KEGG   PATHWAY: ko03050
Entry
ko03050                     Pathway                                
Name
Proteasome
Description
The proteasome is a protein-destroying apparatus involved in many essential cellular functions, such as regulation of cell cycle, cell differentiation, signal transduction pathways, antigen processing for appropriate immune responses, stress signaling, inflammatory responses, and apoptosis. It is capable of degrading a variety of cellular proteins in a rapid and timely fashion and most substrate proteins are modified by ubiquitin before their degradation by the proteasome. The proteasome is a large protein complex consisting of a proteolytic core called the 20S particle and ancillary factors that regulate its activity in various ways. The most common form is the 26S proteasome containing one 20S core particle and two 19S regulatory particles that enable the proteasome to degrade ubiquitinated proteins by an ATP-dependent mechanism. Another form is the immunoproteasome containing two 11S regulatory particles, PA28 alpha and PA28 beta, which are induced by interferon gamma under the conditions of intensified immune response. Other regulatory particles include PA28 gamma and PA200. Although PA28 gamma also belongs to a family of activators of the 20S proteasome, it is localized within the nucleus and forms a homoheptamer. PA28 gamma has been implicated in the regulation of cell cycle progression and apoptosis. PA200 has been identified as a large nuclear protein that stimulates proteasomal hydrolysis of peptides.
Class
Genetic Information Processing; Folding, sorting and degradation
Pathway map
ko03050  Proteasome
ko03050

Other DBs
GO: 0000502
Orthology
K02725  PSMA1; 20S proteasome subunit alpha 6 [EC:3.4.25.1]
K02726  PSMA2; 20S proteasome subunit alpha 2 [EC:3.4.25.1]
K02727  PSMA3; 20S proteasome subunit alpha 7 [EC:3.4.25.1]
K02728  PSMA4; 20S proteasome subunit alpha 3 [EC:3.4.25.1]
K02729  PSMA5; 20S proteasome subunit alpha 5 [EC:3.4.25.1]
K02730  PSMA6; 20S proteasome subunit alpha 1 [EC:3.4.25.1]
K02731  PSMA7; 20S proteasome subunit alpha 4 [EC:3.4.25.1]
K02732  PSMB1; 20S proteasome subunit beta 6 [EC:3.4.25.1]
K02733  PSMB10, MECL1; 20S proteasome subunit beta 10 [EC:3.4.25.1]
K02734  PSMB2; 20S proteasome subunit beta 4 [EC:3.4.25.1]
K02735  PSMB3; 20S proteasome subunit beta 3 [EC:3.4.25.1]
K02736  PSMB4; 20S proteasome subunit beta 7 [EC:3.4.25.1]
K02737  PSMB5; 20S proteasome subunit beta 5 [EC:3.4.25.1]
K02738  PSMB6; 20S proteasome subunit beta 1 [EC:3.4.25.1]
K02739  PSMB7; 20S proteasome subunit beta 2 [EC:3.4.25.1]
K02740  PSMB8, LMP7; 20S proteasome subunit beta 8 [EC:3.4.25.1]
K02741  PSMB9, LMP2; 20S proteasome subunit beta 9 [EC:3.4.25.1]
K03028  PSMD2, RPN1; 26S proteasome regulatory subunit N1
K03029  PSMD4, RPN10; 26S proteasome regulatory subunit N10
K03030  PSMD14, RPN11, POH1; 26S proteasome regulatory subunit N11
K03031  PSMD8, RPN12; 26S proteasome regulatory subunit N12
K03032  PSMD1, RPN2; 26S proteasome regulatory subunit N2
K03033  PSMD3, RPN3; 26S proteasome regulatory subunit N3
K03035  PSMD12, RPN5; 26S proteasome regulatory subunit N5
K03036  PSMD11, RPN6; 26S proteasome regulatory subunit N6
K03037  PSMD6, RPN7; 26S proteasome regulatory subunit N7
K03038  PSMD7, RPN8; 26S proteasome regulatory subunit N8
K03039  PSMD13, RPN9; 26S proteasome regulatory subunit N9
K03061  PSMC2, RPT1; 26S proteasome regulatory subunit T1
K03062  PSMC1, RPT2; 26S proteasome regulatory subunit T2
K03063  PSMC4, RPT3; 26S proteasome regulatory subunit T3
K03064  PSMC6, RPT4; 26S proteasome regulatory subunit T4
K03065  PSMC3, RPT5; 26S proteasome regulatory subunit T5
K03066  PSMC5, RPT6; 26S proteasome regulatory subunit T6
K03420  psmR; proteasome regulatory subunit
K03432  psmA, prcA; proteasome alpha subunit [EC:3.4.25.1]
K03433  psmB, prcB; proteasome beta subunit [EC:3.4.25.1]
K04687  IFNG; interferon gamma
K06691  RPN13; 26S proteasome regulatory subunit N13
K06693  PSMD9, RPN4; 26S proteasome regulatory subunit N4
K06696  PSME1; proteasome activator subunit 1 (PA28 alpha)
K06697  PSME2; proteasome activator subunit 2 (PA28 beta)
K06698  PSME3; proteasome activator subunit 3 (PA28 gamma)
K06699  PSME4; proteasome activator subunit 4
K06700  PSMF1; proteasome inhibitor subunit 1 (PI31)
K10881  SHFM1, DSS1, RPN15; 26 proteasome complex subunit DSS1
K11598  PSMB11; 20S proteasome subunit beta 11 [EC:3.4.25.1]
K11599  POMP, UMP1; proteasome maturation protein
K13527  mpa; proteasome-associated ATPase
Reference
  Authors
Hirano Y, Murata S, Tanaka K
  Title
Large- and small-scale purification of mammalian 26S proteasomes.
  Journal
Methods Enzymol 399:227-40 (2005)
DOI:10.1016/S0076-6879(05)99015-0
Reference
  Authors
Saeki Y, Tanaka K
  Title
Cell biology: two hands for degradation.
  Journal
Nature 453:460-1 (2008)
DOI:10.1038/453460a
Reference
  Authors
Smith DM, Benaroudj N, Goldberg A
  Title
Proteasomes and their associated ATPases: a destructive combination.
  Journal
J Struct Biol 156:72-83 (2006)
DOI:10.1016/j.jsb.2006.04.012
Reference
  Authors
Strehl B, Seifert U, Kruger E, Heink S, Kuckelkorn U, Kloetzel PM
  Title
Interferon-gamma, the functional plasticity of the ubiquitin-proteasome system, and MHC class I antigen processing.
  Journal
Immunol Rev 207:19-30 (2005)
DOI:10.1111/j.0105-2896.2005.00308.x
Reference
  Authors
Darwin KH
  Title
Prokaryotic ubiquitin-like protein (Pup), proteasomes and pathogenesis.
  Journal
Nat Rev Microbiol 7:485-91 (2009)
DOI:10.1038/nrmicro2148
Reference
  Authors
Tomko RJ Jr, Hochstrasser M
  Title
Molecular architecture and assembly of the eukaryotic proteasome.
  Journal
Annu Rev Biochem 82:415-45 (2013)
DOI:10.1146/annurev-biochem-060410-150257
Reference
  Authors
Budenholzer L, Cheng CL, Li Y, Hochstrasser M
  Title
Proteasome Structure and Assembly.
  Journal
J Mol Biol 429:3500-3524 (2017)
DOI:10.1016/j.jmb.2017.05.027
Reference
  Authors
Cloos J, Roeten MS, Franke NE, van Meerloo J, Zweegman S, Kaspers GJ, Jansen G
  Title
(Immuno)proteasomes as therapeutic target in acute leukemia.
  Journal
Cancer Metastasis Rev 36:599-615 (2017)
DOI:10.1007/s10555-017-9699-4
Reference
  Authors
Sakata E, Bohn S, Mihalache O, Kiss P, Beck F, Nagy I, Nickell S, Tanaka K, Saeki Y, Forster F, Baumeister W
  Title
Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy.
  Journal
Proc Natl Acad Sci U S A 109:1479-84 (2012)
DOI:10.1073/pnas.1119394109
Related
pathway
ko04120  Ubiquitin mediated proteolysis

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