Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q8BVG5

Entry ID Method Resolution Chain Position Source
AF-Q8BVG5-F1 Predicted AlphaFoldDB

No variants for Q8BVG5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8BVG5

No associated diseases with Q8BVG5

3 regional properties for Q8BVG5

Type Name Position InterPro Accession
domain Ricin B, lectin domain 420 - 548 IPR000772
domain Glycosyltransferase 2-like 114 - 283 IPR001173
domain N-acetylgalactosaminyltransferase 114 - 408 IPR045885

Functions

Description
EC Number 2.4.1.41 Hexosyltransferases
Subcellular Localization
  • Golgi apparatus membrane ; Single-pass type II membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

3 GO annotations of molecular function

Name Definition
carbohydrate binding Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
metal ion binding Binding to a metal ion.
polypeptide N-acetylgalactosaminyltransferase activity Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. This reaction is the modification of serine or threonine residues in polypeptide chains by the transfer of a N-acetylgalactose from UDP-N-acetylgalactose to the hydroxyl group of the amino acid; it is the first step in O-glycan biosynthesis.

1 GO annotations of biological process

Name Definition
protein O-linked glycosylation A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q10471 GALNT2 Polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens (Human) PR
Q96FL9 GALNT14 Polypeptide N-acetylgalactosaminyltransferase 14 Homo sapiens (Human) PR
Q80VA0 Galnt7 N-acetylgalactosaminyltransferase 7 Mus musculus (Mouse) PR
Q8CF93 Galnt13 Polypeptide N-acetylgalactosaminyltransferase 13 Mus musculus (Mouse) PR
O08912 Galnt1 Polypeptide N-acetylgalactosaminyltransferase 1 Mus musculus (Mouse) PR
Q921L8 Galnt11 Polypeptide N-acetylgalactosaminyltransferase 11 Mus musculus (Mouse) PR
Q8BGT9 Galnt12 Polypeptide N-acetylgalactosaminyltransferase 12 Mus musculus (Mouse) PR
P70419 Galnt3 Polypeptide N-acetylgalactosaminyltransferase 3 Mus musculus (Mouse) PR
Q8I136 gly-4 Polypeptide N-acetylgalactosaminyltransferase 4 Caenorhabditis elegans PR
10 20 30 40 50 60
MRRLTRRLAL PIFGVLWITV LLFFWVTKRK LEVPLGPEVQ TPKPSDADWD DLWEQFDERR
70 80 90 100 110 120
YLNAKKWRVG DDPYKLYAFN QRESERISSN RAVPDTRHKR CSLLVYCTDL PPTSIIITFH
130 140 150 160 170 180
NEARSTLLRT IRSVLNRTPM HLIQEIILVD DFSNDPEDCK QLIKLPKVKC LRNNERQGLV
190 200 210 220 230 240
RSRMRGADIA QGTTLTFLDS HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFNYIE
250 260 270 280 290 300
SASELRGGFD WSLHFQWEQL SLEQKALRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDV
310 320 330 340 350 360
DMDIWGGENF EISFRVWMCG GGLEIIPCSR VGHVFRKKHP YVFPDGNANT YIKNTKRTAE
370 380 390 400 410 420
VWMDEYKQYY YAARPFALER PFGNIENRLN LRKNLHCQTF KWNLENVYPE LRVPPDSSIQ
430 440 450 460 470 480
KGNIRQRQKC LESQKQKKQE ILRLSPCAKV KGDGAKSQVW AFTYTQQIIQ EELCLSVVTL
490 500 510 520 530 540
FPGAPVVLAL CKNGDERQLW TKTGARIEHI ASHLCLDTDM FGDSTEDGKE VVVNPCESSL
MSQHWDIVSS