ALG13

Protein-coding gene in humans
ALG13
Identifiers
AliasesALG13, CDG1S, CXorf45, GLT28D1, MDS031, TDRD13, YGL047W, EIEE36, UDP-N-acetylglucosaminyltransferase subunit, ALG13 UDP-N-acetylglucosaminyltransferase subunit, DEE36
External IDsOMIM: 300776; MGI: 1914824; HomoloGene: 78772; GeneCards: ALG13; OMA:ALG13 - orthologs
Gene location (Human)
X chromosome (human)
Chr.X chromosome (human)[1]
X chromosome (human)
Genomic location for ALG13
Genomic location for ALG13
BandXq23Start111,665,811 bp[1]
End111,760,649 bp[1]
Gene location (Mouse)
X chromosome (mouse)
Chr.X chromosome (mouse)[2]
X chromosome (mouse)
Genomic location for ALG13
Genomic location for ALG13
BandX|X F2Start143,100,800 bp[2]
End143,157,446 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • right uterine tube

  • endothelial cell

  • mucosa of sigmoid colon

  • canal of the cervix

  • left ovary

  • body of uterus

  • anterior pituitary

  • left uterine tube

  • right ovary
Top expressed in
  • zygote

  • morula

  • primary oocyte

  • secondary oocyte

  • tail of embryo

  • embryo

  • yolk sac

  • blastocyst

  • spermatid

  • genital tubercle
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • thiol-dependent deubiquitinase
  • transferase activity
  • peptidase activity
  • cysteine-type peptidase activity
  • hexosyltransferase activity
  • protein binding
  • catalytic activity
  • hydrolase activity
  • glycosyltransferase activity
  • N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity
  • RNA binding
Cellular component
  • endoplasmic reticulum membrane
  • endoplasmic reticulum
  • UDP-N-acetylglucosamine transferase complex
Biological process
  • metabolism
  • proteolysis
  • dolichol-linked oligosaccharide biosynthetic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

79868

67574

Ensembl

ENSG00000101901

ENSMUSG00000041718

UniProt

Q9NP73

Q9D8C3

RefSeq (mRNA)
NM_001039210
NM_001099922
NM_001168385
NM_001257230
NM_001257231

NM_001257234
NM_001257235
NM_001257237
NM_001257239
NM_001257240
NM_001257241
NM_018466
NM_001324290
NM_001324291
NM_001324292
NM_001324293
NM_001324294
NM_024810

NM_026247

RefSeq (protein)
NP_001034299
NP_001093392
NP_001161857
NP_001244159
NP_001244160

NP_001244163
NP_001244164
NP_001244166
NP_001244168
NP_001244169
NP_001244170
NP_001311219
NP_001311220
NP_001311221
NP_001311222
NP_001311223
NP_060936

NP_080523

Location (UCSC)Chr X: 111.67 – 111.76 MbChr X: 143.1 – 143.16 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

UDP-N-acetylglucosamine transferase subunit ALG13 homolog, also known as asparagine-linked glycosylation 13 homolog, is an enzyme that in humans is encoded by the ALG13 gene.[5][6]

Function

The protein encoded by this gene is a subunit of a bipartite UDP-N-acetylglucosamine transferase. It heterodimerizes with asparagine-linked glycosylation 14 (ALG14) homolog to form a functional UDP-GlcNAc glycosyltransferase that catalyzes the second sugar addition of the highly conserved oligosaccharide precursor in endoplasmic reticulum N-linked glycosylation.[5][7]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101901 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000041718 – 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. ^ a b "Entrez Gene: asparagine-linked glycosylation 13 homolog (S. cerevisiae)".
  6. ^ Gao XD, Tachikawa H, Sato T, Jigami Y, Dean N (October 2005). "Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation". J. Biol. Chem. 280 (43): 36254–62. doi:10.1074/jbc.M507569200. PMID 16100110.
  7. ^ Averbeck N, Keppler-Ross S, Dean N (October 2007). "Membrane topology of the Alg14 endoplasmic reticulum UDP-GlcNAc transferase subunit". J. Biol. Chem. 282 (40): 29081–8. doi:10.1074/jbc.M704410200. PMID 17686769.

External links

Further reading

  • Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. Bibcode:2005Natur.434..325R. doi:10.1038/nature03440. PMC 2665286. PMID 15772651.
  • Mizuochi T, Matthews TJ, Kato M, et al. (1990). "Diversity of oligosaccharide structures on the envelope glycoprotein gp 120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N-acetylglucosamine residues". J. Biol. Chem. 265 (15): 8519–24. doi:10.1016/S0021-9258(19)38919-7. PMID 2341393.
  • Shimizu H, Tsuchie H, Honma H, et al. (1990). "Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins". Jpn. J. Med. Sci. Biol. 43 (3): 75–87. doi:10.7883/yoken1952.43.75. PMID 2283726.
  • Yeh JC, Seals JR, Murphy CI, et al. (1993). "Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system". Biochemistry. 32 (41): 11087–99. doi:10.1021/bi00092a019. PMID 8218172.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • 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.
  • Oh JH, Yang JO, Hahn Y, et al. (2005). "Transcriptome analysis of human gastric cancer". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674. S2CID 69278.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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.
  • Epplen C, Epplen JT (1994). "Expression of (cac)n/(gtg)n simple repetitive sequences in mRNA of human lymphocytes". Hum. Genet. 93 (1): 35–41. doi:10.1007/BF00218910. PMID 7505766. S2CID 22998633.
  • Venter JC, Adams MD, Myers EW, et al. (2001). "The sequence of the human genome". Science. 291 (5507): 1304–51. Bibcode:2001Sci...291.1304V. doi:10.1126/science.1058040. PMID 11181995.
  • Kozarsky K, Penman M, Basiripour L, et al. (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". J. Acquir. Immune Defic. Syndr. 2 (2): 163–9. PMID 2649653.


  • v
  • t
  • e