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Protein

Proteasome subunit beta type-2

Gene

Psmb2

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).2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.By similarity

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-446652. Interleukin-1 signaling.
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-8941858. Regulation of RUNX3 expression and activity.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-2 (EC:3.4.25.1By similarity)
Alternative name(s):
Macropain subunit C7-I
Multicatalytic endopeptidase complex subunit C7-I
Proteasome component C7-I
Gene namesi
Name:Psmb2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1347045. Psmb2.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3112378.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001480441 – 201Proteasome subunit beta type-2Add BLAST201

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9R1P3.
MaxQBiQ9R1P3.
PaxDbiQ9R1P3.
PeptideAtlasiQ9R1P3.
PRIDEiQ9R1P3.
TopDownProteomicsiQ9R1P3.

2D gel databases

REPRODUCTION-2DPAGEiQ9R1P3.

PTM databases

iPTMnetiQ9R1P3.
PhosphoSitePlusiQ9R1P3.
SwissPalmiQ9R1P3.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000028837.
GenevisibleiQ9R1P3. 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

Protein-protein interaction databases

BioGridi204996. 2 interactors.
IntActiQ9R1P3. 7 interactors.
MINTiMINT-1856775.
STRINGi10090.ENSMUSP00000030642.

Structurei

Secondary structure

1201
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi13 – 18Combined sources6
Beta strandi21 – 23Combined sources3
Beta strandi26 – 31Combined sources6
Beta strandi35 – 37Combined sources3
Beta strandi39 – 49Combined sources11
Helixi52 – 71Combined sources20
Helixi77 – 92Combined sources16
Beta strandi94 – 96Combined sources3
Beta strandi100 – 108Combined sources9
Turni109 – 111Combined sources3
Beta strandi112 – 118Combined sources7
Beta strandi124 – 126Combined sources3
Beta strandi128 – 133Combined sources6
Helixi136 – 145Combined sources10
Helixi153 – 169Combined sources17
Beta strandi171 – 173Combined sources3
Beta strandi178 – 184Combined sources7
Beta strandi187 – 190Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90J/X/l/z1-201[»]
3UNEX-ray3.20J/X/l/z1-201[»]
3UNFX-ray2.90J/X1-201[»]
3UNHX-ray3.20J/X1-201[»]
ProteinModelPortaliQ9R1P3.
SMRiQ9R1P3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0177. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00640000091536.
HOGENOMiHOG000188743.
HOVERGENiHBG000815.
InParanoidiQ9R1P3.
KOiK02734.
OMAiQLYSMRN.
OrthoDBiEOG091G0K9M.
PhylomeDBiQ9R1P3.
TreeFamiTF106219.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9R1P3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA
60 70 80 90 100
GDTVQFAEYI QKNVQLYKMR NGYELSPTAA ANFTRRNLAD CLRSRTPYHV
110 120 130 140 150
NLLLAGYDEH EGPALYYMDY LAALAKAPFA AHGYGAFLTL SILDRYYTPT
160 170 180 190 200
ISRERAVELL RKCLEELQKR FILNLPTFSV RVIDKDGIHN LENIAFPKRD

S
Length:201
Mass (Da):22,906
Last modified:May 1, 2000 - v1
Checksum:iE9B3121974777958
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060090 mRNA. Translation: AAD50535.1.
BC008265 mRNA. Translation: AAH08265.1.
CCDSiCCDS18657.1.
RefSeqiNP_036100.3. NM_011970.4.
UniGeneiMm.22233.

Genome annotation databases

EnsembliENSMUST00000030642; ENSMUSP00000030642; ENSMUSG00000028837.
GeneIDi26445.
KEGGimmu:26445.
UCSCiuc008utr.2. mouse.

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.

Entry informationi

Entry nameiPSB2_MOUSE
AccessioniPrimary (citable) accession number: Q9R1P3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: June 7, 2017
This is version 149 of the entry and version 1 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