ST6GALNAC4

ST6GALNAC4

Identifiers

ST6GALNAC4, IV, SIAT3-C, SIAT3C, SIAT7-D, SIAT7D, ST6GALNACIV, ST6GalNAc, ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 4

External IDs

OMIM: 606378; MGI: 1341894; HomoloGene: 7939; GeneCards: ST6GALNAC4; OMA:ST6GALNAC4 - orthologs

Gene location (Human)

Chr.	Chromosome 9 (human)^[1]

Band	9q34.11	Start	127,907,886 bp^[1]
Band	9q34.11	End	127,917,041 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)^[2]

Band	2\|2 B	Start	32,477,107 bp^[2]
Band	2\|2 B	End	32,489,710 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

body of pancreas

upper lobe of left lung

spleen

right coronary artery

left ventricle

left coronary artery

blood

trabecular bone

bone marrow

stromal cell of endometrium

Top expressed in

cerebellar cortex

superior frontal gyrus

left colon

body of femur

temporal muscle

vastus lateralis muscle

endocardial cushion

soleus muscle

neural tube

ascending aorta

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity glycosyltransferase activity sialyltransferase activity (alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl-galactosaminide 6-alpha-sialyltransferase activity alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity
Cellular component	integral component of membrane Golgi apparatus membrane Golgi membrane
Biological process	O-glycan processing protein glycosylation oligosaccharide metabolic process glycolipid metabolic process sialylation protein N-linked glycosylation via asparagine
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


27090


20448

Ensembl


ENSG00000136840


ENSMUSG00000079442

UniProt


Q9H4F1


Q9R2B6

RefSeq (mRNA)


NM_014403 NM_175039 NM_175040


NM_001276425 NM_011373

RefSeq (protein)


NP_778204 NP_778205


NP_001263354 NP_035503

Location (UCSC)

Chr 9: 127.91 – 127.92 Mb

Chr 2: 32.48 – 32.49 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, also known as sialyltransferase 3C (SIAT3-C) or sialyltransferase 7D (SIAT7-D) is a sialyltransferase enzyme that in humans is encoded by the ST6GALNAC4 gene.^[5]

Function

ST6GALNAC4 is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein prefers glycoproteins rather than glycolipids as substrates and shows restricted substrate specificity, utilizing only the trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc. In addition, it is involved in the synthesis of ganglioside GD1A from GM1B. The enzyme is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Transcript variants encoding different isoforms have been found for this gene.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000136840 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000079442 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: ST6GALNAC4 ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4".

Lanfranchi G, Muraro T, Caldara F, et al. (1996). "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization". Genome Res. 6 (1): 35–42. doi:10.1101/gr.6.1.35. PMID 8681137.
Lee YC, Kaufmann M, Kitazume-Kawaguchi S, et al. (1999). "Molecular cloning and functional expression of two members of mouse NeuAcalpha2,3Galbeta1,3GalNAc GalNAcalpha2,6-sialyltransferase family, ST6GalNAc III and IV". J. Biol. Chem. 274 (17): 11958–67. doi:10.1074/jbc.274.17.11958. PMID 10207017.
Gilley J, Fried M (1999). "Extensive gene order differences within regions of conserved synteny between the Fugu and human genomes: implications for chromosomal evolution and the cloning of disease genes". Hum. Mol. Genet. 8 (7): 1313–20. doi:10.1093/hmg/8.7.1313. PMID 10369878.
Harduin-Lepers A, Stokes DC, Steelant WF, et al. (2001). "Cloning, expression and gene organization of a human Neu5Ac alpha 2-3Gal beta 1-3GalNAc alpha 2,6-sialyltransferase: hST6GalNAcIV". Biochem. J. 352 Pt 1 (Pt 1): 37–48. PMC 1221430. PMID 11062056.
Moody AM, North SJ, Reinhold B, et al. (2003). "Sialic acid capping of CD8beta core 1-O-glycans controls thymocyte-major histocompatibility complex class I interaction". J. Biol. Chem. 278 (9): 7240–6. doi:10.1074/jbc.M210468200. PMID 12459555.
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.
Kim SW, Kang NY, Lee SH, et al. (2003). "Genomic structure and promoter analysis of human NeuAc alpha2,3Gal beta1,3GalNAc alpha2,6-sialyltransferase (hST6GalNAc IV) gene". Gene. 305 (1): 113–20. doi:10.1016/S0378-1119(02)01234-9. PMID 12594047.
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.
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.
Kang NY, Park YD, Choi HJ, et al. (2005). "Regulatory elements involved in transcription of the human NeuAcalpha2,3Galbeta1,3GalNAcalpha2,6-sialyltransferase (hST6GalNAc IV) gene". Mol. Cells. 18 (2): 157–62. doi:10.1016/S1016-8478(23)13096-2. PMID 15528990.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.

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This page was last edited on 15 January 2024, at 12:24

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Function

References

Further reading