P27808

PR
Gene name
Mgat1 (Gnt1)
Protein name
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
Names
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I, GNT-I, GlcNAc-T I
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:17308
EC number
2.4.1.101: Hexosyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

6-135 (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 P27808

Entry ID Method Resolution Chain Position Source
AF-P27808-F1 Predicted AlphaFoldDB

18 variants for P27808

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3402340266 5 Q>* No EVA
rs3389165335 7 A>V No EVA
rs3389158621 13 G>V No EVA
rs3389152567 20 W>* No EVA
rs3401566390 42 A>G No EVA
rs3389146416 48 A>V No EVA
rs3389116636 68 Q>E No EVA
rs3389146397 68 Q>H No EVA
rs3389154860 88 V>F No EVA
rs263163443 106 V>A No EVA
rs3389158617 139 I>T No EVA
rs3389128962 282 E>V No EVA
rs3389158552 306 I>V No EVA
rs3389161843 320 G>D No EVA
rs3389146464 327 F>L No EVA
rs3389161822 333 F>S No EVA
rs3389161811 334 I>V No EVA
rs3389152405 385 E>V No EVA

No associated diseases with P27808

No regional properties for P27808

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P27808

Functions

Description
EC Number 2.4.1.101 Hexosyltransferases
Subcellular Localization
  • Golgi apparatus membrane ; Single-pass type II membrane protein
  • Cytoplasm, perinuclear region
  • Co-localizes with BRI3 at the perinuclear region
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.
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.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.

3 GO annotations of molecular function

Name Definition
acetylglucosaminyltransferase activity Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar.
alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Catalysis of the reaction: 3-(alpha-D-mannosyl)-beta-D-mannosyl-R + UDP-N-acetyl-alpha-D-glucosamine = 3-(2--alpha-D-mannosyl)-beta-D-mannosyl-R + H(+) + UDP.
manganese ion binding Binding to a manganese ion (Mn).

5 GO annotations of biological process

Name Definition
in utero embryonic development The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus.
protein glycosylation A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.
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.
UDP-N-acetylglucosamine catabolic process The chemical reactions and pathways resulting in the breakdown of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P26572 MGAT1 Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Homo sapiens (Human) PR
Q09325 Mgat1 Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Rattus norvegicus (Rat) PR
Q11068 gly-13 Putative alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Caenorhabditis elegans PR
10 20 30 40 50 60
MLKKQTAGLV LWGAIIFVGW NALLLLFFWT RPAPGRLPSD SALGDDPASL TREVIHLAED
70 80 90 100 110 120
AEAELERQRG LLQQIKEHYA LWRQRWRVPT VAPPAWPRVP VTPSPVQIPI LVIACDRSTV
130 140 150 160 170 180
RRCLDKLLHY RPSAERFPII VSQDCGHEET AQVIASYGTA VTHIRQPDLS NIAVQPDHRK
190 200 210 220 230 240
FQGYYKIARH YRWALGQIFN KFKFPAAVVV EDDLEVAPDF FEYFQATYPL LRTDPSLWCV
250 260 270 280 290 300
SAWNDNGKEQ MVDSSKPELL YRTDFFPGLG WLLLADLWAE LEPKWPKAFW DDWMRRPEQR
310 320 330 340 350 360
KGRACIRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VPFTQLDLSY LQQEAYDRDF
370 380 390 400 410 420
LAQVYGAPQL QVEKVRTNDQ KELGEVRVQY TSRDSFKAFA KALGVMDDLK SGVPRAGYRG
430 440
IVTFQFRGRR VHLAPPQTWT GYDPSWN