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Protein

Proteasome subunit beta type-3

Gene

PSMB3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:HS03083-MONOMER.
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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.983.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-3 (EC:3.4.25.1)
Alternative name(s):
Proteasome chain 13
Proteasome component C10-II
Proteasome theta chain
Gene namesi
Name:PSMB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9540. PSMB3.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: HPA
  • mitochondrion Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome core complex Source: UniProtKB
  • proteasome core complex, beta-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000275903.
ENSG00000277791.
PharmGKBiPA33885.

Chemistry databases

ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Polymorphism and mutation databases

BioMutaiPSMB3.
DMDMi20532411.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001480572 – 205Proteasome subunit beta type-3Add BLAST204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei77N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP49720.
MaxQBiP49720.
PaxDbiP49720.
PeptideAtlasiP49720.
PRIDEiP49720.
TopDownProteomicsiP49720.

2D gel databases

OGPiP49720.
REPRODUCTION-2DPAGEIPI00028004.

PTM databases

iPTMnetiP49720.
PhosphoSitePlusiP49720.
SwissPalmiP49720.

Expressioni

Inductioni

Up-regulated in asthenozoospermic sperm.1 Publication

Gene expression databases

BgeeiENSG00000108294.
CleanExiHS_PSMB3.
ExpressionAtlasiP49720. baseline and differential.
GenevisibleiP49720. HS.

Organism-specific databases

HPAiHPA042775.
HPA048147.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with HIV-1 TAT protein.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMB2P497214EBI-603340,EBI-359335
TRIM27P143735EBI-603340,EBI-719493

Protein-protein interaction databases

BioGridi111664. 99 interactors.
DIPiDIP-33846N.
IntActiP49720. 31 interactors.
MINTiMINT-5001041.
STRINGi9606.ENSP00000225426.

Chemistry databases

BindingDBiP49720.

Structurei

Secondary structure

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Beta strandi10 – 15Combined sources6
Beta strandi20 – 25Combined sources6
Beta strandi28 – 30Combined sources3
Beta strandi33 – 37Combined sources5
Beta strandi42 – 46Combined sources5
Beta strandi49 – 55Combined sources7
Helixi57 – 78Combined sources22
Helixi84 – 97Combined sources14
Turni98 – 100Combined sources3
Beta strandi104 – 112Combined sources9
Turni114 – 116Combined sources3
Beta strandi119 – 124Combined sources6
Beta strandi130 – 140Combined sources11
Helixi143 – 153Combined sources11
Helixi160 – 175Combined sources16
Beta strandi178 – 181Combined sources4
Beta strandi185 – 190Combined sources6
Beta strandi192 – 200Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60J/X2-205[»]
4R67X-ray2.89J/X/l/z2-205[»]
5A0Qelectron microscopy3.50J/X2-205[»]
5GJQelectron microscopy4.50c/q1-205[»]
5GJRelectron microscopy3.50c/q1-205[»]
5L4Gelectron microscopy4.023/W1-205[»]
5LE5X-ray1.80I/W1-205[»]
5LEXX-ray2.20I/W1-205[»]
5LEYX-ray1.90I/W1-205[»]
5LEZX-ray2.19I/W1-205[»]
5LF0X-ray2.41I/W1-205[»]
5LF1X-ray2.00I/W1-205[»]
5LF3X-ray2.10I/W1-205[»]
5LF4X-ray1.99I/W1-205[»]
5LF6X-ray2.07I/W1-205[»]
5LF7X-ray2.00I/W1-205[»]
5T0Celectron microscopy3.80AP/BP2-205[»]
5T0Gelectron microscopy4.40P2-205[»]
5T0Helectron microscopy6.80P2-205[»]
5T0Ielectron microscopy8.00P2-205[»]
5T0Jelectron microscopy8.00P2-205[»]
ProteinModelPortaliP49720.
SMRiP49720.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0180. Eukaryota.
ENOG410XSC8. LUCA.
GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
HOVERGENiHBG004446.
InParanoidiP49720.
KOiK02735.
OMAiYIEPVIA.
OrthoDBiEOG091G0JTX.
PhylomeDBiP49720.
TreeFamiTF106216.

Family and domain databases

CDDicd03759. proteasome_beta_type_3. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR033811. Proteasome_beta_3.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P49720-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY
60 70 80 90 100
IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF
110 120 130 140 150
GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCAEQMYGMC
160 170 180 190 200
ESLWEPNMDP DHLFETISQA MLNAVDRDAV SGMGVIVHII EKDKITTRTL

KARMD
Length:205
Mass (Da):22,949
Last modified:May 10, 2002 - v2
Checksum:i624972384C0112FD
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03441534M → L.1 PublicationCorresponds to variant rs4907dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26598 mRNA. Translation: BAA05645.1.
BC013008 mRNA. Translation: AAH13008.1.
CCDSiCCDS11328.1.
PIRiS55041.
RefSeqiNP_002786.2. NM_002795.3.
UniGeneiHs.82793.

Genome annotation databases

EnsembliENST00000619426; ENSP00000483688; ENSG00000277791.
ENST00000619951; ENSP00000483956; ENSG00000275903.
GeneIDi5691.
KEGGihsa:5691.
UCSCiuc002hqr.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26598 mRNA. Translation: BAA05645.1.
BC013008 mRNA. Translation: AAH13008.1.
CCDSiCCDS11328.1.
PIRiS55041.
RefSeqiNP_002786.2. NM_002795.3.
UniGeneiHs.82793.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60J/X2-205[»]
4R67X-ray2.89J/X/l/z2-205[»]
5A0Qelectron microscopy3.50J/X2-205[»]
5GJQelectron microscopy4.50c/q1-205[»]
5GJRelectron microscopy3.50c/q1-205[»]
5L4Gelectron microscopy4.023/W1-205[»]
5LE5X-ray1.80I/W1-205[»]
5LEXX-ray2.20I/W1-205[»]
5LEYX-ray1.90I/W1-205[»]
5LEZX-ray2.19I/W1-205[»]
5LF0X-ray2.41I/W1-205[»]
5LF1X-ray2.00I/W1-205[»]
5LF3X-ray2.10I/W1-205[»]
5LF4X-ray1.99I/W1-205[»]
5LF6X-ray2.07I/W1-205[»]
5LF7X-ray2.00I/W1-205[»]
5T0Celectron microscopy3.80AP/BP2-205[»]
5T0Gelectron microscopy4.40P2-205[»]
5T0Helectron microscopy6.80P2-205[»]
5T0Ielectron microscopy8.00P2-205[»]
5T0Jelectron microscopy8.00P2-205[»]
ProteinModelPortaliP49720.
SMRiP49720.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111664. 99 interactors.
DIPiDIP-33846N.
IntActiP49720. 31 interactors.
MINTiMINT-5001041.
STRINGi9606.ENSP00000225426.

Chemistry databases

BindingDBiP49720.
ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Protein family/group databases

MEROPSiT01.983.

PTM databases

iPTMnetiP49720.
PhosphoSitePlusiP49720.
SwissPalmiP49720.

Polymorphism and mutation databases

BioMutaiPSMB3.
DMDMi20532411.

2D gel databases

OGPiP49720.
REPRODUCTION-2DPAGEIPI00028004.

Proteomic databases

EPDiP49720.
MaxQBiP49720.
PaxDbiP49720.
PeptideAtlasiP49720.
PRIDEiP49720.
TopDownProteomicsiP49720.

Protocols and materials databases

DNASUi5691.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000619426; ENSP00000483688; ENSG00000277791.
ENST00000619951; ENSP00000483956; ENSG00000275903.
GeneIDi5691.
KEGGihsa:5691.
UCSCiuc002hqr.5. human.

Organism-specific databases

CTDi5691.
GeneCardsiPSMB3.
H-InvDBHIX0030292.
HGNCiHGNC:9540. PSMB3.
HPAiHPA042775.
HPA048147.
MIMi602176. gene.
neXtProtiNX_P49720.
OpenTargetsiENSG00000275903.
ENSG00000277791.
PharmGKBiPA33885.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0180. Eukaryota.
ENOG410XSC8. LUCA.
GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
HOVERGENiHBG004446.
InParanoidiP49720.
KOiK02735.
OMAiYIEPVIA.
OrthoDBiEOG091G0JTX.
PhylomeDBiP49720.
TreeFamiTF106216.

Enzyme and pathway databases

BioCyciZFISH:HS03083-MONOMER.
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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPSMB3. human.
GeneWikiiPSMB3.
GenomeRNAii5691.
PROiP49720.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108294.
CleanExiHS_PSMB3.
ExpressionAtlasiP49720. baseline and differential.
GenevisibleiP49720. HS.

Family and domain databases

CDDicd03759. proteasome_beta_type_3. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR033811. Proteasome_beta_3.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSB3_HUMAN
AccessioniPrimary (citable) accession number: P49720
Secondary accession number(s): P31147, Q0P6J7, Q96E27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2002
Last modified: November 30, 2016
This is version 177 of the entry and version 2 of the sequence. [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

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. 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.