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Protein

Proteasome subunit beta type-5

Gene

Psmb5

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

Functioni

Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity.3 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei60NucleophileBy similarity1
Binding sitei108Bortezomib; via amide nitrogenBy similarity1

GO - Molecular functioni

  • peptidase activity Source: MGI
  • threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  • proteolysis Source: MGI
  • response to oxidative stress Source: MGI

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-382556. ABC-family proteins mediated transport.
R-MMU-446652. Interleukin-1 family signaling.
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-5689603. UCH proteinases.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-MMU-8939236. RUNX1 regulates transcription of genes involved in differentiation of HSCs.
R-MMU-8939902. Regulation of RUNX2 expression and activity.
R-MMU-8941858. Regulation of RUNX3 expression and activity.
R-MMU-8948751. Regulation of PTEN stability and activity.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-5 (EC:3.4.25.1By similarity)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1194513. Psmb5.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1944494.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000265911 – 59Removed in mature formBy similarityAdd BLAST59
ChainiPRO_000002659260 – 264Proteasome subunit beta type-5Add BLAST205

Keywords - PTMi

Zymogen

Proteomic databases

EPDiO55234.
MaxQBiO55234.
PaxDbiO55234.
PeptideAtlasiO55234.
PRIDEiO55234.

PTM databases

iPTMnetiO55234.
PhosphoSitePlusiO55234.
SwissPalmiO55234.

Expressioni

Tissue specificityi

Expressed in uterus at the embryo implantation site.2 Publications

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

BgeeiENSMUSG00000022193.
GenevisibleiO55234. MM.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, PubMed:22341445). Directly interacts with POMP (By similarity). Interacts with ABCB1 and TAP1 (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi202421. 70 interactors.
CORUMiO55234.
IntActiO55234. 69 interactors.
MINTiMINT-4125600.
STRINGi10090.ENSMUSP00000022803.

Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi61 – 67Combined sources7
Beta strandi70 – 75Combined sources6
Beta strandi79 – 81Combined sources3
Beta strandi84 – 88Combined sources5
Beta strandi93 – 97Combined sources5
Beta strandi100 – 103Combined sources4
Helixi108 – 129Combined sources22
Helixi135 – 147Combined sources13
Turni148 – 153Combined sources6
Beta strandi156 – 164Combined sources9
Beta strandi167 – 174Combined sources8
Beta strandi179 – 181Combined sources3
Beta strandi183 – 188Combined sources6
Helixi191 – 200Combined sources10
Helixi208 – 225Combined sources18
Beta strandi226 – 228Combined sources3
Beta strandi231 – 239Combined sources9
Beta strandi242 – 250Combined sources9
Helixi251 – 258Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.901/K/Y/m60-264[»]
3UNEX-ray3.201/K/Y/m60-264[»]
ProteinModelPortaliO55234.
SMRiO55234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0175. Eukaryota.
ENOG410XQRP. LUCA.
GeneTreeiENSGT00510000046395.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
InParanoidiO55234.
KOiK02737.
OMAiTMCAGVT.
OrthoDBiEOG091G0BPS.
PhylomeDBiO55234.
TreeFamiTF106223.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
PfamiView protein in Pfam
PF00227. Proteasome. 1 hit.
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiView protein in PROSITE
PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti110D → N in BAB26942 (PubMed:16141072).Curated1
Sequence conflicti248S → N in AAH12246 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Similar proteinsi

Entry informationi

Entry nameiPSB5_MOUSE
AccessioniPrimary (citable) accession number: O55234
Secondary accession number(s): Q3UZI1
, Q91X53, Q9CWR4, Q9R1P2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 29, 2008
Last modified: November 22, 2017
This is version 154 of the entry and version 3 of the sequence. See 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