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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(Psma1) (Psma2) (Psma3) (Psma4) (Psma5) (Psma6) (Psmb4) (Psmb1) (Psmb8) (Psmb2) (Psmb9) (Psmb3) (Psma7) (Psmb5) (Psmb10) (Psmb6) (Psmb7) (Rpt2) (Psmc2) (Psmc3) (Psmc4) (Psmc5) (Psmc6) (Psmd1) (Psmd3) (Psmd2) (Psmd4) (Psmd5) (Psmd6) (Psmd7) (Psmd8) (Psmd9) (Psmd10) (Psmd11) (Psmd12) (Psmd13) (Psmd14)
State descriptionRpn8/26S Proteasome
Computed namePsma1: Psma2: Psma3: Psma4: Psma5: Psma6: Psmb4: Psmb1: Psmb8: Psmb2: Psmb9: Psmb3: Psma7: Psmb5: Psmb10: Psmb6: Psmb7: Rpt2: 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 namePsma1
Covalent modificationsNone
Small molecules boundNone
Protein namePsma2
Covalent modificationsNone
Small molecules boundNone
Protein namePsma3
Covalent modificationsNone
Small molecules boundNone
Protein namePsma4
Covalent modificationsNone
Small molecules boundNone
Protein namePsma5
Covalent modificationsNone
Small molecules boundNone
Protein namePsma6
Covalent modificationsNone
Small molecules boundNone
Protein namePsmb4
Covalent modificationsNone
Small molecules boundNone
Protein namePsmb1
Covalent modificationsNone
Small molecules boundNone
Protein namePsmb8
Covalent modificationsNone
Small molecules boundNone
Protein namePsmb2
Covalent modificationsNone
Small molecules boundNone
Protein namePsmb9
Covalent modificationsNone
Small molecules boundNone
Protein namePsmb3
Covalent modificationsNone
Small molecules boundNone
Protein namePsma7
Covalent modificationsNone
Small molecules boundNone
Protein namePsmb5
Covalent modificationsNone
Small molecules boundNone
Protein namePsmb10
Covalent modificationsNone
Small molecules boundNone
Protein namePsmb6
Covalent modificationsNone
Small molecules boundNone
Protein namePsmb7
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 26S proteasome is a large protein complex that removes ubiquitinated proteins by breaking them down into short polypeptide sequences. It 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 complexes contain ATPase and ubiquitin binding activity. It is thought that the 19S complex serves to bind, unfold, and feed ubiquitinated protein to 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
10872471Voges D, Zwickl P, Baumeister WThe 26S proteasome: a molecular machine designed for controlled proteolysis.Annu Rev Biochem,
68
1999