Q9NS00 · C1GLT_HUMAN
- ProteinGlycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- GeneC1GALT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids363 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins (PubMed:11677243).
Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development (By similarity).
Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development (By similarity).
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
- an N-acetyl-alpha-D-galactosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + H+ + UDP
Cofactor
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 94 | UDP (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 138 | UDP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 139 | UDP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 140 | UDP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 146 | UDP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 169 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 169 | UDP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 171 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 285 | a glycoprotein (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 309 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 309 | UDP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 310 | UDP (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi membrane | |
Cellular Component | membrane | |
Molecular Function | glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Biological Process | angiogenesis | |
Biological Process | intestinal epithelial cell development | |
Biological Process | kidney development | |
Biological Process | protein O-linked glycosylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- 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 accessionQ9NS00
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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: MASKSW | ||||||
Transmembrane | 7-29 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LNFLTFLCGSAIGFLLCSQLFSI | ||||||
Topological domain | 30-363 | Lumenal | ||||
Sequence: LLGEKVDTQPNVLHNDPHARHSDDNGQNHLEGQMNFNADSSQHKDENTDIAENLYQKVRILCWVMTGPQNLEKKAKHVKATWAQRCNKVLFMSSEENKDFPAVGLKTKEGRDQLYWKTIKAFQYVHEHYLEDADWFLKADDDTYVILDNLRWLLSKYDPEEPIYFGRRFKPYVKQGYMSGGAGYVLSKEALKRFVDAFKTDKCTHSSSIEDLALGRCMEIMNVEAGDSRDTIGKETFHPFVPEHHLIKGYLPRTFWYWNYNYYPPVEGPGCCSDLAVSFHYVDSTTMYELEYLVYHLRPYGYLYRYQPTLPERILKEISQANKNEDTKVKLGNP |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 140 | Reduced activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 201 | Reduced activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 206 | Reduced activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 240 | Inactive. | ||||
Sequence: D → A | ||||||
Mutagenesis | 285 | Inactive. | ||||
Sequence: W → A | ||||||
Mutagenesis | 310 | Reduced activity. | ||||
Sequence: Y → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 440 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000285064 | 1-363 | Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1 | |||
Sequence: MASKSWLNFLTFLCGSAIGFLLCSQLFSILLGEKVDTQPNVLHNDPHARHSDDNGQNHLEGQMNFNADSSQHKDENTDIAENLYQKVRILCWVMTGPQNLEKKAKHVKATWAQRCNKVLFMSSEENKDFPAVGLKTKEGRDQLYWKTIKAFQYVHEHYLEDADWFLKADDDTYVILDNLRWLLSKYDPEEPIYFGRRFKPYVKQGYMSGGAGYVLSKEALKRFVDAFKTDKCTHSSSIEDLALGRCMEIMNVEAGDSRDTIGKETFHPFVPEHHLIKGYLPRTFWYWNYNYYPPVEGPGCCSDLAVSFHYVDSTTMYELEYLVYHLRPYGYLYRYQPTLPERILKEISQANKNEDTKVKLGNP | ||||||
Disulfide bond | 91↔115 | |||||
Sequence: CWVMTGPQNLEKKAKHVKATWAQRC | ||||||
Disulfide bond | 232↔246 | |||||
Sequence: CTHSSSIEDLALGRC | ||||||
Modified residue | 235 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 300↔301 | |||||
Sequence: CC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Highly expressed in kidney, heart, placenta and liver.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer; disulfide-linked (By similarity).
Interacts with the C1GALT1C1 chaperone; required for galactosyltransferase activity (PubMed:12464682).
Interacts with the C1GALT1C1 chaperone; required for galactosyltransferase activity (PubMed:12464682).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NS00 | C1GALT1C1 Q96EU7 | 4 | EBI-8628584, EBI-2837343 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 41-72 | Disordered | ||||
Sequence: VLHNDPHARHSDDNGQNHLEGQMNFNADSSQH |
Sequence similarities
Belongs to the glycosyltransferase 31 family. Beta3-Gal-T subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9NS00-1
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
- Length363
- Mass (Da)42,203
- Last updated2000-10-01 v1
- Checksum01F472B55C5F526F
Q9NS00-2
- Name2
- Differences from canonical
- 297-363: GPGCCSDLAVSFHYVDSTTMYELEYLVYHLRPYGYLYRYQPTLPERILKEISQANKNEDTKVKLGNP → VSLEILLLCQYLD
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9K0C8 | C9K0C8_HUMAN | C1GALT1 | 131 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_024809 | 297-363 | in isoform 2 | |||
Sequence: GPGCCSDLAVSFHYVDSTTMYELEYLVYHLRPYGYLYRYQPTLPERILKEISQANKNEDTKVKLGNP → VSLEILLLCQYLD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF155582 EMBL· GenBank· DDBJ | AAF81981.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ132443 EMBL· GenBank· DDBJ | CAC45046.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ278960 EMBL· GenBank· DDBJ | CAC82373.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ243256 EMBL· GenBank· DDBJ | CAC80435.1 EMBL· GenBank· DDBJ | mRNA | ||
AC005532 EMBL· GenBank· DDBJ | AAQ96887.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH236948 EMBL· GenBank· DDBJ | EAL24308.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003174 EMBL· GenBank· DDBJ | AAH03174.1 EMBL· GenBank· DDBJ | mRNA |