Human Gene MGAT5 (ENST00000281923.4) Description and Page Index
Description: Homo sapiens alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase (MGAT5), transcript variant 2, mRNA. (from RefSeq NM_002410) RefSeq Summary (NM_002410): The protein encoded by this gene belongs to the glycosyltransferase family. It catalyzes the addition of beta-1,6-N-acetylglucosamine to the alpha-linked mannose of biantennary N-linked oligosaccharides present on the newly synthesized glycoproteins. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. Alterations of the oligosaccharides on cell surface glycoproteins cause significant changes in the adhesive or migratory behavior of a cell. Increase in the activity of this enzyme has been correlated with the progression of invasive malignancies. [provided by RefSeq, Oct 2011]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: D17716.1, AF113921.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000281923.4/ ENSP00000281923.2 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Gencode Transcript: ENST00000281923.4 Gencode Gene: ENSG00000152127.9 Transcript (Including UTRs) Position: hg38 chr2:134,254,072-134,454,621 Size: 200,550 Total Exon Count: 16 Strand: + Coding Region Position: hg38 chr2:134,254,404-134,448,847 Size: 194,444 Coding Exon Count: 16
ID:MGT5A_HUMAN DESCRIPTION: RecName: Full=Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A; EC=184.108.40.206; AltName: Full=Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase; AltName: Full=GlcNAc-T V; Short=GNT-V; AltName: Full=Mannoside acetylglucosaminyltransferase 5; AltName: Full=N-acetylglucosaminyl-transferase V; FUNCTION: Catalyzes the addition of N-acetylglucosamine in beta 1- 6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + 6-(2-(N-acetyl- beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 6-(2,6-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D- mannosyl-R. PATHWAY: Protein modification; protein glycosylation. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 18 family. WEB RESOURCE: Name=GGDB; Note=GlycoGene database; URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/Homolog?cat=symbol&symbol=MGAT5"; WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Alpha-1,6-mannosylglycoprotein 6-beta-N- acetylglucosaminyltransferaseV; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_533";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q09328
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.