Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
PH02Gene49679
View in Genome Browser
Position
hic_scaffold_21:97851459-97855195 (-)
3736bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the glycosyl hydrolase 31 family
Organism
Phyllostachys edulis
Also AS AT5G63840

Gene Structure

upstream:
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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
PH02Gene51106 Belongs to the 14-3-3 family
PH02Gene50475 Belongs to the AAA ATPase family
PH02Gene50312 Belongs to the 14-3-3 family
Regulatory gene
PH02Gene00783 tesmin TSO1-like CXC
PH02Gene00867 bZIP transcription factor
PH02Gene01127 Tesmin/TSO1-like CXC domain

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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 Pathway KEGG Pathway
GO Term Description GO Category
GO:0000271 polysaccharide biosynthetic process BP
GO:0000902 cell morphogenesis BP
GO:0003674 molecular_function MF
GO:0003824 catalytic activity MF
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds 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:0005975 carbohydrate metabolic process BP
GO:0005976 polysaccharide metabolic process BP
GO:0006073 cellular glucan metabolic process BP
GO:0006464 protein modification process BP
GO:0006491 N-glycan processing BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006950 response to stress BP
GO:0006952 defense response 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:0009250 glucan biosynthetic process BP
GO:0009507 chloroplast CC
GO:0009536 plastid CC
GO:0009605 response to external stimulus BP
GO:0009607 response to biotic stimulus BP
GO:0009617 response to bacterium BP
GO:0009653 anatomical structure morphogenesis BP
GO:0009826 unidimensional cell growth BP
GO:0009987 cellular process BP
GO:0010035 response to inorganic substance BP
GO:0010038 response to metal ion BP
GO:0012505 endomembrane system CC
GO:0015926 glucosidase activity MF
GO:0016043 cellular component organization BP
GO:0016049 cell growth BP
GO:0016051 carbohydrate biosynthetic process BP
GO:0016787 hydrolase activity MF
GO:0016798 hydrolase activity, acting on glycosyl bonds MF
GO:0019538 protein metabolic process BP
GO:0030243 cellulose metabolic process BP
GO:0030244 cellulose biosynthetic process BP
GO:0030587 sorocarp development BP
GO:0031288 sorocarp morphogenesis BP
GO:0032502 developmental process BP
GO:0032989 cellular component morphogenesis BP
GO:0033692 cellular polysaccharide biosynthetic process BP
GO:0033919 glucan 1,3-alpha-glucosidase activity MF
GO:0034637 cellular carbohydrate biosynthetic process BP
GO:0034645 cellular macromolecule biosynthetic process BP
GO:0036211 protein modification process BP
GO:0040007 growth BP
GO:0042221 response to chemical BP
GO:0042742 defense response to bacterium BP
GO:0043170 macromolecule metabolic process BP
GO:0043207 response to external biotic stimulus 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:0043687 post-translational protein modification BP
GO:0044042 glucan metabolic process 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:0044262 cellular carbohydrate metabolic process BP
GO:0044264 cellular polysaccharide 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:0046686 response to cadmium ion BP
GO:0048589 developmental growth BP
GO:0048856 anatomical structure development BP
GO:0048869 cellular developmental process BP
GO:0050896 response to stimulus BP
GO:0051273 beta-glucan metabolic process BP
GO:0051274 beta-glucan biosynthetic process BP
GO:0051703 biological process involved in intraspecies interaction between organisms BP
GO:0051704 obsolete multi-organism process BP
GO:0051707 response to other organism BP
GO:0060560 developmental growth involved in morphogenesis BP
GO:0071704 organic substance metabolic process BP
GO:0071840 cellular component organization or biogenesis BP
GO:0090599 alpha-glucosidase activity MF
GO:0090600 alpha-1,3-glucosidase activity MF
GO:0090702 socially cooperative development BP
GO:0098542 defense response to other organism BP
GO:0099120 socially cooperative development BP
GO:1901135 carbohydrate derivative metabolic process BP
GO:1901564 organonitrogen compound metabolic process BP
GO:1901576 organic substance biosynthetic process BP
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 -
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].