Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
ACNE_29021.g
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Position
acne_107:3616084-3618200 (-)
2116bp
Gene Type
gene
Gene Description (Protein Product)
Heat shock cognate 70 kDa
Organism
Acer negundo
Also AS AT3G12580

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
ACNE_29858.g Belongs to the 14-3-3 family
ACNE_29106.g The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH
ACNE_30064.g Pre-mRNA-splicing 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:0002020 protease binding MF
GO:0003674 molecular_function MF
GO:0005488 binding MF
GO:0005515 protein 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:0005634 nucleus CC
GO:0005730 nucleolus CC
GO:0005737 cytoplasm CC
GO:0005773 vacuole CC
GO:0005774 vacuolar membrane CC
GO:0005794 Golgi apparatus CC
GO:0005829 cytosol CC
GO:0005840 ribosome CC
GO:0005886 plasma membrane CC
GO:0005911 cell-cell junction CC
GO:0006950 response to stress BP
GO:0006952 defense response BP
GO:0008150 biological_process BP
GO:0009266 response to temperature stimulus BP
GO:0009408 response to heat BP
GO:0009409 response to cold BP
GO:0009506 plasmodesma CC
GO:0009507 chloroplast CC
GO:0009526 plastid envelope CC
GO:0009536 plastid CC
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:0009620 response to fungus BP
GO:0009628 response to abiotic stimulus BP
GO:0009941 chloroplast envelope CC
GO:0009987 cellular process BP
GO:0010029 regulation of seed germination BP
GO:0010035 response to inorganic substance BP
GO:0010038 response to metal ion BP
GO:0010118 stomatal movement BP
GO:0010187 negative regulation of seed germination BP
GO:0012505 endomembrane system CC
GO:0016020 membrane CC
GO:0016363 nuclear matrix CC
GO:0019899 enzyme binding MF
GO:0022626 cytosolic ribosome CC
GO:0030054 cell junction CC
GO:0030312 external encapsulating structure CC
GO:0031090 organelle membrane CC
GO:0031967 organelle envelope CC
GO:0031974 membrane-enclosed lumen CC
GO:0031975 envelope CC
GO:0031981 nuclear lumen CC
GO:0032991 protein-containing complex CC
GO:0034399 nuclear periphery CC
GO:0042221 response to chemical BP
GO:0042742 defense response to bacterium BP
GO:0043207 response to external biotic stimulus 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:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044428 obsolete nuclear 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:0044445 obsolete cytosolic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044464 obsolete cell part CC
GO:0046686 response to cadmium ion BP
GO:0048046 apoplast CC
GO:0048519 negative regulation of biological process BP
GO:0048580 regulation of post-embryonic development BP
GO:0048581 negative regulation of post-embryonic development BP
GO:0050789 regulation of biological process BP
GO:0050793 regulation of developmental process BP
GO:0050832 defense response to fungus BP
GO:0050896 response to stimulus BP
GO:0051093 negative regulation of developmental process BP
GO:0051239 regulation of multicellular organismal process BP
GO:0051241 negative regulation of multicellular organismal process BP
GO:0051704 obsolete multi-organism process BP
GO:0051707 response to other organism BP
GO:0055044 symplast CC
GO:0065007 biological regulation BP
GO:0070013 intracellular organelle lumen CC
GO:0071944 cell periphery CC
GO:0080167 response to karrikin BP
GO:0090332 stomatal closure BP
GO:0098542 defense response to other organism BP
GO:0098588 bounding membrane of organelle CC
GO:0098805 membrane CC
GO:1900140 regulation of seedling development BP
GO:1990904 ribonucleoprotein complex CC
GO:2000026 regulation of multicellular organismal development 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.