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 O19071

Entry ID Method Resolution Chain Position Source
AF-O19071-F1 Predicted AlphaFoldDB

No variants for O19071

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O19071

No associated diseases with O19071

No regional properties for O19071

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O19071

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

3 GO annotations of cellular component

Name Definition
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.

3 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.
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
Q921V5 Mgat2 Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Mus musculus (Mouse) PR
Q09326 Mgat2 Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MRFRIYKRKV LILTFVVAAC GFVLWSSNGR QRKNEALAPP LLDAEPVRGA GARAGDHPAI
70 80 90 100 110 120
SVGIRRGSND SAAPLVAAAP QPEVDNLTLR YRSLVYQLNF DQTLRNVDKV SSWVPRELVL
130 140 150 160 170 180
VVQVHNRAEY LKLLLDSLRK AQGIDNVLVI FSHDFWSTEI NQLIAGVDFC PVLQVFFPFS
190 200 210 220 230 240
IQLYPNEFPG TDPRDCPRDL EKNAALKMGC INAEYPDSFG HYREAKFSQT KHHWWWKLHF
250 260 270 280 290 300
VWERVKVLRD YAGLILFLEE DHYVAPDFYH VFKKMWNLKQ QECPECDVLS LGTYTTVRSF
310 320 330 340 350 360
RDVADKVDVK TWKSTEHNMG LALTRDAYQK LIECTDTFCT YDDYNWDWTL QYLTVSCLPK
370 380 390 400 410 420
FWKVLVPQVP RIFHAGDCGM HHKKTCRPST QSAQIESLLN SNKQYMFPET LTISEKLTAA
430 440
LSPPRKNGGW GDIRDHELCK SYRRLQ