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Protein

Proteasome subunit beta type-5

Gene

Psmb5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

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-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-8951664 Neddylation
R-MMU-9020702 Interleukin-1 signaling
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 Expressed in 20 organ(s), highest expression level in skeletal muscle tissue
ExpressionAtlasiO55234 baseline and differential
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, 69 interactors
CORUMiO55234
IntActiO55234, 69 interactors
MINTiO55234
STRINGi10090.ENSMUSP00000022803

Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
IPR037558 Proteasome_beta_5
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF51 PTHR11599:SF51, 1 hit
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

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.iShow all

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q8BTY5Q8BTY5_MOUSE
Proteasome subunit beta type-5
Psmb5
177Annotation score:

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: September 12, 2018
This is version 158 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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