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Q9ULC5

- ACSL5_HUMAN

UniProt

Q9ULC5 - ACSL5_HUMAN

Protein

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

Gene

ACSL5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    Magnesium.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

    1. ATP binding Source: UniProtKB-KW
    2. long-chain fatty acid-CoA ligase activity Source: UniProtKB

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. long-chain fatty acid metabolic process Source: UniProtKB
    3. long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
    4. regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. triglyceride biosynthetic process Source: Reactome

    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: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:16526. ACSL5.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum membrane Source: Reactome
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: UniProtKB
    5. mitochondrial inner membrane Source: Ensembl
    6. mitochondrial outer membrane Source: UniProtKB-SubCell
    7. mitochondrion Source: HPA
    8. nucleolus Source: HPA
    9. nucleus Source: HPA

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27969.

    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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9ULC5.
    PaxDbiQ9ULC5.
    PRIDEiQ9ULC5.

    PTM databases

    PhosphoSiteiQ9ULC5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9ULC5.
    BgeeiQ9ULC5.
    CleanExiHS_ACSL5.
    GenevestigatoriQ9ULC5.

    Organism-specific databases

    HPAiCAB062546.
    HPA007162.

    Interactioni

    Protein-protein interaction databases

    BioGridi119687. 1 interaction.
    IntActiQ9ULC5. 3 interactions.
    STRINGi9606.ENSP00000348429.

    Structurei

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini33 – 683651CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

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

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1022.
    HOGENOMiHOG000159459.
    HOVERGENiHBG050452.
    InParanoidiQ9ULC5.
    KOiK01897.
    OMAiIFVHPEP.
    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. Align

    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

    MLFIFNFLFS PLPTPALICI LTFGAAIFLW LITRPQPVLP LLDLNNQSVG    50
    IEGGARKGVS QKNNDLTSCC FSDAKTMYEV FQRGLAVSDN GPCLGYRKPN 100
    QPYRWLSYKQ VSDRAEYLGS CLLHKGYKSS PDQFVGIFAQ NRPEWIISEL 150
    ACYTYSMVAV PLYDTLGPEA IVHIVNKADI AMVICDTPQK ALVLIGNVEK 200
    GFTPSLKVII LMDPFDDDLK QRGEKSGIEI LSLYDAENLG KEHFRKPVPP 250
    SPEDLSVICF TSGTTGDPKG AMITHQNIVS NAAAFLKCVE HAYEPTPDDV 300
    AISYLPLAHM FERIVQAVVY SCGARVGFFQ GDIRLLADDM KTLKPTLFPA 350
    VPRLLNRIYD KVQNEAKTPL KKFLLKLAVS SKFKELQKGI IRHDSFWDKL 400
    IFAKIQDSLG GRVRVIVTGA APMSTSVMTF FRAAMGCQVY EAYGQTECTG 450
    GCTFTLPGDW TSGHVGVPLA CNYVKLEDVA DMNYFTVNNE GEVCIKGTNV 500
    FKGYLKDPEK TQEALDSDGW LHTGDIGRWL PNGTLKIIDR KKNIFKLAQG 550
    EYIAPEKIEN IYNRSQPVLQ IFVHGESLRS SLVGVVVPDT DVLPSFAAKL 600
    GVKGSFEELC QNQVVREAIL EDLQKIGKES GLKTFEQVKA IFLHPEPFSI 650
    ENGLLTPTLK AKRGELSKYF RTQIDSLYEH IQD 683

    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

    Note: Contains a phosphoserine at position 32.

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

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

    Polymorphism databases

    DMDMi13431659.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS7572.1. [Q9ULC5-3 ]
    CCDS7573.1. [Q9ULC5-1 ]
    RefSeqi NP_057318.2. NM_016234.3. [Q9ULC5-3 ]
    NP_976313.1. NM_203379.1. [Q9ULC5-1 ]
    NP_976314.1. NM_203380.1. [Q9ULC5-1 ]
    UniGenei Hs.11638.

    3D structure databases

    ProteinModelPortali Q9ULC5.
    SMRi Q9ULC5. Positions 104-620.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119687. 1 interaction.
    IntActi Q9ULC5. 3 interactions.
    STRINGi 9606.ENSP00000348429.

    PTM databases

    PhosphoSitei Q9ULC5.

    Polymorphism databases

    DMDMi 13431659.

    Proteomic databases

    MaxQBi Q9ULC5.
    PaxDbi Q9ULC5.
    PRIDEi Q9ULC5.

    Protocols and materials databases

    DNASUi 51703.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354273 ; ENSP00000346223 ; ENSG00000197142 . [Q9ULC5-1 ]
    ENST00000354655 ; ENSP00000346680 ; ENSG00000197142 . [Q9ULC5-1 ]
    ENST00000356116 ; ENSP00000348429 ; ENSG00000197142 . [Q9ULC5-3 ]
    ENST00000393081 ; ENSP00000376796 ; ENSG00000197142 . [Q9ULC5-1 ]
    ENST00000433418 ; ENSP00000403647 ; ENSG00000197142 . [Q9ULC5-4 ]
    GeneIDi 51703.
    KEGGi hsa:51703.
    UCSCi uc001kzs.3. human. [Q9ULC5-1 ]
    uc001kzu.3. human. [Q9ULC5-3 ]

    Organism-specific databases

    CTDi 51703.
    GeneCardsi GC10P114123.
    HGNCi HGNC:16526. ACSL5.
    HPAi CAB062546.
    HPA007162.
    MIMi 605677. gene.
    neXtProti NX_Q9ULC5.
    PharmGKBi PA27969.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1022.
    HOGENOMi HOG000159459.
    HOVERGENi HBG050452.
    InParanoidi Q9ULC5.
    KOi K01897.
    OMAi IFVHPEP.
    OrthoDBi EOG71CFKN.
    PhylomeDBi Q9ULC5.
    TreeFami TF313877.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01349-MONOMER.
    Reactomei REACT_380. Synthesis of very long-chain fatty acyl-CoAs.

    Miscellaneous databases

    ChiTaRSi ACSL5. human.
    GeneWikii ACSL5.
    GenomeRNAii 51703.
    NextBioi 35462376.
    PROi Q9ULC5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ULC5.
    Bgeei Q9ULC5.
    CleanExi HS_ACSL5.
    Genevestigatori Q9ULC5.

    Family and domain databases

    InterProi IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    [Graphical view ]
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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: October 1, 2014
    This is version 136 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