Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
Potra2n3c6917
View in Genome Browser
Position
chr3:4138762-4144167 (-)
5405bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the chaperonin (HSP60) family
Organism
Populus tremula
Also AS Potri.003G173900AT3G23990Potri.003G173900.v4.1

Gene Structure

upstream:
Get Sequence

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Potra2n9c19421 Belongs to the heat shock protein 70 family
Potra2n5c11442 Belongs to the 14-3-3 family
Potra2n6c13766 Nucleoporin
Regulatory gene
Potra2n10c20174 ABSCISIC ACID-INSENSITIVE 5-like protein
Potra2n10c20228 basic region leucin zipper
Potra2n10c20360 ZINC FINGER protein

Load All Networks

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:0003735 structural constituent of ribosome MF
GO:0005198 structural molecule activity MF
GO:0005488 binding MF
GO:0005507 copper ion binding MF
GO:0005515 protein binding MF
GO:0005524 ATP binding MF
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005739 mitochondrion CC
GO:0005759 mitochondrial matrix CC
GO:0005773 vacuole CC
GO:0005774 vacuolar membrane CC
GO:0005829 cytosol CC
GO:0005840 ribosome CC
GO:0005844 polysome CC
GO:0005886 plasma membrane CC
GO:0006457 protein folding BP
GO:0006458 'de novo' protein folding BP
GO:0006605 protein targeting BP
GO:0006626 protein targeting to mitochondrion BP
GO:0006810 transport BP
GO:0006839 mitochondrial transport BP
GO:0006886 intracellular protein transport BP
GO:0006950 response to stress BP
GO:0006996 organelle organization BP
GO:0007005 mitochondrion organization BP
GO:0008104 protein localization BP
GO:0008144 obsolete drug binding MF
GO:0008150 biological_process BP
GO:0009266 response to temperature stimulus BP
GO:0009408 response to heat BP
GO:0009507 chloroplast CC
GO:0009526 plastid envelope CC
GO:0009532 plastid stroma CC
GO:0009536 plastid CC
GO:0009570 chloroplast stroma CC
GO:0009628 response to abiotic stimulus BP
GO:0009719 response to endogenous stimulus BP
GO:0009725 response to hormone BP
GO:0009735 response to cytokinin BP
GO:0009941 chloroplast envelope CC
GO:0009987 cellular process BP
GO:0010033 response to organic substance BP
GO:0010035 response to inorganic substance BP
GO:0010038 response to metal ion BP
GO:0015031 protein transport BP
GO:0015833 peptide transport BP
GO:0016020 membrane CC
GO:0016043 cellular component organization BP
GO:0017038 protein import BP
GO:0017076 purine nucleotide binding MF
GO:0022626 cytosolic ribosome CC
GO:0030554 adenyl nucleotide binding MF
GO:0031090 organelle membrane CC
GO:0031967 organelle envelope CC
GO:0031974 membrane-enclosed lumen CC
GO:0031975 envelope CC
GO:0032553 ribonucleotide binding MF
GO:0032555 purine ribonucleotide binding MF
GO:0032559 adenyl ribonucleotide binding MF
GO:0032991 protein-containing complex CC
GO:0033036 macromolecule localization BP
GO:0033365 protein localization to organelle BP
GO:0034613 protein localization BP
GO:0035639 purine ribonucleoside triphosphate binding MF
GO:0036094 small molecule binding MF
GO:0042221 response to chemical BP
GO:0042788 polysomal ribosome CC
GO:0042886 amide transport BP
GO:0043167 ion binding MF
GO:0043168 anion binding MF
GO:0043169 cation binding MF
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:0044183 protein folding chaperone MF
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044429 obsolete mitochondrial 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:0044743 protein transmembrane import into intracellular organelle BP
GO:0045041 protein import into mitochondrial intermembrane space BP
GO:0045184 establishment of protein localization BP
GO:0046686 response to cadmium ion BP
GO:0046872 metal ion binding MF
GO:0046907 intracellular transport BP
GO:0046914 transition metal ion binding MF
GO:0050896 response to stimulus BP
GO:0051082 unfolded protein binding MF
GO:0051179 localization BP
GO:0051234 establishment of localization BP
GO:0051641 cellular localization BP
GO:0051649 establishment of localization in cell BP
GO:0055085 transmembrane transport BP
GO:0061077 chaperone-mediated protein folding BP
GO:0065002 intracellular protein transmembrane transport BP
GO:0070013 intracellular organelle lumen CC
GO:0070585 protein localization to mitochondrion BP
GO:0070727 cellular macromolecule localization BP
GO:0071702 organic substance transport BP
GO:0071705 nitrogen compound transport BP
GO:0071806 protein transmembrane transport BP
GO:0071840 cellular component organization or biogenesis BP
GO:0071944 cell periphery CC
GO:0072594 establishment of protein localization to organelle BP
GO:0072655 establishment of protein localization to mitochondrion BP
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:1990542 mitochondrial transmembrane transport BP
GO:1990904 ribonucleoprotein complex CC
KEGG Term Name Description
map03018 RNA degradation The correct processing, quality control and turnover of cellular RNA molecules are critical to many aspects in the expression of genetic information. In eukaryotes, two major pathways of mRNA decay exist and both pathways are initiated by poly(A) shortening of the mRNA. In the 5' to 3' pathway, this is followed by decapping which then permits the 5' to 3' exonucleolytic degradation of transcripts. In the 3' to 5' pathway, the exosome, a large multisubunit complex, plays a key role. The exosome exists in archaeal cells, too. In bacteria, endoribonuclease E, a key enzyme involved in RNA decay and processing, organizes a protein complex called degradosome. RNase E or R interacts with the phosphate-dependent exoribonuclease polynucleotide phosphorylase, DEAD-box helicases, and additional factors in the RNA-degrading complex.