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Q9BYC5

- FUT8_HUMAN

UniProt

Q9BYC5 - FUT8_HUMAN

Protein

Alpha-(1,6)-fucosyltransferase

Gene

FUT8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (05 Mar 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans.2 Publications

    Catalytic activityi

    GDP-beta-L-fucose + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)asparagine = GDP + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-(alpha-L-fucosyl-(1->6))-N-acetyl-beta-D-glucosaminyl)asparagine.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. glycoprotein 6-alpha-L-fucosyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. cell migration Source: Ensembl
    2. cellular protein metabolic process Source: Reactome
    3. GDP-L-fucose metabolic process Source: UniProtKB
    4. integrin-mediated signaling pathway Source: Ensembl
    5. in utero embryonic development Source: UniProtKB
    6. L-fucose catabolic process Source: UniProtKB
    7. N-glycan fucosylation Source: GOC
    8. N-glycan processing Source: UniProtKB
    9. oligosaccharide biosynthetic process Source: ProtInc
    10. post-translational protein modification Source: Reactome
    11. protein glycosylation in Golgi Source: InterPro
    12. protein N-linked glycosylation Source: ProtInc
    13. protein N-linked glycosylation via asparagine Source: UniProtKB
    14. receptor metabolic process Source: Ensembl
    15. respiratory gaseous exchange Source: Ensembl
    16. transforming growth factor beta receptor signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.1.68. 2681.
    ReactomeiREACT_25302. Reactions specific to the complex N-glycan synthesis pathway.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT23. Glycosyltransferase Family 23.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-(1,6)-fucosyltransferase (EC:2.4.1.68)
    Short name:
    Alpha1-6FucT
    Alternative name(s):
    Fucosyltransferase 8
    GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase
    GDP-fucose--glycoprotein fucosyltransferase
    Glycoprotein 6-alpha-L-fucosyltransferase
    Gene namesi
    Name:FUT8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:4019. FUT8.

    Subcellular locationi

    Golgi apparatusGolgi stack membrane By similarity; Single-pass type II membrane protein By similarity
    Note: Membrane-bound form in trans cisternae of Golgi.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi apparatus Source: UniProtKB
    4. Golgi cisterna membrane Source: UniProtKB-SubCell
    5. Golgi membrane Source: Reactome
    6. integral component of membrane Source: UniProtKB-KW
    7. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi365 – 3651R → A or K: Complete loss of activity. 2 Publications
    Mutagenesisi366 – 3661R → A or K: Decreases activity to 3%. 1 Publication
    Mutagenesisi368 – 3681D → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi369 – 3691K → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi373 – 3731E → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi382 – 3821Y → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi409 – 4091D → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi410 – 4101D → A: No effect on enzyme activity. 1 Publication
    Mutagenesisi453 – 4531D → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi469 – 4691S → A: Loss of enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA28435.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 575575Alpha-(1,6)-fucosyltransferasePRO_0000080526Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi204 ↔ 2661 Publication
    Disulfide bondi212 ↔ 2301 Publication
    Disulfide bondi218 ↔ 2221 Publication
    Disulfide bondi465 ↔ 4721 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ9BYC5.
    PaxDbiQ9BYC5.
    PRIDEiQ9BYC5.

    PTM databases

    PhosphoSiteiQ9BYC5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BYC5.
    BgeeiQ9BYC5.
    CleanExiHS_FUT8.
    GenevestigatoriQ9BYC5.

    Organism-specific databases

    HPAiCAB017129.
    HPA040863.
    HPA043410.

    Interactioni

    Protein-protein interaction databases

    BioGridi108806. 6 interactions.
    IntActiQ9BYC5. 2 interactions.
    STRINGi9606.ENSP00000353910.

    Structurei

    Secondary structure

    1
    575
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi110 – 13829
    Helixi142 – 17231
    Turni173 – 1753
    Helixi176 – 19924
    Helixi204 – 2063
    Beta strandi209 – 2135
    Helixi220 – 23617
    Beta strandi240 – 2445
    Helixi255 – 2573
    Helixi282 – 2854
    Beta strandi287 – 2915
    Helixi294 – 2963
    Helixi310 – 3123
    Helixi313 – 3197
    Helixi323 – 33513
    Helixi340 – 35314
    Beta strandi357 – 3648
    Helixi379 – 39416
    Beta strandi403 – 4097
    Helixi411 – 42010
    Beta strandi424 – 4274
    Helixi437 – 4415
    Helixi446 – 45914
    Beta strandi460 – 4656
    Helixi470 – 47910
    Beta strandi482 – 4843
    Beta strandi490 – 4945
    Beta strandi506 – 5094
    Beta strandi528 – 5347
    Beta strandi536 – 5449
    Turni545 – 5473
    Beta strandi550 – 5545
    Helixi555 – 5573
    Beta strandi558 – 5603

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DE0X-ray2.61X68-575[»]
    ProteinModelPortaliQ9BYC5.
    SMRiQ9BYC5. Positions 108-572.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BYC5.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 99CytoplasmicSequence Analysis
    Topological domaini31 – 575545LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini206 – 493288GT23PROSITE-ProRule annotationAdd
    BLAST
    Domaini502 – 56362SH3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni365 – 3662Important for donor substrate binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi299 – 3057SH3-bindingSequence Analysis

    Sequence similaritiesi

    Belongs to the glycosyltransferase 23 family.PROSITE-ProRule annotation
    Contains 1 GT23 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.Curated

    Keywords - Domaini

    SH3 domain, SH3-binding, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG251249.
    HOGENOMiHOG000007175.
    HOVERGENiHBG028260.
    InParanoidiQ9BYC5.
    KOiK00717.
    OMAiRMHVDKK.
    OrthoDBiEOG7N37C3.
    PhylomeDBiQ9BYC5.
    TreeFamiTF106108.

    Family and domain databases

    InterProiIPR015827. Alpha1_6FUT_euk.
    IPR027350. GT23_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF14604. SH3_9. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000472. Alpha1_6FUT_euk. 1 hit.
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS51659. GT23. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BYC5-1) [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

    MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL    50
    ERLKQQNEDL RRMAESLRIP EGPIDQGPAI GRVRVLEEQL VKAKEQIENY 100
    KKQTRNGLGK DHEILRRRIE NGAKELWFFL QSELKKLKNL EGNELQRHAD 150
    EFLLDLGHHE RSIMTDLYYL SQTDGAGDWR EKEAKDLTEL VQRRITYLQN 200
    PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT LILESQNWRY 250
    ATGGWETVFR PVSETCTDRS GISTGHWSGE VKDKNVQVVE LPIVDSLHPR 300
    PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT 350
    KKLGFKHPVI GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD 400
    KKRVYLATDD PSLLKEAKTK YPNYEFISDN SISWSAGLHN RYTENSLRGV 450
    ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ TLHPDASANF HSLDDIYYFG 500
    GQNAHNQIAI YAHQPRTADE IPMEPGDIIG VAGNHWDGYS KGVNRKLGRT 550
    GLYPSYKVRE KIETVKYPTY PEAEK 575
    Length:575
    Mass (Da):66,516
    Last modified:March 5, 2002 - v2
    Checksum:i5AE24A93881E18D0
    GO
    Isoform 2 (identifier: Q9BYC5-2) [UniParc]FASTAAdd to Basket

    Also known as: Retinal

    The sequence of this isoform differs from the canonical sequence as follows:
         280-329: EVKDKNVQVV...HGDPAVWWVS → TPIMNLLVITLFPGQLDCTIDTQKIHFVE
         330-575: Missing.

    Show »
    Length:308
    Mass (Da):35,795
    Checksum:iFB52A33CFD91A366
    GO
    Isoform 3 (identifier: Q9BYC5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-163: Missing.

    Show »
    Length:412
    Mass (Da):47,255
    Checksum:i837F36AF48E7E4C3
    GO
    Isoform 4 (identifier: Q9BYC5-4) [UniParc]FASTAAdd to Basket

    Also known as: Retina-1, Retina-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: MRPWTGSWRWIMLI → MHRQIWHLHWTLVR
         15-420: Missing.

    Note: Seems to be only expressed in retina, inactive as a fucosyltransferase.

    Show »
    Length:169
    Mass (Da):19,520
    Checksum:i0ACD43AA0F56AB31
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti214 – 2141I → T in BAG57538. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011K → Q.
    Corresponds to variant rs2229678 [ dbSNP | Ensembl ].
    VAR_054038
    Natural varianti267 – 2671T → K.
    Corresponds to variant rs35949016 [ dbSNP | Ensembl ].
    VAR_033537

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 163163Missing in isoform 3. 1 PublicationVSP_046837Add
    BLAST
    Alternative sequencei1 – 1414MRPWT…WIMLI → MHRQIWHLHWTLVR in isoform 4. 2 PublicationsVSP_053361Add
    BLAST
    Alternative sequencei15 – 420406Missing in isoform 4. 2 PublicationsVSP_053362Add
    BLAST
    Alternative sequencei280 – 32950EVKDK…VWWVS → TPIMNLLVITLFPGQLDCTI DTQKIHFVE in isoform 2. 1 PublicationVSP_001807Add
    BLAST
    Alternative sequencei330 – 575246Missing in isoform 2. 1 PublicationVSP_001808Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89289 mRNA. Translation: BAA19764.1.
    AH005745 Genomic DNA. Translation: AAB92372.2.
    Y17979 mRNA. Translation: CAA76988.1.
    Y17976 mRNA. Translation: CAA76985.1.
    Y17977 mRNA. Translation: CAA76986.1.
    Y17978 mRNA. Translation: CAA76987.1.
    AB049828 Genomic DNA. Translation: BAB40975.1.
    AB049740 mRNA. Translation: BAB40929.2.
    AB032573 Genomic DNA. Translation: BAA92859.2.
    AB032573 Genomic DNA. Translation: BAA92858.1.
    AJ514324 mRNA. Translation: CAD55804.1.
    AJ514325 mRNA. Translation: CAD55805.1.
    AK294242 mRNA. Translation: BAG57538.1.
    AL109847 Genomic DNA. No translation available.
    AL161871 Genomic DNA. No translation available.
    AL355840 Genomic DNA. No translation available.
    AL359236 Genomic DNA. No translation available.
    BC093889 mRNA. Translation: AAH93889.1.
    BC101816 mRNA. Translation: AAI01817.1.
    CCDSiCCDS9775.1. [Q9BYC5-1]
    CCDS9776.2. [Q9BYC5-3]
    PIRiJC5432.
    RefSeqiNP_004471.4. NM_004480.4. [Q9BYC5-3]
    NP_835368.1. NM_178155.2. [Q9BYC5-1]
    NP_835369.1. NM_178156.2. [Q9BYC5-1]
    XP_006720159.1. XM_006720096.1. [Q9BYC5-1]
    XP_006720160.1. XM_006720097.1. [Q9BYC5-1]
    UniGeneiHs.597649.
    Hs.654961.

    Genome annotation databases

    EnsembliENST00000342677; ENSP00000345865; ENSG00000033170. [Q9BYC5-2]
    ENST00000360689; ENSP00000353910; ENSG00000033170. [Q9BYC5-1]
    ENST00000394586; ENSP00000378087; ENSG00000033170. [Q9BYC5-1]
    ENST00000557164; ENSP00000452433; ENSG00000033170. [Q9BYC5-3]
    GeneIDi2530.
    KEGGihsa:2530.
    UCSCiuc001xin.3. human. [Q9BYC5-1]

    Polymorphism databases

    DMDMi20138326.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Fucosyltransferase 8

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89289 mRNA. Translation: BAA19764.1 .
    AH005745 Genomic DNA. Translation: AAB92372.2 .
    Y17979 mRNA. Translation: CAA76988.1 .
    Y17976 mRNA. Translation: CAA76985.1 .
    Y17977 mRNA. Translation: CAA76986.1 .
    Y17978 mRNA. Translation: CAA76987.1 .
    AB049828 Genomic DNA. Translation: BAB40975.1 .
    AB049740 mRNA. Translation: BAB40929.2 .
    AB032573 Genomic DNA. Translation: BAA92859.2 .
    AB032573 Genomic DNA. Translation: BAA92858.1 .
    AJ514324 mRNA. Translation: CAD55804.1 .
    AJ514325 mRNA. Translation: CAD55805.1 .
    AK294242 mRNA. Translation: BAG57538.1 .
    AL109847 Genomic DNA. No translation available.
    AL161871 Genomic DNA. No translation available.
    AL355840 Genomic DNA. No translation available.
    AL359236 Genomic DNA. No translation available.
    BC093889 mRNA. Translation: AAH93889.1 .
    BC101816 mRNA. Translation: AAI01817.1 .
    CCDSi CCDS9775.1. [Q9BYC5-1 ]
    CCDS9776.2. [Q9BYC5-3 ]
    PIRi JC5432.
    RefSeqi NP_004471.4. NM_004480.4. [Q9BYC5-3 ]
    NP_835368.1. NM_178155.2. [Q9BYC5-1 ]
    NP_835369.1. NM_178156.2. [Q9BYC5-1 ]
    XP_006720159.1. XM_006720096.1. [Q9BYC5-1 ]
    XP_006720160.1. XM_006720097.1. [Q9BYC5-1 ]
    UniGenei Hs.597649.
    Hs.654961.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DE0 X-ray 2.61 X 68-575 [» ]
    ProteinModelPortali Q9BYC5.
    SMRi Q9BYC5. Positions 108-572.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108806. 6 interactions.
    IntActi Q9BYC5. 2 interactions.
    STRINGi 9606.ENSP00000353910.

    Protein family/group databases

    CAZyi GT23. Glycosyltransferase Family 23.

    PTM databases

    PhosphoSitei Q9BYC5.

    Polymorphism databases

    DMDMi 20138326.

    Proteomic databases

    MaxQBi Q9BYC5.
    PaxDbi Q9BYC5.
    PRIDEi Q9BYC5.

    Protocols and materials databases

    DNASUi 2530.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342677 ; ENSP00000345865 ; ENSG00000033170 . [Q9BYC5-2 ]
    ENST00000360689 ; ENSP00000353910 ; ENSG00000033170 . [Q9BYC5-1 ]
    ENST00000394586 ; ENSP00000378087 ; ENSG00000033170 . [Q9BYC5-1 ]
    ENST00000557164 ; ENSP00000452433 ; ENSG00000033170 . [Q9BYC5-3 ]
    GeneIDi 2530.
    KEGGi hsa:2530.
    UCSCi uc001xin.3. human. [Q9BYC5-1 ]

    Organism-specific databases

    CTDi 2530.
    GeneCardsi GC14P065877.
    HGNCi HGNC:4019. FUT8.
    HPAi CAB017129.
    HPA040863.
    HPA043410.
    MIMi 602589. gene.
    neXtProti NX_Q9BYC5.
    PharmGKBi PA28435.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG251249.
    HOGENOMi HOG000007175.
    HOVERGENi HBG028260.
    InParanoidi Q9BYC5.
    KOi K00717.
    OMAi RMHVDKK.
    OrthoDBi EOG7N37C3.
    PhylomeDBi Q9BYC5.
    TreeFami TF106108.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.68. 2681.
    Reactomei REACT_25302. Reactions specific to the complex N-glycan synthesis pathway.

    Miscellaneous databases

    ChiTaRSi FUT8. human.
    EvolutionaryTracei Q9BYC5.
    GeneWikii FUT8.
    GenomeRNAii 2530.
    NextBioi 13637592.
    PROi Q9BYC5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BYC5.
    Bgeei Q9BYC5.
    CleanExi HS_FUT8.
    Genevestigatori Q9BYC5.

    Family and domain databases

    InterProi IPR015827. Alpha1_6FUT_euk.
    IPR027350. GT23_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000472. Alpha1_6FUT_euk. 1 hit.
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51659. GT23. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human gastric cancer MKN45 cells."
      Yanagidani S., Uozumi N., Ihara Y., Miyoshi E., Yamaguchi N., Taniguchi N.
      J. Biochem. 121:626-632(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    2. "Differential splice variants of human FUT8 embryonic cDNA."
      Cailleau A., Balanzino L., Candelier J.J., Oriol R., Mollicone R.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Embryo.
    3. "Genomic structure and promoter analysis of the human alpha1,6-fucosyltransferase gene (FUT8)."
      Yamaguchi Y., Ikeda Y., Takahashi T., Ihara H., Tanaka T., Sasho C., Uozumi N., Yanagidani S., Inoue S., Fujii J., Taniguchi N.
      Glycobiology 10:637-643(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
    4. "Activity and tissue distribution of splice variants of alpha6-fucosyltransferase in human embryogenesis."
      Martinez-Duncker I., Michalski J.C., Bauvy C., Candelier J.J., Mennesson B., Codogno P., Oriol R., Mollicone R.
      Glycobiology 14:13-25(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING.
      Tissue: Embryo.
    5. "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).
      Tissue: Amygdala.
    6. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      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 4).
      Tissue: Lung.
    8. "A sequence motif involved in the donor substrate binding by alpha1,6-fucosyltransferase: the role of the conserved arginine residues."
      Takahashi T., Ikeda Y., Tateishi A., Yamaguchi Y., Ishikawa M., Taniguchi N.
      Glycobiology 10:503-510(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DONOR SUBSTRATE-BINDING, MUTAGENESIS OF ARG-365 AND ARG-366.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 68-575, FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BOND, MUTAGENESIS OF ARG-365; ASP-368; LYS-369; GLU-373; TYR-382; ASP-409; ASP-410; ASP-453 AND SER-469.

    Entry informationi

    Entry nameiFUT8_HUMAN
    AccessioniPrimary (citable) accession number: Q9BYC5
    Secondary accession number(s): B4DFS7
    , G3V5N0, O00235, Q8IUA5, Q9BYC6, Q9P2U5, Q9P2U6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: March 5, 2002
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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