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Protein

Proteasome subunit beta type-6

Gene

Psmb6

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). Within the 20S core complex, PSMB6 displays a peptidylglutamyl-hydrolyzing activity also termed postacidic or caspase-like activity, meaning that the peptides bond hydrolysis occurs directly after acidic residues.2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei34NucleophileBy similarity1

GO - Molecular functioni

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

MEROPSiT01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-6 (EC:3.4.25.1By similarity)
Alternative name(s):
Low molecular mass protein 19
Macropain delta chain
Multicatalytic endopeptidase complex delta chain
Proteasome delta chain
Proteasome subunit Y
Gene namesi
Name:Psmb6
Synonyms:Lmp19
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:104880. Psmb6.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1944493.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
PropeptideiPRO_00000266152 – 33Removed in mature formBy similarityAdd BLAST32
ChainiPRO_000002661634 – 238Proteasome subunit beta type-6Add BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei68PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

EPDiQ60692.
MaxQBiQ60692.
PaxDbiQ60692.
PeptideAtlasiQ60692.
PRIDEiQ60692.

2D gel databases

REPRODUCTION-2DPAGEiQ60692.

PTM databases

iPTMnetiQ60692.
PhosphoSitePlusiQ60692.
SwissPalmiQ60692.

Expressioni

Inductioni

Up-regulated by the antioxidant dithiolethione (D3T) in liver, lung and small intestine (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000018286.
GenevisibleiQ60692. 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 PSMB7.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202423. 2 interactors.
IntActiQ60692. 9 interactors.
MINTiMINT-1850570.
STRINGi10090.ENSMUSP00000018430.

Structurei

Secondary structure

1238
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 40Combined sources5
Beta strandi42 – 49Combined sources8
Beta strandi53 – 55Combined sources3
Beta strandi58 – 63Combined sources6
Beta strandi67 – 69Combined sources3
Beta strandi71 – 80Combined sources10
Helixi82 – 103Combined sources22
Helixi109 – 122Combined sources14
Turni123 – 126Combined sources4
Beta strandi129 – 137Combined sources9
Turni138 – 140Combined sources3
Beta strandi141 – 147Combined sources7
Beta strandi157 – 162Combined sources6
Helixi163 – 168Combined sources6
Helixi169 – 175Combined sources7
Helixi182 – 199Combined sources18
Beta strandi200 – 202Combined sources3
Beta strandi207 – 213Combined sources7
Beta strandi216 – 222Combined sources7
Helixi224 – 226Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.904/N/b/p34-238[»]
3UNEX-ray3.204/N/b/p34-238[»]
ProteinModelPortaliQ60692.
SMRiQ60692.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0174. Eukaryota.
ENOG410XS23. LUCA.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiQ60692.
KOiK02738.
OMAiTSIMAVQ.
OrthoDBiEOG091G0GUI.
PhylomeDBiQ60692.
TreeFamiTF106221.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
PfamiView protein in Pfam
PF00227. Proteasome. 1 hit.
PRINTSiPR00141. PROTEASOME.
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.

Q60692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAALAVRRA GSAPAFGPEA LTPDWENREV STGTTIMAVQ FNGGVVLGAD
60 70 80 90 100
SRTTTGSYIA NRVTDKLTPI HDHIFCCRSG SAADTQAVAD AVTYQLGFHS
110 120 130 140 150
IELNEPPLVH TAASLFKEMC YRYREDLMAG IIIAGWDPQE GGQVYSVPMG
160 170 180 190 200
GMMVRQSFAI GGSGSSYIYG YVDATYREGM TKDECLQFTA NALALAMERD
210 220 230
GSSGGVIRLA AIQESGVERQ VLLGDQIPKF TIATLPPP
Length:238
Mass (Da):25,379
Last modified:December 20, 2005 - v3
Checksum:i5A4EB82C4374C6FE
GO

Sequence cautioni

The sequence AAA75375 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAA75376 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAH13897 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAE20959 differs from that shown. Reason: Frameshift at position 224.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2A → T (PubMed:7797265).Curated1
Sequence conflicti6A → S (PubMed:7797265).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti38A → T1 Publication1
Natural varianti89A → T1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13393 mRNA. Translation: AAA75375.1. Different initiation.
U13394 Genomic DNA. Translation: AAA75376.1. Different initiation.
AK078437 mRNA. Translation: BAC37272.1.
AK132042 mRNA. Translation: BAE20959.1. Frameshift.
AK167123 mRNA. Translation: BAE39271.1.
AK167227 mRNA. Translation: BAE39351.1.
AL592547 Genomic DNA. Translation: CAI24014.1.
BC013897 mRNA. Translation: AAH13897.1. Different initiation.
CCDSiCCDS48836.1.
RefSeqiNP_032972.3. NM_008946.4.
UniGeneiMm.98.

Genome annotation databases

EnsembliENSMUST00000018430; ENSMUSP00000018430; ENSMUSG00000018286.
GeneIDi19175.
KEGGimmu:19175.
UCSCiuc007jve.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13393 mRNA. Translation: AAA75375.1. Different initiation.
U13394 Genomic DNA. Translation: AAA75376.1. Different initiation.
AK078437 mRNA. Translation: BAC37272.1.
AK132042 mRNA. Translation: BAE20959.1. Frameshift.
AK167123 mRNA. Translation: BAE39271.1.
AK167227 mRNA. Translation: BAE39351.1.
AL592547 Genomic DNA. Translation: CAI24014.1.
BC013897 mRNA. Translation: AAH13897.1. Different initiation.
CCDSiCCDS48836.1.
RefSeqiNP_032972.3. NM_008946.4.
UniGeneiMm.98.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.904/N/b/p34-238[»]
3UNEX-ray3.204/N/b/p34-238[»]
ProteinModelPortaliQ60692.
SMRiQ60692.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202423. 2 interactors.
IntActiQ60692. 9 interactors.
MINTiMINT-1850570.
STRINGi10090.ENSMUSP00000018430.

Chemistry databases

ChEMBLiCHEMBL1944493.

Protein family/group databases

MEROPSiT01.010.

PTM databases

iPTMnetiQ60692.
PhosphoSitePlusiQ60692.
SwissPalmiQ60692.

2D gel databases

REPRODUCTION-2DPAGEiQ60692.

Proteomic databases

EPDiQ60692.
MaxQBiQ60692.
PaxDbiQ60692.
PeptideAtlasiQ60692.
PRIDEiQ60692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018430; ENSMUSP00000018430; ENSMUSG00000018286.
GeneIDi19175.
KEGGimmu:19175.
UCSCiuc007jve.2. mouse.

Organism-specific databases

CTDi5694.
MGIiMGI:104880. Psmb6.

Phylogenomic databases

eggNOGiKOG0174. Eukaryota.
ENOG410XS23. LUCA.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiQ60692.
KOiK02738.
OMAiTSIMAVQ.
OrthoDBiEOG091G0GUI.
PhylomeDBiQ60692.
TreeFamiTF106221.

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

ChiTaRSiPsmb6. mouse.
PROiPR:Q60692.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000018286.
GenevisibleiQ60692. MM.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
PfamiView protein in Pfam
PF00227. Proteasome. 1 hit.
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiView protein in PROSITE
PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPSB6_MOUSE
AccessioniPrimary (citable) accession number: Q60692
Secondary accession number(s): Q3V240
, Q60693, Q8BJX9, Q91VH5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: December 20, 2005
Last modified: May 10, 2017
This is version 152 of the entry and version 3 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.