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Protein

Proteasome subunit beta type-8

Gene

Psmb8

Organism
Mus musculus (Mouse)
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 subunit is involved in antigen processing to generate class I binding peptides. May be involved in the inflammatory response pathway. Required for adipocyte differentiation.3 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei73Nucleophile1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Differentiation, Immunity

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

MEROPSiT01.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-8 (EC:3.4.25.1)
Alternative name(s):
Low molecular mass protein 7
Macropain subunit C13
Multicatalytic endopeptidase complex subunit C13
Proteasome component C13
Proteasome subunit beta-5i
Gene namesi
Name:Psmb8
Synonyms:Lmp7, Mc13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1346527. Psmb8.

Subcellular locationi

  • Cytoplasm PROSITE-ProRule annotation
  • Nucleus By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • nucleus Source: UniProtKB-SubCell
  • proteasome complex Source: MGI
  • proteasome core complex Source: UniProtKB
  • spermatoproteasome complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1944492.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000265991 – 72Removed in mature formBy similarityAdd BLAST72
ChainiPRO_000002660073 – 276Proteasome subunit beta type-8Add BLAST204

Post-translational modificationi

Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei72 – 73Cleavage; by autolysisBy similarity2

Keywords - PTMi

Zymogen

Proteomic databases

EPDiP28063.
MaxQBiP28063.
PaxDbiP28063.
PeptideAtlasiP28063.
PRIDEiP28063.

PTM databases

iPTMnetiP28063.
PhosphoSitePlusiP28063.
SwissPalmiP28063.

Expressioni

Tissue specificityi

Detected in liver (at protein level). Expressed in spleen, thymus, lung, liver, heart and, at a very low level, in kidney. Not expressed in brain nor testis.2 Publications

Inductioni

Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1. Down-regulated in spleen by deoxynivalenol (DON), a mycotoxin that alters immune functions. Down-regulated by the selective inhibitor PR-957. Up-regulated by heat shock treatment. Down-regulated by EGR1 in neuronal cells.5 Publications

Gene expression databases

BgeeiENSMUSG00000024338.
ExpressionAtlasiP28063. baseline and differential.
GenevisibleiP28063. MM.

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. Component of the immunoproteasome, where it displaces the equivalent housekeeping subunit PSMB5. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP. Interacts with TAP1.3 Publications

Protein-protein interaction databases

IntActiP28063. 4 interactors.
MINTiMINT-1856641.
STRINGi10090.ENSMUSP00000025196.

Structurei

Secondary structure

1276
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi74 – 80Combined sources7
Beta strandi83 – 88Combined sources6
Beta strandi92 – 94Combined sources3
Beta strandi97 – 102Combined sources6
Beta strandi106 – 108Combined sources3
Beta strandi113 – 116Combined sources4
Helixi121 – 142Combined sources22
Helixi148 – 161Combined sources14
Turni162 – 164Combined sources3
Beta strandi171 – 177Combined sources7
Beta strandi180 – 186Combined sources7
Beta strandi188 – 190Combined sources3
Beta strandi192 – 194Combined sources3
Beta strandi196 – 201Combined sources6
Helixi204 – 212Combined sources9
Helixi221 – 238Combined sources18
Beta strandi244 – 252Combined sources9
Beta strandi255 – 263Combined sources9
Helixi264 – 271Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90K/Y73-276[»]
3UNHX-ray3.20K/Y73-276[»]
ProteinModelPortaliP28063.
SMRiP28063.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0175. Eukaryota.
ENOG410XQRP. LUCA.
GeneTreeiENSGT00510000046395.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
InParanoidiP28063.
KOiK02740.
OMAiATIRVNK.
OrthoDBiEOG091G0BPS.
PhylomeDBiP28063.
TreeFamiTF106223.

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.

P28063-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLDLCGAA RGQRPEWAAL DAGSGGRSDP GHYSFSAQAP ELALPRGMQP
60 70 80 90 100
TAFLRSFGGD QERNVQIEMA HGTTTLAFKF QHGVIVAVDS RATAGSYISS
110 120 130 140 150
LRMNKVIEIN PYLLGTMSGC AADCQYWERL LAKECRLYYL RNGERISVSA
160 170 180 190 200
ASKLLSNMML QYRGMGLSMG SMICGWDKKG PGLYYVDDNG TRLSGQMFST
210 220 230 240 250
GSGNTYAYGV MDSGYRQDLS PEEAYDLGRR AIAYATHRDN YSGGVVNMYH
260 270
MKEDGWVKVE SSDVSDLLYK YGEAAL
Length:276
Mass (Da):30,260
Last modified:November 1, 1995 - v2
Checksum:iD9FCCF3EF83CD3C3
GO

Sequence cautioni

The sequence CAA45780 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti39A → R in CAB60065 (PubMed:8406612).Curated1
Sequence conflicti148V → M in BAE26960 (PubMed:16141072).Curated1
Sequence conflicti199S → P in AAH51450 (PubMed:15489334).Curated1

Polymorphismi

The allele, LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7 found in strains NMRI, B10.BR, SJL, A.CA, B10.RIII, B10.cas4 and NOD may be post-translationally modified. Allele LMP7q is found in strain DBA/1J.2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti272G → R in LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7. 2 Publications1
Natural varianti275A → S in LMP7q. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64449 mRNA. Translation: CAA45779.1.
X64449 mRNA. Translation: CAA45780.1. Different initiation.
L11145 mRNA. Translation: AAB46392.1.
Z21847 Genomic DNA. Translation: CAB60065.1. Sequence problems.
U22031 mRNA. Translation: AAA75033.1.
U22032 mRNA. Translation: AAA75034.1.
U22033 mRNA. Translation: AAA75035.1.
U22034 mRNA. Translation: AAA75036.1.
U22035 mRNA. Translation: AAA75037.1.
AK031801 mRNA. Translation: BAC27555.1.
AK050627 mRNA. Translation: BAE20682.1.
AK146182 mRNA. Translation: BAE26960.1.
AK150674 mRNA. Translation: BAE29756.1.
AK159971 mRNA. Translation: BAE35524.1.
AF027865 Genomic DNA. Translation: AAB81532.1.
BC013785 mRNA. Translation: AAH13785.1.
BC051450 mRNA. Translation: AAH51450.1.
CCDSiCCDS50073.1.
PIRiI54513.
RefSeqiNP_034854.2. NM_010724.2.
UniGeneiMm.180191.
Mm.484878.

Genome annotation databases

EnsembliENSMUST00000025196; ENSMUSP00000025196; ENSMUSG00000024338.
GeneIDi16913.
KEGGimmu:16913.
UCSCiuc012apv.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64449 mRNA. Translation: CAA45779.1.
X64449 mRNA. Translation: CAA45780.1. Different initiation.
L11145 mRNA. Translation: AAB46392.1.
Z21847 Genomic DNA. Translation: CAB60065.1. Sequence problems.
U22031 mRNA. Translation: AAA75033.1.
U22032 mRNA. Translation: AAA75034.1.
U22033 mRNA. Translation: AAA75035.1.
U22034 mRNA. Translation: AAA75036.1.
U22035 mRNA. Translation: AAA75037.1.
AK031801 mRNA. Translation: BAC27555.1.
AK050627 mRNA. Translation: BAE20682.1.
AK146182 mRNA. Translation: BAE26960.1.
AK150674 mRNA. Translation: BAE29756.1.
AK159971 mRNA. Translation: BAE35524.1.
AF027865 Genomic DNA. Translation: AAB81532.1.
BC013785 mRNA. Translation: AAH13785.1.
BC051450 mRNA. Translation: AAH51450.1.
CCDSiCCDS50073.1.
PIRiI54513.
RefSeqiNP_034854.2. NM_010724.2.
UniGeneiMm.180191.
Mm.484878.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90K/Y73-276[»]
3UNHX-ray3.20K/Y73-276[»]
ProteinModelPortaliP28063.
SMRiP28063.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28063. 4 interactors.
MINTiMINT-1856641.
STRINGi10090.ENSMUSP00000025196.

Chemistry databases

ChEMBLiCHEMBL1944492.

Protein family/group databases

MEROPSiT01.015.

PTM databases

iPTMnetiP28063.
PhosphoSitePlusiP28063.
SwissPalmiP28063.

Proteomic databases

EPDiP28063.
MaxQBiP28063.
PaxDbiP28063.
PeptideAtlasiP28063.
PRIDEiP28063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025196; ENSMUSP00000025196; ENSMUSG00000024338.
GeneIDi16913.
KEGGimmu:16913.
UCSCiuc012apv.1. mouse.

Organism-specific databases

CTDi5696.
MGIiMGI:1346527. Psmb8.

Phylogenomic databases

eggNOGiKOG0175. Eukaryota.
ENOG410XQRP. LUCA.
GeneTreeiENSGT00510000046395.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
InParanoidiP28063.
KOiK02740.
OMAiATIRVNK.
OrthoDBiEOG091G0BPS.
PhylomeDBiP28063.
TreeFamiTF106223.

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

PROiP28063.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024338.
ExpressionAtlasiP28063. baseline and differential.
GenevisibleiP28063. MM.

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 nameiPSB8_MOUSE
AccessioniPrimary (citable) accession number: P28063
Secondary accession number(s): Q3UK42
, Q64300, Q792S8, Q7TMX9, Q91VH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.