Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
gene-IMY05_C4827000200
View in Genome Browser
Position
JAEQKX010001012.1:4311-5911 (+)
1600bp
Gene Type
gene
Gene Description (Protein Product)
heat shock protein 70
Organism
Salix suchowensis
Also AS AT1G16030

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
gene-IMY05_C5274000100 Calreticulin-3-like
gene-IMY05_C5091003200 Heat shock 70 kDa protein
gene-IMY05_C5089000500 Tetratricopeptide repeat

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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:0000054 ribosomal subunit export from nucleus BP
GO:0002181 cytoplasmic translation BP
GO:0003674 molecular_function MF
GO:0003824 catalytic activity MF
GO:0005488 binding MF
GO:0005515 protein binding MF
GO:0005516 calmodulin binding MF
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005829 cytosol CC
GO:0005844 polysome CC
GO:0005886 plasma membrane CC
GO:0006139 nucleobase-containing compound metabolic process BP
GO:0006364 rRNA processing BP
GO:0006396 RNA processing BP
GO:0006403 RNA localization BP
GO:0006405 RNA export from nucleus BP
GO:0006412 translation BP
GO:0006414 translational elongation BP
GO:0006415 translational termination BP
GO:0006450 regulation of translational fidelity BP
GO:0006452 translational frameshifting BP
GO:0006457 protein folding BP
GO:0006458 'de novo' protein folding BP
GO:0006518 peptide metabolic process BP
GO:0006611 protein export from nucleus BP
GO:0006725 cellular aromatic compound metabolic process BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006810 transport BP
GO:0006886 intracellular protein transport BP
GO:0006913 nucleocytoplasmic transport BP
GO:0006950 response to stress BP
GO:0007154 cell communication BP
GO:0008104 protein localization BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0009058 biosynthetic process BP
GO:0009059 macromolecule biosynthetic process BP
GO:0009267 cellular response to starvation BP
GO:0009605 response to external stimulus BP
GO:0009987 cellular process BP
GO:0009991 response to extracellular stimulus BP
GO:0010467 gene expression BP
GO:0010494 cytoplasmic stress granule CC
GO:0015031 protein transport BP
GO:0015833 peptide transport BP
GO:0015931 nucleobase-containing compound transport BP
GO:0016020 membrane CC
GO:0016043 cellular component organization BP
GO:0016070 RNA metabolic process BP
GO:0016072 rRNA metabolic process BP
GO:0016462 pyrophosphatase activity MF
GO:0016787 hydrolase activity MF
GO:0016817 hydrolase activity, acting on acid anhydrides MF
GO:0016818 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides MF
GO:0016887 ATP hydrolysis activity MF
GO:0017111 ribonucleoside triphosphate phosphatase activity MF
GO:0019538 protein metabolic process BP
GO:0022411 cellular component disassembly BP
GO:0022613 ribonucleoprotein complex biogenesis BP
GO:0031503 protein-containing complex localization BP
GO:0031667 response to nutrient levels BP
GO:0031668 cellular response to extracellular stimulus BP
GO:0031669 cellular response to nutrient levels BP
GO:0032984 protein-containing complex disassembly BP
GO:0032991 protein-containing complex CC
GO:0033036 macromolecule localization BP
GO:0033554 cellular response to stress BP
GO:0033750 ribosome localization BP
GO:0034470 ncRNA processing BP
GO:0034613 protein localization BP
GO:0034641 cellular nitrogen compound metabolic process BP
GO:0034645 cellular macromolecule biosynthetic process BP
GO:0034660 ncRNA metabolic process BP
GO:0035770 ribonucleoprotein granule CC
GO:0036464 cytoplasmic ribonucleoprotein granule CC
GO:0042149 cellular response to glucose starvation BP
GO:0042254 ribosome biogenesis BP
GO:0042594 response to starvation BP
GO:0042886 amide transport BP
GO:0043043 peptide biosynthetic process BP
GO:0043170 macromolecule metabolic process BP
GO:0043226 organelle CC
GO:0043228 non-membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043232 intracellular non-membrane-bounded organelle CC
GO:0043603 amide metabolic process BP
GO:0043604 amide biosynthetic process BP
GO:0043624 protein-containing complex disassembly BP
GO:0043933 protein-containing complex organization BP
GO:0044085 cellular component biogenesis BP
GO:0044237 cellular metabolic process BP
GO:0044238 primary metabolic process BP
GO:0044249 cellular biosynthetic process BP
GO:0044260 cellular macromolecule metabolic process BP
GO:0044267 protein metabolic process BP
GO:0044271 cellular nitrogen compound biosynthetic process BP
GO:0044424 obsolete intracellular part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044464 obsolete cell part CC
GO:0045184 establishment of protein localization BP
GO:0046483 heterocycle metabolic process BP
GO:0046907 intracellular transport BP
GO:0050657 nucleic acid transport BP
GO:0050658 RNA transport BP
GO:0050896 response to stimulus BP
GO:0051082 unfolded protein binding MF
GO:0051083 'de novo' cotranslational protein folding BP
GO:0051168 nuclear export BP
GO:0051169 nuclear transport BP
GO:0051179 localization BP
GO:0051234 establishment of localization BP
GO:0051236 establishment of RNA localization BP
GO:0051640 organelle localization BP
GO:0051641 cellular localization BP
GO:0051649 establishment of localization in cell BP
GO:0051656 establishment of organelle localization BP
GO:0051716 cellular response to stimulus BP
GO:0061077 chaperone-mediated protein folding BP
GO:0065007 biological regulation BP
GO:0065008 regulation of biological quality BP
GO:0070727 cellular macromolecule localization BP
GO:0071166 ribonucleoprotein complex localization BP
GO:0071426 obsolete ribonucleoprotein complex export from nucleus BP
GO:0071428 obsolete rRNA-containing ribonucleoprotein complex export from nucleus BP
GO:0071496 cellular response to external stimulus BP
GO:0071702 organic substance transport BP
GO:0071704 organic substance metabolic process BP
GO:0071705 nitrogen compound transport BP
GO:0071840 cellular component organization or biogenesis BP
GO:0071944 cell periphery CC
GO:0090304 nucleic acid metabolic process BP
GO:1901360 organic cyclic compound metabolic process BP
GO:1901564 organonitrogen compound metabolic process BP
GO:1901566 organonitrogen compound biosynthetic process BP
GO:1901576 organic substance biosynthetic process BP
GO:1990904 ribonucleoprotein complex CC
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.