Proteasome subunit beta type-5 precursor

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Reviewed, UniProtKB/Swiss-Prot P28074 (PSB5_HUMAN)

Last modified July 7, 2009. Version 107. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Proteasome subunit beta type-5
    EC=3.4.25.1
Alternative name(s):
    Proteasome epsilon chain
    Macropain epsilon chain
    Multicatalytic endopeptidase complex epsilon chain
    Proteasome subunit X
    Proteasome chain 6
    Proteasome subunit MB1

Gene names

Name:	PSMB5
Synonyms:	LMPX

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. May catalyze basal processing of intracellular antigens.
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. This subunit can be displaced by the equivalent immune-specific subunit PSMB8. Directly interacts with POMP. Ref.11
Subcellular location	Cytoplasm. Nucleus.
Sequence similarities	Belongs to the peptidase T1B family.

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Threonine protease
PTM	Zymogen
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
LSM1	O15116	1	EBI-357828,EBI-347619
PSMD6	Q15008	1	EBI-357828,EBI-359701

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 59

Ref.7

PRO_0000026589

Chain

60 – 263

204

Proteasome subunit beta type-5

PRO_0000026590

Sites

Active site

Nucleophile

Natural variations

Natural variant

R → C: dbSNP rs11543947.

VAR_051549

Experimental info

Sequence conflict

3 – 6

LASV → IRGR in BAA06097. Ref.4

Sequence conflict

3 – 5

LAS → HEG in BC004146. Ref.3

Sequence conflict

I → F AA sequence Ref.7

Sequence conflict

109

A → G in AAB33092. Ref.5

Sequence conflict

158

T → S in AAB33092. Ref.5

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Sequences

Sequence

Length

Mass (Da)

Tools

P28074-1 [UniParc].

Last modified April 29, 2008. Version 3.
Checksum: AED4A73DF41AA6EF
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FASTA

263

28,480

        10         20         30         40         50         60 
MALASVLERP LPVNQRGFFG LGGRADLLDL GPGSLSDGLS LAAPGWGVPE EPGIEMLHGT 

        70         80         90        100        110        120 
TTLAFKFRHG VIVAADSRAT AGAYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR 

       130        140        150        160        170        180 
QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI 

       190        200        210        220        230        240 
SGATFSVGSG SVYAYGVMDR GYSYDLEVEQ AYDLARRAIY QATYRDAYSG GAVNLYHVRE 

       250        260 
DGWIRVSSDN VADLHEKYSG STP

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Divergent intron arrangement in the MB1/LMP7 proteasome gene pair." Abdulla S., Beck S., Belich M., Jackson A., Nakamura T., Trowsdale J. Immunogenetics 44:254-258(1996) [PubMed: 8753855] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Endometrial adenocarcinoma.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Hypothalamus and Skin.
[4]	"cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y." Akiyama K.-Y., Yokota K.-Y., Kagawa S., Shimbara N., Tamura T., Akioka H., Nothwang H.G., Noda C., Tanaka K., Ichihara A. Science 265:1231-1234(1994) [PubMed: 8066462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-263.
[5]	"Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins." Belich M.P., Glynne R.J., Senger G., Sheer D., Trowsdale J. Curr. Biol. 4:769-776(1994) [PubMed: 7820546] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-263.
[6]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-263.
[7]	"Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)." Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A. Biochim. Biophys. Acta 1037:178-185(1990) [PubMed: 2306472] [Abstract] Cited for: PROTEIN SEQUENCE OF 60-85.
[8]	"Human proteasome subunits from 2-dimensional gels identified by partial sequencing." Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B. Biochem. Biophys. Res. Commun. 205:1785-1789(1994) [PubMed: 7811265] [Abstract] Cited for: PROTEIN SEQUENCE OF 201-216 AND 226-239.
[9]	"Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon-gamma for acquirement of the functional diversity responsible for antigen processing." Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M., Kristensen P., Hendil K.B., Tanaka K., Ichihara A. FEBS Lett. 343:85-88(1994) [PubMed: 8163024] [Abstract] Cited for: PROTEIN SEQUENCE OF 201-216. Tissue: Kidney.
[10]	Erratum Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B. Biochem. Biophys. Res. Commun. 207:1059-1059(1995) [PubMed: 7864893] [Abstract]
[11]	"IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response." Heink S., Ludwig D., Kloetzel P.-M., Krueger E. Proc. Natl. Acad. Sci. U.S.A. 102:9241-9246(2005) [PubMed: 15944226] [Abstract] Cited for: INTERACTION WITH POMP.
[12]	"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex." Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L. Biochemistry 46:3553-3565(2007) [PubMed: 17323924] [Abstract] Cited for: PROTEOLYTIC PROCESSING [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X95586 Genomic DNA. Translation: CAA64838.1. BX538001 mRNA. Translation: CAD97956.1. Different initiation. BC004146 mRNA. No translation available. BC057840 mRNA. Translation: AAH57840.1. BC107720 mRNA. Translation: AAI07721.1. D29011 mRNA. Translation: BAA06097.1. Different initiation. S74378 mRNA. Translation: AAB33092.1. BT006777 mRNA. Translation: AAP35423.1. Different initiation.
IPI	IPI00479306.
PIR	A54589. I52906. PC2328. S08189.
RefSeq	NP_001124197.1. NP_002788.1.
UniGene	Hs.422990
3D structure databases
HSSP	HSSP built from PDB template 1RYP based on UniProtKB P30656.
SMR	P28074. Positions 5-205.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:27540N.
IntAct	P28074. 20 interactions.
Protein family/group databases
MEROPS	T01.012.
PTM databases
PhosphoSite	P28074.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00479306.
Proteomic databases
PRIDE	P28074.
Genome annotation databases
Ensembl	ENSG00000100804. Homo sapiens. [Contig view]
GeneID	5693.
KEGG	hsa:5693.
UCSC	uc001wii.1. human.
Organism-specific databases
GeneCards	GC14M022564.
H-InvDB	HIX0011529. HIX0026673.
HGNC	HGNC:9542. PSMB5.
MIM	600306. gene.
PharmGKB	PA33887.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P28074.
OMA	P28074. QTFAYGV.
Enzyme and pathway databases
BRENDA	3.4.25.1. 247.
Reactome	REACT_11045. Signaling by Wnt. REACT_13. Metabolism of amino acids. REACT_13635. Regulation of activated PAK-2p34 by proteasome mediated degradation. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6185. HIV Infection. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.
Gene expression databases
ArrayExpress	P28074.
Bgee	P28074.
CleanEx	HS_PSMB5.
GermOnline	ENSG00000100804. Homo sapiens.
Family and domain databases
InterPro	IPR000243. Pept_T1A_subB. IPR001353. Proteasome_alpha_beta_su. IPR016050. Proteasome_bsu_CS. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PRINTS	PR00141. PROTEASOME.
PROSITE	PS00854. PROTEASOME_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00188. Bortezomib.
NextBio	22114.
SOURCE	Search...

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Entry information

Entry name

PSB5_HUMAN

Accession

Primary (citable) accession number: P28074
Secondary accession number(s): Q16242

Q9TNN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	April 29, 2008
Last modified:	July 7, 2009
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

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Human chromosome 14: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents