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ARATH:CH10
Contents
| Species (Taxon ID) | Arabidopsis thaliana (Mouse-ear cress). (3702) | |
| Gene Name(s) | CPN10 | |
| Protein Name(s) | 10 kDa chaperonin
Chaperonin 10 CPN10 Protein groES | |
| External Links | ||
| UniProt | P34893 | |
| EMBL | L02843 D88314 AC012189 CP002684 AY063928 AY091252 AY086708 | |
| PIR | S65597 | |
| RefSeq | NP_563961.1 | |
| UniGene | At.295 | |
| ProteinModelPortal | P34893 | |
| SMR | P34893 | |
| MINT | MINT-8058965 | |
| STRING | 3702.AT1G14980.1-P | |
| PaxDb | P34893 | |
| PRIDE | P34893 | |
| EnsemblPlants | AT1G14980.1 | |
| GeneID | 838063 | |
| KEGG | ath:AT1G14980 | |
| GeneFarm | 2381 | |
| TAIR | AT1G14980 | |
| eggNOG | COG0234 | |
| HOGENOM | HOG000133897 | |
| InParanoid | P34893 | |
| KO | K04078 | |
| OMA | TSIKSIR | |
| PhylomeDB | P34893 | |
| Proteomes | UP000006548 | |
| Genevestigator | P34893 | |
| GO | GO:0005739 GO:0005524 GO:0005507 GO:0006457 GO:0009408 | |
| Gene3D | 2.30.33.40 | |
| InterPro | IPR020818 IPR018369 IPR011032 | |
| PANTHER | PTHR10772 | |
| Pfam | PF00166 | |
| PRINTS | PR00297 | |
| SMART | SM00883 | |
| SUPFAM | SSF50129 | |
| PROSITE | PS00681 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
involved_in |
GO:0009408 |
response to heat |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005507 |
copper ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051087 |
chaperone binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000080668 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0051085 |
chaperone cofactor-dependent protein refolding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10600 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0051082 |
unfolded protein binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000080668 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000080668 |
F |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005759 |
mitochondrial matrix |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000080669 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006457 |
protein folding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Koumoto, Y et al. (1996) Isolation and characterization of a cDNA encoding mitochondrial chaperonin 10 from Arabidopsis thaliana by functional complementation of an Escherichia coli groES mutant. Plant J. 10 1119-25 PubMed GONUTS page
- ↑ Nikolovski, N et al. (2012) Putative glycosyltransferases and other plant Golgi apparatus proteins are revealed by LOPIT proteomics. Plant Physiol. 160 1037-51 PubMed GONUTS page
- ↑ Lee, CP et al. (2008) Heterogeneity of the mitochondrial proteome for photosynthetic and non-photosynthetic Arabidopsis metabolism. Mol. Cell Proteomics 7 1297-316 PubMed GONUTS page
- ↑ Heazlewood, JL et al. (2004) Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16 241-56 PubMed GONUTS page
- ↑ Sweetlove, LJ et al. (2002) The impact of oxidative stress on Arabidopsis mitochondria. Plant J. 32 891-904 PubMed GONUTS page
- ↑ Tan, YF et al. (2010) Divalent metal ions in plant mitochondria and their role in interactions with proteins and oxidative stress-induced damage to respiratory function. Plant Physiol. 152 747-61 PubMed GONUTS page
- ↑ 7.0 7.1 7.2 7.3 7.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
