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Q8NFF5

- FAD1_HUMAN

UniProt

Q8NFF5 - FAD1_HUMAN

Protein

FAD synthase

Gene

FLAD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.

    Catalytic activityi

    ATP + FMN = diphosphate + FAD.1 Publication

    Cofactori

    Magnesium.2 Publications

    Kineticsi

    1. KM=1.5 µM for FMN2 Publications
    2. KM=0.36 µM for FMN (isoform 2)2 Publications

    Vmax=6.1 nmol/min/mg enzyme2 Publications

    Vmax=3.9 nmol/min/mg enzyme (isoform 2)2 Publications

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. FMN adenylyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. FAD biosynthetic process Source: UniProtKB-UniPathway
    2. Mo-molybdopterin cofactor biosynthetic process Source: InterPro
    3. riboflavin metabolic process Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. vitamin metabolic process Source: Reactome
    6. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08520-MONOMER.
    BRENDAi2.7.7.2. 2681.
    ReactomeiREACT_11070. Vitamin B2 (riboflavin) metabolism.
    SABIO-RKQ8NFF5.
    UniPathwayiUPA00277; UER00407.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FAD synthase (EC:2.7.7.2)
    Alternative name(s):
    FAD pyrophosphorylase
    FMN adenylyltransferase
    Flavin adenine dinucleotide synthase
    Including the following 2 domains:
    Molybdenum cofactor biosynthesis protein-like region
    FAD synthase region
    Gene namesi
    Name:FLAD1
    ORF Names:PP591
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24671. FLAD1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671759.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1717MitochondrionSequence AnalysisAdd
    BLAST
    Chaini18 – 587570FAD synthasePRO_0000302737Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei106 – 1061Phosphoserine2 Publications
    Modified residuei378 – 3781N6-acetyllysine; alternateBy similarity
    Modified residuei378 – 3781N6-succinyllysine; alternateBy similarity
    Modified residuei563 – 5631Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8NFF5.
    PaxDbiQ8NFF5.
    PRIDEiQ8NFF5.

    PTM databases

    PhosphoSiteiQ8NFF5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8NFF5.
    BgeeiQ8NFF5.
    CleanExiHS_FLAD1.
    GenevestigatoriQ8NFF5.

    Organism-specific databases

    HPAiHPA028476.
    HPA028486.
    HPA028563.

    Interactioni

    Protein-protein interaction databases

    BioGridi123221. 17 interactions.
    IntActiQ8NFF5. 13 interactions.
    MINTiMINT-3042841.
    STRINGi9606.ENSP00000292180.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NFF5.
    SMRiQ8NFF5. Positions 113-269, 349-560.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni114 – 20592Molybdenum cofactor biosynthesis protein-likeAdd
    BLAST
    Regioni398 – 555158FAD synthaseAdd
    BLAST

    Domaini

    The molybdenum cofactor biosynthesis protein-like region may not be functional.

    Sequence similaritiesi

    In the N-terminal section; belongs to the MoaB/Mog family.Curated
    In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0175.
    HOVERGENiHBG058211.
    InParanoidiQ8NFF5.
    KOiK00953.
    OMAiAIAVEIS.
    OrthoDBiEOG7C5M9F.
    PhylomeDBiQ8NFF5.
    TreeFamiTF314056.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    3.40.980.10. 1 hit.
    InterProiIPR012183. FAD_synth_Mopterin-bd.
    IPR001453. Mopterin-bd_dom.
    IPR002500. PAPS_reduct.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00994. MoCF_biosynth. 1 hit.
    PF01507. PAPS_reduct. 2 hits.
    [Graphical view]
    PIRSFiPIRSF036620. MPTbdFAD. 1 hit.
    SMARTiSM00852. MoCF_biosynth. 1 hit.
    [Graphical view]
    SUPFAMiSSF53218. SSF53218. 1 hit.

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8NFF5-1) [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

    MGWDLGTRLF QRQEQRSRLS RIWLEKTRVF LEGSTRTPAL PHCLFWLLQV    50
    PSTQDPLFPG YGPQCPVDLA GPPCLRPLFG GLGGYWRALQ RGREGRTMTS 100
    RASELSPGRS VTAGIIIVGD EILKGHTQDT NTFFLCRTLR SLGVQVCRVS 150
    VVPDEVATIA AEVTSFSNRF THVLTAGGIG PTHDDVTFEA VAQAFGDELK 200
    PHPKLEAATK ALGGEGWEKL SLVPSSARLH YGTDPCTGQP FRFPLVSVRN 250
    VYLFPGIPEL LRRVLEGMKG LFQNPAVQFH SKELYVAADE ASIAPILAEA 300
    QAHFGRRLGL GSYPDWGSNY YQVKLTLDSE EEGPLEECLA YLTARLPQGS 350
    LVPYMPNAVE QASEAVYKLA ESGSSLGKKV AGALQTIETS LAQYSLTQLC 400
    VGFNGGKDCT ALLHLFHAAV QRKLPDVPNP LQILYIRSIS PFPELEQFLQ 450
    DTIKRYNLQM LEAEGSMKQA LGELQARHPQ LEAVLMGTRR TDPYSCSLCP 500
    FSPTDPGWPA FMRINPLLDW TYRDIWDFLR QLFVPYCILY DRGYTSLGSR 550
    ENTVRNPALK CLSPGGHPTY RPAYLLENEE EERNSRT 587
    Length:587
    Mass (Da):65,266
    Last modified:October 1, 2002 - v1
    Checksum:iF95918B15D9D8106
    GO
    Isoform 2 (identifier: Q8NFF5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-97: Missing.

    Show »
    Length:490
    Mass (Da):54,188
    Checksum:i633D7949AB88E059
    GO
    Isoform 3 (identifier: Q8NFF5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-97: Missing.
         544-587: Missing.

    Show »
    Length:446
    Mass (Da):49,198
    Checksum:i2983E4FA84020CDF
    GO
    Isoform 4 (identifier: Q8NFF5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-30: Missing.
         31-124: LEGSTRTPAL...IIIVGDEILK → MQPSSSTPPLHPYSTDGLIFPFNPQ
         374-393: SSLGKKVAGALQTIETSLAQ → RDLMEEGHYAQSHWWHPRSQ
         394-587: Missing.

    Show »
    Length:294
    Mass (Da):32,369
    Checksum:i5CEF3426F7FEDEF5
    GO
    Isoform 5 (identifier: Q8NFF5-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-30: Missing.
         31-124: LEGSTRTPAL...IIIVGDEILK → MQPSSSTPPLHPYSTDGLIFPFNPQ
         374-437: SSLGKKVAGA...PNPLQILYIR → NYLMFQTPSR...WMGPFPGQQG
         438-587: Missing.

    Show »
    Length:338
    Mass (Da):36,865
    Checksum:i2BB52386763E2A9B
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9797Missing in isoform 2 and isoform 3. 2 PublicationsVSP_027947Add
    BLAST
    Alternative sequencei1 – 3030Missing in isoform 4 and isoform 5. 2 PublicationsVSP_027948Add
    BLAST
    Alternative sequencei31 – 12494LEGST…DEILK → MQPSSSTPPLHPYSTDGLIF PFNPQ in isoform 4 and isoform 5. 2 PublicationsVSP_027949Add
    BLAST
    Alternative sequencei374 – 43764SSLGK…ILYIR → NYLMFQTPSRSCISAASPLS LSWNSFYRTLSREQAIPENQ IASPPSEAKGAEEPWMGPFP GQQG in isoform 5. 1 PublicationVSP_027950Add
    BLAST
    Alternative sequencei374 – 39320SSLGK…TSLAQ → RDLMEEGHYAQSHWWHPRSQ in isoform 4. 1 PublicationVSP_027951Add
    BLAST
    Alternative sequencei394 – 587194Missing in isoform 4. 1 PublicationVSP_027952Add
    BLAST
    Alternative sequencei438 – 587150Missing in isoform 5. 1 PublicationVSP_027953Add
    BLAST
    Alternative sequencei544 – 58744Missing in isoform 3. 1 PublicationVSP_027954Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ458779 mRNA. Translation: ABE65383.1.
    AF481877 mRNA. Translation: AAO49318.1.
    AF520568 mRNA. Translation: AAM77338.1.
    AF218022 mRNA. Translation: AAG17264.1.
    AL451085 Genomic DNA. Translation: CAI13259.1.
    AL451085 Genomic DNA. Translation: CAI13260.1.
    AL451085 Genomic DNA. Translation: CAI13261.1.
    AL451085 Genomic DNA. Translation: CAI13262.1.
    CH471121 Genomic DNA. Translation: EAW53154.1.
    CH471121 Genomic DNA. Translation: EAW53155.1.
    CH471121 Genomic DNA. Translation: EAW53158.1.
    CH471121 Genomic DNA. Translation: EAW53159.1.
    BC011378 mRNA. Translation: AAH11378.1.
    BC014012 mRNA. Translation: AAH14012.2.
    BC020253 mRNA. Translation: AAH20253.1.
    BC021096 mRNA. Translation: AAH21096.2.
    BC032323 mRNA. Translation: AAH32323.1.
    U79241 mRNA. Translation: AAB50199.1.
    CCDSiCCDS1078.1. [Q8NFF5-1]
    CCDS1079.1. [Q8NFF5-2]
    CCDS53371.1. [Q8NFF5-3]
    CCDS53372.1. [Q8NFF5-4]
    RefSeqiNP_001171820.1. NM_001184891.1. [Q8NFF5-3]
    NP_001171821.1. NM_001184892.1. [Q8NFF5-4]
    NP_079483.3. NM_025207.4. [Q8NFF5-1]
    NP_958800.1. NM_201398.2. [Q8NFF5-2]
    UniGeneiHs.118666.

    Genome annotation databases

    EnsembliENST00000292180; ENSP00000292180; ENSG00000160688. [Q8NFF5-1]
    ENST00000315144; ENSP00000317296; ENSG00000160688. [Q8NFF5-2]
    ENST00000368431; ENSP00000357416; ENSG00000160688. [Q8NFF5-4]
    ENST00000368432; ENSP00000357417; ENSG00000160688. [Q8NFF5-3]
    GeneIDi80308.
    KEGGihsa:80308.
    UCSCiuc001fgc.3. human. [Q8NFF5-4]
    uc001fgd.2. human. [Q8NFF5-1]

    Polymorphism databases

    DMDMi74751275.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ458779 mRNA. Translation: ABE65383.1 .
    AF481877 mRNA. Translation: AAO49318.1 .
    AF520568 mRNA. Translation: AAM77338.1 .
    AF218022 mRNA. Translation: AAG17264.1 .
    AL451085 Genomic DNA. Translation: CAI13259.1 .
    AL451085 Genomic DNA. Translation: CAI13260.1 .
    AL451085 Genomic DNA. Translation: CAI13261.1 .
    AL451085 Genomic DNA. Translation: CAI13262.1 .
    CH471121 Genomic DNA. Translation: EAW53154.1 .
    CH471121 Genomic DNA. Translation: EAW53155.1 .
    CH471121 Genomic DNA. Translation: EAW53158.1 .
    CH471121 Genomic DNA. Translation: EAW53159.1 .
    BC011378 mRNA. Translation: AAH11378.1 .
    BC014012 mRNA. Translation: AAH14012.2 .
    BC020253 mRNA. Translation: AAH20253.1 .
    BC021096 mRNA. Translation: AAH21096.2 .
    BC032323 mRNA. Translation: AAH32323.1 .
    U79241 mRNA. Translation: AAB50199.1 .
    CCDSi CCDS1078.1. [Q8NFF5-1 ]
    CCDS1079.1. [Q8NFF5-2 ]
    CCDS53371.1. [Q8NFF5-3 ]
    CCDS53372.1. [Q8NFF5-4 ]
    RefSeqi NP_001171820.1. NM_001184891.1. [Q8NFF5-3 ]
    NP_001171821.1. NM_001184892.1. [Q8NFF5-4 ]
    NP_079483.3. NM_025207.4. [Q8NFF5-1 ]
    NP_958800.1. NM_201398.2. [Q8NFF5-2 ]
    UniGenei Hs.118666.

    3D structure databases

    ProteinModelPortali Q8NFF5.
    SMRi Q8NFF5. Positions 113-269, 349-560.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123221. 17 interactions.
    IntActi Q8NFF5. 13 interactions.
    MINTi MINT-3042841.
    STRINGi 9606.ENSP00000292180.

    PTM databases

    PhosphoSitei Q8NFF5.

    Polymorphism databases

    DMDMi 74751275.

    Proteomic databases

    MaxQBi Q8NFF5.
    PaxDbi Q8NFF5.
    PRIDEi Q8NFF5.

    Protocols and materials databases

    DNASUi 80308.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000292180 ; ENSP00000292180 ; ENSG00000160688 . [Q8NFF5-1 ]
    ENST00000315144 ; ENSP00000317296 ; ENSG00000160688 . [Q8NFF5-2 ]
    ENST00000368431 ; ENSP00000357416 ; ENSG00000160688 . [Q8NFF5-4 ]
    ENST00000368432 ; ENSP00000357417 ; ENSG00000160688 . [Q8NFF5-3 ]
    GeneIDi 80308.
    KEGGi hsa:80308.
    UCSCi uc001fgc.3. human. [Q8NFF5-4 ]
    uc001fgd.2. human. [Q8NFF5-1 ]

    Organism-specific databases

    CTDi 80308.
    GeneCardsi GC01P154955.
    HGNCi HGNC:24671. FLAD1.
    HPAi HPA028476.
    HPA028486.
    HPA028563.
    MIMi 610595. gene.
    neXtProti NX_Q8NFF5.
    PharmGKBi PA142671759.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0175.
    HOVERGENi HBG058211.
    InParanoidi Q8NFF5.
    KOi K00953.
    OMAi AIAVEIS.
    OrthoDBi EOG7C5M9F.
    PhylomeDBi Q8NFF5.
    TreeFami TF314056.

    Enzyme and pathway databases

    UniPathwayi UPA00277 ; UER00407 .
    BioCyci MetaCyc:HS08520-MONOMER.
    BRENDAi 2.7.7.2. 2681.
    Reactomei REACT_11070. Vitamin B2 (riboflavin) metabolism.
    SABIO-RK Q8NFF5.

    Miscellaneous databases

    ChiTaRSi FLAD1. human.
    GenomeRNAii 80308.
    NextBioi 70783.
    PROi Q8NFF5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8NFF5.
    Bgeei Q8NFF5.
    CleanExi HS_FLAD1.
    Genevestigatori Q8NFF5.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    3.40.980.10. 1 hit.
    InterProi IPR012183. FAD_synth_Mopterin-bd.
    IPR001453. Mopterin-bd_dom.
    IPR002500. PAPS_reduct.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00994. MoCF_biosynth. 1 hit.
    PF01507. PAPS_reduct. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF036620. MPTbdFAD. 1 hit.
    SMARTi SM00852. MoCF_biosynth. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53218. SSF53218. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase."
      Brizio C., Galluccio M., Wait R., Torchetti E.M., Bafunno V., Accardi R., Gianazza E., Indiveri C., Barile M.
      Biochem. Biophys. Res. Commun. 344:1008-1016(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
      Tissue: Skin.
    2. "Cloning, expression and characterization of a human FAD synthetase."
      Fischer M.J., Kempter K., Bacher A.
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Liver.
    3. Chen X.G., Li Y.
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Skin.
    4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [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] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-587 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-587 (ISOFORM 1).
      Tissue: Brain, Colon, Placenta and Skin.
    8. "Large-scale concatenation cDNA sequencing."
      Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
      Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-587 (ISOFORM 1).
      Tissue: Brain.
    9. "Over-expression in Escherichia coli, purification and characterization of isoform 2 of human FAD synthetase."
      Galluccio M., Brizio C., Torchetti E.M., Ferranti P., Gianazza E., Indiveri C., Barile M.
      Protein Expr. Purif. 52:175-181(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    10. "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-106 AND SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: SUBCELLULAR LOCATION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFAD1_HUMAN
    AccessioniPrimary (citable) accession number: Q8NFF5
    Secondary accession number(s): Q8N5J1
    , Q8N686, Q8WU93, Q8WUJ4, Q96CR8, Q99764, Q9HBN6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 103 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 1
      Human chromosome 1: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3