Basic Information
Gene ID
Position
chr2:22739986-22748619 (-)
8633bp
Gene Type
gene
Gene Description (Protein Product)
Dolichol-phosphate
Cytochrome p450
Belongs to the cytochrome P450 family
Organism
Also AS Potri.001G109100Potri.002G010300Potri.002G010466AT1G12740AT1G20575Potri.001G109100.v4.1Potri.002G010300.v4.1Potri.002G010466.v4.1

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Potra2n7c16447 Lipid phosphate phosphatase epsilon
Potra2n3c6526 Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis
Potra2n6c14162 Lipid phosphate phosphatase gamma
Regulatory gene
Potra2n10c20596 Dof zinc finger protein
Potra2n10c20949 Cyclic dof factor
Potra2n10c21715 Protein 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


Pathway
GO Term Description GO Category
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:0008150 biological_process BP
GO:0012505 endomembrane system CC
GO:0031501 mannosyltransferase complex CC
GO:0032991 protein-containing complex CC
GO:0033185 dolichol-phosphate-mannose synthase complex CC
GO:0042221 response to chemical BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0044424 obsolete intracellular part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044464 obsolete cell part CC
GO:0050896 response to stimulus BP
GO:0060359 response to ammonium ion BP
GO:1901698 response to nitrogen compound BP
GO:1902494 catalytic complex CC
GO:1990234 transferase complex CC
KEGG Term Name Description
map01100 Metabolic pathways -
map01100 Metabolic pathways -
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].