EXTL2

Protein-coding gene in the species Homo sapiens
EXTL2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1OMX, 1OMZ, 1ON6, 1ON8

Identifiers
AliasesEXTL2, EXTR2, exostosin-like glycosyltransferase 2, exostosin like glycosyltransferase 2
External IDsOMIM: 602411; MGI: 1889574; HomoloGene: 1102; GeneCards: EXTL2; OMA:EXTL2 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for EXTL2
Genomic location for EXTL2
Band1p21.2Start100,872,372 bp[1]
End100,895,179 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for EXTL2
Genomic location for EXTL2
Band3|3 G1Start115,801,111 bp[2]
End115,822,666 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • periodontal fiber

  • postcentral gyrus

  • Brodmann area 46

  • lateral nuclear group of thalamus

  • ventricular zone

  • right adrenal cortex

  • superior frontal gyrus

  • left adrenal gland

  • left adrenal cortex

  • stromal cell of endometrium
Top expressed in
  • facial motor nucleus

  • motor neuron

  • substantia nigra

  • anterior horn of spinal cord

  • lobe of cerebellum

  • cerebellar vermis

  • pineal gland

  • habenula

  • deep cerebellar nuclei

  • medial vestibular nucleus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity
  • metal ion binding
  • glycosyltransferase activity
  • glycosaminoglycan binding
  • manganese ion binding
  • alpha-1,4-N-acetylgalactosaminyltransferase activity
  • glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity
Cellular component
  • integral component of membrane
  • extracellular region
  • endoplasmic reticulum
  • membrane
  • endoplasmic reticulum membrane
Biological process
  • heparan sulfate proteoglycan biosynthetic process
  • N-acetylglucosamine metabolic process
  • UDP-N-acetylgalactosamine metabolic process
  • IRE1-mediated unfolded protein response
  • protein glycosylation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2135

58193

Ensembl

ENSG00000162694

ENSMUSG00000027963

UniProt

Q9UBQ6

Q9ES89

RefSeq (mRNA)

NM_001033025
NM_001261440
NM_001261441
NM_001261442
NM_001439

NM_001163514
NM_001163515
NM_021388

RefSeq (protein)

NP_001028197
NP_001248369
NP_001248370
NP_001248371
NP_001430

NP_001156986
NP_001156987
NP_067363

Location (UCSC)Chr 1: 100.87 – 100.9 MbChr 3: 115.8 – 115.82 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Exostosin-like 2 is a protein that in humans is encoded by the EXTL2 gene.[5][6][7] EXTL2 Glycosyltransferase is required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains. (https://www.phosphosite.org/overviewExecuteAction?id=5020882)

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000162694 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027963 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Wuyts W, Van Hul W, Hendrickx J, Speleman F, Wauters J, De Boulle K, Van Roy N, Van Agtmael T, Bossuyt P, Willems PJ (Mar 1998). "Identification and characterization of a novel member of the EXT gene family, EXTL2". Eur J Hum Genet. 5 (6): 382–9. doi:10.1159/000484796. PMID 9450183.
  6. ^ Sobhany M, Dong J, Negishi M (Jun 2005). "Two-step mechanism that determines the donor binding specificity of human UDP-N-acetylhexosaminyltransferase". J Biol Chem. 280 (25): 23441–5. doi:10.1074/jbc.M413379200. PMID 15831490.
  7. ^ "Entrez Gene: EXTL2 exostoses (multiple)-like 2".

Further reading

  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • McCormick C, Duncan G, Goutsos KT, Tufaro F (2000). "The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate". Proc. Natl. Acad. Sci. U.S.A. 97 (2): 668–73. Bibcode:2000PNAS...97..668M. doi:10.1073/pnas.97.2.668. PMC 15388. PMID 10639137.
  • Kitagawa H, Shimakawa H, Sugahara K (1999). "The tumor suppressor EXT-like gene EXTL2 encodes an alpha1, 4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate". J. Biol. Chem. 274 (20): 13933–7. doi:10.1074/jbc.274.20.13933. PMID 10318803.
  • Saito T, Seki N, Yamauchi M, et al. (1998). "Structure, chromosomal location, and expression profile of EXTR1 and EXTR2, new members of the multiple exostoses gene family". Biochem. Biophys. Res. Commun. 243 (1): 61–6. doi:10.1006/bbrc.1997.8062. PMID 9473480.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • PDBe-KB provides an overview of all the structure information available in the PDB for Mouse Exostosin-like 2


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