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InterPro: IPR000426 Proteasome, alpha-subunit, conserved site

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1552 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR000426 Proteasome_asu_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
Pfam	PF10584	Proteasome_A_N	1552
PROSITE pattern	PS00388	PROTEASOME_A	1375
Signatures in BioMart

InterPro Relationships Help

Found in

IPR019982 Proteasome, alpha subunit, archaeal

GO Term annotation Help

Process

GO:0006511 ubiquitin-dependent protein catabolic process

Function

GO:0004175 endopeptidase activity

Component

GO:0019773 proteasome core complex, alpha-subunit complex

InterPro annotation

Entry Details in BioMart

Abstract

The proteasome (or macropain) (EC:3.4.25.1) [1, 2, 3, 4, 5] is a eukaryotic and archaeal multicatalytic proteinase complex that seems to be involved in an ATP/ubiquitin-dependent nonlysosomal proteolytic pathway. In eukaryotes the proteasome is composed of about 28 distinct subunits which form a highly ordered ring-shaped structure (20S ring) of about 700 kDa. Most proteasome subunits can be classified, on the basis on sequence similarities into two groups, alpha (A) and beta (B).

This family contains the alpha subunit sequences which range from 210 to 290 amino acids. These sequences are classified as non-peptidase homologues in MEROPS peptidase family T1 (clan PB(T)).

Structural links Help

PDB - click here

SCOP: d.153.1.4

CATH: 3.60.20.10

Database links Help

PDBe-motif: PS00388

Enzyme: EC:3.4.25.1

PROSITE doc: PDOC00326

Blocks: IPB000426

MEROPS: T1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000426

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O14818 Proteasome subunit alpha type-7

O17586 Proteasome subunit alpha type-6

O70435 Proteasome subunit alpha type-3

P12881 Proteasome subunit alpha type-1

P21242 Proteasome component C1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001353	Proteasome, subunit alpha/beta
IPR000426	Proteasome, alpha-subunit, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Rivett AJ. Proteasomes: multicatalytic proteinase complexes. Biochem. J. 291 ( Pt 1) 1-10 1993 [PubMed: 7682410] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=7682410
2.	Rivett AJ. The multicatalytic proteinase of mammalian cells. Arch. Biochem. Biophys. 268 1-8 1989 [PubMed: 2643381] http://dx.doi.org/10.1016/0003-9861(89)90558-4
3.	Goldberg AL, Rock KL. Proteolysis, proteasomes and antigen presentation. Nature 357 375-9 1992 [PubMed: 1317508] http://dx.doi.org/10.1038/357375a0
4.	Wilk S. Proteasomes. Multicatalytic proteinase complexes. Enzyme Protein 47 187-8 1993 [PubMed: 7697118]
5.	Hilt W, Wolf DH. Proteasomes: destruction as a programme. Trends Biochem. Sci. 21 96-102 1996 [PubMed: 8882582] http://dx.doi.org/10.1016/0968-0004(96)10012-8

Additional Reading Open in usermanual
	Rawlings ND, Barrett AJ. Families of serine peptidases. Meth. Enzymol. 244 1994 19-61 [PubMed: 7845208] http://dx.doi.org/10.1016/0076-6879(94)44004-2
	Groll M, Larionov OV, Huber R, de Meijere A. Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation. Proc. Natl. Acad. Sci. U.S.A. 103 2006 4576-9 [PubMed: 16537370] http://dx.doi.org/10.1073/pnas.0600647103
	Groll M, Schellenberg B, Bachmann AS, Archer CR, Huber R, Powell TK, Lindow S, Kaiser M, Dudler R. A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism. Nature 452 2008 755-8 [PubMed: 18401409] http://dx.doi.org/10.1038/nature06782
	Hines J, Groll M, Fahnestock M, Crews CM. Proteasome inhibition by fellutamide B induces nerve growth factor synthesis. Chem. Biol. 15 2008 501-12 [PubMed: 18482702] http://dx.doi.org/10.1016/j.chembiol.2008.03.020
	Groll M, Gotz M, Kaiser M, Weyher E, Moroder L. TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome. Chem. Biol. 13 2006 607-14 [PubMed: 16793518] http://dx.doi.org/10.1016/j.chembiol.2006.04.005
	Groll M, Berkers CR, Ploegh HL, Ovaa H. Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome. Structure 14 2006 451-6 [PubMed: 16531229] http://dx.doi.org/10.1016/j.str.2005.11.019

InterPro 23.1