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O60427

- FADS1_HUMAN

UniProt

O60427 - FADS1_HUMAN

Protein

Fatty acid desaturase 1

Gene

FADS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 3 (11 Dec 2013)
      Previous versions | rss
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    Functioni

    Isoform 2 does not exhibit any catalytic activity toward 20:3n-6, but it may enhance FADS2 activity By similarity. Isoform 1 is a component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the desaturation of dihomo-gamma-linoleic acid (DHGLA) (20:3n-6) and eicosatetraenoic acid (20:4n-3) to generate arachidonic acid (AA) (20:4n-6) and eicosapentaenoic acid (EPA)(20:5n-3), respectively.By similarity2 Publications

    Pathwayi

    GO - Molecular functioni

    1. C-5 sterol desaturase activity Source: ProtInc
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro
    4. oxidoreductase activity Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. alpha-linolenic acid metabolic process Source: Reactome
    3. arachidonic acid metabolic process Source: Ensembl
    4. cell-cell signaling Source: UniProtKB
    5. cellular lipid metabolic process Source: Reactome
    6. cellular response to starvation Source: UniProtKB
    7. icosanoid biosynthetic process Source: UniProtKB
    8. linoleic acid metabolic process Source: Reactome
    9. phospholipid biosynthetic process Source: UniProtKB
    10. regulation of cell differentiation Source: UniProtKB
    11. regulation of transcription, DNA-templated Source: UniProtKB
    12. response to insulin Source: Ensembl
    13. response to organic cyclic compound Source: Ensembl
    14. response to sucrose Source: Ensembl
    15. response to vitamin A Source: Ensembl
    16. small molecule metabolic process Source: Reactome
    17. unsaturated fatty acid biosynthetic process Source: UniProtKB
    18. unsaturated fatty acid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07617-MONOMER.
    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_121100. Linoleic acid (LA) metabolism.
    REACT_121147. alpha-linolenic acid (ALA) metabolism.
    UniPathwayiUPA00658.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid desaturase 1 (EC:1.14.19.-)
    Alternative name(s):
    Delta(5) fatty acid desaturase
    Short name:
    D5D
    Short name:
    Delta(5) desaturase
    Short name:
    Delta-5 desaturase
    Gene namesi
    Name:FADS1
    Synonyms:FADSD5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3574. FADS1.

    Subcellular locationi

    Isoform 1 : Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity. Mitochondrion 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB
    3. intracellular membrane-bounded organelle Source: UniProtKB
    4. membrane Source: UniProtKB
    5. mitochondrion Source: UniProtKB-SubCell
    6. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27973.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Fatty acid desaturase 1PRO_0000307096Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO60427.
    PaxDbiO60427.
    PRIDEiO60427.

    PTM databases

    PhosphoSiteiO60427.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest levels in liver, brain, adrenal gland and heart. Highly expressed in fetal liver and brain.3 Publications

    Inductioni

    Strongly down-regulated upon differentiation in a neuroblastoma cell line (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiO60427.
    BgeeiO60427.
    GenevestigatoriO60427.

    Organism-specific databases

    HPAiHPA042705.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DHCR7Q9UBM71EBI-1055473,EBI-1054468
    PAAF1Q9BRP41EBI-1055473,EBI-1056358

    Protein-protein interaction databases

    BioGridi110180. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliO60427.
    SMRiO60427. Positions 19-107.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 121121CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini143 – 1453LumenalSequence Analysis
    Topological domaini171 – 26797CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini289 – 30517LumenalSequence AnalysisAdd
    BLAST
    Topological domaini327 – 444118CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei122 – 14221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei146 – 17025HelicalSequence AnalysisAdd
    BLAST
    Transmembranei268 – 28821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei306 – 32621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 9478Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi179 – 1835Histidine box-1
    Motifi216 – 2205Histidine box-2
    Motifi382 – 3865Histidine box-3

    Domaini

    The histidine box domains may contain the active site and/or be involved in metal ion binding.

    Sequence similaritiesi

    Belongs to the fatty acid desaturase family.Curated
    Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5274.
    HOVERGENiHBG002839.
    InParanoidiO60427.
    KOiK10224.
    OrthoDBiEOG7G1V6P.
    PhylomeDBiO60427.
    TreeFamiTF313604.

    Family and domain databases

    Gene3Di3.10.120.10. 1 hit.
    InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR012171. Fatty_acid/sphinglp_desaturase.
    IPR005804. Fatty_acid_desaturase-1.
    [Graphical view]
    PfamiPF00173. Cyt-b5. 1 hit.
    PF00487. FA_desaturase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
    PRINTSiPR00363. CYTOCHROMEB5.
    SUPFAMiSSF55856. SSF55856. 1 hit.
    PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60427-1) [UniParc]FASTAAdd to Basket

    Also known as: FADS1CS

    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

    MAPDPVAAET AAQGPTPRYF TWDEVAQRSG CEERWLVIDR KVYNISEFTR    50
    RHPGGSRVIS HYAGQDATDP FVAFHINKGL VKKYMNSLLI GELSPEQPSF 100
    EPTKNKELTD EFRELRATVE RMGLMKANHV FFLLYLLHIL LLDGAAWLTL 150
    WVFGTSFLPF LLCAVLLSAV QAQAGWLQHD FGHLSVFSTS KWNHLLHHFV 200
    IGHLKGAPAS WWNHMHFQHH AKPNCFRKDP DINMHPFFFA LGKILSVELG 250
    KQKKKYMPYN HQHKYFFLIG PPALLPLYFQ WYIFYFVIQR KKWVDLAWMI 300
    TFYVRFFLTY VPLLGLKAFL GLFFIVRFLE SNWFVWVTQM NHIPMHIDHD 350
    RNMDWVSTQL QATCNVHKSA FNDWFSGHLN FQIEHHLFPT MPRHNYHKVA 400
    PLVQSLCAKH GIEYQSKPLL SAFADIIHSL KESGQLWLDA YLHQ 444
    Length:444
    Mass (Da):51,964
    Last modified:December 11, 2013 - v3
    Checksum:iCC3C28D82AA49BF2
    GO
    Isoform 2 (identifier: O60427-2) [UniParc]FASTAAdd to Basket

    Also known as: FADS1AT1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-84: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:360
    Mass (Da):42,474
    Checksum:iCD55B8317E4BF21E
    GO

    Sequence cautioni

    The sequence BAC11182.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAC11229.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61V → L in AAF29378. (PubMed:16554811)Curated
    Sequence conflicti9 – 91E → G in BAB55103. (PubMed:10601301)Curated
    Sequence conflicti15 – 151P → L in AAF29378. (PubMed:16554811)Curated
    Sequence conflicti100 – 1001F → L in BAC11182. (PubMed:10601301)Curated
    Sequence conflicti143 – 1431D → E in BAC11182. (PubMed:10601301)Curated
    Sequence conflicti180 – 1801D → G in BAD96626. (PubMed:17974005)Curated
    Sequence conflicti212 – 2121W → R in BAB55173. (PubMed:10601301)Curated
    Sequence conflicti213 – 2131N → S in BAC11182. (PubMed:10601301)Curated
    Sequence conflicti255 – 2551K → N in AAF29378. (PubMed:16554811)Curated
    Sequence conflicti319 – 3191F → L in BAB55103. (PubMed:10601301)Curated
    Sequence conflicti361 – 3611Q → L in AAF70457. (PubMed:15489334)Curated
    Sequence conflicti381 – 3811F → S in BAC11229. (PubMed:10601301)Curated
    Sequence conflicti410 – 4101H → R in AAF70457. (PubMed:15489334)Curated
    Sequence conflicti431 – 4311K → E in BAC11229. (PubMed:10601301)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti272 – 2721P → S.1 Publication
    Corresponds to variant rs17856235 [ dbSNP | Ensembl ].
    VAR_035340

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8484Missing in isoform 2. 1 PublicationVSP_047521Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027427 mRNA. Translation: BAB55103.1.
    AK027522 mRNA. Translation: BAB55173.1.
    AK074754 mRNA. Translation: BAC11182.1. Different initiation.
    AK074819 mRNA. Translation: BAC11229.1. Different initiation.
    AK096275 mRNA. Translation: BAG53244.1.
    AK289552 mRNA. Translation: BAF82241.1.
    AK314199 mRNA. Translation: BAG36877.1.
    AC004770 Genomic DNA. Translation: AAC23397.1.
    AP002380 Genomic DNA. No translation available.
    AF084558 mRNA. Translation: AAG23120.1.
    AL512760 mRNA. Translation: CAC21679.1.
    AL834479 mRNA. Translation: CAD39138.1.
    AK222906 mRNA. Translation: BAD96626.1.
    BC007846 mRNA. Translation: AAH07846.1.
    AF199596 mRNA. Translation: AAF29378.1.
    AF226273 mRNA. Translation: AAF70457.1.
    RefSeqiNP_037534.3. NM_013402.4.
    UniGeneiHs.503546.

    Genome annotation databases

    EnsembliENST00000433932; ENSP00000405087; ENSG00000149485. [O60427-2]
    ENST00000542506; ENSP00000441403; ENSG00000149485. [O60427-2]
    GeneIDi3992.
    KEGGihsa:3992.
    UCSCiuc001nsh.3. human. [O60427-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027427 mRNA. Translation: BAB55103.1 .
    AK027522 mRNA. Translation: BAB55173.1 .
    AK074754 mRNA. Translation: BAC11182.1 . Different initiation.
    AK074819 mRNA. Translation: BAC11229.1 . Different initiation.
    AK096275 mRNA. Translation: BAG53244.1 .
    AK289552 mRNA. Translation: BAF82241.1 .
    AK314199 mRNA. Translation: BAG36877.1 .
    AC004770 Genomic DNA. Translation: AAC23397.1 .
    AP002380 Genomic DNA. No translation available.
    AF084558 mRNA. Translation: AAG23120.1 .
    AL512760 mRNA. Translation: CAC21679.1 .
    AL834479 mRNA. Translation: CAD39138.1 .
    AK222906 mRNA. Translation: BAD96626.1 .
    BC007846 mRNA. Translation: AAH07846.1 .
    AF199596 mRNA. Translation: AAF29378.1 .
    AF226273 mRNA. Translation: AAF70457.1 .
    RefSeqi NP_037534.3. NM_013402.4.
    UniGenei Hs.503546.

    3D structure databases

    ProteinModelPortali O60427.
    SMRi O60427. Positions 19-107.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110180. 4 interactions.

    Chemistry

    BindingDBi O60427.
    ChEMBLi CHEMBL5840.
    DrugBanki DB00132. Alpha-Linolenic Acid.
    DB00159. Icosapent.

    PTM databases

    PhosphoSitei O60427.

    Proteomic databases

    MaxQBi O60427.
    PaxDbi O60427.
    PRIDEi O60427.

    Protocols and materials databases

    DNASUi 3992.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000433932 ; ENSP00000405087 ; ENSG00000149485 . [O60427-2 ]
    ENST00000542506 ; ENSP00000441403 ; ENSG00000149485 . [O60427-2 ]
    GeneIDi 3992.
    KEGGi hsa:3992.
    UCSCi uc001nsh.3. human. [O60427-1 ]

    Organism-specific databases

    CTDi 3992.
    GeneCardsi GC11M061567.
    HGNCi HGNC:3574. FADS1.
    HPAi HPA042705.
    MIMi 606148. gene.
    neXtProti NX_O60427.
    PharmGKBi PA27973.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5274.
    HOVERGENi HBG002839.
    InParanoidi O60427.
    KOi K10224.
    OrthoDBi EOG7G1V6P.
    PhylomeDBi O60427.
    TreeFami TF313604.

    Enzyme and pathway databases

    UniPathwayi UPA00658 .
    BioCyci MetaCyc:HS07617-MONOMER.
    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_121100. Linoleic acid (LA) metabolism.
    REACT_121147. alpha-linolenic acid (ALA) metabolism.

    Miscellaneous databases

    ChiTaRSi FADS1. human.
    GeneWikii FADS1.
    GenomeRNAii 3992.
    NextBioi 15660.
    PROi O60427.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60427.
    Bgeei O60427.
    Genevestigatori O60427.

    Family and domain databases

    Gene3Di 3.10.120.10. 1 hit.
    InterProi IPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR012171. Fatty_acid/sphinglp_desaturase.
    IPR005804. Fatty_acid_desaturase-1.
    [Graphical view ]
    Pfami PF00173. Cyt-b5. 1 hit.
    PF00487. FA_desaturase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015921. FA_sphinglp_des. 1 hit.
    PRINTSi PR00363. CYTOCHROMEB5.
    SUPFAMi SSF55856. SSF55856. 1 hit.
    PROSITEi PS50255. CYTOCHROME_B5_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and fatty acid regulation of the human Delta-5 desaturase."
      Cho H.P., Nakamura M., Clarke S.D.
      J. Biol. Chem. 274:37335-37339(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    2. "cDNA cloning and characterization of human Delta5-desaturase involved in the biosynthesis of arachidonic acid."
      Leonard A.E., Kelder B., Bobik E.G., Chuang L.-T., Parker-Barnes J.M., Thurmond J.M., Kroeger P.E., Kopchick J.J., Huang Y.-S., Mukerji P.
      Biochem. J. 347:719-724(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "cDNA cloning, genomic structure, and chromosomal localization of three members of the human fatty acid desaturase family."
      Marquardt A., Stoehr H., White K., Weber B.H.
      Genomics 66:175-183(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Retina.
    4. "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 1 AND 2).
      Tissue: Cerebellum, Neuroblastoma and Teratocarcinoma.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Melanoma.
    6. 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 1).
      Tissue: Kidney epithelium.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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), VARIANT SER-272.
      Tissue: Brain.
    9. "A novel FADS1 isoform potentiates FADS2-mediated production of eicosanoid precursor fatty acids."
      Park W.J., Kothapalli K.S., Reardon H.T., Lawrence P., Qian S.B., Brenna J.T.
      J. Lipid Res. 53:1502-1512(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORM 1), INDUCTION.
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFADS1_HUMAN
    AccessioniPrimary (citable) accession number: O60427
    Secondary accession number(s): A8K0I7
    , B2RAI0, Q53GM5, Q8N3A6, Q8NCC7, Q8NCG0, Q96I39, Q96SV3, Q96T10, Q9NRP8, Q9NYX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: December 11, 2013
    Last modified: October 1, 2014
    This is version 123 of the entry and version 3 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 11
      Human chromosome 11: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3