Q8N428 · GLT16_HUMAN
- ProteinPolypeptide N-acetylgalactosaminyltransferase 16
- GeneGALNT16
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids558 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Catalytic activity
- L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H+ + UDP
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
251 μM | Muc5AC | |||||
310 μM | Muc5AC-3 | |||||
390 μM | Muc5AC-13 | |||||
332 μM | EA2 |
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 163 | substrate | ||||
Sequence: D | ||||||
Binding site | 188 | substrate | ||||
Sequence: R | ||||||
Binding site | 211 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 212 | substrate | ||||
Sequence: S | ||||||
Binding site | 213 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 317 | substrate | ||||
Sequence: W | ||||||
Binding site | 345 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 348 | substrate | ||||
Sequence: R | ||||||
Binding site | 351 | substrate | ||||
Sequence: H | ||||||
Binding site | 353 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Molecular Function | carbohydrate binding | |
Molecular Function | metal ion binding | |
Molecular Function | polypeptide N-acetylgalactosaminyltransferase activity | |
Biological Process | protein O-linked glycosylation | |
Biological Process | protein O-linked glycosylation via serine | |
Biological Process | protein O-linked glycosylation via threonine |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePolypeptide N-acetylgalactosaminyltransferase 16
- 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 accessionQ8N428
- 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 | 1-6 | Cytoplasmic | ||||
Sequence: MRKIRA | ||||||
Transmembrane | 7-26 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: NAIAILTVAWILGTFYYLWQ | ||||||
Topological domain | 27-558 | Lumenal | ||||
Sequence: DNRAHAASSGGRGAQRAGRRSEQLREDRTIPLIVTGTPSKGFDEKAYLSAKQLKAGEDPYRQHAFNQLESDKLSPDRPIRDTRHYSCPSVSYSSDLPATSVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLLTRIPKVKCLRNDRREGLIRSRVRGADVAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKMTRTDPTRPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFRKRHPYNFPEGNALTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMNCKSFRWYLENVYPELTVPVKEALPGIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLFSDHLIQQQGKCLAATSTLMSSPGSPVILQMCNPREGKQKWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPHT |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_055848 | 201 | in dbSNP:rs12879377 | |||
Sequence: V → M | ||||||
Natural variant | VAR_061195 | 497 | in dbSNP:rs59840366 | |||
Sequence: P → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 669 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059135 | 1-558 | Polypeptide N-acetylgalactosaminyltransferase 16 | |||
Sequence: MRKIRANAIAILTVAWILGTFYYLWQDNRAHAASSGGRGAQRAGRRSEQLREDRTIPLIVTGTPSKGFDEKAYLSAKQLKAGEDPYRQHAFNQLESDKLSPDRPIRDTRHYSCPSVSYSSDLPATSVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLLTRIPKVKCLRNDRREGLIRSRVRGADVAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKMTRTDPTRPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFRKRHPYNFPEGNALTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMNCKSFRWYLENVYPELTVPVKEALPGIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLFSDHLIQQQGKCLAATSTLMSSPGSPVILQMCNPREGKQKWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPHT | ||||||
Disulfide bond | 113↔340 | |||||
Sequence: CPSVSYSSDLPATSVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLLTRIPKVKCLRNDRREGLIRSRVRGADVAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKMTRTDPTRPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPC | ||||||
Disulfide bond | 331↔409 | |||||
Sequence: CGGSLEIVPCSRVGHVFRKRHPYNFPEGNALTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMNC | ||||||
Disulfide bond | 441↔460 | |||||
Sequence: CLESQGQNTAGDFLLGMGIC | ||||||
Disulfide bond | 486↔506 | |||||
Sequence: CLAATSTLMSSPGSPVILQMC | ||||||
Disulfide bond | 530↔543 | |||||
Sequence: CLETKPAQLVTSKC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 33-54 | Disordered | ||||
Sequence: ASSGGRGAQRAGRRSEQLREDR | ||||||
Region | 122-227 | Catalytic subdomain A | ||||
Sequence: LPATSVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLLTRIPKVKCLRNDRREGLIRSRVRGADVAAATVLTFLDSHCEVNTEWLPPMLQR | ||||||
Region | 286-348 | Catalytic subdomain B | ||||
Sequence: PIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFR | ||||||
Domain | 428-555 | Ricin B-type lectin | ||||
Sequence: KEALPGIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLFSDHLIQQQGKCLAATSTLMSSPGSPVILQMCNPREGKQKWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLL |
Domain
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
Sequence similarities
Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8N428-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length558
- Mass (Da)63,074
- Last updated2004-08-16 v2
- ChecksumFF35C5606B5291B8
Q8N428-2
- Name2
- Differences from canonical
- 514-558: KWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPHT → VSLLASGPEAQQPEGPCLRVADLGRRAPD
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_011231 | 514-558 | in isoform 2 | |||
Sequence: KWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPHT → VSLLASGPEAQQPEGPCLRVADLGRRAPD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB032956 EMBL· GenBank· DDBJ | BAA86444.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB078143 EMBL· GenBank· DDBJ | BAD93178.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289745 EMBL· GenBank· DDBJ | BAF82434.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471061 EMBL· GenBank· DDBJ | EAW80987.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC036812 EMBL· GenBank· DDBJ | AAH36812.2 EMBL· GenBank· DDBJ | mRNA | ||
BC098578 EMBL· GenBank· DDBJ | AAH98578.1 EMBL· GenBank· DDBJ | mRNA |