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SGD:PRE10
Contents |
| Species (Taxon ID) | Saccharomyces cerevisiae (baker's yeast) (taxon:4932) | |
| Gene Name(s) | PRE10 ( synonyms: YOR362C ) | |
| Protein Name(s) | Alpha 7 subunit of the 20S proteasome, | |
| External Links | ||
| SGD | S000005889 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0000502 |
proteasome complex |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0647 |
C |
From SGD |
||
| GO:0003729 |
mRNA binding |
SGD_REF:S000141174 |
IDA: Inferred from Direct Assay |
F |
From SGD |
|||
| GO:0004175 |
endopeptidase activity |
SGD_REF:S000124036 |
IEA: Inferred from Electronic Annotation |
F |
From SGD |
|||
| GO:0004298 |
threonine-type endopeptidase activity |
SGD_REF:S000124036 |
IEA: Inferred from Electronic Annotation |
F |
From SGD |
|||
| GO:0004298 |
threonine-type endopeptidase activity |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0888 |
F |
From SGD |
||
| GO:0005634 |
nucleus |
SGD_REF:S000040877 |
IC: Inferred by Curator |
GO:0019773 |
C |
From SGD |
||
| GO:0005634 |
nucleus |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0539 |
C |
From SGD |
||
| GO:0005634 |
nucleus |
SGD_REF:S000148671 |
IEA: Inferred from Electronic Annotation |
UniProtKB-SubCell:SL-0191 |
C |
From SGD |
||
| GO:0005737 |
cytoplasm |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0963 |
C |
From SGD |
||
| GO:0005737 |
cytoplasm |
SGD_REF:S000148671 |
IEA: Inferred from Electronic Annotation |
UniProtKB-SubCell:SL-0086 |
C |
From SGD |
||
| GO:0005739 |
mitochondrion |
SGD_REF:S000040877 |
IC: Inferred by Curator |
GO:0019774 |
C |
From SGD |
||
| GO:0005839 |
proteasome core complex |
SGD_REF:S000124036 |
IEA: Inferred from Electronic Annotation |
C |
From SGD |
|||
| GO:0006508 |
proteolysis |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0645 |
P |
From SGD |
||
| GO:0006511 |
ubiquitin-dependent protein catabolic process |
SGD_REF:S000124036 |
IEA: Inferred from Electronic Annotation |
P |
From SGD |
|||
| GO:0008233 |
peptidase activity |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0645 |
F |
From SGD |
||
| GO:0010499 |
proteasomal ubiquitin-independent protein catabolic process |
SGD_REF:S000129028 |
IDA: Inferred from Direct Assay |
P |
From SGD |
|||
| GO:0016787 |
hydrolase activity |
SGD_REF:S000148669 |
IEA: Inferred from Electronic Annotation |
UniProtKB-KW:KW-0378 |
F |
From SGD |
||
| GO:0019773 |
proteasome core complex, alpha-subunit complex |
SGD_REF:S000040877 |
IDA: Inferred from Direct Assay |
C |
From SGD |
|||
| GO:0019773 |
proteasome core complex, alpha-subunit complex |
SGD_REF:S000124036 |
IEA: Inferred from Electronic Annotation |
C |
From SGD |
|||
| GO:0034515 |
proteasome storage granule |
SGD_REF:S000126567 |
IDA: Inferred from Direct Assay |
C |
From SGD |
|||
| GO:0042175 |
nuclear outer membrane-endoplasmic reticulum membrane network |
SGD_REF:S000040877 |
IC: Inferred by Curator |
GO:0019773 |
C |
From SGD |
||
| GO:0043161 |
proteasomal ubiquitin-dependent protein catabolic process |
SGD_REF:S000074510 |
IDA: Inferred from Direct Assay |
P |
From SGD |
|||
| GO:0043161 |
proteasomal ubiquitin-dependent protein catabolic process |
SGD_REF:S000128471 |
IDA: Inferred from Direct Assay |
P |
From SGD |
|||
| GO:0051603 |
proteolysis involved in cellular protein catabolic process |
SGD_REF:S000124036 |
IEA: Inferred from Electronic Annotation |
P |
From SGD |
| ||
| edit table |
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Scherrer T et al. (2010) A screen for RNA-binding proteins in yeast indicates dual functions for many enzymes. PLoS One 5: e15499 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 Groll M et al. (1997) Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386: 463-71 PubMed GONUTS page
- ↑ Baugh JM et al. (2009) Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination. J Mol Biol 386: 814-27 PubMed GONUTS page
- ↑ Laporte D et al. (2008) Reversible cytoplasmic localization of the proteasome in quiescent yeast cells. J Cell Biol 181: 737-45 PubMed GONUTS page
- ↑ Verma R et al. (2001) Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-Cdk. Mol Cell 8: 439-48 PubMed GONUTS page
- ↑ Prakash S et al. (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat Chem Biol 5: 29-36 PubMed GONUTS page
