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Protein

Proteasome subunit beta type-4

Gene

Psmb4

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). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1.3 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.By similarity

GO - Molecular functioni

  • lipopolysaccharide binding Source: UniProtKB
  • 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-9020702 Interleukin-1 signaling
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MEROPSiT01.987

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-4 (EC:3.4.25.1By similarity)
Alternative name(s):
Low molecular mass protein 3
Macropain beta chain
Multicatalytic endopeptidase complex beta chain
Proteasome beta chain
Proteasome chain 3
Gene namesi
Name:Psmb4
Synonyms:Lmp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1098257 Psmb4

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000265811 – 452 PublicationsAdd BLAST45
ChainiPRO_000002658246 – 264Proteasome subunit beta type-4Add BLAST219

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei102PhosphotyrosineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

EPDiP99026
MaxQBiP99026
PaxDbiP99026
PeptideAtlasiP99026
PRIDEiP99026

2D gel databases

REPRODUCTION-2DPAGEiP99026
SWISS-2DPAGEiP99026

PTM databases

iPTMnetiP99026
PhosphoSitePlusiP99026
SwissPalmiP99026

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Inductioni

Up-regulated in liver tumor tissues (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000005779
GenevisibleiP99026 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). Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome (By similarity). Interacts with PRPF19 (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi202420, 43 interactors
CORUMiP99026
DIPiDIP-35152N
IntActiP99026, 46 interactors
MINTiP99026
STRINGi10090.ENSMUSP00000005923

Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi51 – 53Combined sources3
Beta strandi56 – 61Combined sources6
Beta strandi64 – 70Combined sources7
Beta strandi73 – 75Combined sources3
Beta strandi78 – 83Combined sources6
Beta strandi87 – 89Combined sources3
Beta strandi91 – 101Combined sources11
Helixi102 – 122Combined sources21
Helixi130 – 146Combined sources17
Beta strandi153 – 161Combined sources9
Beta strandi164 – 170Combined sources7
Beta strandi172 – 174Combined sources3
Beta strandi176 – 178Combined sources3
Beta strandi180 – 183Combined sources4
Helixi187 – 201Combined sources15
Helixi207 – 224Combined sources18
Beta strandi232 – 237Combined sources6
Beta strandi242 – 248Combined sources7
Helixi255 – 257Combined sources3
Turni258 – 260Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.903/M/a/o46-264[»]
3UNEX-ray3.203/M/a/o46-264[»]
3UNFX-ray2.90M/a46-264[»]
3UNHX-ray3.20M/a46-264[»]
ProteinModelPortaliP99026
SMRiP99026
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0185 Eukaryota
ENOG410YAMA LUCA
GeneTreeiENSGT00390000000698
HOVERGENiHBG018194
InParanoidiP99026
KOiK02736
OMAiKECMKVL
OrthoDBiEOG091G0JV7
PhylomeDBiP99026
TreeFamiTF106220

Family and domain databases

CDDicd03760 proteasome_beta_type_4, 1 hit
Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR016050 Proteasome_bsu_CS
IPR016295 Proteasome_endopept_cplx_B
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF5 PTHR11599:SF5, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PIRSFiPIRSF001213 Psome_endopept_beta, 1 hit
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.

P99026-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAFWESRAG HWAGGPAPGQ FYRIPATPSG LMDPASAPCE GPITRTQNPM
60 70 80 90 100
VTGTSVLGVK FDGGVVIAAD MLGSYGSLAR FRNISRIMRV NDSTMLGASG
110 120 130 140 150
DYADFQYLKQ VLGQMVIDEE LLGDGHSYSP RAIHSWLTRA MYSRRSKMNP
160 170 180 190 200
LWNTMVIGGY ADGESFLGYV DMLGVAYEAP SLATGYGAYL AQPLLREVLE
210 220 230 240 250
KQPVLSQTEA RELVERCMRV LYYRDARSYN RFQIATVTEK GVEIEGPLSA
260
QTNWDIAHMI SGFE
Length:264
Mass (Da):29,116
Last modified:December 15, 1998 - v1
Checksum:i6B6B42B21DFA2B74
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti26A → S in BAE33781 (PubMed:16141072).Curated1
Sequence conflicti26A → S in AAH08241 (PubMed:15489334).Curated1
Sequence conflicti27T → A in BAE33781 (PubMed:16141072).Curated1
Sequence conflicti42P → H in BAE40213 (PubMed:16141072).Curated1
Sequence conflicti215E → G in BAE23215 (PubMed:16141072).Curated1
Sequence conflicti224R → K in BAC36805 (PubMed:16141072).Curated1
Sequence conflicti234I → V in BAE33781 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65636 mRNA Translation: AAC53263.1
AK077448 mRNA Translation: BAC36805.1
AK137044 mRNA Translation: BAE23215.1
AK156624 mRNA Translation: BAE33781.1
AK168265 mRNA Translation: BAE40213.1
AK168340 mRNA Translation: BAE40277.1
BC008241 mRNA Translation: AAH08241.1
M74556 mRNA Translation: AAA39863.1
CCDSiCCDS17597.1
RefSeqiNP_032971.2, NM_008945.3
UniGeneiMm.368

Genome annotation databases

EnsembliENSMUST00000005923; ENSMUSP00000005923; ENSMUSG00000005779
GeneIDi19172
KEGGimmu:19172
UCSCiuc008qhe.2 mouse

Similar proteinsi

Entry informationi

Entry nameiPSB4_MOUSE
AccessioniPrimary (citable) accession number: P99026
Secondary accession number(s): Q3THC0
, Q3THI3, Q3U0S0, Q3UVQ4, Q62008, Q8BK27, Q91VV7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: May 23, 2018
This is version 159 of the entry and version 1 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

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