Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P33121

- ACSL1_HUMAN

UniProt

P33121 - ACSL1_HUMAN

Protein

Long-chain-fatty-acid--CoA ligase 1

Gene

ACSL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate.

    Catalytic activityi

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

    Cofactori

    Magnesium.

    GO - Molecular functioni

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

    GO - Biological processi

    1. adiponectin-activated signaling pathway Source: Ensembl
    2. alpha-linolenic acid metabolic process Source: Reactome
    3. cellular lipid metabolic process Source: Reactome
    4. linoleic acid metabolic process Source: Reactome
    5. lipid biosynthetic process Source: UniProtKB
    6. long-chain fatty acid import Source: UniProtKB
    7. long-chain fatty acid metabolic process Source: UniProtKB
    8. long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
    9. positive regulation of protein serine/threonine kinase activity Source: Ensembl
    10. response to drug Source: Ensembl
    11. response to nutrient Source: Ensembl
    12. response to oleic acid Source: Ensembl
    13. response to organic cyclic compound Source: Ensembl
    14. small molecule metabolic process Source: Reactome
    15. triglyceride biosynthetic process Source: Reactome
    16. unsaturated fatty acid metabolic process Source: Reactome
    17. xenobiotic catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07766-MONOMER.
    BRENDAi6.2.1.3. 2681.
    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_121100. Linoleic acid (LA) metabolism.
    REACT_121147. alpha-linolenic acid (ALA) metabolism.
    REACT_380. Synthesis of very long-chain fatty acyl-CoAs.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase 1 (EC:6.2.1.3)
    Alternative name(s):
    Acyl-CoA synthetase 1
    Short name:
    ACS1
    Long-chain acyl-CoA synthetase 1
    Short name:
    LACS 1
    Long-chain acyl-CoA synthetase 2
    Short name:
    LACS 2
    Long-chain fatty acid-CoA ligase 2
    Palmitoyl-CoA ligase 1
    Palmitoyl-CoA ligase 2
    Gene namesi
    Name:ACSL1
    Synonyms:FACL1, FACL2, LACS, LACS1, LACS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:3569. ACSL1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB
    4. mitochondrial outer membrane Source: Reactome
    5. mitochondrion Source: UniProtKB
    6. peroxisomal membrane Source: UniProtKB-SubCell
    7. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane, Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27966.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 698698Long-chain-fatty-acid--CoA ligase 1PRO_0000193104Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei9 – 91Nitrated tyrosineBy similarity
    Modified residuei84 – 841PhosphotyrosineBy similarity
    Glycosylationi135 – 1351O-linked (GlcNAc)By similarity
    Modified residuei207 – 2071N6-acetyllysineBy similarity
    Modified residuei356 – 3561N6-acetyllysineBy similarity
    Modified residuei386 – 3861N6-acetyllysineBy similarity
    Modified residuei620 – 6201PhosphoserineBy similarity
    Modified residuei632 – 6321N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiP33121.
    PaxDbiP33121.
    PRIDEiP33121.

    PTM databases

    PhosphoSiteiP33121.

    Expressioni

    Tissue specificityi

    Highly expressed in liver, heart, skeletal muscle, kidney and erythroid cells, and to a lesser extent in brain, lung, placenta and pancreas.1 Publication

    Developmental stagei

    Expressed during the early stages of erythroid development while expression is very low in reticulocytes and young erythrocytes.

    Gene expression databases

    ArrayExpressiP33121.
    BgeeiP33121.
    CleanExiHS_ACSL1.
    GenevestigatoriP33121.

    Organism-specific databases

    HPAiHPA011316.
    HPA011964.

    Interactioni

    Protein-protein interaction databases

    BioGridi108476. 6 interactions.
    IntActiP33121. 3 interactions.
    STRINGi9606.ENSP00000281455.

    Structurei

    3D structure databases

    ProteinModelPortaliP33121.
    SMRiP33121. Positions 81-639.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini46 – 698653CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei25 – 4521Helical; 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.
    InParanoidiP33121.
    KOiK01897.
    OMAiWDRLIFH.
    OrthoDBiEOG71CFKN.
    PhylomeDBiP33121.
    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: P33121-1) [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

    MQAHELFRYF RMPELVDFRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKP    50
    LKPPCDLSMQ SVEVAGSGGA RRSALLDSDE PLVYFYDDVT TLYEGFQRGI 100
    QVSNNGPCLG SRKPDQPYEW LSYKQVAELS ECIGSALIQK GFKTAPDQFI 150
    GIFAQNRPEW VIIEQGCFAY SMVIVPLYDT LGNEAITYIV NKAELSLVFV 200
    DKPEKAKLLL EGVENKLIPG LKIIVVMDAY GSELVERGQR CGVEVTSMKA 250
    MEDLGRANRR KPKPPAPEDL AVICFTSGTT GNPKGAMVTH RNIVSDCSAF 300
    VKATENTVNP CPDDTLISFL PLAHMFERVV ECVMLCHGAK IGFFQGDIRL 350
    LMDDLKVLQP TVFPVVPRLL NRMFDRIFGQ ANTTLKRWLL DFASKRKEAE 400
    LRSGIIRNNS LWDRLIFHKV QSSLGGRVRL MVTGAAPVSA TVLTFLRAAL 450
    GCQFYEGYGQ TECTAGCCLT MPGDWTAGHV GAPMPCNLIK LVDVEEMNYM 500
    AAEGEGEVCV KGPNVFQGYL KDPAKTAEAL DKDGWLHTGD IGKWLPNGTL 550
    KIIDRKKHIF KLAQGEYIAP EKIENIYMRS EPVAQVFVHG ESLQAFLIAI 600
    VVPDVETLCS WAQKRGFEGS FEELCRNKDV KKAILEDMVR LGKDSGLKPF 650
    EQVKGITLHP ELFSIDNGLL TPTMKAKRPE LRNYFRSQID DLYSTIKV 698
    Length:698
    Mass (Da):77,943
    Last modified:October 1, 1993 - v1
    Checksum:iFD6669453589D362
    GO
    Isoform 2 (identifier: P33121-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         508-517: Missing.

    Note: May be due to a competing acceptor splice site. No experimental confirmation available.

    Show »
    Length:688
    Mass (Da):76,871
    Checksum:i815DF2AA8EE8A6B4
    GO
    Isoform 3 (identifier: P33121-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         306-331: NTVNPCPDDTLISFLPLAHMFERVVE → KALPLSASDTHISYLPLAHIYEQLLK

    Note: No experimental confirmation available.

    Show »
    Length:698
    Mass (Da):77,907
    Checksum:i1EDBB04923DD129F
    GO

    Sequence cautioni

    The sequence BAC04704.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 233YVR → CV in AAB00959. (PubMed:8584017)Curated
    Sequence conflicti37 – 382AA → SRR in AAB00959. (PubMed:8584017)Curated
    Sequence conflicti44 – 474YATR → RPRH in AAB00959. (PubMed:8584017)Curated
    Sequence conflicti55 – 562CD → WH in AAB00959. (PubMed:8584017)Curated
    Sequence conflicti229 – 2291A → S in AAB00959. (PubMed:8584017)Curated
    Sequence conflicti385 – 3851L → V in AAB00959. (PubMed:8584017)Curated
    Sequence conflicti400 – 4012EL → DV in AAB00959. (PubMed:8584017)Curated
    Sequence conflicti477 – 4771A → T in AAB00959. (PubMed:8584017)Curated
    Sequence conflicti492 – 4943VDV → GWQL in AAB00959. (PubMed:8584017)Curated
    Sequence conflicti502 – 5021A → S in AAB00959. (PubMed:8584017)Curated
    Sequence conflicti695 – 6951T → I in AAB00959. (PubMed:8584017)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei306 – 33126NTVNP…ERVVE → KALPLSASDTHISYLPLAHI YEQLLK in isoform 3. 1 PublicationVSP_054391Add
    BLAST
    Alternative sequencei508 – 51710Missing in isoform 2. 1 PublicationVSP_009604

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10040 mRNA. Translation: BAA00931.1.
    L09229 mRNA. Translation: AAB00959.1.
    AK096117 mRNA. Translation: BAC04704.1. Different initiation.
    AK296826 mRNA. Translation: BAH12438.1.
    AC079257 Genomic DNA. No translation available.
    AC084871 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX04662.1.
    CH471056 Genomic DNA. Translation: EAX04663.1.
    CH471056 Genomic DNA. Translation: EAX04665.1.
    BC026290 mRNA. Translation: AAH26290.1.
    BC050073 mRNA. Translation: AAH50073.1.
    CCDSiCCDS3839.1. [P33121-1]
    CCDS68826.1. [P33121-3]
    PIRiJX0202.
    RefSeqiNP_001273637.1. NM_001286708.1. [P33121-1]
    NP_001273639.1. NM_001286710.1. [P33121-3]
    NP_001273640.1. NM_001286711.1.
    NP_001273641.1. NM_001286712.1.
    NP_001986.2. NM_001995.3. [P33121-1]
    XP_005262885.1. XM_005262828.1. [P33121-1]
    XP_005262886.1. XM_005262829.1. [P33121-1]
    XP_005262888.1. XM_005262831.1. [P33121-1]
    UniGeneiHs.406678.

    Genome annotation databases

    EnsembliENST00000281455; ENSP00000281455; ENSG00000151726. [P33121-1]
    ENST00000504342; ENSP00000425006; ENSG00000151726. [P33121-1]
    ENST00000513317; ENSP00000426150; ENSG00000151726. [P33121-3]
    ENST00000515030; ENSP00000422607; ENSG00000151726. [P33121-1]
    GeneIDi2180.
    KEGGihsa:2180.
    UCSCiuc003iwt.1. human. [P33121-1]

    Polymorphism databases

    DMDMi417241.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10040 mRNA. Translation: BAA00931.1 .
    L09229 mRNA. Translation: AAB00959.1 .
    AK096117 mRNA. Translation: BAC04704.1 . Different initiation.
    AK296826 mRNA. Translation: BAH12438.1 .
    AC079257 Genomic DNA. No translation available.
    AC084871 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX04662.1 .
    CH471056 Genomic DNA. Translation: EAX04663.1 .
    CH471056 Genomic DNA. Translation: EAX04665.1 .
    BC026290 mRNA. Translation: AAH26290.1 .
    BC050073 mRNA. Translation: AAH50073.1 .
    CCDSi CCDS3839.1. [P33121-1 ]
    CCDS68826.1. [P33121-3 ]
    PIRi JX0202.
    RefSeqi NP_001273637.1. NM_001286708.1. [P33121-1 ]
    NP_001273639.1. NM_001286710.1. [P33121-3 ]
    NP_001273640.1. NM_001286711.1.
    NP_001273641.1. NM_001286712.1.
    NP_001986.2. NM_001995.3. [P33121-1 ]
    XP_005262885.1. XM_005262828.1. [P33121-1 ]
    XP_005262886.1. XM_005262829.1. [P33121-1 ]
    XP_005262888.1. XM_005262831.1. [P33121-1 ]
    UniGenei Hs.406678.

    3D structure databases

    ProteinModelPortali P33121.
    SMRi P33121. Positions 81-639.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108476. 6 interactions.
    IntActi P33121. 3 interactions.
    STRINGi 9606.ENSP00000281455.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.
    DB00171. Adenosine triphosphate.

    PTM databases

    PhosphoSitei P33121.

    Polymorphism databases

    DMDMi 417241.

    Proteomic databases

    MaxQBi P33121.
    PaxDbi P33121.
    PRIDEi P33121.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000281455 ; ENSP00000281455 ; ENSG00000151726 . [P33121-1 ]
    ENST00000504342 ; ENSP00000425006 ; ENSG00000151726 . [P33121-1 ]
    ENST00000513317 ; ENSP00000426150 ; ENSG00000151726 . [P33121-3 ]
    ENST00000515030 ; ENSP00000422607 ; ENSG00000151726 . [P33121-1 ]
    GeneIDi 2180.
    KEGGi hsa:2180.
    UCSCi uc003iwt.1. human. [P33121-1 ]

    Organism-specific databases

    CTDi 2180.
    GeneCardsi GC04M185676.
    HGNCi HGNC:3569. ACSL1.
    HPAi HPA011316.
    HPA011964.
    MIMi 152425. gene.
    neXtProti NX_P33121.
    PharmGKBi PA27966.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1022.
    HOGENOMi HOG000159459.
    HOVERGENi HBG050452.
    InParanoidi P33121.
    KOi K01897.
    OMAi WDRLIFH.
    OrthoDBi EOG71CFKN.
    PhylomeDBi P33121.
    TreeFami TF313877.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07766-MONOMER.
    BRENDAi 6.2.1.3. 2681.
    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_121100. Linoleic acid (LA) metabolism.
    REACT_121147. alpha-linolenic acid (ALA) metabolism.
    REACT_380. Synthesis of very long-chain fatty acyl-CoAs.

    Miscellaneous databases

    ChiTaRSi ACSL1. human.
    GeneWikii ACSL1.
    GenomeRNAii 2180.
    NextBioi 35479388.
    PROi P33121.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P33121.
    Bgeei P33121.
    CleanExi HS_ACSL1.
    Genevestigatori P33121.

    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. "Human long-chain acyl-CoA synthetase: structure and chromosomal location."
      Abe T., Fujino T., Fukuyama R., Minoshima S., Shimizu N., Toh H., Suzuki H., Yamamoto T.
      J. Biochem. 111:123-128(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression."
      Ghosh B., Barbosa E., Singh I.
      Mol. Cell. Biochem. 151:77-81(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-698 (ISOFORM 2).
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1).
      Tissue: Testis.
    7. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-8; 12-19; 341-349; 377-386; 562-572; 633-640 AND 655-675, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    8. "Identification and molecular characterization of acyl-CoA synthetase in human red cells and erythroid precursor."
      Malhotra K.T., Malhotra K., Lubin B.H., Kuypers F.A.
      Biochem. J. 344:135-143(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiACSL1_HUMAN
    AccessioniPrimary (citable) accession number: P33121
    Secondary accession number(s): B7Z452
    , D3DP57, P41215, Q8N8V7, Q8TA99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 140 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3