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O55234 (PSB5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit beta type-5

EC=3.4.25.1
Alternative name(s):
Macropain epsilon chain
Multicatalytic endopeptidase complex epsilon chain
Proteasome chain 6
Proteasome epsilon chain
Proteasome subunit X
Gene names
Name:Psmb5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib By similarity. Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway. Ref.11

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. Interacts with ABCB1 and TAP1. Ref.12

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Expressed in uterus at the embryo implantation site. Ref.8

Induction

Up-regulated in embryonic fibroblasts and neuroblastoma cells by antioxidants through the Nrf2-ARE pathway (at protein level). Up-regulated by the antioxidant dithiolethione (D3T) in liver, small intestine and brain (at protein level). Down-regulated under lithium treatment. Ref.6 Ref.7 Ref.9 Ref.10

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5959Removed in mature form By similarity
PRO_0000026591
Chain60 – 264205Proteasome subunit beta type-5
PRO_0000026592

Sites

Active site601Nucleophile By similarity
Binding site1081Bortezomib; via amide nitrogen By similarity

Experimental info

Sequence conflict1101D → N in BAB26942. Ref.3
Sequence conflict2481S → N in AAH12246. Ref.4

Secondary structure

.................................... 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O55234 [UniParc].

Last modified April 29, 2008. Version 3.
Checksum: FCCD619734EF3C57

FASTA26428,532
        10         20         30         40         50         60 
MALASVLQRP MPVNQHGFFG LGGGADLLDL GPGSPGDGLS LAAPSWGVPE EPRIEMLHGT 

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

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

       190        200        210        220        230        240 
SGTAFSVGSG SVYAYGVMDR GYSYDLKVEE AYDLARRAIY QATYRDAYSG GAVNLYHVRE 

       250        260 
DGWIRVSSDN VADLHDKYSS VSVP 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis and chromosomal localization of the mouse Psmb5 gene coding for the constitutively expressed beta-type proteasome subunit."
Kohda K., Matsuda Y., Ishibashi T., Tanaka K., Kasahara M.
Immunogenetics 47:77-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ and C57BL/6.
[2]"The complete primary structure of mouse 20S proteasomes."
Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N., Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.
Immunogenetics 49:835-842(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: B10.A.
Tissue: Macrophage.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Embryonic stem cell.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor and Salivary gland.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 79-91; 141-150 AND 167-179, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway."
Kwak M.K., Wakabayashi N., Greenlaw J.L., Yamamoto M., Kensler T.W.
Mol. Cell. Biol. 23:8786-8794(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY ANTIOXIDANTS.
[7]"Induction of 26S proteasome subunit PSMB5 by the bifunctional inducer 3-methylcholanthrene through the Nrf2-ARE, but not the AhR/Arnt-XRE, pathway."
Kwak M.K., Kensler T.W.
Biochem. Biophys. Res. Commun. 345:1350-1357(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY ANTIOXIDANTS.
[8]"Serial analysis of gene expression in mouse uterus at the implantation site."
Ma X.H., Hu S.J., Ni H., Zhao Y.C., Tian Z., Liu J.L., Ren G., Liang X.H., Yu H., Wan P., Yang Z.M.
J. Biol. Chem. 281:9351-9360(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Tissue specific increase of the catalytic subunits of the 26S proteasome by indirect antioxidant dithiolethione in mice: enhanced activity for degradation of abnormal protein."
Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.
Life Sci. 80:2411-2420(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY DITHIOLETHIONE.
[10]"Microarray gene expression profiling of mouse brain mRNA in a model of lithium treatment."
Chetcuti A., Adams L.J., Mitchell P.B., Schofield P.R.
Psychiatr. Genet. 18:64-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY LITHIUM.
[11]"Protection against amyloid beta cytotoxicity by sulforaphane: role of the proteasome."
Park H.M., Kim J.A., Kwak M.K.
Arch. Pharm. Res. 32:109-115(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Mapping the murine cardiac 26S proteasome complexes."
Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J., Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.
Circ. Res. 99:362-371(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB003304 mRNA. Translation: BAA24916.1.
AB003306 Genomic DNA. Translation: BAA24917.1.
AF060091 mRNA. Translation: AAD50536.1.
AK010441 mRNA. Translation: BAB26942.1.
AK133839 mRNA. Translation: BAE21876.1.
BC012246 mRNA. Translation: AAH12246.1.
BC106144 mRNA. Translation: AAI06145.1.
CCDSCCDS27095.1.
RefSeqNP_035316.1. NM_011186.1.
UniGeneMm.8911.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.901/K/Y/m60-264[»]
3UNEX-ray3.201/K/Y/m60-264[»]
ProteinModelPortalO55234.
SMRO55234. Positions 60-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202421. 4 interactions.
IntActO55234. 7 interactions.
MINTMINT-4125600.

Chemistry

ChEMBLCHEMBL1944494.

Protein family/group databases

MEROPST01.P01.

PTM databases

PhosphoSiteO55234.

Proteomic databases

MaxQBO55234.
PaxDbO55234.
PRIDEO55234.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022803; ENSMUSP00000022803; ENSMUSG00000022193.
GeneID19173.
KEGGmmu:19173.
UCSCuc007twl.1. mouse.

Organism-specific databases

CTD5693.
MGIMGI:1194513. Psmb5.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00510000046395.
HOGENOMHOG000091082.
HOVERGENHBG108297.
InParanoidO55234.
KOK02737.
OMALRAIMHA.
OrthoDBEOG7FNC86.
PhylomeDBO55234.
TreeFamTF106223.

Gene expression databases

BgeeO55234.
GenevestigatorO55234.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295850.
PROO55234.
SOURCESearch...

Entry information

Entry namePSB5_MOUSE
AccessionPrimary (citable) accession number: O55234
Secondary accession number(s): Q3UZI1 expand/collapse secondary AC list , Q91X53, Q9CWR4, Q9R1P2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 29, 2008
Last modified: July 9, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot