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Q9BYC5 (FUT8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-(1,6)-fucosyltransferase

Short name=Alpha1-6FucT
EC=2.4.1.68
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 names
Name:FUT8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

Sequence similarities

Belongs to the glycosyltransferase 23 family.

Contains 1 GT23 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH3 domain
SH3-binding
Signal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-fucose catabolic process

Non-traceable author statement PubMed 11698403. Source: UniProtKB

N-glycan processing

Traceable author statement PubMed 11698403. Source: UniProtKB

cell migration

Inferred from electronic annotation. Source: Compara

in utero embryonic development

Non-traceable author statement PubMed 11698403. Source: UniProtKB

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: Compara

oligosaccharide biosynthetic process

Traceable author statement Ref.1. Source: ProtInc

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein glycosylation in Golgi

Inferred from electronic annotation. Source: InterPro

receptor metabolic process

Inferred from electronic annotation. Source: Compara

respiratory gaseous exchange

Inferred from electronic annotation. Source: Compara

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Compara

   Cellular_componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglycoprotein 6-alpha-L-fucosyltransferase activity

Traceable author statement PubMed 11698403. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BYC5-1)

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.
Isoform 2 (identifier: Q9BYC5-2)

Also known as: Retinal;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Alpha-(1,6)-fucosyltransferase
PRO_0000080526

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain31 – 575545Lumenal Potential
Domain206 – 493288GT23
Domain502 – 56362SH3
Region365 – 3662Important for donor substrate binding
Motif299 – 3057SH3-binding Potential

Natural variations

Alternative sequence280 – 32950EVKDK…VWWVS → TPIMNLLVITLFPGQLDCTI DTQKIHFVE in isoform 2.
VSP_001807
Alternative sequence330 – 575246Missing in isoform 2.
VSP_001808
Natural variant1011K → Q.
Corresponds to variant rs2229678 [ dbSNP | Ensembl ].
VAR_054038
Natural variant2671T → K.
Corresponds to variant rs35949016 [ dbSNP | Ensembl ].
VAR_033537

Experimental info

Mutagenesis3651R → A or K: Complete loss of activity. Ref.4
Mutagenesis3661R → A or K: Decreases activity to 3%. Ref.4

Secondary structure

.............................................................. 575
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 5, 2002. Version 2.
Checksum: 5AE24A93881E18D0

FASTA57566,516
        10         20         30         40         50         60 
MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL ERLKQQNEDL 

        70         80         90        100        110        120 
RRMAESLRIP EGPIDQGPAI GRVRVLEEQL VKAKEQIENY KKQTRNGLGK DHEILRRRIE 

       130        140        150        160        170        180 
NGAKELWFFL QSELKKLKNL EGNELQRHAD EFLLDLGHHE RSIMTDLYYL SQTDGAGDWR 

       190        200        210        220        230        240 
EKEAKDLTEL VQRRITYLQN PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT 

       250        260        270        280        290        300 
LILESQNWRY ATGGWETVFR PVSETCTDRS GISTGHWSGE VKDKNVQVVE LPIVDSLHPR 

       310        320        330        340        350        360 
PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT KKLGFKHPVI 

       370        380        390        400        410        420 
GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD KKRVYLATDD PSLLKEAKTK 

       430        440        450        460        470        480 
YPNYEFISDN SISWSAGLHN RYTENSLRGV ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ 

       490        500        510        520        530        540 
TLHPDASANF HSLDDIYYFG GQNAHNQIAI YAHQPRTADE IPMEPGDIIG VAGNHWDGYS 

       550        560        570 
KGVNRKLGRT GLYPSYKVRE KIETVKYPTY PEAEK 

« Hide

Isoform 2 (Retinal) [UniParc].

Checksum: FB52A33CFD91A366
Show »

FASTA30835,795

References

[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 (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 (ISOFORMS 1 AND 2).
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00004668.
IPI00215828.
PIRJC5432.
RefSeqNP_835368.1. NM_178155.2.
NP_835369.1. NM_178156.2.
UniGeneHs.597649.
Hs.654961.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DE0X-ray2.61X68-575[»]
ProteinModelPortalQ9BYC5.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9BYC5. 2 interactions.
STRING9606.ENSP00000353910.

Protein family/group databases

CAZyGT23. Glycosyltransferase Family 23.

PTM databases

PhosphoSiteQ9BYC5.

Polymorphism databases

DMDM20138326.

Proteomic databases

PaxDbQ9BYC5.
PRIDEQ9BYC5.

Protocols and materials databases

DNASU2530.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342677; ENSP00000345865; ENSG00000033170.
ENST00000360689; ENSP00000353910; ENSG00000033170.
ENST00000394585; ENSP00000378086; ENSG00000033170.
ENST00000394586; ENSP00000378087; ENSG00000033170.
GeneID2530.
KEGGhsa:2530.
UCSCuc001xin.3. human.

Organism-specific databases

CTD2530.
GeneCardsGC14P065877.
HGNCHGNC:4019. FUT8.
HPACAB017129.
HPA043410.
MIM602589. gene.
neXtProtNX_Q9BYC5.
PharmGKBPA28435.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251249.
HOGENOMHOG000007175.
HOVERGENHBG028260.
InParanoidQ9BYC5.
KOK00717.
OMARKLVCNI.
OrthoDBEOG4JWVD1.

Enzyme and pathway databases

BRENDA2.4.1.68. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9BYC5.
BgeeQ9BYC5.
CleanExHS_FUT8.
GenevestigatorQ9BYC5.
GermOnlineENSG00000033170. Homo sapiens.

Family and domain databases

InterProIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PIRSFPIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SH3. 1 hit.
PROSITEPS51659. GT23. 1 hit.
PS50002. SH3. False negative.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFUT8. human.
EvolutionaryTraceQ9BYC5.
GenomeRNAi2530.
NextBio9971.
SOURCESearch...

Entry information

Entry nameFUT8_HUMAN
AccessionPrimary (citable) accession number: Q9BYC5
Secondary accession number(s): O00235 expand/collapse secondary AC list , Q9BYC6, Q9P2U5, Q9P2U6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: May 29, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families