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O55234

- PSB5_MOUSE

UniProt

O55234 - PSB5_MOUSE

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Protein

Proteasome subunit beta type-5

Gene

Psmb5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei60 – 601NucleophileBy similarity
Binding sitei108 – 1081Bortezomib; via amide nitrogenBy similarity

GO - Molecular functioni

  1. peptidase activity Source: MGI
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  2. response to oxidative stress Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Psmb5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1194513. Psmb5.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: UniProtKB-KW
  4. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 5959Removed in mature formBy similarityPRO_0000026591Add
BLAST
Chaini60 – 264205Proteasome subunit beta type-5PRO_0000026592Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiO55234.
PaxDbiO55234.
PRIDEiO55234.

PTM databases

PhosphoSiteiO55234.

Expressioni

Tissue specificityi

Expressed in uterus at the embryo implantation site.1 Publication

Inductioni

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.4 Publications

Gene expression databases

BgeeiO55234.
GenevestigatoriO55234.

Interactioni

Subunit structurei

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 TAP1.1 Publication

Protein-protein interaction databases

BioGridi202421. 4 interactions.
IntActiO55234. 7 interactions.
MINTiMINT-4125600.

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 677
Beta strandi70 – 756
Beta strandi79 – 813
Beta strandi84 – 885
Beta strandi93 – 975
Beta strandi100 – 1034
Helixi108 – 12922
Helixi135 – 14713
Turni148 – 1536
Beta strandi156 – 1649
Beta strandi167 – 1748
Beta strandi179 – 1813
Beta strandi183 – 1886
Helixi191 – 20010
Helixi208 – 22518
Beta strandi226 – 2283
Beta strandi231 – 2399
Beta strandi242 – 2509
Helixi251 – 2588

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.901/K/Y/m60-264[»]
3UNEX-ray3.201/K/Y/m60-264[»]
ProteinModelPortaliO55234.
SMRiO55234. Positions 31-260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046395.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
InParanoidiO55234.
KOiK02737.
OMAiLRAIMHA.
OrthoDBiEOG7FNC86.
PhylomeDBiO55234.
TreeFamiTF106223.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O55234-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALASVLQRP MPVNQHGFFG LGGGADLLDL GPGSPGDGLS LAAPSWGVPE
60 70 80 90 100
EPRIEMLHGT TTLAFKFLHG VIVAADSRAT AGAYIASQTV KKVIEINPYL
110 120 130 140 150
LGTMAGGAAD CSFWERLLAR QCRIYELRNK ERISVAAASK LLANMVYQYK
160 170 180 190 200
GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI SGTAFSVGSG SVYAYGVMDR
210 220 230 240 250
GYSYDLKVEE AYDLARRAIY QATYRDAYSG GAVNLYHVRE DGWIRVSSDN
260
VADLHDKYSS VSVP
Length:264
Mass (Da):28,532
Last modified:April 29, 2008 - v3
Checksum:iFCCD619734EF3C57
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101D → N in BAB26942. (PubMed:16141072)Curated
Sequence conflicti248 – 2481S → N in AAH12246. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS27095.1.
RefSeqiNP_035316.1. NM_011186.1.
UniGeneiMm.8911.

Genome annotation databases

EnsembliENSMUST00000022803; ENSMUSP00000022803; ENSMUSG00000022193.
GeneIDi19173.
KEGGimmu:19173.
UCSCiuc007twl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS27095.1.
RefSeqi NP_035316.1. NM_011186.1.
UniGenei Mm.8911.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNB X-ray 2.90 1/K/Y/m 60-264 [» ]
3UNE X-ray 3.20 1/K/Y/m 60-264 [» ]
ProteinModelPortali O55234.
SMRi O55234. Positions 31-260.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202421. 4 interactions.
IntActi O55234. 7 interactions.
MINTi MINT-4125600.

Chemistry

ChEMBLi CHEMBL1944494.

PTM databases

PhosphoSitei O55234.

Proteomic databases

MaxQBi O55234.
PaxDbi O55234.
PRIDEi O55234.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022803 ; ENSMUSP00000022803 ; ENSMUSG00000022193 .
GeneIDi 19173.
KEGGi mmu:19173.
UCSCi uc007twl.1. mouse.

Organism-specific databases

CTDi 5693.
MGIi MGI:1194513. Psmb5.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00510000046395.
HOGENOMi HOG000091082.
HOVERGENi HBG108297.
InParanoidi O55234.
KOi K02737.
OMAi LRAIMHA.
OrthoDBi EOG7FNC86.
PhylomeDBi O55234.
TreeFami TF106223.

Enzyme and pathway databases

Reactomei REACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Miscellaneous databases

NextBioi 295850.
PROi O55234.
SOURCEi Search...

Gene expression databases

Bgeei O55234.
Genevestigatori O55234.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.

Entry informationi

Entry nameiPSB5_MOUSE
AccessioniPrimary (citable) accession number: O55234
Secondary accession number(s): Q3UZI1
, Q91X53, Q9CWR4, Q9R1P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 29, 2008
Last modified: October 29, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3