ST3GAL5

Protein-coding gene in the species Homo sapiens
ST3GAL5
Identifiers
AliasesST3GAL5, SATI, SIAT9, SIATGM3S, ST3GalV, ST3 beta-galactoside alpha-2,3-sialyltransferase 5, SPDRS, ST3Gal V
External IDsOMIM: 604402; MGI: 1339963; HomoloGene: 2893; GeneCards: ST3GAL5; OMA:ST3GAL5 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for ST3GAL5
Genomic location for ST3GAL5
Band2p11.2Start85,837,120 bp[1]
End85,905,199 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for ST3GAL5
Genomic location for ST3GAL5
Band6|6 C1Start72,074,576 bp[2]
End72,131,555 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right adrenal gland

  • right adrenal cortex

  • left adrenal gland

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • left adrenal cortex

  • C1 segment

  • lateral nuclear group of thalamus

  • decidua

  • middle temporal gyrus
Top expressed in
  • granulocyte

  • fetal liver hematopoietic progenitor cell

  • adrenal gland

  • soleus muscle

  • blood

  • tibiofemoral joint

  • choroid plexus of fourth ventricle

  • superior frontal gyrus

  • epithelium of lens

  • temporal muscle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • lactosylceramide alpha-2,3-sialyltransferase activity
  • glycosyltransferase activity
  • neolactotetraosylceramide alpha-2,3-sialyltransferase activity
  • sialyltransferase activity
  • beta-galactoside (CMP) alpha-2,3-sialyltransferase activity
Cellular component
  • integral component of membrane
  • Golgi apparatus
  • membrane
  • integral component of plasma membrane
  • Golgi membrane
Biological process
  • glycosphingolipid biosynthetic process
  • protein glycosylation
  • oligosaccharide metabolic process
  • sialylation
  • protein N-linked glycosylation via asparagine
  • ganglioside biosynthetic process
  • carbohydrate metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8869

20454

Ensembl

ENSG00000115525

ENSMUSG00000056091

UniProt

Q9UNP4

O88829

RefSeq (mRNA)
NM_001042437
NM_003896
NM_001354226
NM_001354227
NM_001354233

NM_001354234
NM_001354238
NM_001354247
NM_001354248
NM_001354223
NM_001354224
NM_001354229
NM_001363847

NM_001035228
NM_011375

RefSeq (protein)
NP_001035902
NP_003887
NP_001341155
NP_001341156
NP_001341162

NP_001341163
NP_001341167
NP_001341176
NP_001341177
NP_001341152
NP_001341153
NP_001341158
NP_001350776

NP_001030305
NP_035505

Location (UCSC)Chr 2: 85.84 – 85.91 MbChr 6: 72.07 – 72.13 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Lactosylceramide alpha-2,3-sialyltransferase is an enzyme that in humans is encoded by the ST3GAL5 gene.[5][6]

Ganglioside GM3 is known to participate in the induction of cell differentiation, modulation of cell proliferation, maintenance of fibroblast morphology, signal transduction, and integrin-mediated cell adhesion. The protein encoded by this gene is a type II membrane protein which catalyzes the formation of GM3 using lactosylceramide as the substrate. The encoded protein is a member of glycosyltransferase family 29 and may be localized to the Golgi apparatus. Mutation in this gene has been associated with Amish infantile epilepsy syndrome. Transcript variants encoding different isoforms have been found for this gene.[6]

Mutations in this gene have also been associated to ‘Salt & Pepper’ syndrome: an autosomal recessive condition characterized by severe intellectual disability, epilepsy, scoliosis, choreoathetosis, dysmorphic facial features and altered dermal pigmentation. (doi: 10.1093/hmg/ddt434)

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000115525 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000056091 – 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. ^ Ishii A, Ohta M, Watanabe Y, Matsuda K, Ishiyama K, Sakoe K, Nakamura M, Inokuchi J, Sanai Y, Saito M (Dec 1998). "Expression cloning and functional characterization of human cDNA for ganglioside GM3 synthase". J Biol Chem. 273 (48): 31652–5. doi:10.1074/jbc.273.48.31652. PMID 9822625.
  6. ^ a b "Entrez Gene: ST3GAL5 ST3 beta-galactoside alpha-2,3-sialyltransferase 5".

Further reading

  • 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.
  • Fukumoto S, Miyazaki H, Goto G, et al. (1999). "Expression cloning of mouse cDNA of CMP-NeuAc:Lactosylceramide alpha2,3-sialyltransferase, an enzyme that initiates the synthesis of gangliosides". J. Biol. Chem. 274 (14): 9271–6. doi:10.1074/jbc.274.14.9271. PMID 10092602.
  • Kapitonov D, Bieberich E, Yu RK (2000). "Combinatorial PCR approach to homology-based cloning: cloning and expression of mouse and human GM3-synthase". Glycoconj. J. 16 (7): 337–50. doi:10.1023/A:1007091926413. PMID 10619706. S2CID 24374714.
  • Allende ML, Li J, Darling DS, et al. (2000). "Evidence supporting a late Golgi location for lactosylceramide to ganglioside GM3 conversion". Glycobiology. 10 (10): 1025–32. doi:10.1093/glycob/10.10.1025. PMID 11030748.
  • Kim KW, Kim SW, Min KS, et al. (2001). "Genomic structure of human GM3 synthase gene (hST3Gal V) and identification of mRNA isoforms in the 5'-untranslated region". Gene. 273 (2): 163–71. doi:10.1016/S0378-1119(01)00595-9. PMID 11595162.
  • Kim SW, Lee SH, Kim KS, et al. (2002). "Isolation and characterization of the promoter region of the human GM3 synthase gene". Biochim. Biophys. Acta. 1578 (1–3): 84–9. doi:10.1016/s0167-4781(02)00505-5. PMID 12393190.
  • 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.
  • Zeng G, Gao L, Xia T, et al. (2003). "Characterization of the 5'-flanking fragment of the human GM3-synthase gene". Biochim. Biophys. Acta. 1625 (1): 30–5. doi:10.1016/s0167-4781(02)00573-0. PMID 12527423.
  • Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
  • 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.
  • Chung TW, Choi HJ, Lee YC, Kim CH (2005). "Molecular mechanism for transcriptional activation of ganglioside GM3 synthase and its function in differentiation of HL-60 cells". Glycobiology. 15 (3): 233–44. doi:10.1093/glycob/cwh156. PMID 15385432.
  • Simpson MA, Cross H, Proukakis C, et al. (2004). "Infantile-onset symptomatic epilepsy syndrome caused by a homozygous loss-of-function mutation of GM3 synthase". Nat. Genet. 36 (11): 1225–9. doi:10.1038/ng1460. PMID 15502825.
  • Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMID 15815621.
  • Berselli P, Zava S, Sottocornola E, et al. (2006). "Human GM3 synthase: a new mRNA variant encodes an NH2-terminal extended form of the protein". Biochim. Biophys. Acta. 1759 (7): 348–58. doi:10.1016/j.bbaexp.2006.07.001. PMID 16934889.
  • Szabo R, Skropeta D, et al. (2017). "Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities". Med. Res. Rev. 37 (2): 210–270. doi:10.1002/med.21407. PMID 27678392. S2CID 26280291.


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