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Protein

Proteasome subunit beta type-4

Gene

PSMB4

Organism
Homo sapiens (Human)
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 SNIP1.4 Publications

Caution

A report observed N-glycosylation at Asn-83 (PubMed:19139490). However, as the protein does not localize in an extracellular compartment of the cell, additional evidences are required to confirm this result.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processHost-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MEROPSiT01.987

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-4 (EC:3.4.25.11 Publication)
Alternative name(s):
26 kDa prosomal protein
Short name:
HsBPROS26
Short name:
PROS-26
Macropain beta chain
Multicatalytic endopeptidase complex beta chain
Proteasome beta chain
Proteasome chain 3
Short name:
HsN3
Gene namesi
Name:PSMB4
Synonyms:PROS26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000159377.10
HGNCiHGNC:9541 PSMB4
MIMi602177 gene
neXtProtiNX_P28070

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

Organism-specific databases

DisGeNETi5692
OpenTargetsiENSG00000159377
PharmGKBiPA33886

Chemistry databases

ChEMBLiCHEMBL3831201

Polymorphism and mutation databases

BioMutaiPSMB4
DMDMi116242733

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000265791 – 452 PublicationsAdd BLAST45
ChainiPRO_000002658046 – 264Proteasome subunit beta type-4Add BLAST219

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Modified residuei102PhosphotyrosineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

EPDiP28070
MaxQBiP28070
PaxDbiP28070
PeptideAtlasiP28070
PRIDEiP28070
TopDownProteomicsiP28070

2D gel databases

DOSAC-COBS-2DPAGEiP28070
OGPiP28070
REPRODUCTION-2DPAGEiIPI00555956
SWISS-2DPAGEiP28070

PTM databases

iPTMnetiP28070
PhosphoSitePlusiP28070

Expressioni

Inductioni

Up-regulated in fibrolamellar carcinomas.1 Publication

Gene expression databases

BgeeiENSG00000159377
CleanExiHS_PSMB4
ExpressionAtlasiP28070 baseline and differential
GenevisibleiP28070 HS

Organism-specific databases

HPAiHPA006700

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. Interacts with HIV-1 TAT and HIV-1 NEF proteins (PubMed:14550573). Interaction with HTLV-1 TAX protein favors NFKB1 activation (PubMed:8692272). Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome. Interacts with PRPF19 (PubMed:11571290, PubMed:12097147).11 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111665, 98 interactors
CORUMiP28070
DIPiDIP-33844N
IntActiP28070, 51 interactors
MINTiP28070
STRINGi9606.ENSP00000290541

Chemistry databases

BindingDBiP28070

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 – 81Combined sources4
Beta strandi87 – 91Combined sources5
Beta strandi94 – 101Combined sources8
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 – 190Combined sources4
Helixi192 – 201Combined sources10
Beta strandi202 – 204Combined sources3
Helixi207 – 224Combined sources18
Beta strandi232 – 238Combined sources7
Beta strandi241 – 248Combined sources8
Helixi255 – 258Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.602/N46-262[»]
4R67X-ray2.892/N/b/p46-262[»]
5A0Qelectron microscopy3.50N/b46-264[»]
5GJQelectron microscopy4.50g/u1-264[»]
5GJRelectron microscopy3.50g/u1-264[»]
5L4Gelectron microscopy4.024/X1-264[»]
5LE5X-ray1.80M/a46-264[»]
5LEXX-ray2.20M/a46-264[»]
5LEYX-ray1.90M/a46-264[»]
5LEZX-ray2.19M/a46-264[»]
5LF0X-ray2.41M/a46-264[»]
5LF1X-ray2.00M/a46-264[»]
5LF3X-ray2.10M/a46-264[»]
5LF4X-ray1.99M/a46-264[»]
5LF6X-ray2.07M/a46-264[»]
5LF7X-ray2.00M/a46-264[»]
5LN3electron microscopy6.8071-264[»]
5M32electron microscopy3.80M/a1-264[»]
5T0Celectron microscopy3.80AT/BT2-264[»]
5T0Gelectron microscopy4.40T2-264[»]
5T0Helectron microscopy6.80T2-264[»]
5T0Ielectron microscopy8.00T2-264[»]
5T0Jelectron microscopy8.00T2-264[»]
6AVOelectron microscopy3.80W/a46-264[»]
ProteinModelPortaliP28070
SMRiP28070
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0185 Eukaryota
ENOG410YAMA LUCA
GeneTreeiENSGT00390000000698
HOGENOMiHOG000181719
HOVERGENiHBG018194
InParanoidiP28070
KOiK02736
OMAiKECMKVL
OrthoDBiEOG091G0JV7
PhylomeDBiP28070
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.

P28070-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAFLGSRSG LWAGGPAPGQ FYRIPSTPDS FMDPASALYR GPITRTQNPM
60 70 80 90 100
VTGTSVLGVK FEGGVVIAAD MLGSYGSLAR FRNISRIMRV NNSTMLGASG
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 RDLVERCMRV LYYRDARSYN RFQIATVTEK GVEIEGPLST
260
ETNWDIAHMI SGFE
Length:264
Mass (Da):29,204
Last modified:October 17, 2006 - v4
Checksum:iB8701C565069F563
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti264E → D in CAG33101 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01207295M → I. Corresponds to variant dbSNP:rs1804241Ensembl.1
Natural variantiVAR_075255212 – 214Missing Found in a patient with Nakajo syndrome; unknown pathological significance; patients' cells show proteasome assembly defects. 1 Publication3
Natural variantiVAR_013115234I → T5 PublicationsCorresponds to variant dbSNP:rs4603Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26600 mRNA Translation: BAA05647.1
AK313825 mRNA Translation: BAG36560.1
CR456820 mRNA Translation: CAG33101.1
BT006917 mRNA Translation: AAP35563.1
AL589764 Genomic DNA No translation available.
CH471121 Genomic DNA Translation: EAW53442.1
S71381 mRNA Translation: AAB31085.1
CCDSiCCDS996.1
PIRiS08186
S45719
S50147
RefSeqiNP_002787.2, NM_002796.2
UniGeneiHs.89545

Genome annotation databases

EnsembliENST00000290541; ENSP00000290541; ENSG00000159377
GeneIDi5692
KEGGihsa:5692
UCSCiuc001eyc.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPSB4_HUMAN
AccessioniPrimary (citable) accession number: P28070
Secondary accession number(s): B2R9L3
, P31148, Q5SZS5, Q6IBI4, Q969L6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 17, 2006
Last modified: April 25, 2018
This is version 205 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health