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Protein

Proteasome subunit beta type-6

Gene

Psmb6

Organism
Mus musculus (Mouse)
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). 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-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-8939902 Regulation of RUNX2 expression and activity
R-MMU-8941858 Regulation of RUNX3 expression and activity
R-MMU-8948751 Regulation of PTEN stability and activity
R-MMU-9020702 Interleukin-1 signaling
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

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

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
CORUMiQ60692
IntActiQ60692, 9 interactors
MINTiQ60692
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
OMAiHDRIYCC
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
IPR035140 Proteasome_beta6
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF46 PTHR11599:SF46, 1 hit
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

Similar proteinsi

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: February 28, 2018
This is version 158 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
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Main funding by: National Institutes of Health