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Protein

Proteasome subunit beta type-4

Gene

Psmb4

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). 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-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1098257. Psmb4.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
  • proteasome complex Source: MGI
  • proteasome core complex Source: UniProtKB

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.

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. 44 interactors.
DIPiDIP-35152N.
IntActiP99026. 46 interactors.
MINTiMINT-1850556.
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.
OMAiRIMRVND.
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:SF72. PTHR11599:SF72. 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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi202420. 44 interactors.
DIPiDIP-35152N.
IntActiP99026. 46 interactors.
MINTiMINT-1850556.
STRINGi10090.ENSMUSP00000005923.

Protein family/group databases

MEROPSiT01.987.

PTM databases

iPTMnetiP99026.
PhosphoSitePlusiP99026.

2D gel databases

REPRODUCTION-2DPAGEiP99026.
SWISS-2DPAGEiP99026.

Proteomic databases

EPDiP99026.
MaxQBiP99026.
PaxDbiP99026.
PeptideAtlasiP99026.
PRIDEiP99026.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5692.
MGIiMGI:1098257. Psmb4.

Phylogenomic databases

eggNOGiKOG0185. Eukaryota.
ENOG410YAMA. LUCA.
GeneTreeiENSGT00390000000698.
HOVERGENiHBG018194.
InParanoidiP99026.
KOiK02736.
OMAiRIMRVND.
OrthoDBiEOG091G0JV7.
PhylomeDBiP99026.
TreeFamiTF106220.

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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPsmb4. mouse.
PROiPR:P99026.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005779.
GenevisibleiP99026. MM.

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:SF72. PTHR11599:SF72. 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.
ProtoNetiSearch...

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: March 15, 2017
This is version 150 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.