ULC5.
    PRIDEiQ9ULC5.

    Protocols and materials databases

    DNASUi51703.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000354273; ENSP00000346223; ENSG00000197142.
    ENST00000354655; ENSP00000346680; ENSG00000197142.
    ENST00000356116; ENSP00000348429; ENSG00000197142. [Q9ULC5-3]
    ENST00000393081; ENSP00000376796; ENSG00000197142.
    ENST00000433418; ENSP00000403647; ENSG00000197142. [Q9ULC5-4]
    GeneIDi51703.
    KEGGihsa:51703.
    UCSCiuc001kzs.3. human. [Q9ULC5-1]
    uc001kzu.3. human. [Q9ULC5-3]

    Organism-specific databases

    CTDi51703.
    GeneCardsiGC10P114123.
    HGNCiHGNC:16526. ACSL5.
    HPAiCAB062546.
    HPA007162.
    MIMi605677. gene.
    neXtProtiNX_Q9ULC5.
    PharmGKBiPA27969.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1022.
    GeneTreeiENSGT00690000101725.
    HOGENOMiHOG000159459.
    HOVERGENiHBG050452.
    InParanoidiQ9ULC5.
    KOiK01897.
    OMAiQENKCLT.
    OrthoDBiEOG71CFKN.
    PhylomeDBiQ9ULC5.
    TreeFamiTF313877.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01349-MONOMER.
    ReactomeiREACT_380. Synthesis of very long-chain fatty acyl-CoAs.

    Miscellaneous databases

    ChiTaRSiACSL5. human.
    GeneWikiiACSL5.
    GenomeRNAii51703.
    NextBioi35462376.
    PROiQ9ULC5.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9ULC5.
    CleanExiHS_ACSL5.
    GenevisibleiQ9ULC5. HS.

    Family and domain databases

    InterProiIPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Small intestine mucosa.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "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 1).
      Tissue: Hepatoma.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Liver.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 2).
      Tissue: Colon.
    8. "Human FACL5 (or ACS5)."
      Yamashita Y.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Acyl-CoA synthetase as a cancer survival factor: its inhibition enhances the efficacy of etoposide."
      Mashima T., Sato S., Okabe S., Miyata S., Matsuura M., Sugimoto Y., Tsuruo T., Seimiya H.
      Cancer Sci. 100:1556-1562(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Promotion of glioma cell survival by acyl-CoA synthetase 5 under extracellular acidosis conditions."
      Mashima T., Sato S., Sugimoto Y., Tsuruo T., Seimiya H.
      Oncogene 28:9-19(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    14. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-388 AND ASP-466.

    Entry informationi

    Entry nameiACSL5_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULC5
    Secondary accession number(s): A6GV77
    , D3DRB3, Q6UX44, Q9UIU4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 1, 2000
    Last modified: July 22, 2015
    This is version 143 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 10
      Human chromosome 10: 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. 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.