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P16219

- ACADS_HUMAN

UniProt

P16219 - ACADS_HUMAN

Protein

Short-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.

    Cofactori

    FAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei161 – 1611Substrate; via carbonyl oxygen
    Binding sitei297 – 2971FAD; shared with dimeric partner1 Publication
    Binding sitei308 – 3081FAD1 Publication
    Active sitei392 – 3921Proton acceptorBy similarity
    Binding sitei393 – 3931Substrate; via amide nitrogen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi152 – 16110FAD1 Publication
    Nucleotide bindingi185 – 1873FAD1 Publication
    Nucleotide bindingi365 – 3695FAD; shared with dimeric partner1 Publication
    Nucleotide bindingi394 – 3963FAD1 Publication

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: Reactome
    2. butyryl-CoA dehydrogenase activity Source: UniProtKB-EC
    3. fatty-acyl-CoA binding Source: Ensembl
    4. flavin adenine dinucleotide binding Source: InterPro

    GO - Biological processi

    1. butyrate catabolic process Source: Ensembl
    2. cellular lipid metabolic process Source: Reactome
    3. fatty acid beta-oxidation Source: Reactome
    4. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: Ensembl
    5. protein homotetramerization Source: Ensembl
    6. response to glucocorticoid Source: Ensembl
    7. response to starvation Source: Ensembl
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04619-MONOMER.
    ReactomeiREACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
    REACT_419. Beta oxidation of butanoyl-CoA to acetyl-CoA.
    SABIO-RKP16219.
    UniPathwayiUPA00660.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Short-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.1)
    Short name:
    SCAD
    Alternative name(s):
    Butyryl-CoA dehydrogenase
    Gene namesi
    Name:ACADS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:90. ACADS.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrial membrane Source: Ensembl
    3. mitochondrion Source: MGI
    4. nucleus Source: UniProt

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Acyl-CoA dehydrogenase short-chain deficiency (ACADSD) [MIM:201470]: An inborn error of mitochondrial fatty acid beta-oxidation resulting in acute acidosis and muscle weakness in infants, and a form of lipid-storage myopathy in adults.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461R → W in ACADSD.
    VAR_000310
    Natural varianti90 – 901G → S in ACADSD; no detectable activity. 1 Publication
    VAR_013565
    Natural varianti92 – 921G → C in ACADSD. 1 Publication
    VAR_000311
    Natural varianti104 – 1041Missing in ACADSD; no detectable activity. 1 Publication
    VAR_013566
    Natural varianti107 – 1071R → C in ACADSD.
    VAR_000312
    Natural varianti177 – 1771W → R in ACADSD. 1 Publication
    Corresponds to variant rs57443665 [ dbSNP | Ensembl ].
    VAR_000314
    Natural varianti192 – 1921A → V in ACADSD; no detectable activity. 1 Publication
    Corresponds to variant rs28940874 [ dbSNP | Ensembl ].
    VAR_013568
    Natural varianti325 – 3251R → W in ACADSD; no detectable activity. 1 Publication
    VAR_013569
    Natural varianti353 – 3531S → L in ACADSD; no detectable activity. 1 Publication
    Corresponds to variant rs28941773 [ dbSNP | Ensembl ].
    VAR_013570
    Natural varianti380 – 3801R → W in ACADSD; no detectable activity. 1 Publication
    Corresponds to variant rs28940875 [ dbSNP | Ensembl ].
    VAR_013571
    Natural varianti383 – 3831R → C in ACADSD. 1 Publication
    Corresponds to variant rs28940872 [ dbSNP | Ensembl ].
    VAR_000316

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi201470. phenotype.
    Orphaneti26792. Short chain acyl-CoA dehydrogenase deficiency.
    PharmGKBiPA24426.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2424Mitochondrion1 PublicationAdd
    BLAST
    Chaini25 – 412388Short-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000498Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei51 – 511N6-acetyllysine; alternateBy similarity
    Modified residuei51 – 511N6-succinyllysine; alternateBy similarity
    Modified residuei72 – 721N6-acetyllysineBy similarity
    Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
    Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
    Modified residuei208 – 2081N6-acetyllysineBy similarity
    Modified residuei262 – 2621N6-acetyllysine; alternateBy similarity
    Modified residuei262 – 2621N6-succinyllysine; alternateBy similarity
    Modified residuei306 – 3061N6-acetyllysine; alternateBy similarity
    Modified residuei306 – 3061N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP16219.
    PaxDbiP16219.
    PeptideAtlasiP16219.
    PRIDEiP16219.

    2D gel databases

    DOSAC-COBS-2DPAGEP16219.
    SWISS-2DPAGEP16219.
    UCD-2DPAGEP16219.

    PTM databases

    PhosphoSiteiP16219.

    Expressioni

    Gene expression databases

    ArrayExpressiP16219.
    BgeeiP16219.
    CleanExiHS_ACADS.
    GenevestigatoriP16219.

    Organism-specific databases

    HPAiCAB019284.
    HPA004799.
    HPA022271.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi106553. 1 interaction.
    IntActiP16219. 2 interactions.
    STRINGi9606.ENSP00000242592.

    Structurei

    Secondary structure

    1
    412
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 5217
    Turni53 – 564
    Helixi57 – 637
    Helixi68 – 7710
    Turni78 – 803
    Helixi86 – 883
    Helixi95 – 10814
    Helixi110 – 12112
    Helixi124 – 1307
    Helixi133 – 1397
    Helixi141 – 1433
    Beta strandi144 – 1474
    Beta strandi150 – 1534
    Beta strandi159 – 1624
    Helixi163 – 1653
    Beta strandi169 – 1735
    Beta strandi176 – 18712
    Turni188 – 1914
    Beta strandi193 – 2008
    Beta strandi203 – 2053
    Beta strandi210 – 2189
    Beta strandi222 – 2243
    Beta strandi230 – 2323
    Beta strandi238 – 24912
    Helixi250 – 2523
    Beta strandi253 – 2564
    Helixi260 – 29637
    Helixi304 – 3063
    Helixi308 – 33629
    Helixi342 – 36726
    Helixi368 – 3725
    Helixi378 – 38811
    Turni389 – 3924
    Helixi395 – 41117

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VIGX-ray1.90A/B/C/D/E/F/G/H30-412[»]
    ProteinModelPortaliP16219.
    SMRiP16219. Positions 34-412.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16219.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni269 – 2724Substrate binding

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1960.
    HOGENOMiHOG000131659.
    HOVERGENiHBG000224.
    InParanoidiP16219.
    KOiK00248.
    OMAiAVTLNNC.
    OrthoDBiEOG74FF0S.
    PhylomeDBiP16219.
    TreeFamiTF105019.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProiIPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16219-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAALLARAS GPARRALCPR AWRQLHTIYQ SVELPETHQM LLQTCRDFAE    50
    KELFPIAAQV DKEHLFPAAQ VKKMGGLGLL AMDVPEELGG AGLDYLAYAI 100
    AMEEISRGCA STGVIMSVNN SLYLGPILKF GSKEQKQAWV TPFTSGDKIG 150
    CFALSEPGNG SDAGAASTTA RAEGDSWVLN GTKAWITNAW EASAAVVFAS 200
    TDRALQNKGI SAFLVPMPTP GLTLGKKEDK LGIRGSSTAN LIFEDCRIPK 250
    DSILGEPGMG FKIAMQTLDM GRIGIASQAL GIAQTALDCA VNYAENRMAF 300
    GAPLTKLQVI QFKLADMALA LESARLLTWR AAMLKDNKKP FIKEAAMAKL 350
    AASEAATAIS HQAIQILGGM GYVTEMPAER HYRDARITEI YEGTSEIQRL 400
    VIAGHLLRSY RS 412
    Length:412
    Mass (Da):44,297
    Last modified:April 1, 1990 - v1
    Checksum:i3E946ADFC3DA3C0E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461R → W in ACADSD.
    VAR_000310
    Natural varianti90 – 901G → S in ACADSD; no detectable activity. 1 Publication
    VAR_013565
    Natural varianti92 – 921G → C in ACADSD. 1 Publication
    VAR_000311
    Natural varianti104 – 1041Missing in ACADSD; no detectable activity. 1 Publication
    VAR_013566
    Natural varianti107 – 1071R → C in ACADSD.
    VAR_000312
    Natural varianti171 – 1711R → W 69% of wild-type activity; confers susceptibility to ethylmalonicaciduria. 2 Publications
    Corresponds to variant rs1800556 [ dbSNP | Ensembl ].
    VAR_013567
    Natural varianti177 – 1771W → R in ACADSD. 1 Publication
    Corresponds to variant rs57443665 [ dbSNP | Ensembl ].
    VAR_000314
    Natural varianti192 – 1921A → V in ACADSD; no detectable activity. 1 Publication
    Corresponds to variant rs28940874 [ dbSNP | Ensembl ].
    VAR_013568
    Natural varianti209 – 2091G → S 86% of wild-type activity; confers susceptibility to ethylmalonicaciduria. 2 Publications
    Corresponds to variant rs1799958 [ dbSNP | Ensembl ].
    VAR_000315
    Natural varianti325 – 3251R → W in ACADSD; no detectable activity. 1 Publication
    VAR_013569
    Natural varianti353 – 3531S → L in ACADSD; no detectable activity. 1 Publication
    Corresponds to variant rs28941773 [ dbSNP | Ensembl ].
    VAR_013570
    Natural varianti380 – 3801R → W in ACADSD; no detectable activity. 1 Publication
    Corresponds to variant rs28940875 [ dbSNP | Ensembl ].
    VAR_013571
    Natural varianti383 – 3831R → C in ACADSD. 1 Publication
    Corresponds to variant rs28940872 [ dbSNP | Ensembl ].
    VAR_000316
    Natural varianti383 – 3831R → H.
    Corresponds to variant rs35233375 [ dbSNP | Ensembl ].
    VAR_033458

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26393 mRNA. Translation: AAA60307.1.
    Z80345, Z80347 Genomic DNA. Translation: CAB02492.1.
    U83992, U83991 Genomic DNA. Translation: AAD00552.1.
    BC025963 mRNA. Translation: AAH25963.1.
    CCDSiCCDS9207.1.
    PIRiA30605.
    RefSeqiNP_000008.1. NM_000017.2.
    UniGeneiHs.507076.

    Genome annotation databases

    EnsembliENST00000242592; ENSP00000242592; ENSG00000122971.
    GeneIDi35.
    KEGGihsa:35.
    UCSCiuc001tza.4. human.

    Polymorphism databases

    DMDMi113019.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Butyryl-CoA dehydrogenase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26393 mRNA. Translation: AAA60307.1 .
    Z80345 , Z80347 Genomic DNA. Translation: CAB02492.1 .
    U83992 , U83991 Genomic DNA. Translation: AAD00552.1 .
    BC025963 mRNA. Translation: AAH25963.1 .
    CCDSi CCDS9207.1.
    PIRi A30605.
    RefSeqi NP_000008.1. NM_000017.2.
    UniGenei Hs.507076.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VIG X-ray 1.90 A/B/C/D/E/F/G/H 30-412 [» ]
    ProteinModelPortali P16219.
    SMRi P16219. Positions 34-412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106553. 1 interaction.
    IntActi P16219. 2 interactions.
    STRINGi 9606.ENSP00000242592.

    Chemistry

    DrugBanki DB03147. Flavin adenine dinucleotide.

    PTM databases

    PhosphoSitei P16219.

    Polymorphism databases

    DMDMi 113019.

    2D gel databases

    DOSAC-COBS-2DPAGE P16219.
    SWISS-2DPAGE P16219.
    UCD-2DPAGE P16219.

    Proteomic databases

    MaxQBi P16219.
    PaxDbi P16219.
    PeptideAtlasi P16219.
    PRIDEi P16219.

    Protocols and materials databases

    DNASUi 35.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000242592 ; ENSP00000242592 ; ENSG00000122971 .
    GeneIDi 35.
    KEGGi hsa:35.
    UCSCi uc001tza.4. human.

    Organism-specific databases

    CTDi 35.
    GeneCardsi GC12P121163.
    GeneReviewsi ACADS.
    HGNCi HGNC:90. ACADS.
    HPAi CAB019284.
    HPA004799.
    HPA022271.
    MIMi 201470. phenotype.
    606885. gene.
    neXtProti NX_P16219.
    Orphaneti 26792. Short chain acyl-CoA dehydrogenase deficiency.
    PharmGKBi PA24426.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1960.
    HOGENOMi HOG000131659.
    HOVERGENi HBG000224.
    InParanoidi P16219.
    KOi K00248.
    OMAi AVTLNNC.
    OrthoDBi EOG74FF0S.
    PhylomeDBi P16219.
    TreeFami TF105019.

    Enzyme and pathway databases

    UniPathwayi UPA00660 .
    BioCyci MetaCyc:HS04619-MONOMER.
    Reactomei REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
    REACT_419. Beta oxidation of butanoyl-CoA to acetyl-CoA.
    SABIO-RK P16219.

    Miscellaneous databases

    EvolutionaryTracei P16219.
    GenomeRNAii 35.
    NextBioi 135.
    PROi P16219.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16219.
    Bgeei P16219.
    CleanExi HS_ACADS.
    Genevestigatori P16219.

    Family and domain databases

    Gene3Di 1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProi IPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view ]
    Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of complementary DNAs encoding human short chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short chain acyl-coenzyme A dehydrogenase deficiency."
      Naito E., Ozasa H., Ikeda Y., Tanaka K.
      J. Clin. Invest. 83:1605-1613(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural organization of the human short-chain acyl-CoA dehydrogenase gene."
      Corydon M.J., Andresen B.S., Bross P., Kjeldsen M., Andreasen P.H., Eiberg H., Koelvraa S., Gregersen N.
      Mamm. Genome 8:922-926(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Transcription map of the 5cM region surrounding the hepatocyte nuclear factor-1a/MODY3 gene on chromosome 12."
      Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., Lathrop M., Cox R.D., Bell G.I.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [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].
      Tissue: Retinal pigment epithelium.
    5. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-34.
      Tissue: Liver.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Crystal structure of human RAB14."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-412 IN COMPLEX WITH FAD AND SUBSTRATE ANALOG.
    8. "Identification of two variant short chain acyl-coenzyme A dehydrogenase alleles, each containing a different point mutation in a patient with short chain acyl-coenzyme A dehydrogenase deficiency."
      Naito E., Indo Y., Tanaka K.
      J. Clin. Invest. 85:1575-1582(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ACADSD.
    9. "Identification of four new mutations in the short-chain acyl-CoA dehydrogenase (SCAD) gene in two patients: one of the variant alleles, 511C-->T, is present at an unexpectedly high frequency in the general population, as was the case for 625G-->A, together conferring susceptibility to ethylmalonic aciduria."
      Gregersen N., Winter V.S., Corydon M.J., Corydon T.J., Rinaldo P., Ribes A., Martinez G., Bennett M.J., Vianey-Saban C., Bhala A., Hale D.E., Lehnert W., Kmoch S., Roig M., Riudor E., Eiberg H., Andresen B.S., Bross P., Bolund L.A., Koelvraa S.
      Hum. Mol. Genet. 7:619-627(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ACADSD CYS-92; ARG-177 AND CYS-383, VARIANTS TRP-171 AND SER-209.
    10. "Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency."
      Corydon M.J., Vockley J., Rinaldo P., Rhead W.J., Kjeldsen M., Winter V.S., Riggs C., Babovic-Vuksanovic D., Smeitink J., De Jong J., Levy H., Sewell A.C., Roe C., Matern D., Dasouki M., Gregersen N.
      Pediatr. Res. 49:18-23(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ACADSD SER-90; GLU-104 DEL; VAL-192; TRP-325; LEU-353 AND TRP-380, VARIANTS TRP-171 AND SER-209.

    Entry informationi

    Entry nameiACADS_HUMAN
    AccessioniPrimary (citable) accession number: P16219
    Secondary accession number(s): P78331
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 171 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

    Miscellaneous

    A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3