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Protein

Proteasome subunit beta type-6

Gene

PSMB6

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. This unit is responsible of the peptidyl glutamyl-like activity. May catalyze basal processing of intracellular antigens.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei35NucleophileBy similarity1

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • endopeptidase activity Source: UniProtKB
  • threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:HS06927-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

MEROPSiT01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-6 (EC:3.4.25.1)
Alternative name(s):
Macropain delta chain
Multicatalytic endopeptidase complex delta chain
Proteasome delta chain
Proteasome subunit Y
Gene namesi
Name:PSMB6
Synonyms:LMPY, Y
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9543. PSMB6.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5694.
OpenTargetsiENSG00000142507.
PharmGKBiPA33888.

Chemistry databases

ChEMBLiCHEMBL1944496.
DrugBankiDB00188. Bortezomib.

Polymorphism and mutation databases

BioMutaiPSMB6.
DMDMi20532407.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
PropeptideiPRO_00000266132 – 34Removed in mature form2 PublicationsAdd BLAST33
ChainiPRO_000002661435 – 239Proteasome subunit beta type-6Add BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei69PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

EPDiP28072.
PaxDbiP28072.
PeptideAtlasiP28072.
PRIDEiP28072.

2D gel databases

OGPiP28072.
SWISS-2DPAGEP28072.

PTM databases

iPTMnetiP28072.
PhosphoSitePlusiP28072.
SwissPalmiP28072.

Expressioni

Inductioni

Down-regulated by IFNG/IFN-gamma (at protein level). Up-regulated in anaplastic thyroid cancer cell lines.2 Publications

Gene expression databases

BgeeiENSG00000142507.
CleanExiHS_PSMB6.
ExpressionAtlasiP28072. baseline and differential.
GenevisibleiP28072. HS.

Organism-specific databases

HPAiHPA023312.
HPA063656.

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. This subunit can be displaced by the equivalent immune-specific subunit PSMB9. Interacts with HIV-1 TAT protein.2 Publications

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi111667. 82 interactors.
DIPiDIP-33847N.
IntActiP28072. 24 interactors.
MINTiMINT-5004163.
STRINGi9606.ENSP00000270586.

Chemistry databases

BindingDBiP28072.

Structurei

Secondary structure

1239
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 42Combined sources6
Beta strandi45 – 50Combined sources6
Beta strandi54 – 56Combined sources3
Beta strandi59 – 64Combined sources6
Beta strandi68 – 72Combined sources5
Beta strandi75 – 81Combined sources7
Helixi83 – 104Combined sources22
Helixi110 – 123Combined sources14
Helixi125 – 127Combined sources3
Beta strandi130 – 138Combined sources9
Turni139 – 141Combined sources3
Beta strandi142 – 148Combined sources7
Beta strandi158 – 163Combined sources6
Helixi164 – 169Combined sources6
Helixi170 – 176Combined sources7
Helixi183 – 200Combined sources18
Beta strandi201 – 203Combined sources3
Beta strandi208 – 214Combined sources7
Beta strandi217 – 223Combined sources7
Helixi225 – 227Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60H/V35-236[»]
4R67X-ray2.89H/V/j/x35-236[»]
5A0Qelectron microscopy3.50H/V35-239[»]
5GJQelectron microscopy4.50a/o1-239[»]
5GJRelectron microscopy3.50a/o1-239[»]
5L4Gelectron microscopy4.026/Z1-239[»]
5LE5X-ray1.80N/b35-239[»]
5LEXX-ray2.20N/b35-239[»]
5LEYX-ray1.90N/b35-239[»]
5LEZX-ray2.19N/b35-239[»]
5LF0X-ray2.41N/b35-239[»]
5LF1X-ray2.00N/b35-239[»]
5LF3X-ray2.10N/b36-239[»]
5LF4X-ray1.99N/b35-239[»]
5LF6X-ray2.07N/b35-239[»]
5LF7X-ray2.00N/b35-239[»]
5T0Celectron microscopy3.80AN/BN2-239[»]
5T0Gelectron microscopy4.40N2-239[»]
5T0Helectron microscopy6.80N2-239[»]
5T0Ielectron microscopy8.00N2-239[»]
5T0Jelectron microscopy8.00N2-239[»]
ProteinModelPortaliP28072.
SMRiP28072.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0174. Eukaryota.
ENOG410XS23. LUCA.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiP28072.
KOiK02738.
OMAiTSIMAVQ.
OrthoDBiEOG091G0GUI.
PhylomeDBiP28072.
TreeFamiTF106221.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
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.

P28072-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATLLAARG AGPAPAWGPE AFTPDWESRE VSTGTTIMAV QFDGGVVLGA
60 70 80 90 100
DSRTTTGSYI ANRVTDKLTP IHDRIFCCRS GSAADTQAVA DAVTYQLGFH
110 120 130 140 150
SIELNEPPLV HTAASLFKEM CYRYREDLMA GIIIAGWDPQ EGGQVYSVPM
160 170 180 190 200
GGMMVRQSFA IGGSGSSYIY GYVDATYREG MTKEECLQFT ANALALAMER
210 220 230
DGSSGGVIRL AAIAESGVER QVLLGDQIPK FAVATLPPA
Length:239
Mass (Da):25,358
Last modified:May 10, 2002 - v4
Checksum:i7DF4081DC735930C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145V → G in BAA06098 (PubMed:8066462).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020030107P → A.Corresponds to variant rs2304974dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29012 mRNA. Translation: BAA06098.1.
BC000835 mRNA. Translation: AAH00835.1.
X61971 mRNA. Translation: CAA43963.1.
CCDSiCCDS11056.1.
PIRiB54589.
S17522.
RefSeqiNP_002789.1. NM_002798.2.
UniGeneiHs.77060.

Genome annotation databases

EnsembliENST00000270586; ENSP00000270586; ENSG00000142507.
GeneIDi5694.
KEGGihsa:5694.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29012 mRNA. Translation: BAA06098.1.
BC000835 mRNA. Translation: AAH00835.1.
X61971 mRNA. Translation: CAA43963.1.
CCDSiCCDS11056.1.
PIRiB54589.
S17522.
RefSeqiNP_002789.1. NM_002798.2.
UniGeneiHs.77060.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60H/V35-236[»]
4R67X-ray2.89H/V/j/x35-236[»]
5A0Qelectron microscopy3.50H/V35-239[»]
5GJQelectron microscopy4.50a/o1-239[»]
5GJRelectron microscopy3.50a/o1-239[»]
5L4Gelectron microscopy4.026/Z1-239[»]
5LE5X-ray1.80N/b35-239[»]
5LEXX-ray2.20N/b35-239[»]
5LEYX-ray1.90N/b35-239[»]
5LEZX-ray2.19N/b35-239[»]
5LF0X-ray2.41N/b35-239[»]
5LF1X-ray2.00N/b35-239[»]
5LF3X-ray2.10N/b36-239[»]
5LF4X-ray1.99N/b35-239[»]
5LF6X-ray2.07N/b35-239[»]
5LF7X-ray2.00N/b35-239[»]
5T0Celectron microscopy3.80AN/BN2-239[»]
5T0Gelectron microscopy4.40N2-239[»]
5T0Helectron microscopy6.80N2-239[»]
5T0Ielectron microscopy8.00N2-239[»]
5T0Jelectron microscopy8.00N2-239[»]
ProteinModelPortaliP28072.
SMRiP28072.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111667. 82 interactors.
DIPiDIP-33847N.
IntActiP28072. 24 interactors.
MINTiMINT-5004163.
STRINGi9606.ENSP00000270586.

Chemistry databases

BindingDBiP28072.
ChEMBLiCHEMBL1944496.
DrugBankiDB00188. Bortezomib.

Protein family/group databases

MEROPSiT01.010.

PTM databases

iPTMnetiP28072.
PhosphoSitePlusiP28072.
SwissPalmiP28072.

Polymorphism and mutation databases

BioMutaiPSMB6.
DMDMi20532407.

2D gel databases

OGPiP28072.
SWISS-2DPAGEP28072.

Proteomic databases

EPDiP28072.
PaxDbiP28072.
PeptideAtlasiP28072.
PRIDEiP28072.

Protocols and materials databases

DNASUi5694.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000270586; ENSP00000270586; ENSG00000142507.
GeneIDi5694.
KEGGihsa:5694.

Organism-specific databases

CTDi5694.
DisGeNETi5694.
GeneCardsiPSMB6.
HGNCiHGNC:9543. PSMB6.
HPAiHPA023312.
HPA063656.
MIMi600307. gene.
neXtProtiNX_P28072.
OpenTargetsiENSG00000142507.
PharmGKBiPA33888.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0174. Eukaryota.
ENOG410XS23. LUCA.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiP28072.
KOiK02738.
OMAiTSIMAVQ.
OrthoDBiEOG091G0GUI.
PhylomeDBiP28072.
TreeFamiTF106221.

Enzyme and pathway databases

BioCyciZFISH:HS06927-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

ChiTaRSiPSMB6. human.
GeneWikiiPSMB6.
GenomeRNAii5694.
PROiP28072.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000142507.
CleanExiHS_PSMB6.
ExpressionAtlasiP28072. baseline and differential.
GenevisibleiP28072. HS.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSB6_HUMAN
AccessioniPrimary (citable) accession number: P28072
Secondary accession number(s): Q96J55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 10, 2002
Last modified: November 30, 2016
This is version 184 of the entry and version 4 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.