Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proteasome subunit beta type-8

Gene

Psmb8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

  • antigen processing and presentation Source: MGI
  • fat cell differentiation Source: UniProtKB
  • proteolysis involved in cellular protein catabolic process Source: InterPro
  • regulation of endopeptidase activity Source: MGI

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processDifferentiation, 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-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

MEROPSiT01.012

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1346527 Psmb8

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

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

CORUMiP28063
IntActiP28063, 5 interactors
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 – 101Combined sources5
Beta strandi106 – 110Combined sources5
Beta strandi113 – 116Combined sources4
Helixi121 – 142Combined sources22
Helixi148 – 161Combined sources14
Turni162 – 166Combined sources5
Beta strandi169 – 177Combined sources9
Beta strandi180 – 187Combined sources8
Beta strandi188 – 190Combined sources3
Beta strandi192 – 194Combined sources3
Beta strandi196 – 201Combined sources6
Helixi204 – 210Combined sources7
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[»]
5L65X-ray2.90K/Y73-210[»]
5L66X-ray2.80K/Y73-210[»]
5L67X-ray2.60K/Y73-210[»]
5L68X-ray2.80K/Y73-210[»]
5L69X-ray2.70K/Y73-210[»]
5L6AX-ray2.80K/Y73-210[»]
5L6BX-ray2.60K/Y73-210[»]
5L6CX-ray2.60K/Y73-210[»]
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
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000243 Pept_T1A_subB
IPR035705 Proteasome_beta8
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF53 PTHR11599:SF53, 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.

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

Similar proteinsi

Entry informationi

Entry nameiPSB8_MOUSE
AccessioniPrimary (citable) accession number: P28063
Secondary accession number(s): Q3UK42
, Q64300, Q792S8, Q7TMX9, Q91VH7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1995
Last modified: February 28, 2018
This is version 169 of the entry and version 2 of the sequence. See 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health