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SGD:PRE1

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Contents

Species (Taxon ID) Saccharomyces cerevisiae (baker's yeast) (taxon:4932)
Gene Name(s) PRE1 ( synonyms: YER012W )
Protein Name(s) Beta 4 subunit of the 20S proteasome,
External Links
SGD S000000814

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:0004175

endopeptidase activity

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR016050

F

From SGD

GO:0004298

threonine-type endopeptidase activity

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR001353
InterPro:IPR023333

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:S000047509
PMID:10419517[1]

IDA: Inferred from Direct Assay

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:0005789

endoplasmic reticulum membrane

SGD_REF:S000086512
PMID:15973433[2]

IDA: Inferred from Direct Assay

C

From SGD

GO:0005839

proteasome core complex

SGD_REF:S000124036

IEA: Inferred from Electronic Annotation

InterPro:IPR001353
InterPro:IPR016050

C

From SGD

GO:0006508

proteolysis

SGD_REF:S000148669

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0645

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
PMID:19162040[3]

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:0019774

proteasome core complex, beta-subunit complex

SGD_REF:S000040877
PMID:9087403[4]

IDA: Inferred from Direct Assay

C

From SGD

GO:0034515

proteasome storage granule

SGD_REF:S000040877
PMID:9087403[4]

IC: Inferred by Curator

GO:0019774

C

From SGD

GO:0043161

proteasomal ubiquitin-dependent protein catabolic process

SGD_REF:S000074510
PMID:11545745[5]

IDA: Inferred from Direct Assay

P

From SGD

GO:0043161

proteasomal ubiquitin-dependent protein catabolic process

SGD_REF:S000128471
PMID:19029916[6]

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

InterPro:IPR001353
InterPro:IPR016050

P

From SGD

GO:0061133

endopeptidase activator activity

SGD_REF:S000053140
PMID:8808631[7]

IMP: Inferred from Mutant Phenotype

F

From SGD


Notes

References

See Help:References for how to manage references in GONUTS.
  1. Russell SJ et al. (1999) Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast. J Biol Chem 274: 21943-52 PubMed GONUTS page
  2. Kalies KU et al. (2005) The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane. EMBO J 24: 2284-93 PubMed GONUTS page
  3. 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
  4. 4.0 4.1 Groll M et al. (1997) Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386: 463-71 PubMed GONUTS page
  5. 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
  6. Prakash S et al. (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat Chem Biol 5: 29-36 PubMed GONUTS page
  7. Chen P & Hochstrasser M (1996) Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 86: 961-72 PubMed GONUTS page
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