Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
Juni_Chr1.1164.g
View in Genome Browser
Position
Chr1:10835282-10841605 (-)
6323bp
Gene Type
gene
Gene Description (Protein Product)
disulfide-isomerase
Organism
Juglans nigra
Also AS AT1G21750

Gene Structure

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

Regulation&Interaction
Protein-protein interaction (PPI)
Juni_Chr6.593.g Belongs to the peptidase C1 family
Juni_Chr15.374.g Belongs to the peptidase C1 family
Juni_Chr4.1297.g Endoplasmic
Regulatory gene
Juni_Chr1.2751.g tesmin TSO1-like CXC
Juni_Chr10.2068.g tesmin TSO1-like CXC
Juni_Chr11.2485.g 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

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:0000003 reproduction BP
GO:0000322 storage vacuole CC
GO:0000323 lytic vacuole CC
GO:0000325 plant-type vacuole CC
GO:0000326 protein storage vacuole CC
GO:0000327 lytic vacuole within protein storage vacuole CC
GO:0003006 developmental process involved in reproduction BP
GO:0003674 molecular_function MF
GO:0003756 protein disulfide isomerase activity MF
GO:0003824 catalytic activity MF
GO:0005575 cellular_component CC
GO:0005618 cell wall CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005773 vacuole CC
GO:0005774 vacuolar membrane CC
GO:0005783 endoplasmic reticulum CC
GO:0005788 endoplasmic reticulum lumen CC
GO:0005794 Golgi apparatus CC
GO:0005886 plasma membrane CC
GO:0006457 protein folding BP
GO:0006950 response to stress BP
GO:0006970 response to osmotic stress BP
GO:0007275 multicellular organism development BP
GO:0008150 biological_process BP
GO:0009314 response to radiation BP
GO:0009416 response to light stimulus BP
GO:0009505 plant-type cell wall CC
GO:0009507 chloroplast CC
GO:0009532 plastid stroma CC
GO:0009536 plastid CC
GO:0009570 chloroplast stroma CC
GO:0009579 thylakoid CC
GO:0009628 response to abiotic stimulus BP
GO:0009642 response to light intensity BP
GO:0009644 response to high light intensity BP
GO:0009651 response to salt stress BP
GO:0009719 response to endogenous stimulus BP
GO:0009725 response to hormone BP
GO:0009735 response to cytokinin BP
GO:0009790 embryo development BP
GO:0009791 post-embryonic development BP
GO:0009793 embryo development ending in seed dormancy BP
GO:0009888 tissue development BP
GO:0009892 negative regulation of metabolic process BP
GO:0009960 endosperm development BP
GO:0009987 cellular process BP
GO:0010033 response to organic substance BP
GO:0010035 response to inorganic substance BP
GO:0010038 response to metal ion BP
GO:0010043 response to zinc ion BP
GO:0010109 regulation of photosynthesis BP
GO:0010154 fruit development BP
GO:0010205 photoinhibition BP
GO:0010941 regulation of cell death BP
GO:0012505 endomembrane system CC
GO:0016020 membrane CC
GO:0016853 isomerase activity MF
GO:0016860 intramolecular oxidoreductase activity MF
GO:0016864 intramolecular oxidoreductase activity, transposing S-S bonds MF
GO:0019222 regulation of metabolic process BP
GO:0022414 reproductive process BP
GO:0030312 external encapsulating structure CC
GO:0031090 organelle membrane CC
GO:0031323 regulation of cellular metabolic process BP
GO:0031324 negative regulation of cellular metabolic process BP
GO:0031974 membrane-enclosed lumen CC
GO:0032501 multicellular organismal process BP
GO:0032502 developmental process BP
GO:0033554 cellular response to stress BP
GO:0034975 protein folding in endoplasmic reticulum BP
GO:0034976 response to endoplasmic reticulum stress BP
GO:0042221 response to chemical BP
GO:0042548 regulation of photosynthesis, light reaction BP
GO:0043067 regulation of programmed cell death BP
GO:0043155 negative regulation of photosynthesis, light reaction BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043233 organelle lumen CC
GO:0043467 regulation of generation of precursor metabolites and energy BP
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044432 obsolete endoplasmic reticulum part CC
GO:0044434 obsolete chloroplast part CC
GO:0044435 obsolete plastid 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:0046686 response to cadmium ion BP
GO:0048316 seed development BP
GO:0048519 negative regulation of biological process BP
GO:0048523 negative regulation of cellular process BP
GO:0048608 reproductive structure development BP
GO:0048731 system development BP
GO:0048856 anatomical structure development BP
GO:0050789 regulation of biological process BP
GO:0050794 regulation of cellular process BP
GO:0050896 response to stimulus BP
GO:0051716 cellular response to stimulus BP
GO:0061458 reproductive system development BP
GO:0065007 biological regulation BP
GO:0070013 intracellular organelle lumen CC
GO:0071944 cell periphery CC
GO:0098588 bounding membrane of organelle CC
GO:0098805 membrane CC
GO:0140096 catalytic activity, acting on a protein MF
GO:1905156 negative regulation of photosynthesis 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.