Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
Lchi04244.g
View in Genome Browser
Position
Scaffold32:7580483-7588388 (-)
7905bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the small heat shock protein (HSP20) family
Organism
Liriodendron chinense
Also AS AT1G53540

Gene Structure

upstream:
Get Sequence

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Lchi28031.g Belongs to the small heat shock protein (HSP20) family
Lchi04244.g Belongs to the small heat shock protein (HSP20) family
Lchi26034.g Ankyrin repeat domain-containing protein
Regulatory gene
Lchi00798.g ZINC FINGER protein
Lchi01186.g Protein BASIC PENTACYSTEINE7-like
Lchi01564.g 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:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0009507 chloroplast CC
GO:0009536 plastid CC
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
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.