Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
AALBA5B960692
Position
aalba5_s00047479:6436-6768 (-)
332bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the heat shock protein 70 family
Organism
Abies alba
Also AS AT3G09440

Gene Structure

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

Regulation&Interaction
Protein-protein interaction (PPI)
AALBA5B961227 Hsp90 protein
AALBA5B986380 heat shock protein
AALBA5B990968 Belongs to the 14-3-3 family
Regulatory gene
AALBA5B003860 Myb-like protein L
AALBA5B008339 Dehydration-responsive element-binding protein 3-like
AALBA5B014981 transcription factor

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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:0000302 response to reactive oxygen species BP
GO:0003674 molecular_function MF
GO:0005488 binding MF
GO:0005515 protein binding MF
GO:0005524 ATP binding MF
GO:0005575 cellular_component CC
GO:0005576 extracellular region 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:0005773 vacuole CC
GO:0005774 vacuolar membrane CC
GO:0005794 Golgi apparatus CC
GO:0005829 cytosol CC
GO:0005886 plasma membrane CC
GO:0006464 protein modification process BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006950 response to stress BP
GO:0006979 response to oxidative stress BP
GO:0008144 obsolete drug binding MF
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0009266 response to temperature stimulus BP
GO:0009314 response to radiation BP
GO:0009408 response to heat BP
GO:0009416 response to light stimulus BP
GO:0009605 response to external stimulus BP
GO:0009607 response to biotic stimulus BP
GO:0009615 response to virus BP
GO:0009617 response to bacterium BP
GO:0009628 response to abiotic stimulus BP
GO:0009636 response to toxic substance BP
GO:0009642 response to light intensity BP
GO:0009644 response to high light intensity 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:0016020 membrane CC
GO:0016567 protein ubiquitination BP
GO:0017076 purine nucleotide binding MF
GO:0019538 protein metabolic process BP
GO:0019899 enzyme binding MF
GO:0030312 external encapsulating structure CC
GO:0030554 adenyl nucleotide binding MF
GO:0031090 organelle membrane CC
GO:0031625 ubiquitin protein ligase binding MF
GO:0032446 protein modification by small protein conjugation BP
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:0036211 protein modification process BP
GO:0042221 response to chemical BP
GO:0042493 response to xenobiotic stimulus BP
GO:0042542 response to hydrogen peroxide BP
GO:0043167 ion binding MF
GO:0043168 anion binding MF
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:0044237 cellular metabolic process BP
GO:0044238 primary metabolic process BP
GO:0044260 cellular macromolecule metabolic process BP
GO:0044267 protein metabolic process BP
GO:0044389 ubiquitin-like protein ligase binding MF
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular 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:0046677 response to antibiotic BP
GO:0046686 response to cadmium ion BP
GO:0048046 apoplast CC
GO:0050896 response to stimulus BP
GO:0051704 obsolete multi-organism process BP
GO:0051707 response to other organism BP
GO:0070647 protein modification by small protein conjugation or removal BP
GO:0071704 organic substance metabolic process BP
GO:0071944 cell periphery CC
GO:0097159 organic cyclic compound binding MF
GO:0097367 carbohydrate derivative binding MF
GO:0098588 bounding membrane of organelle CC
GO:0098805 membrane CC
GO:1901265 nucleoside phosphate binding MF
GO:1901363 heterocyclic compound binding MF
GO:1901564 organonitrogen compound metabolic process BP
GO:1901700 response to oxygen-containing compound BP
KEGG Term Name Description
map04144 Endocytosis Endocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins entering through clathrin-dependent endocytosis (CDE) have sequences in their cytoplasmic domains that bind to the APs (adaptor-related protein complexes) and enable their rapid removal from the PM. In addition to APs and clathrin, there are numerous accessory proteins including dynamin. Depending on the various proteins that enter the endosome membrane, these cargoes are sorted to distinct destinations. Some cargoes, such as nutrient receptors, are recycled back to the PM. Ubiquitylated membrane proteins, such as activated growth-factor receptors, are sorted into intraluminal vesicles and eventually end up in the lysosome lumen via multivesicular endosomes (MVEs). There are distinct mechanisms of clathrin-independent endocytosis (CIE) depending upon the cargo and the cell type.
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.
map03040 Spliceosome After transcription, eukaryotic mRNA precursors contain protein-coding exons and noncoding introns. In the following splicing, introns are excised and exons are joined by a macromolecular complex, the spliceosome. The standard spliceosome is made up of five small nuclear ribonucleoproteins (snRNPs), U1, U2, U4, U5, and U6 snRNPs, and several spliceosome-associated proteins (SAPs). Spliceosomes are not a simple stable complex, but a dynamic family of particles that assemble on the mRNA precursor and help fold it into a conformation that allows transesterification to proceed. Various spliceosome forms (e.g. A-, B- and C-complexes) have been identified.