Q921V5

PR
Gene name
Mgat2
Protein name
Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
Names
Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, GNT-II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:217664
EC number
2.4.1.143: Hexosyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-70 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q921V5

Entry ID Method Resolution Chain Position Source
AF-Q921V5-F1 Predicted AlphaFoldDB

7 variants for Q921V5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs586106993 73 A>G No EVA
rs3403006849 120 H>P No EVA
rs3403394495 175 S>R No EVA
rs3403575605 253 L>Q No EVA
rs3403315906 256 D>G No EVA
rs3389249826 287 G>E No EVA
rs3389215952 294 S>I No EVA

No associated diseases with Q921V5

No regional properties for Q921V5

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q921V5

Functions

Description
EC Number 2.4.1.143 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

4 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.
Golgi stack The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.
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.

4 GO annotations of molecular function

Name Definition
alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
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.
manganese ion binding Binding to a manganese ion (Mn).
protein homodimerization activity Binding to an identical protein to form a homodimer.

3 GO annotations of biological process

Name Definition
oligosaccharide biosynthetic process The chemical reactions and pathways resulting in the formation of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
protein N-linked glycosylation A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
protein N-linked glycosylation via asparagine The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q10469 MGAT2 Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Homo sapiens (Human) PR
O19071 MGAT2 Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Sus scrofa (Pig) PR
Q09326 Mgat2 Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKSDALGPP LLDAEPVRGA GHLAVSVGIR
70 80 90 100 110 120
RVSNESAAPL VPAVPRPEVD NLTLRYRSLV YQLNFDQMLR NVGNDGTWSP GELVLVVQVH
130 140 150 160 170 180
NRPEYLRLLI DSLRKAQGIQ EVLVIFSHDF WSAEINSLIS RVDFCPVLQV FFPFSIQLYP
190 200 210 220 230 240
NEFPGSDPRD CPRDLKKNAA LKLGCINAEY PDSFGHYREA KFSQTKHHWW WKLHFVWERV
250 260 270 280 290 300
KVLQDYTGLI LFLEEDHYLA PDFYHVFKKM WKLKQQECPG CDVLSLGTYT TIRSFYGIAD
310 320 330 340 350 360
KVDVKTWKST EHNMGLALTR DAYQKLIECT DTFCTYDDYN WDWTLQYLTL ACLPKIWKVL
370 380 390 400 410 420
VPQAPRIFHA GDCGMHHKKT CRPSTQSAQI ESLLNSNKQY LFPETLVIGE KFPMAAISPP
430 440
RKNGGWGDIR DHELCKSYRR LQ