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Q9BYC5

- FUT8_HUMAN

UniProt

Q9BYC5 - FUT8_HUMAN

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Protein

Alpha-(1,6)-fucosyltransferase

Gene

FUT8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini31 – 575545LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ9BYC5.
PaxDbiQ9BYC5.
PRIDEiQ9BYC5.

PTM databases

PhosphoSiteiQ9BYC5.

Expressioni

Gene expression databases

BgeeiQ9BYC5.
CleanExiHS_FUT8.
ExpressionAtlasiQ9BYC5. baseline and differential.
GenevestigatoriQ9BYC5.

Organism-specific databases

HPAiCAB017129.
HPA040863.
HPA043410.

Interactioni

Protein-protein interaction databases

BioGridi108806. 16 interactions.
IntActiQ9BYC5. 2 interactions.
STRINGi9606.ENSP00000353910.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9BYC5.

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.
GeneTreeiENSGT00530000063737.
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

        10         20         30         40         50
MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL
60 70 80 90 100
ERLKQQNEDL RRMAESLRIP EGPIDQGPAI GRVRVLEEQL VKAKEQIENY
110 120 130 140 150
KKQTRNGLGK DHEILRRRIE NGAKELWFFL QSELKKLKNL EGNELQRHAD
160 170 180 190 200
EFLLDLGHHE RSIMTDLYYL SQTDGAGDWR EKEAKDLTEL VQRRITYLQN
210 220 230 240 250
PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT LILESQNWRY
260 270 280 290 300
ATGGWETVFR PVSETCTDRS GISTGHWSGE VKDKNVQVVE LPIVDSLHPR
310 320 330 340 350
PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT
360 370 380 390 400
KKLGFKHPVI GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD
410 420 430 440 450
KKRVYLATDD PSLLKEAKTK YPNYEFISDN SISWSAGLHN RYTENSLRGV
460 470 480 490 500
ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ TLHPDASANF HSLDDIYYFG
510 520 530 540 550
GQNAHNQIAI YAHQPRTADE IPMEPGDIIG VAGNHWDGYS KGVNRKLGRT
560 570
GLYPSYKVRE KIETVKYPTY PEAEK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 16 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.
GeneTreei ENSGT00530000063737.
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

Bgeei Q9BYC5.
CleanExi HS_FUT8.
ExpressionAtlasi Q9BYC5. baseline and differential.
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

« Hide 'large scale' publications
  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: PHOSPHORYLATION.
  10. 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: November 26, 2014
This is version 139 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