GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

BOVIN:GALT1

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Bos taurus (Bovine). (9913)
Gene Name(s) GALNT1
Protein Name(s) Polypeptide N-acetylgalactosaminyltransferase 1

Polypeptide GalNAc transferase 1 GalNAc-T1 pp-GaNTase 1 Protein-UDP acetylgalactosaminyltransferase 1 UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 Polypeptide N-acetylgalactosaminyltransferase 1 soluble form

External Links
UniProt Q07537
EMBL L07780
L17437
PIR A45987
RefSeq NP_803485.1
UniGene Bt.65693
ProteinModelPortal Q07537
SMR Q07537
STRING 9913.ENSBTAP00000014882
CAZy CBM13
GT27
PRIDE Q07537
Ensembl ENSBTAT00000014882
GeneID 282241
KEGG bta:282241
CTD 2589
eggNOG NOG239675
GeneTree ENSGT00760000118828
HOGENOM HOG000038227
HOVERGEN HBG051699
InParanoid Q07537
KO K00710
OMA IKHDRKT
OrthoDB EOG7J9VP2
TreeFam TF313267
BRENDA 2.4.1.41
Reactome REACT_208023
UniPathway UPA00378
NextBio 20806060
Proteomes UP000009136
GO GO:0005576
GO:0032580
GO:0016021
GO:0048471
GO:0030246
GO:0030145
GO:0004653
GO:0006493
GO:0018242
GO:0018243
Gene3D 3.90.550.10
InterPro IPR001173
IPR029044
IPR000772
Pfam PF00535
PF00652
SMART SM00458
SUPFAM SSF50370
SSF53448
PROSITE PS50231

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004653

polypeptide N-acetylgalactosaminyltransferase activity

PMID:9359852[1]

ECO:0000314

F

Table 2 is a list of Km values determined from an kinetics experiment, the purified wild-type is the first entry in table, and all mutant proteins are normalized to wild-type activity. The glycoproteins formed were separated later with anion-exchanged chromatography.

complete
CACAO 3615

enables

GO:0004653

polypeptide N-acetylgalactosaminyltransferase activity

PMID:19460755[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006493

protein O-linked glycosylation

PMID:19460755[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004653

polypeptide N-acetylgalactosaminyltransferase activity

PMID:9359852[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

PMID:3082881[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006493

protein O-linked glycosylation

PMID:3082881[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004653

polypeptide N-acetylgalactosaminyltransferase activity

PMID:3082881[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005794

Golgi apparatus

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0027558
PANTHER:PTN000187024
UniProtKB:Q10471
UniProtKB:Q10472
UniProtKB:Q14435
UniProtKB:Q8N4A0
UniProtKB:Q8NCL4

C

Seeded From UniProt

complete

involved_in

GO:0006493

protein O-linked glycosylation

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O08912
ensembl:ENSMUSP00000132142

P

Seeded From UniProt

complete

enables

GO:0004653

polypeptide N-acetylgalactosaminyltransferase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O08912
ensembl:ENSMUSP00000132142

F

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q10472
ensembl:ENSP00000269195

C

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q10472
ensembl:ENSP00000269195

F

Seeded From UniProt

complete

involved_in

GO:0018243

protein O-linked glycosylation via threonine

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q10472
ensembl:ENSP00000269195

P

Seeded From UniProt

complete

involved_in

GO:0018242

protein O-linked glycosylation via serine

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q10472
ensembl:ENSP00000269195

P

Seeded From UniProt

complete

involved_in

GO:0006493

protein O-linked glycosylation

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q10472
ensembl:ENSP00000269195

P

Seeded From UniProt

complete

part_of

GO:0005794

Golgi apparatus

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q10472
ensembl:ENSP00000269195

C

Seeded From UniProt

complete

enables

GO:0004653

polypeptide N-acetylgalactosaminyltransferase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q10472
ensembl:ENSP00000269195

F

Seeded From UniProt

complete

enables

GO:0004653

polypeptide N-acetylgalactosaminyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.4.1.41

F

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964
UniProtKB-SubCell:SL-0243

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0328

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005794

Golgi apparatus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0333

C

Seeded From UniProt

complete

enables

GO:0030246

carbohydrate binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0430

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0032580

Golgi cisterna membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0136

C

Seeded From UniProt

complete

involved_in

GO:0006486

protein glycosylation

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00378

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Wragg, S et al. (1997) Identification of essential histidine residues in UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1. Biochem. J. 328 ( Pt 1) 193-7 PubMed GONUTS page
  2. 2.0 2.1 Perrine, CL et al. (2009) Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2. J. Biol. Chem. 284 20387-97 PubMed GONUTS page
  3. 3.0 3.1 3.2 Elhammer, A & Kornfeld, S (1986) Purification and characterization of UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells. J. Biol. Chem. 261 5249-55 PubMed GONUTS page
  4. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page