ST3GAL3

Protein-coding gene in the species Homo sapiens

ST3GAL3

Identifiers
Aliases| ST3GAL3, EIEE15, MRT12, SIAT6, ST3GALII, ST3GalIII, ST3N, ST3 beta-galactoside alpha-2,3-sialyltransferase 3, ST3Gal III, DEE15
External IDs| OMIM: 606494; MGI: 1316659; HomoloGene: 7539; GeneCards: ST3GAL3; OMA:ST3GAL3 - orthologs
| Gene location (Human)

Chr.| Chromosome 1 (human)[1]

Band| 1p34.1| Start| 43,705,824 bp[1]
End| 43,931,165 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 4 (mouse)[2]

Band| 4|4 D1- D2.1| Start| 117,789,351 bp[2]
End| 117,992,111 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* muscle of thigh

* gastrocnemius muscle

* left testis

* right testis

* right frontal lobe

* ganglionic eminence

* apex of heart

* epithelium of nasopharynx

* ventricular zone

* anterior cingulate cortex

| Top expressed in

* muscle of thigh

* motor neuron

* right ventricle

* masseter muscle

* ankle

* medial head of gastrocnemius muscle

* lumbar subsegment of spinal cord

* internal carotid artery

* intercostal muscle

* left lobe of liver

More reference expression data
BioGPS| | n/a

| Gene ontology

Molecular function|

* transferase activity
* glycosyltransferase activity
* sialyltransferase activity
* beta-galactoside (CMP) alpha-2,3-sialyltransferase activity
* N-acetyllactosaminide alpha-2,3-sialyltransferase activity

Cellular component|

* integral component of membrane
* Golgi apparatus
* membrane
* extracellular region
* Golgi cisterna membrane
* Golgi membrane

Biological process|

* sialylation
* protein glycosylation
* O-glycan processing
* keratan sulfate biosynthetic process
* oligosaccharide metabolic process
* protein N-linked glycosylation via asparagine

Sources:Amigo / QuickGO
| Orthologs

Species| Human| Mouse
Entrez| |

6487

20441

Ensembl| |

ENSG00000126091

ENSMUSG00000028538

UniProt| |

Q11203

P97325

RefSeq (mRNA)| | NM_001270459
NM_001270460
NM_001270461
NM_001270462
NM_001270463

NM_001270464
NM_001270465
NM_001270466
NM_006279
NM_174963
NM_174964
NM_174965
NM_174966
NM_174967
NM_174968
NM_174969
NM_174970
NM_174971
NM_174972
NM_001350619
NM_001350620
NM_001350621
NM_001363573

NM_001161774
NM_001285520
NM_001285521
NM_009176

RefSeq (protein)| | NP_001257388
NP_001257389
NP_001257390
NP_001257391
NP_001257392

NP_001257393
NP_001257394
NP_001257395
NP_006270
NP_777623
NP_777624
NP_777625
NP_777626
NP_777627
NP_777628
NP_777629
NP_777630
NP_777631
NP_001337548
NP_001337549
NP_001337550
NP_001350502

NP_001155246
NP_001272449
NP_001272450
NP_033202

Location (UCSC)| Chr 1: 43.71 – 43.93 Mb| Chr 4: 117.79 – 117.99 Mb
PubMed search| [3]| [4]
Wikidata
| View/Edit Human| View/Edit Mouse

|

ST3 beta-galactoside alpha-2,3-sialyltransferase 3, also known as ST3GAL3, is a protein which in humans is encoded by the ST3GAL3 gene.[5][6]

## Function

[edit]

The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein 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. Multiple transcript variants encoding several different isoforms have been found for this gene.[6]

Mutations in the ST3GAL3 gene was recently shown to be the cause of autosomal recessive mental retardation 12. Since the mutations disrupt a glycosylation pathway, this disorder may be considered a congenital disorder of glycosylation.

## See also

[edit]

* Sialyltransferase

## References

[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000126091 - Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028538 - 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. ^ Kitagawa H, Paulson JC (Jul 1993). "Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase". Biochemical and Biophysical Research Communications. 194 (1): 375–82\. doi:10.1006/bbrc.1993.1830. PMID 8333853.375-82&rft.date=1993-07&rft_id=info:doi/10.1006/bbrc.1993.1830&rft_id=info:pmid/8333853&rft.aulast=Kitagawa&rft.aufirst=H&rft.au=Paulson,+JC&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
6. ^ a b "Entrez Gene: ST3GAL3 ST3 beta-galactoside alpha-2,3-sialyltransferase 3".

## Further reading

[edit]

* Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG (Mar 1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1". AIDS Research and Human Retroviruses. 6 (3): 371–80\. doi:10.1089/aid.1990.6.371. PMID 2187500.371-80&rft.date=1990-03&rft_id=info:doi/10.1089/aid.1990.6.371&rft_id=info:pmid/2187500&rft.aulast=Kalyanaraman&rft.aufirst=VS&rft.au=Rodriguez,+V&rft.au=Veronese,+F&rft.au=Rahman,+R&rft.au=Lusso,+P&rft.au=DeVico,+AL&rft.au=Copeland,+T&rft.au=Oroszlan,+S&rft.au=Gallo,+RC&rft.au=Sarngadharan,+MG&rft_id=https://zenodo.org/record/1235229&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Pal R, Hoke GM, Sarngadharan MG (May 1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proceedings of the National Academy of Sciences of the United States of America. 86 (9): 3384–8\. Bibcode:1989PNAS...86.3384P. doi:10.1073/pnas.86.9.3384. PMC 287137. PMID 2541446.3384-8&rft.date=1989-05&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC287137#id-name=PMC&rft_id=info:pmid/2541446&rft_id=info:doi/10.1073/pnas.86.9.3384&rft_id=info:bibcode/1989PNAS...86.3384P&rft.aulast=Pal&rft.aufirst=R&rft.au=Hoke,+GM&rft.au=Sarngadharan,+MG&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC287137&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (Jun 1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". Journal of Virology. 63 (6): 2452–6\. doi:10.1128/JVI.63.6.2452-2456.1989. PMC 250699. PMID 2542563.2452-6&rft.date=1989-06&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC250699#id-name=PMC&rft_id=info:pmid/2542563&rft_id=info:doi/10.1128/JVI.63.6.2452-2456.1989&rft.aulast=Dewar&rft.aufirst=RL&rft.au=Vasudevachari,+MB&rft.au=Natarajan,+V&rft.au=Salzman,+NP&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC250699&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". Journal of Acquired Immune Deficiency Syndromes. 2 (2): 163–9\. PMID 2649653.163-9&rft.date=1989&rft_id=info:pmid/2649653&rft.aulast=Kozarsky&rft.aufirst=K&rft.au=Penman,+M&rft.au=Basiripour,+L&rft.au=Haseltine,+W&rft.au=Sodroski,+J&rft.au=Krieger,+M&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Research and Human Retroviruses. 3 (3): 265–82\. doi:10.1089/aid.1987.3.265. PMID 2829950.265-82&rft.date=1988&rft_id=info:doi/10.1089/aid.1987.3.265&rft_id=info:pmid/2829950&rft.aulast=Robinson&rft.aufirst=WE&rft.au=Montefiori,+DC&rft.au=Mitchell,+WM&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Kitagawa H, Paulson JC (Jul 1994). "Differential expression of five sialyltransferase genes in human tissues". The Journal of Biological Chemistry. 269 (27): 17872–8\. doi:10.1016/S0021-9258(17)32390-6. PMID 8027041.17872-8&rft.date=1994-07&rft_id=info:doi/10.1016/S0021-9258(17)32390-6&rft_id=info:pmid/8027041&rft.aulast=Kitagawa&rft.aufirst=H&rft.au=Paulson,+JC&rft_id=https://doi.org/10.1016%2FS0021-9258%2817%2932390-6&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Kitagawa H, Paulson JC (Jul 1993). "Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase". Biochemical and Biophysical Research Communications. 194 (1): 375–82\. doi:10.1006/bbrc.1993.1830. PMID 8333853.375-82&rft.date=1993-07&rft_id=info:doi/10.1006/bbrc.1993.1830&rft_id=info:pmid/8333853&rft.aulast=Kitagawa&rft.aufirst=H&rft.au=Paulson,+JC&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Burger PC, Lötscher M, Streiff M, Kleene R, Kaissling B, Berger EG (Mar 1998). "Immunocytochemical localization of alpha2,3(N)-sialyltransferase (ST3Gal III) in cell lines and rat kidney tissue sections: evidence for golgi and post-golgi localization". Glycobiology. 8 (3): 245–57\. doi:10.1093/glycob/8.3.245. PMID 9451034.245-57&rft.date=1998-03&rft_id=info:doi/10.1093/glycob/8.3.245&rft_id=info:pmid/9451034&rft.aulast=Burger&rft.aufirst=PC&rft.au=Lötscher,+M&rft.au=Streiff,+M&rft.au=Kleene,+R&rft.au=Kaissling,+B&rft.au=Berger,+EG&rft_id=https://doi.org/10.1093%2Fglycob%2F8.3.245&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Taniguchi A, Morishima T, Tsujita Y, Matsumoto Y, Matsumoto K (Jan 2003). "Genomic structure, expression, and transcriptional regulation of human Gal beta 1,3 GalNAc alpha 2,3-sialyltransferase gene". Biochemical and Biophysical Research Communications. 300 (2): 570–6\. doi:10.1016/S0006-291X(02)02899-1. PMID 12504121.570-6&rft.date=2003-01&rft_id=info:doi/10.1016/S0006-291X(02)02899-1&rft_id=info:pmid/12504121&rft.aulast=Taniguchi&rft.aufirst=A&rft.au=Morishima,+T&rft.au=Tsujita,+Y&rft.au=Matsumoto,+Y&rft.au=Matsumoto,+K&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Taniguchi A, Saito K, Kubota T, Matsumoto K (Apr 2003). "Characterization of the promoter region of the human Galbeta1,3(4)GlcNAc alpha2,3-sialyltransferase III (hST3Gal III) gene". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1626 (1–3): 92–6\. doi:10.1016/s0167-4781(03)00021-6. PMID 12697334.1–3&rft.pages=92-6&rft.date=2003-04&rft_id=info:doi/10.1016/s0167-4781(03)00021-6&rft_id=info:pmid/12697334&rft.aulast=Taniguchi&rft.aufirst=A&rft.au=Saito,+K&rft.au=Kubota,+T&rft.au=Matsumoto,+K&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Saito S, Aoki H, Ito A, Ueno S, Wada T, Mitsuzuka K, Satoh M, Arai Y, Miyagi T (Jul 2003). "Human alpha2,3-sialyltransferase (ST3Gal II) is a stage-specific embryonic antigen-4 synthase". The Journal of Biological Chemistry. 278 (29): 26474–9\. doi:10.1074/jbc.M213223200. PMID 12716912.26474-9&rft.date=2003-07&rft_id=info:doi/10.1074/jbc.M213223200&rft_id=info:pmid/12716912&rft.aulast=Saito&rft.aufirst=S&rft.au=Aoki,+H&rft.au=Ito,+A&rft.au=Ueno,+S&rft.au=Wada,+T&rft.au=Mitsuzuka,+K&rft.au=Satoh,+M&rft.au=Arai,+Y&rft.au=Miyagi,+T&rft_id=https://doi.org/10.1074%2Fjbc.M213223200&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Grahn A, Barkhordar GS, Larson G (Mar 2002). "Cloning and sequencing of nineteen transcript isoforms of the human alpha2,3-sialyltransferase gene, ST3Gal III; its genomic organisation and expression in human tissues". Glycoconjugate Journal. 19 (3): 197–210\. doi:10.1023/A:1024253808424. PMID 12815231. S2CID 23897339.197-210&rft.date=2002-03&rft_id=https://api.semanticscholar.org/CorpusID:23897339#id-name=S2CID&rft_id=info:pmid/12815231&rft_id=info:doi/10.1023/A:1024253808424&rft.aulast=Grahn&rft.aufirst=A&rft.au=Barkhordar,+GS&rft.au=Larson,+G&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Gretschel S, Haensch W, Schlag PM, Kemmner W (2003). "Clinical relevance of sialyltransferases ST6GAL-I and ST3GAL-III in gastric cancer". Oncology. 65 (2): 139–45\. doi:10.1159/000072339. PMID 12931020. S2CID 6438454.139-45&rft.date=2003&rft_id=https://api.semanticscholar.org/CorpusID:6438454#id-name=S2CID&rft_id=info:pmid/12931020&rft_id=info:doi/10.1159/000072339&rft.aulast=Gretschel&rft.aufirst=S&rft.au=Haensch,+W&rft.au=Schlag,+PM&rft.au=Kemmner,+W&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Jeanneau C, Chazalet V, Augé C, Soumpasis DM, Harduin-Lepers A, Delannoy P, Imberty A, Breton C (Apr 2004). "Structure-function analysis of the human sialyltransferase ST3Gal I: role of n-glycosylation and a novel conserved sialylmotif". The Journal of Biological Chemistry. 279 (14): 13461–8\. doi:10.1074/jbc.M311764200. PMID 14722111.13461-8&rft.date=2004-04&rft_id=info:doi/10.1074/jbc.M311764200&rft_id=info:pmid/14722111&rft.aulast=Jeanneau&rft.aufirst=C&rft.au=Chazalet,+V&rft.au=Augé,+C&rft.au=Soumpasis,+DM&rft.au=Harduin-Lepers,+A&rft.au=Delannoy,+P&rft.au=Imberty,+A&rft.au=Breton,+C&rft_id=https://doi.org/10.1074%2Fjbc.M311764200&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Grahn A, Barkhordar GS, Larson G (2005). "Identification of seven new alpha2,3-sialyltransferase III, ST3Gal III, transcripts from human foetal brain". Glycoconjugate Journal. 20 (7–8): 493–500\. doi:10.1023/B:GLYC.0000038295.87747.0b. PMID 15316282. S2CID 1544031.7–8&rft.pages=493-500&rft.date=2005&rft_id=https://api.semanticscholar.org/CorpusID:1544031#id-name=S2CID&rft_id=info:pmid/15316282&rft_id=info:doi/10.1023/B:GLYC.0000038295.87747.0b&rft.aulast=Grahn&rft.aufirst=A&rft.au=Barkhordar,+GS&rft.au=Larson,+G&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Van Dyken SJ, Green RS, Marth JD (Feb 2007). "Structural and mechanistic features of protein O glycosylation linked to CD8+ T-cell apoptosis". Molecular and Cellular Biology. 27 (3): 1096–111\. doi:10.1128/MCB.01750-06. PMC 1800694. PMID 17101770.1096-111&rft.date=2007-02&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1800694#id-name=PMC&rft_id=info:pmid/17101770&rft_id=info:doi/10.1128/MCB.01750-06&rft.aulast=Van+Dyken&rft.aufirst=SJ&rft.au=Green,+RS&rft.au=Marth,+JD&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1800694&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* Hu H, Eggers K, Chen W, Garshasbi M, Motazacker MM, Wrogemann K, Kahrizi K, Tzschach A, Hosseini M, Bahman I, Hucho T, Mühlenhoff M, Gerardy-Schahn R, Najmabadi H, Ropers HH, Kuss AW (Sep 2011). "ST3GAL3 mutations impair the development of higher cognitive functions". American Journal of Human Genetics. 89 (3): 407–14\. doi:10.1016/j.ajhg.2011.08.008. PMC 3169827. PMID 21907012.407-14&rft.date=2011-09&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3169827#id-name=PMC&rft_id=info:pmid/21907012&rft_id=info:doi/10.1016/j.ajhg.2011.08.008&rft.aulast=Hu&rft.aufirst=H&rft.au=Eggers,+K&rft.au=Chen,+W&rft.au=Garshasbi,+M&rft.au=Motazacker,+MM&rft.au=Wrogemann,+K&rft.au=Kahrizi,+K&rft.au=Tzschach,+A&rft.au=Hosseini,+M&rft.au=Bahman,+I&rft.au=Hucho,+T&rft.au=Mühlenhoff,+M&rft.au=Gerardy-Schahn,+R&rft.au=Najmabadi,+H&rft.au=Ropers,+HH&rft.au=Kuss,+AW&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3169827&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">
* 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 26280291.210-270&rft.date=2017&rft_id=https://api.semanticscholar.org/CorpusID:26280291#id-name=S2CID&rft_id=info:pmid/27678392&rft_id=info:doi/10.1002/med.21407&rft.aulast=Szabo&rft.aufirst=R&rft.au=Skropeta,+D&rft_id=http://ro.uow.edu.au/cgi/viewcontent.cgi?article=5226&context;=smhpapers&rfr_id=info:sid/en.wikipedia.org:ST3GAL3" class="Z3988">

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