|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 201 to 245 out of 245 for Extl2

<< First    < Previous  |  Next >    Last >>
0.019s

Categories

Hits by Pathway

Hits by Strain

Hits by Category

Type Details Score
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
•
•
•
•
•
Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
•
•
•
•
•
Protein
Q9ES89
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
•
•
•
•
•
Publication
9037597 | -
First Author: Wise CA
Year: 1997
Journal: Genome Res
Title: Identification and localization of the gene for EXTL, a third member of the multiple exostoses gene family.
Volume: 7
Issue: 1
Pages: 10-6
•
•
•
•
•
Protein Domain
IPR027675 | Exostosin-like_1
Type: Family
Description: There are five identiied human EXT family proteins (EXT1, EXT2, EXTL1, EXTL2 and EXTL3), which are members of the hereditary multiple exostoses family of tumor suppressors [, ]. Exostosin-like 1 (EXTL1) is a probable glycosyltransferase involved in the biosynthesis of heparan-sulfate [].
•
•
•
•
•
Publication
9620772 | J:113833
First Author: McCormick C
Year: 1998
Journal: Nat Genet
Title: The putative tumour suppressor EXT1 alters the expression of cell-surface heparan sulfate.
Volume: 19
Issue: 2
Pages: 158-61
•
•
•
•
•
Publication
11518722 | -
First Author: Duncan G
Year: 2001
Journal: J Clin Invest
Title: The link between heparan sulfate and hereditary bone disease: finding a function for the EXT family of putative tumor suppressor proteins.
Volume: 108
Issue: 4
Pages: 511-6
•
•
•
•
•
Publication
10545594 | J:58434
First Author: Simmons AD
Year: 1999
Journal: Hum Mol Genet
Title: A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses.
Volume: 8
Issue: 12
Pages: 2155-64
•
•
•
•
•
Protein Domain
IPR027670 | Exostosin-1
Type: Family
Description: There are five identified human EXT family proteins (EXT1, EXT2, EXTL1, EXTL2 and EXTL3), which are members of the hereditary multiple exostoses family of tumor suppressors []. Exostosin-1 (EXT1) is a glycosyltransferase required for the biosynthesis of heparan-sulfate []. Hereditary multiple exostoses, a genetic disorder characterised by multiple cartilaginous tumors, is caused by mutations in members of the EXT gene family, EXT1 or EXT2. EXT1 and EXT2 form a hetero-oligomeric complex that leads to the accumulation of both proteins in the Golgi apparatus [].
•
•
•
•
•
Protein Domain
IPR027673 | Exostosin-2
Type: Family
Description: There are five identified human EXT family proteins (EXT1, EXT2, EXTL1, EXTL2 and EXTL3), which are members of the hereditary multiple exostoses family of tumour suppressors []. Exostosin-2 (EXT2) is a glycosyltransferase required for the biosynthesis of heparan-sulfate []. Hereditary multiple exostoses, a genetic disorder characterised by multiple cartilaginous tumours, is caused by mutations in members of the EXT gene family, EXT1 or EXT2. EXT1 and EXT2 form a hetero-oligomeric complex that leads to the accumulation of both proteins in the Golgi apparatus []. The Golgi-localised EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone [].
•
•
•
•
•
Publication
10639137 | J:113870
First Author: McCormick C
Year: 2000
Journal: Proc Natl Acad Sci U S A
Title: The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate.
Volume: 97
Issue: 2
Pages: 668-73
•
•
•
•
•
Protein
A2AIG6
Organism: Mus musculus/domesticus
Length: 122  
Fragment?: true
•
•
•
•
•
Protein
E9Q1M5
Organism: Mus musculus/domesticus
Length: 407  
Fragment?: false
•
•
•
•
•
Protein
A2AIG3
Organism: Mus musculus/domesticus
Length: 213  
Fragment?: true
•
•
•
•
•
Protein
Q8BUJ1
Organism: Mus musculus/domesticus
Length: 190  
Fragment?: false
•
•
•
•
•
Publication
9473480 | -
First Author: Saito T
Year: 1998
Journal: Biochem Biophys Res Commun
Title: Structure, chromosomal location, and expression profile of EXTR1 and EXTR2, new members of the multiple exostoses gene family.
Volume: 243
Issue: 1
Pages: 61-6
•
•
•
•
•
Publication
17237233 | -
First Author: Kitagawa H
Year: 2007
Journal: J Biol Chem
Title: Expression of rib-1, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes, is indispensable for heparan sulfate synthesis and embryonic morphogenesis.
Volume: 282
Issue: 11
Pages: 8533-44
•
•
•
•
•
Publication
12837954 | -
First Author: Madson M
Year: 2003
Journal: Plant Cell
Title: The MUR3 gene of Arabidopsis encodes a xyloglucan galactosyltransferase that is evolutionarily related to animal exostosins.
Volume: 15
Issue: 7
Pages: 1662-70
•
•
•
•
•
Publication
14998928 | -
First Author: Han C
Year: 2004
Journal: Development
Title: Distinct and collaborative roles of Drosophila EXT family proteins in morphogen signalling and gradient formation.
Volume: 131
Issue: 7
Pages: 1563-75
•
•
•
•
•
Protein Domain
IPR004263 | Exostosin
Type: Family
Description: There are five identified human EXT family proteins (EXT1, EXT2, EXTL1, EXTL2 and EXTL3), which are members of the hereditary multiple exostoses family of tumor suppressors []. They are glycosyltransferases required for the biosynthesis of heparan sulfate. Hereditary multiple exostoses (EXT) is an autosomal dominant disorder that is characterised by the appearance of multiple outgrowths of the long bones (exostoses) at their epiphyses []. Mutations in two homologous genes, EXT1 and EXT2, are responsible for the EXT syndrome. The human and mouse EXT genes have at least two homologues in the invertebrate Caenorhabditis elegans, indicating that they do not function exclusively as regulators of bone growth. EXT1 and EXT2 have both been shown to encode glycosyltransferases involved in the chain elongation step of heparan sulphate biosynthesis [].This entry also includes Arabidopsis Xyloglucan galactosyltransferase KATAMARI1 []and Drosophila melanogaster EXT homologues [].
•
•
•
•
•
Protein
P70428
Organism: Mus musculus/domesticus
Length: 718  
Fragment?: false
•
•
•
•
•
Protein
P97464
Organism: Mus musculus/domesticus
Length: 746  
Fragment?: false
•
•
•
•
•
Protein
Q9JKV7
Organism: Mus musculus/domesticus
Length: 669  
Fragment?: false
•
•
•
•
•
Protein
Q0VAW4
Organism: Mus musculus/domesticus
Length: 669  
Fragment?: false
•
•
•
•
•
Protein
Q3V1P4
Organism: Mus musculus/domesticus
Length: 746  
Fragment?: false
•
•
•
•
•
Protein
Q3UFQ0
Organism: Mus musculus/domesticus
Length: 701  
Fragment?: false
•
•
•
•
•
Protein
Q3T9C7
Organism: Mus musculus/domesticus
Length: 669  
Fragment?: false
•
•
•
•
•
Protein
Q3U8D5
Organism: Mus musculus/domesticus
Length: 690  
Fragment?: true
•
•
•
•
•
Protein
V9GX32
Organism: Mus musculus/domesticus
Length: 586  
Fragment?: false
•
•
•
•
•
Protein
Q3UDB5
Organism: Mus musculus/domesticus
Length: 786  
Fragment?: true
•
•
•
•
•
Protein
Q3UYR9
Organism: Mus musculus/domesticus
Length: 435  
Fragment?: true
•
•
•
•
•
Protein
Q3TSP4
Organism: Mus musculus/domesticus
Length: 636  
Fragment?: true
•
•
•
•
•
Publication
20377530 | J:163045
First Author: Okada M
Year: 2010
Journal: Biochem J
Title: Biosynthesis of heparan sulfate in EXT1-deficient cells.
Volume: 428
Issue: 3
Pages: 463-71
•
•
•
•
•
Publication
9756849 | -
First Author: Lind T
Year: 1998
Journal: J Biol Chem
Title: The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate.
Volume: 273
Issue: 41
Pages: 26265-8
•
•
•
•
•
Publication
10864928 | J:64512
First Author: Wei G
Year: 2000
Journal: J Biol Chem
Title: Location of the glucuronosyltransferase domain in the heparan sulfate copolymerase EXT1 by analysis of Chinese hamster ovary cell mutants.
Volume: 275
Issue: 36
Pages: 27733-40
•
•
•
•
•
Publication
14659703 | -
First Author: Zhong R
Year: 2003
Journal: Trends Plant Sci
Title: Unraveling the functions of glycosyltransferase family 47 in plants.
Volume: 8
Issue: 12
Pages: 565-8
•
•
•
•
•
Protein Domain
IPR040911 | Exostosin_GT47
Type: Domain
Description: There are five identified human EXT family proteins (EXT1, EXT2, EXTL1, EXTL2 and EXTL3), which are members of the hereditary multiple exostoses family of tumor suppressors []. They are glycosyltransferases required for the biosynthesis of heparan sulfate. Hereditary multiple exostoses (EXT) is an autosomal dominant disorder that is characterised by the appearance of multiple outgrowths of the long bones (exostoses) at their epiphyses []. Mutations in two homologous genes, EXT1 and EXT2, are responsible for the EXT syndrome. The human and mouse EXT genes have at least two homologues in the invertebrate Caenorhabditis elegans, indicating that they do not function exclusively as regulators of bone growth. EXT1 and EXT2 have both been shown to encode glycosyltransferases involved in the chain elongation step of heparan sulphate biosynthesis [].In addition to a b-glucuronyltransferase domain, exostosins contain anadditional alpha 1,4-N-acetylglucosaminyltransferase domain that belongs to family GT64 [, ]. Activities of both exostosin GT domains are required for synthesizing the backbone of glycosaminoglycan, heparan sulfate. In plants, many genes have been shown to encode proteins with significant sequence similarity to the exostosinb-glucuronyltransferase domain and therefore are grouped into family GT47 []. This entry represents the GT47 domain of exostosins.
•
•
•
•
•
Protein
Q9WVL6
Organism: Mus musculus/domesticus
Length: 918  
Fragment?: false
•
•
•
•
•
Protein
Q6P1H4
Organism: Mus musculus/domesticus
Length: 919  
Fragment?: false
•
•
•
•
•
Protein
Q5DU26
Organism: Mus musculus/domesticus
Length: 921  
Fragment?: true
•
•
•
•
•
Protein
Q3UUW7
Organism: Mus musculus/domesticus
Length: 832  
Fragment?: true
•
•
•
•
•
Protein
Q3TXF7
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
•
•
•
•
•
Protein
Q8C197
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
•
•
•
•
•
Protein
Q8C089
Organism: Mus musculus/domesticus
Length: 274  
Fragment?: true
•
•
•
•
•
Protein
Q3TSR0
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom