Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
PH02Gene48919
View in Genome Browser
Position
hic_scaffold_10:36294771-36300129 (-)
5358bp
Gene Type
gene
Gene Description (Protein Product)
Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser Thr consensus motif in nascent polypeptide chains
Organism
Phyllostachys edulis
Also AS AT5G66680

Gene Structure

upstream:
Get Sequence

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
PH02Gene49228 Glycosyl hydrolase family 63 C-terminal domain
PH02Gene49003 Ergosterol biosynthesis ERG4/ERG24 family
PH02Gene49679 Belongs to the glycosyl hydrolase 31 family
Regulatory gene
PH02Gene00185 GAGA binding protein-like family
PH02Gene00452 DNA-binding domain in plant proteins such as APETALA2 and EREBPs
PH02Gene00769 TCP family transcription factor

Load All Networks

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 Pathway KEGG Pathway
GO Term Description GO Category
GO:0000902 cell morphogenesis BP
GO:0005575 cellular_component CC
GO:0005618 cell wall CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005634 nucleus CC
GO:0005730 nucleolus CC
GO:0005737 cytoplasm CC
GO:0005773 vacuole CC
GO:0005774 vacuolar membrane CC
GO:0005783 endoplasmic reticulum CC
GO:0005789 endoplasmic reticulum membrane CC
GO:0005794 Golgi apparatus CC
GO:0005886 plasma membrane CC
GO:0005911 cell-cell junction CC
GO:0006464 protein modification process BP
GO:0006486 protein glycosylation BP
GO:0006487 protein N-linked glycosylation BP
GO:0006807 nitrogen compound metabolic process BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0008250 oligosaccharyltransferase complex CC
GO:0009058 biosynthetic process BP
GO:0009059 macromolecule biosynthetic process BP
GO:0009100 glycoprotein metabolic process BP
GO:0009101 glycoprotein biosynthetic process BP
GO:0009505 plant-type cell wall CC
GO:0009506 plasmodesma CC
GO:0009653 anatomical structure morphogenesis BP
GO:0009664 plant-type cell wall organization BP
GO:0009826 unidimensional cell growth BP
GO:0009987 cellular process BP
GO:0012505 endomembrane system CC
GO:0016020 membrane CC
GO:0016043 cellular component organization BP
GO:0016049 cell growth BP
GO:0018193 peptidyl-amino acid modification BP
GO:0018196 obsolete peptidyl-asparagine modification BP
GO:0018279 protein N-linked glycosylation via asparagine BP
GO:0019538 protein metabolic process BP
GO:0030054 cell junction CC
GO:0030312 external encapsulating structure CC
GO:0031090 organelle membrane CC
GO:0031974 membrane-enclosed lumen CC
GO:0031981 nuclear lumen CC
GO:0031984 organelle subcompartment CC
GO:0032502 developmental process BP
GO:0032989 cellular component morphogenesis BP
GO:0032991 protein-containing complex CC
GO:0034645 cellular macromolecule biosynthetic process BP
GO:0036211 protein modification process BP
GO:0040007 growth BP
GO:0042175 nuclear outer membrane-endoplasmic reticulum membrane network CC
GO:0043170 macromolecule metabolic process BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043228 non-membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043232 intracellular non-membrane-bounded organelle CC
GO:0043233 organelle lumen 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:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044425 obsolete membrane part CC
GO:0044428 obsolete nuclear part CC
GO:0044432 obsolete endoplasmic reticulum part CC
GO:0044437 obsolete vacuolar part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044464 obsolete cell part CC
GO:0045229 external encapsulating structure organization BP
GO:0048589 developmental growth BP
GO:0048856 anatomical structure development BP
GO:0048869 cellular developmental process BP
GO:0055044 symplast CC
GO:0060560 developmental growth involved in morphogenesis BP
GO:0070013 intracellular organelle lumen CC
GO:0070085 glycosylation BP
GO:0071554 cell wall organization or biogenesis BP
GO:0071555 cell wall organization BP
GO:0071669 plant-type cell wall organization or biogenesis BP
GO:0071704 organic substance metabolic process BP
GO:0071840 cellular component organization or biogenesis BP
GO:0071944 cell periphery CC
GO:0098588 bounding membrane of organelle CC
GO:0098796 membrane protein complex CC
GO:0098805 membrane CC
GO:0098827 endoplasmic reticulum subcompartment CC
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
GO:1902494 catalytic complex CC
GO:1990234 transferase complex CC
KEGG Term Name Description
map04141 Protein processing in endoplasmic reticulum The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.
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].