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 Q8I136

Entry ID Method Resolution Chain Position Source
AF-Q8I136-F1 Predicted AlphaFoldDB

No variants for Q8I136

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8I136

No associated diseases with Q8I136

3 regional properties for Q8I136

Type Name Position InterPro Accession
domain Ricin B, lectin domain 461 - 583 IPR000772
domain Glycosyltransferase 2-like 154 - 332 IPR001173
domain N-acetylgalactosaminyltransferase 154 - 449 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.

2 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.
protein O-linked glycosylation via threonine The glycosylation of protein via the O3 atom of peptidyl-threonine, forming O3-glycosyl-L-threonine; the most common forms are N-acetylgalactosaminyl, mannosyl, and galactosyl threonine.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q10471 GALNT2 Polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens (Human) PR
Q8BVG5 Galnt14 Polypeptide N-acetylgalactosaminyltransferase 14 Mus musculus (Mouse) PR
O61397 gly-7 Probable N-acetylgalactosaminyltransferase 7 Caenorhabditis elegans PR
Q7K755 gly-11 Putative polypeptide N-acetylgalactosaminyltransferase 11 Caenorhabditis elegans PR
P34678 gly-3 Polypeptide N-acetylgalactosaminyltransferase 3 Caenorhabditis elegans PR
10 20 30 40 50 60
MLPRMLKMKT VGTVLAVIWL FGLAFIYVQS TSSSLRPPGR HPPPLPQLDP LIPQNPPQND
70 80 90 100 110 120
EIRPKKSAPP IPTINLAEDT TIHERTEKDV TWKTFDVEKF LNKGKWHQGE DKYKANSFNQ
130 140 150 160 170 180
EASDALNPTR KIPDSREPQC RDVDYSKVGM QPTTVIITYH NEARSSLLRT VFSVFNQSPE
190 200 210 220 230 240
ELLLEIVLVD DNSQDVEIGK ELAQIQRITV LRNNQREGLI RSRVKGAQVA RAPVLTFLDS
250 260 270 280 290 300
HIECNQKWLE PLLARIAENP KAVVAPIIDV INVDNFNYVG ASADLRGGFD WTLVFRWEFM
310 320 330 340 350 360
NEQLRKERHA HPTAPIRSPT MAGGLFAISK EWFNELGTYD LDMEVWGGEN LEMSFRVWQC
370 380 390 400 410 420
GGSLEIMPCS RVGHVFRKKH PYTFPGGSGN VFQKNTRRAA EVWMDEYKAI YLKNVPSARF
430 440 450 460 470 480
VNFGDITDRL AIRDRLQCKS FKWYLENVYP QLEIPRKTPG KSFQMKIGNL CLDSMARKES
490 500 510 520 530 540
EAPGLFGCHG TGGNQEWVFD QLTKTFKNAI SQLCLDFSSN TENKTVTMVK CENLRPDTMV
550 560 570 580
VEKNGWLTQG GKCLTVNQGS GGDWLIYGAH CELNNGAQRW IFEKLDTYE