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UniProtKB/Swiss-Prot entry P28074


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PSB5_HUMAN
Primary accession number P28074
Secondary accession numbers Q16242 Q6PEW2 Q7Z3B5 Q9TNN9
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on April 29, 2008 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 100)
Name and origin of the protein
Protein name Proteasome subunit beta type-5 [Precursor]
Synonyms EC 3.4.25.1
Proteasome epsilon chain
Macropain epsilon chain
Multicatalytic endopeptidase complex epsilon chain
Proteasome subunit X
Proteasome chain 6
Proteasome subunit MB1
Gene name
Name: PSMB5
Synonyms: LMPX
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/s002510050121; PubMed=8753855 [NCBI, ExPASy, EBI, Israel, Japan]
Abdulla S., Beck S., Belich M., Jackson A., Nakamura T., Trowsdale J.;
"Divergent intron arrangement in the MB1/LMP7 proteasome gene pair.";
Immunogenetics 44:254-258(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Endometrial adenocarcinoma;
The German cDNA consortium;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hypothalamus, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-263.
PubMed=8066462 [NCBI, ExPASy, EBI, Israel, Japan]
Akiyama K.-Y., Yokota K.-Y., Kagawa S., Shimbara N., Tamura T., Akioka H., Nothwang H.G., Noda C., Tanaka K., Ichihara A.;
"cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y.";
Science 265:1231-1234(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 49-263.
DOI=10.1016/S0960-9822(00)00174-3; PubMed=7820546 [NCBI, ExPASy, EBI, Israel, Japan]
Belich M.P., Glynne R.J., Senger G., Sheer D., Trowsdale J.;
"Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins.";
Curr. Biol. 4:769-776(1994).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-263.
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 60-85.
DOI=10.1016/0167-4838(90)90165-C; PubMed=2306472 [NCBI, ExPASy, EBI, Israel, Japan]
Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A.;
"Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome).";
Biochim. Biophys. Acta 1037:178-185(1990).
[8]
PROTEIN SEQUENCE OF 201-216 AND 226-239.
DOI=10.1006/bbrc.1994.2876; PubMed=7811265 [NCBI, ExPASy, EBI, Israel, Japan]
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
"Human proteasome subunits from 2-dimensional gels identified by partial sequencing.";
Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
[9]
PROTEIN SEQUENCE OF 201-216.
TISSUE=Kidney;
DOI=10.1016/0014-5793(94)80612-8; PubMed=8163024 [NCBI, ExPASy, EBI, Israel, Japan]
Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M., Kristensen P., Hendil K.B., Tanaka K., Ichihara A.;
"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.";
FEBS Lett. 343:85-88(1994).
[10]
ERRATUM.
DOI=10.1006/bbrc.1995.1294; PubMed=7864893 [NCBI, ExPASy, EBI, Israel, Japan]
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
Biochem. Biophys. Res. Commun. 207:1059-1059(1995).
[11]
INTERACTION WITH POMP.
DOI=10.1073/pnas.0501711102; PubMed=15944226 [NCBI, ExPASy, EBI, Israel, Japan]
Heink S., Ludwig D., Kloetzel P.-M., Krueger E.;
"IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response.";
Proc. Natl. Acad. Sci. U.S.A. 102:9241-9246(2005).
[12]
PROTEOLYTIC PROCESSING [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/bi061994u; PubMed=17323924 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
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: 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.
  • INTERACTION:
    O15116:LSM1; NbExp=1; IntAct=EBI-357828, EBI-347619;
    Q15008:PSMD6; NbExp=1; IntAct=EBI-357828, EBI-359701;
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
  • SIMILARITY: Belongs to the peptidase T1B family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X95586; CAA64838.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX538001; CAD97956.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004146; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
BC057840; AAH57840.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC107720; AAI07721.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D29011; BAA06097.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S74378; AAB33092.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006777; AAP35423.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A54589; A54589.
I52906; I52906.
PC2328; PC2328.
S08189; S08189.
RefSeq NP_001124197.1; -.
NP_002788.1; -.
UniGene Hs.422990
3D structure databases
HSSP P30656; 1RYP. [HSSP ENTRY / PDB]
SMR P28074; 5-205.
ModBase P28074.
Protein-protein interaction databases
DIP DIP:27540N; -.
IntAct P28074; -.
Protein family/group databases
MEROPS T01.012; -.
PTM databases
PhosphoSite P28074; -.
Enzyme and pathway databases
Reactome REACT_11045; Signaling by Wnt.
REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_383; DNA Replication.
REACT_6185; HIV Infection.
REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_9035; APC/C:Cdh1-mediated degradation of Skp2.
2D gel databases
REPRODUCTION-2DPAGE IPI00479306; -.
Organism-specific databases
H-InvDB HIX0011529; -.
HIX0026673; -.
HGNC HGNC:9542; PSMB5.
GenAtlas PSMB5.
MIM 600306; gene. [NCBI / EBI]
PharmGKB PA33887; -.
GeneCards P28074.
Gene expression databases
ArrayExpress P28074; -.
CleanEx HS_PSMB5; -.
GermOnline ENSG00000100804; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005839; Cellular component: proteasome core complex (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004298; Molecular function: threonine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0051436; Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR000243; Pept_T1A_subB.
IPR001353; Proteasome_A_B_su.
IPR016050; Proteasome_bsu_CS.
Graphical view of domain structure.
Pfam PF00227; Proteasome; 1.
Pfam graphical view of domain structure.
PRINTS PR00141; PROTEASOME.
PROSITE PS00854; PROTEASOME_B; 1.
BLOCKS P28074.
ProtoNet P28074.
Genome annotation databases
Ensembl ENSG00000100804; Homo sapiens. [Contig view]
GeneID 5693; -.
KEGG hsa:5693; -.
Phylogenomic databases
HOVERGEN P28074; -.
Other
DrugBank DB00188; Bortezomib.
LinkHub P28074; -.
NextBio 22114; -.
SOURCE PSMB5; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus; Protease; Proteasome; Threonine protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   1    59  59      PRO_0000026589
CHAIN   60   263  204     Proteasome subunit beta type-5. PRO_0000026590
ACT_SITE   60    60        Nucleophile. 
CONFLICT   3     6        LASV -> IRGR (in Ref. 4; BAA06097). 
CONFLICT   3     5        LAS -> HEG (in Ref. 3; BC004146). 
CONFLICT   85    85        I -> F (in Ref. 7; AA sequence). 
CONFLICT   109   109        A -> G (in Ref. 5; AAB33092). 
CONFLICT   158   158        T -> S (in Ref. 5; AAB33092). 
Sequence information
Length: 263 AA [This is the length of the unprocessed precursor] Molecular weight: 28480 Da [This is the MW of the unprocessed precursor] CRC64: AED4A73DF41AA6EF [This is a checksum on the sequence]
        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 

P28074 in FASTA format

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View entry in raw text format (no links)
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