Basic Information
Gene ID
Pop_G14G045087
Position
chrG14:8489175-8501833 (-)
12658bp
Gene Type
gene
Gene Description (Protein Product)
Dol-P-Man Man(5)GlcNAc(2)-PP-Dol
Organism
Also AS Potri.014G131600AT2G47760Potri.014G131600.v4.1

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Pop_G18G019063 Functions as component of the Arp2 3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks
Pop_G18G080184 GPI mannosyltransferase
Pop_G14G088851 N-acetylglucosaminyltransferase II (MGAT2)
Regulatory gene
Pop_A01G004199 GAGA binding protein-like family
Pop_A01G004498 Tesmin/TSO1-like CXC domain
Pop_A01G032290 tesmin TSO1-like CXC

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail

Expression Profile
DataSet Number of Samples expressed(TPM>1) Mean Min Max Standard deviation(SD) Coeffcient variation(CV)


Pathway
GO Term Description GO Category
GO:0000030 mannosyltransferase activity MF
GO:0000033 alpha-1,3-mannosyltransferase activity MF
GO:0003674 molecular_function MF
GO:0003824 catalytic activity MF
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005783 endoplasmic reticulum CC
GO:0006464 protein modification process BP
GO:0006486 protein glycosylation BP
GO:0006807 nitrogen compound metabolic process BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0009058 biosynthetic process BP
GO:0009059 macromolecule biosynthetic process BP
GO:0009100 glycoprotein metabolic process BP
GO:0009101 glycoprotein biosynthetic process BP
GO:0009987 cellular process BP
GO:0012505 endomembrane system CC
GO:0016740 transferase activity MF
GO:0016757 glycosyltransferase activity MF
GO:0016758 hexosyltransferase activity MF
GO:0019538 protein metabolic process BP
GO:0034645 cellular macromolecule biosynthetic process BP
GO:0036211 protein modification process BP
GO:0043170 macromolecule metabolic process BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043412 macromolecule modification BP
GO:0043413 macromolecule glycosylation BP
GO:0044237 cellular metabolic process BP
GO:0044238 primary metabolic process BP
GO:0044249 cellular biosynthetic process BP
GO:0044260 cellular macromolecule metabolic process BP
GO:0044267 protein metabolic process BP
GO:0044424 obsolete intracellular part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044464 obsolete cell part CC
GO:0070085 glycosylation BP
GO:0071704 organic substance metabolic process BP
GO:0097502 mannosylation BP
GO:1901135 carbohydrate derivative metabolic process BP
GO:1901137 carbohydrate derivative biosynthetic process BP
GO:1901564 organonitrogen compound metabolic process BP
GO:1901566 organonitrogen compound biosynthetic process BP
GO:1901576 organic substance biosynthetic process BP
KEGG Term Name Description
map01100 Metabolic pathways -
map00513 Various types of N-glycan biosynthesis -
map00510 N-Glycan biosynthesis N-glycans or asparagine-linked glycans are major constituents of glycoproteins in eukaryotes. N-glycans are covalently attached to asparagine with the consensus sequence of Asn-X-Ser/Thr by an N-glycosidic bond, GlcNAc b1- Asn. Biosynthesis of N-glycans begins on the cytoplasmic face of the ER membrane with the transferase reaction of UDP-GlcNAc and the lipid-like precursor P-Dol (dolichol phosphate) to generate GlcNAc a1- PP-Dol. After sequential addition of monosaccharides by ALG glycosyltransferases [MD:M00055], the N-glycan precursor is attached by the OST (oligosaccharyltransferase) complex to the polypeptide chain that is being synthesized and translocated through the ER membrane. The protein-bound N-glycan precursor is subsequently trimmed, extended, and modified in the ER and Golgi by a complex series of reactions catalyzed by membrane-bound glycosidases and glycosyltransferases. N-glycans thus synthesized are classified into three types: high-mannose type, complex type, and hybrid type. Defects in N-glycan biosynthesis lead to a variety of human diseases known as congenital disorders of glycosylation [DS:H00118 H00119].