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Search results 101 to 126 out of 126 for Fut8

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0.017s

Type

Details

Score

Publication

- | J:164563

First Author:	The Gene Ontology Consortium
Year:	2010

Title:	Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs

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Publication

- | J:157972

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2010
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).

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Publication

- | J:161428

First Author:	Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year:	2010

Title:	Annotation inferences using phylogenetic trees

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Publication

- | J:85324

First Author:	Mouse Genome Informatics Group
Year:	2003
Journal:	Database Procedure
Title:	Automatic Encodes (AutoE) Reference

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Publication

- | J:144086

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2009
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform

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Publication

- | J:144087

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2009
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform

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Publication

- | J:53168

First Author:	Bairoch A
Year:	1999
Journal:	Database Release
Title:	SWISS-PROT Annotated protein sequence database

•

Publication

- | J:90438

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and loading genome assembly coordinates from NCBI annotations

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Publication

- | J:63103

First Author:	Mouse Genome Database and National Center for Biotechnology Information
Year:	2000
Journal:	Database Release
Title:	Entrez Gene Load

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Publication

- | J:155721

First Author:	Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year:	2010
Journal:	Database Download
Title:	Consensus CDS project

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Publication

- | J:155221

First Author:	Mouse Genome Informatics
Year:	2010
Journal:	Database Release
Title:	Protein Ontology Association Load.

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Publication

- | J:262123

First Author:	Allen Institute for Brain Science
Year:	2004
Journal:	Allen Institute
Title:	Allen Brain Atlas: mouse riboprobes

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Publication

- | J:91388

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations

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Protein Domain

IPR035653 | Fut8_SH3

Type:

Domain

Description:

Alpha-(1,6)-fucosyltransferase Fut8 catalyses the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation, early death, and a pulmonary emphysema-like phenotype []. Fut8 is also implicated to play roles in ageing []and cancer metastasis []. It contains an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The SH3 domain of Fut8 is located in the lumen and its role in glycosyl transfer is unclear []. This entry represents the SH3 domain of Fut8.

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Protein Domain

IPR045573 | Fut8_N_cat

Type:

Domain

Description:

This domain includes the N-terminal coil-coiled domain and the catalytic domain of alpha-(1,6)-fucosyltransferase Fut8. The catalytic domain comprises two structures, an open sheet α/β structure, which contains five helices and three β-strands at the N-terminal, and a Rossmann fold that contains five helices and five β-strands at the C-terminal. The latter is conserved among the alpha1,2-, alpha1,6-, and protein O-fucosyltransferases and is similar to GT-B group glycosyltransferases [].Alpha-(1,6)-fucosyltransferase Fut8 catalyses the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation, early death, and a pulmonary emphysema-like phenotype []. Fut8 is also implicated to play roles in ageing []and cancer metastasis []. It contains an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The SH3 domain of Fut8 is located in the lumen and its role in glycosyl transfer is unclear [].

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Publication

9368041 | J:44172

First Author:	Costache M
Year:	1997
Journal:	J Biol Chem
Title:	Evolution of fucosyltransferase genes in vertebrates.
Volume:	272
Issue:	47
Pages:	29721-8

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Protein

B2X2D8

Organism:	Mus musculus/domesticus
Length:	386
Fragment?:	false

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Protein

B2X2D7

Organism:	Mus musculus/domesticus
Length:	412
Fragment?:	false

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Publication

17762900 | -

First Author:	Brzezinski K
Year:	2007
Journal:	Acta Biochim Pol
Title:	High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor.
Volume:	54
Issue:	3
Pages:	537-49

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Publication

22281745 | -

First Author:	Brzezinski K
Year:	2012
Journal:	Acta Crystallogr D Biol Crystallogr
Title:	Structures of NodZ α1,6-fucosyltransferase in complex with GDP and GDP-fucose.
Volume:	68
Issue:	Pt 2
Pages:	160-8

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Publication

20466647 | -

First Author:	Ihara H
Year:	2010
Journal:	Glycobiology
Title:	Fucosylation of chitooligosaccharides by human alpha1,6-fucosyltransferase requires a nonreducing terminal chitotriose unit as a minimal structure.
Volume:	20
Issue:	8
Pages:	1021-33

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Protein Domain

IPR027350 | GT23_dom

Type:

Domain

Description:

The fucosylation of glycoconjugates in mammalian organisms is related to awide variety of biological preocesses, including cell adhesion, blood antigens, and some severe diseases including cancer metastasis, congenital disorders of glycosylation, and various microbial and virus infections. Fucosylation via alpha1,2-, alpha1,3- alpha1,4, and alpha1,6-linkages, and protein O-fucosylation are accomplished by the cation of specific individual fucosyltransferases [].FUT8, a eukaryotic alpha1,6-fucosyltransferase, catalyses the transfer of afucosyl residue from guanine nucleotide diphosphate (GDP)-beta-L-fucose to thereducing terminal N-acetylglucosamine (GlcNAc) of asparagine-linkedoligosaccharides (N-glycan). The catalytic domain of FUT8 is structurallysimilar to that of BodZ, a bacterial alpha1,6-fucosyltransferase. NodZ plays arole in the synthesis of the Nod factor, which is involved in the nodulationof legume roots for nitrogen fixing, and is known to catalyse the alpha1,6-fucosylation of lipo-chitooligosaccharides and variations thereof, includingchitooligosaccharides. Both the eukaryotic and bacterial fucoslytransferaseare classified into the GT23 family of Carbohydrate-Active enZYmes and share GDP-beta-L-fucose as the donor substrate. Although the acceptor substrates are different, a "common"chitobiose unit is contained in the reducing terminals of both substrates [].The GT23 domain is comprised of two structures, a N-terminal open sheet alpha/beta structure and a C-terminal Rossmann fold which is frequently found innucleotide binding proteins including glycosyltransferases[, , ]. The entry represents the GT23 domain.

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Publication

25531332 | J:224797

First Author:	Kumar S
Year:	2015
Journal:	Oncogene
Title:	NCOA3-mediated upregulation of mucin expression via transcriptional and post-translational changes during the development of pancreatic cancer.
Volume:	34
Issue:	37
Pages:	4879-89

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Publication

36692036 | J:348482

First Author:	Jin LW
Year:	2023
Journal:	Glia
Title:	The role of FUT8-catalyzed core fucosylation in Alzheimer's amyloid-β oligomer-induced activation of human microglia.
Volume:	71
Issue:	5
Pages:	1346-1359

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Publication

32999320 | J:296393

First Author:	Chen YT
Year:	2020
Journal:	Sci Rep
Title:	NT5C2 methylation regulatory interplay between DNMT1 and insulin receptor in type 2 diabetes.
Volume:	10
Issue:	1
Pages:	16087

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Publication

28706275 | J:252366

First Author:	Yu M
Year:	2017
Journal:	Sci Rep
Title:	Novel function of pregnancy-associated plasma protein A: promotes endometrium receptivity by up-regulating N-fucosylation.
Volume:	7
Issue:	1
Pages:	5315

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