Basic Information
Gene ID
AALBA5B513940
Position
aalba5_s00903857:142-794 (+)
652bp
Gene Type
gene
Gene Description (Protein Product)
Chaperone protein dnaJ
Organism
Also AS AT5G22060

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
AALBA5B625303 MADS-box transcription factor
AALBA5B843458 Agamous-like MADS-box protein
AALBA5B762863 ubiquitin-NEDD8-like protein

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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:0000003 reproduction BP
GO:0003006 developmental process involved in reproduction 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:0005829 cytosol CC
GO:0005886 plasma membrane CC
GO:0005911 cell-cell junction CC
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:0009506 plasmodesma CC
GO:0009628 response to abiotic stimulus BP
GO:0009648 photoperiodism BP
GO:0009651 response to salt stress BP
GO:0009791 post-embryonic development BP
GO:0009909 regulation of flower development BP
GO:0009911 positive regulation of flower development BP
GO:0010228 vegetative to reproductive phase transition of meristem BP
GO:0016020 membrane CC
GO:0022414 reproductive process BP
GO:0030054 cell junction CC
GO:0030312 external encapsulating structure CC
GO:0031974 membrane-enclosed lumen CC
GO:0031981 nuclear lumen CC
GO:0032501 multicellular organismal process BP
GO:0032502 developmental 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:0043462 regulation of ATP-dependent activity BP
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044428 obsolete nuclear part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044464 obsolete cell part CC
GO:0048518 positive regulation of biological process BP
GO:0048573 photoperiodism, flowering BP
GO:0048580 regulation of post-embryonic development BP
GO:0048582 positive regulation of post-embryonic development BP
GO:0048608 reproductive structure development BP
GO:0048731 system development BP
GO:0048831 regulation of shoot system development BP
GO:0048856 anatomical structure development BP
GO:0050789 regulation of biological process BP
GO:0050790 regulation of catalytic activity BP
GO:0050793 regulation of developmental process BP
GO:0050896 response to stimulus BP
GO:0051094 positive regulation of developmental process BP
GO:0051239 regulation of multicellular organismal process BP
GO:0051240 positive regulation of multicellular organismal process BP
GO:0051336 regulation of hydrolase activity BP
GO:0055044 symplast CC
GO:0061458 reproductive system development BP
GO:0065007 biological regulation BP
GO:0065009 regulation of molecular function BP
GO:0070013 intracellular organelle lumen CC
GO:0071944 cell periphery CC
GO:2000026 regulation of multicellular organismal development BP
GO:2000241 regulation of reproductive process BP
GO:2000243 positive regulation of reproductive 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.