Q9UJ37 · SIA7B_HUMAN
- ProteinAlpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2
- GeneST6GALNAC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids374 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins (PubMed:10742600, PubMed:29251719).
Shows a preference for N-acetylgalactosamine (GalNAc) residues already modified by the addition of galactose or galactose followed by sialic acid in alpha-2,3 linkage (PubMed:10742600).
Shows a preference for N-acetylgalactosamine (GalNAc) residues already modified by the addition of galactose or galactose followed by sialic acid in alpha-2,3 linkage (PubMed:10742600).
Miscellaneous
Aberrant O-galactosylation of IgA1 molecules plays a role in the development and progression of IgA nephropathy (IgAN). Genetic interactions of C1GALT1 and ST6GALNAC2 variants influence IgA1 O-glycosylation, disease predisposition, and disease severity, and may contribute to the polygenic nature of IgAN.
Catalytic activity
- a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + CMP-N-acetyl-beta-neuraminate = a beta-D-galactosyl-(1->3)-[N-acetyl-alpha-neuraminyl-(2->6)]-N-acetyl-alpha-D-galactosaminyl derivative + CMP + H+This reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
130 μM | CMP-N-acetylneuraminate | |||||
104 μM | CMP-N-acetylneuraminate |
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 156 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 179 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 304 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 336 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi membrane | |
Molecular Function | alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity | |
Molecular Function | sialyltransferase activity | |
Biological Process | O-glycan processing | |
Biological Process | protein glycosylation | |
Biological Process | protein O-linked glycosylation | |
Biological Process | protein sialylation | |
Biological Process | viral protein processing |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UJ37
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-7 | Cytoplasmic | ||||
Sequence: MGLPRGS | ||||||
Transmembrane | 8-28 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: FFWLLLLLTAACSGLLFALYF | ||||||
Topological domain | 29-374 | Lumenal | ||||
Sequence: SAVQRYPGPAAGARDTTSFEAFFQSKASNSWTGKGQACRHLLHLAIQRHPHFRGLFNLSIPVLLWGDLFTPALWDRLSQHKAPYGWRGLSHQVIASTLSLLNGSESAKLFAPPRDTPPKCIRCAVVGNGGILNGSRQGPNIDAHDYVFRLNGAVIKGFERDVGTKTSFYGFTVNTMKNSLVSYWNLGFTSVPQGQDLQYIFIPSDIRDYVMLRSAILGVPVPEGLDKGDRPHAYFGPEASASKFKLLHPDFISYLTERFLKSKLINTHFGDLYMPSTGALMLLTALHTCDQVSAYGFITSNYWKFSDHYFERKMKPLIFYANHDLSLEAALWRDLHKAGILQLYQR |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 437 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000149272 | 1-374 | Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 | |||
Sequence: MGLPRGSFFWLLLLLTAACSGLLFALYFSAVQRYPGPAAGARDTTSFEAFFQSKASNSWTGKGQACRHLLHLAIQRHPHFRGLFNLSIPVLLWGDLFTPALWDRLSQHKAPYGWRGLSHQVIASTLSLLNGSESAKLFAPPRDTPPKCIRCAVVGNGGILNGSRQGPNIDAHDYVFRLNGAVIKGFERDVGTKTSFYGFTVNTMKNSLVSYWNLGFTSVPQGQDLQYIFIPSDIRDYVMLRSAILGVPVPEGLDKGDRPHAYFGPEASASKFKLLHPDFISYLTERFLKSKLINTHFGDLYMPSTGALMLLTALHTCDQVSAYGFITSNYWKFSDHYFERKMKPLIFYANHDLSLEAALWRDLHKAGILQLYQR | ||||||
Disulfide bond | 66↔148 | |||||
Sequence: CRHLLHLAIQRHPHFRGLFNLSIPVLLWGDLFTPALWDRLSQHKAPYGWRGLSHQVIASTLSLLNGSESAKLFAPPRDTPPKC | ||||||
Glycosylation | 85 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 130 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 151↔317 | |||||
Sequence: CAVVGNGGILNGSRQGPNIDAHDYVFRLNGAVIKGFERDVGTKTSFYGFTVNTMKNSLVSYWNLGFTSVPQGQDLQYIFIPSDIRDYVMLRSAILGVPVPEGLDKGDRPHAYFGPEASASKFKLLHPDFISYLTERFLKSKLINTHFGDLYMPSTGALMLLTALHTC | ||||||
Glycosylation | 161 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in skeletal muscle, heart, kidney, placenta, lung and leukocytes.
Gene expression databases
Organism-specific databases
Structure
Sequence
- Sequence statusComplete
- Length374
- Mass (Da)41,939
- Last updated2000-05-01 v1
- ChecksumE0BD439E4C6BB427
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 11 | in Ref. 2; AAA52228 | ||||
Sequence: L → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ251053 EMBL· GenBank· DDBJ | CAB61434.1 EMBL· GenBank· DDBJ | mRNA | ||
U14550 EMBL· GenBank· DDBJ | AAA52228.1 EMBL· GenBank· DDBJ | mRNA | ||
BT019972 EMBL· GenBank· DDBJ | AAV38775.1 EMBL· GenBank· DDBJ | mRNA | ||
BC040455 EMBL· GenBank· DDBJ | AAH40455.1 EMBL· GenBank· DDBJ | mRNA |