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 Q6BVB2

Entry ID Method Resolution Chain Position Source
AF-Q6BVB2-F1 Predicted AlphaFoldDB

No variants for Q6BVB2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6BVB2

No associated diseases with Q6BVB2

2 regional properties for Q6BVB2

Type Name Position InterPro Accession
domain Glycosyl transferase, family 1 352 - 513 IPR001296
domain ALG11 mannosyltransferase, N-terminal 113 - 324 IPR031814

Functions

Description
EC Number 2.4.1.131 Hexosyltransferases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
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.

1 GO annotations of molecular function

Name Definition
GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity Catalysis of the reaction: an alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H+. This reaction is the transfer of an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.

1 GO annotations of biological process

Name Definition
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGYLVVIGVI ACVAYGILQV VSTVLPRLLL VPSQNWQDKI KKEIEQPMVR YLKVGNKRSS
70 80 90 100 110 120
YRRRLVLASK QPSFYTNFVN NKIKVASVDS QNDEGEFLAE MKKRDVRDPQ RKIIYGFFHP
130 140 150 160 170 180
YANNGGGGER VLWQAVQATL ATSDRNIVAI YTTNYESDPT SILDKVEAKF QISRLDEDRI
190 200 210 220 230 240
VFVYLRKYAR LIDGDYWKRF TLIGQLFGSM VLSWEAMFEL SPDVWIDTIG LPGSYLLVSL
250 260 270 280 290 300
VLKIPIMSYV HYPIIQPEMF NKLKFQGLSQ IRVPKLSEIK TDVFSIGKLI YWSGVFYFYK
310 320 330 340 350 360
YLGSLVNITL ANGSWTFNHI SNIWTINKDE AGYEMDILYP PCGTETLTKN VETLGSRENK
370 380 390 400 410 420
LLFIAQFRPE KRHSLILRQY SKFLVNATSI GTPLKNIPTL VFLGSCRTPD DTKTLHDLKQ
430 440 450 460 470 480
EVDDLELNGY VEFVVDCSYE DIMVWLSKVK FGLNAMWNEH FGIGVVEYMS RGVIPLCHAS
490 500 510 520 530 540
AGPLLDIVTN WDNEPTSVSW YNNTGFFFKD KSDPDFDLSL QSDTASEFLQ FSSRDNKDST
550 560 570 580 590 600
STYPTLARLL DELFITNPDL ISETRLQSMR ENGVKSVLEK FSNGVFTLKW MQYSNQLGDL
610
EKSYREERRS GIEKVY