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

3 structures for Q12001

Entry ID Method Resolution Chain Position Source
6SNH EM 390 A X 1-544 PDB
6SNI EM 300 A X 1-544 PDB
AF-Q12001-F1 Predicted AlphaFoldDB

8 variants for Q12001

Variant ID(s) Position Change Description Diseaes Association Provenance
s15-329426 3 I>M No SGRP
s15-329428 4 G>D No SGRP
s15-329545 43 F>S No SGRP
s15-329562 49 L>V No SGRP
s15-330439 341 I>T No SGRP
s15-330567 384 I>V No SGRP
s15-330813 466 D>N No SGRP
s15-330883 489 A>V No SGRP

No associated diseases with Q12001

4 regional properties for Q12001

Type Name Position InterPro Accession
conserved_site Aldo/keto reductase, conserved site 39 - 56 IPR018170-1
conserved_site Aldo/keto reductase, conserved site 145 - 162 IPR018170-2
conserved_site Aldo/keto reductase, conserved site 261 - 276 IPR018170-3
domain NADP-dependent oxidoreductase domain 17 - 289 IPR023210

Functions

Description
EC Number 2.4.1.267 Hexosyltransferases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
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.

2 GO annotations of molecular function

Name Definition
dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity Catalysis of the addition of the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation; the transfer of glucose from dolichyl phosphate glucose (Dol-P-Glc) on to the lipid-linked oligosaccharide Man(9)GlcNAc(2)-PP-Dol.
hexosyltransferase activity Catalysis of the transfer of a hexosyl group from one compound (donor) to another (acceptor).

5 GO annotations of biological process

Name Definition
aerobic respiration The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which requires oxygen as the terminal electron acceptor.
dolichol-linked oligosaccharide biosynthetic process The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
oligosaccharide-lipid intermediate biosynthetic process The chemical reactions and pathways resulting in the formation of an oligosaccharide-lipid intermediate, such as a molecule of dolichol-P-man or dolicol-P-Glc used in N-linked glycosylation.
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.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P40351 ALG8 Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MAIGKRLLVN KPAEESFYAS PMYDFLYPFR PVGNQWLPEY IIFVCAVILR CTIGLGPYSG
70 80 90 100 110 120
KGSPPLYGDF EAQRHWMEIT QHLPLSKWYW YDLQYWGLDY PPLTAFHSYL LGLIGSFFNP
130 140 150 160 170 180
SWFALEKSRG FESPDNGLKT YMRSTVIISD ILFYFPAVIY FTKWLGRYRN QSPIGQSIAA
190 200 210 220 230 240
SAILFQPSLM LIDHGHFQYN SVMLGLTAYA INNLLDEYYA MAAVCFVLSI CFKQMALYYA
250 260 270 280 290 300
PIFFAYLLSR SLLFPKFNIA RLTVIAFATL ATFAIIFAPL YFLGGGLKNI HQCIHRIFPF
310 320 330 340 350 360
ARGIFEDKVA NFWCVTNVFV KYKERFTIQQ LQLYSLIATV IGFLPAMIMT LLHPKKHLLP
370 380 390 400 410 420
YVLIACSMSF FLFSFQVHEK TILIPLLPIT LLYSSTDWNV LSLVSWINNV ALFTLWPLLK
430 440 450 460 470 480
KDGLHLQYAV SFLLSNWLIG NFSFITPRFL PKSLTPGPSI SSINSDYRRR SLLPYNVVWK
490 500 510 520 530 540
SFIIGTYIAM GFYHFLDQFV APPSKYPDLW VLLNCAVGFI CFSIFWLWSY YKIFTSGSKS
MKDL