Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
AALBA5B986380
Position
aalba5_s00289116:732-11945 (+)
11213bp
Gene Type
gene
Gene Description (Protein Product)
heat shock protein
Organism
Abies alba
Also AS AT2G04030

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
AALBA5B995290 Belongs to the heat shock protein 70 family
AALBA5B998808 H ACA ribonucleoprotein complex subunit 2-like
Regulatory gene
AALBA5B014147 Transcription factor
AALBA5B018380 transcription factor
AALBA5B023305 dof zinc finger protein

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail


Pathway
Go Pathway KEGG Pathway
GO Term Description GO Category
GO:0000166 nucleotide binding MF
GO:0003674 molecular_function MF
GO:0005488 binding MF
GO:0005524 ATP binding 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:0005739 mitochondrion CC
GO:0008144 obsolete drug binding MF
GO:0009507 chloroplast CC
GO:0009532 plastid stroma CC
GO:0009536 plastid CC
GO:0009570 chloroplast stroma CC
GO:0017076 purine nucleotide binding MF
GO:0030312 external encapsulating structure CC
GO:0030554 adenyl nucleotide binding MF
GO:0032553 ribonucleotide binding MF
GO:0032555 purine ribonucleotide binding MF
GO:0032559 adenyl ribonucleotide binding MF
GO:0035639 purine ribonucleoside triphosphate binding MF
GO:0036094 small molecule binding MF
GO:0043167 ion binding MF
GO:0043168 anion binding MF
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044434 obsolete chloroplast part CC
GO:0044435 obsolete plastid part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044464 obsolete cell part CC
GO:0071944 cell periphery CC
GO:0097159 organic cyclic compound binding MF
GO:0097367 carbohydrate derivative binding MF
GO:1901265 nucleoside phosphate binding MF
GO:1901363 heterocyclic compound binding MF
KEGG Term Name Description
map04626 Plant-pathogen interaction Plants lack animal-like adaptive immunity mechanisms, and therefore have evolved a specific system with multiple layers against invading pathogens. The primary response includes the perception of pathogens by cell-surface pattern-recognition receptors (PRRs) and is referred to as PAMP-triggered immunity (PTI). Activation of FLS2 and EFR triggers MAPK signaling pathway that activates defense genes for antimictobial compounds. The increase in the cytosolic Ca2+ concentration is also a regulator for production of reactive oxygen species and localized programmed cell death/hypersensitive response. The secondary response is called effector-triggered immunity (ETI). Pathogens can acquire the ability to suppress PTI by directly injecting effector proteins into the plant cell through secretion systems. In addition, pathogens can manipulate plant hormone signaling pathways to evade host immune responses using coronatine toxin. Some plants possess specific intracellular surveillance proteins (R proteins) to monitor the presence of pathogen virulence proteins. This ETI occurs with localized programmed cell death to arrest pathogen growth, resulting in cultivar-specific disease resistance.
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.