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Protein A003584
Author-entered Data
V1.0, Peer Reviewed
Published 17 May 2005
Automated Data
Not Reviewed
As At Publication
Automated Data
Not Reviewed
Latest from 6 Jun 2014

UCSD Nature Molecule Pages
Published online: 17 May 2005 | doi:10.1038/mp.a003584.01

Rpn8

Basis Sequence: Mouse

H. Garrett R Thompson1, James P Brody1

1Department of Biomedical Engineering, University of California, Irvine, CA 92697, US.

Correspondence should be addressed to James P Brody: jpbrody@uci.edu

State summary
State name(Rpt2) (Psmc2) (Psmc3) (Psmc4) (Psmc5) (Psmc6) (Psmd1) (Psmd3) (Psmd2) (Psmd4) (Psmd5) (Psmd6) (Psmd7) (Psmd8) (Psmd9) (Psmd10) (Psmd11) (Psmd12) (Psmd13) (Psmd14)
State descriptionRpn8/19S complex
Computed nameRpt2: Rpt1: Rpt5: Rpt3: Rpt6: Rpt4: Rpn2: Psmd3: Rpn1: Rpn10: Psmd5: Rpn7: Rpn8: Rpn12: Psmd9: Psmd10: Rpn6: Rpn5: Rpn9: Rpn11
Cellular compartmentUnknown
 
State constituents
Protein nameRpn8
Covalent modificationsNone
Small molecules boundNone
Protein nameRpt2
Covalent modificationsNone
Small molecules boundNone
Protein nameRpt1
Covalent modificationsNone
Small molecules boundNone
Protein nameRpt5
Covalent modificationsNone
Small molecules boundNone
Protein nameRpt3
Covalent modificationsNone
Small molecules boundNone
Protein nameRpt6
Covalent modificationsNone
Small molecules boundNone
Protein nameRpt4
Covalent modificationsNone
Small molecules boundNone
Protein nameRpn2
Covalent modificationsNone
Small molecules boundNone
Protein namePsmd3
Covalent modificationsNone
Small molecules boundNone
Protein nameRpn1
Covalent modificationsNone
Small molecules boundNone
Protein nameRpn10
Covalent modificationsNone
Small molecules boundNone
Protein namePsmd5
Covalent modificationsNone
Small molecules boundNone
Protein nameRpn7
Covalent modificationsNone
Small molecules boundNone
Protein nameRpn12
Covalent modificationsNone
Small molecules boundNone
Protein namePsmd9
Covalent modificationsNone
Small molecules boundNone
Protein namePsmd10
Covalent modificationsNone
Small molecules boundNone
Protein nameRpn6
Covalent modificationsNone
Small molecules boundNone
Protein nameRpn5
Covalent modificationsNone
Small molecules boundNone
Protein nameRpn9
Covalent modificationsNone
Small molecules boundNone
Protein nameRpn11
Covalent modificationsNone
Small molecules boundNone
 
State functions

No functional data are associated with this state.

 
Author comments associated with this state

The 19S complex forms a component of the 26S proteasome, which is composed of a barrel-shaped particle, the 20S proteasome, capped at each end by 19S complexes. The 20S proteasome has proteolytic activity, while the 19S complex contains ATPase and ubiquitin binding activity. It is thought that the 19S complex serves to bind, unfold, and feed ubiquitinated protein to the 20S proteasome. In addition, the 19S complex, or at least a subset of it, is thought to play a role in transcription, independent of the 20S proteasome.

 
Citations associated with this state
PM IDAuthorsTitleJournalPub Date
9476896Baumeister W, Walz J, Zühl F, Seemüller EThe proteasome: paradigm of a self-compartmentalizing protease.Cell,
92, 3
6 Feb 1998
10410804Bochtler M, Ditzel L, Groll M, Hartmann C, Huber RThe proteasome.Annu Rev Biophys Biomol Struct,
28
1999
7830725Coux O, Nothwang HG, Silva Pereira I, Recillas Targa F, Bey F, Scherrer KPhylogenic relationships of the amino acid sequences of prosome (proteasome, MCP) subunits.Mol Gen Genet,
245, 6
15 Dec 1994
10428771DeMartino GN, Slaughter CAThe proteasome, a novel protease regulated by multiple mechanisms.J Biol Chem,
274, 32
6 Aug 1999
9647729Tanaka KMolecular biology of the proteasome.Biochem Biophys Res Commun,
247, 3
29 Jun 1998
9797452Tanaka K, Chiba TThe proteasome: a protein-destroying machine.Genes Cells,
3, 8
Aug 1998
10872471Voges D, Zwickl P, Baumeister WThe 26S proteasome: a molecular machine designed for controlled proteolysis.Annu Rev Biochem,
68
1999