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Q9R1P3

- PSB2_MOUSE

UniProt

Q9R1P3 - PSB2_MOUSE

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Protein

Proteasome subunit beta type-2

Gene

Psmb2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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 has a chymotrypsin-like activity.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
  2. response to organic cyclic compound Source: Ensembl
  3. response to organonitrogen compound Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.
REACT_232069. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_232469. Hh ligand biogenesis disease.
REACT_233316. Hedgehog ligand biogenesis.
REACT_234963. Regulation of ornithine decarboxylase (ODC).
REACT_244558. CDT1 association with the CDC6:ORC:origin complex.
REACT_245230. Orc1 removal from chromatin.
REACT_249922. CDK-mediated phosphorylation and removal of Cdc6.
REACT_263467. Ubiquitin-dependent degradation of Cyclin D1.
REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_268705. Degradation of GLI1 by the proteasome.
REACT_270923. Degradation of GLI2 by the proteasome.

Protein family/group databases

MEROPSiT01.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-2 (EC:3.4.25.1)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1347045. Psmb2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: UniProtKB-KW
  4. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Proteasome subunit beta type-2PRO_0000148044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9R1P3.
PaxDbiQ9R1P3.
PRIDEiQ9R1P3.

2D gel databases

REPRODUCTION-2DPAGEQ9R1P3.

PTM databases

PhosphoSiteiQ9R1P3.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiQ9R1P3.
GenevestigatoriQ9R1P3.

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.2 Publications

Protein-protein interaction databases

BioGridi204996. 2 interactions.
IntActiQ9R1P3. 7 interactions.
MINTiMINT-1856775.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi13 – 186Combined sources
Beta strandi21 – 233Combined sources
Beta strandi26 – 316Combined sources
Beta strandi35 – 373Combined sources
Beta strandi39 – 4911Combined sources
Helixi52 – 7120Combined sources
Helixi77 – 9216Combined sources
Beta strandi94 – 963Combined sources
Beta strandi100 – 1089Combined sources
Turni109 – 1113Combined sources
Beta strandi112 – 1187Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1336Combined sources
Helixi136 – 14510Combined sources
Helixi153 – 16917Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi187 – 1904Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00640000091536.
HOGENOMiHOG000188743.
HOVERGENiHBG000815.
InParanoidiQ9R1P3.
KOiK02734.
OMAiHFVRGEL.
OrthoDBiEOG7N63NQ.
PhylomeDBiQ9R1P3.
TreeFamiTF106219.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060090 mRNA. Translation: AAD50535.1 .
BC008265 mRNA. Translation: AAH08265.1 .
CCDSi CCDS18657.1.
RefSeqi NP_036100.3. NM_011970.4.
UniGenei Mm.22233.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNB X-ray 2.90 J/X/l/z 1-201 [» ]
3UNE X-ray 3.20 J/X/l/z 1-201 [» ]
3UNF X-ray 2.90 J/X 1-201 [» ]
3UNH X-ray 3.20 J/X 1-201 [» ]
ProteinModelPortali Q9R1P3.
SMRi Q9R1P3. Positions 1-196.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204996. 2 interactions.
IntActi Q9R1P3. 7 interactions.
MINTi MINT-1856775.

Chemistry

ChEMBLi CHEMBL3112378.

Protein family/group databases

MEROPSi T01.984.

PTM databases

PhosphoSitei Q9R1P3.

2D gel databases

REPRODUCTION-2DPAGE Q9R1P3.

Proteomic databases

MaxQBi Q9R1P3.
PaxDbi Q9R1P3.
PRIDEi Q9R1P3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030642 ; ENSMUSP00000030642 ; ENSMUSG00000028837 .
GeneIDi 26445.
KEGGi mmu:26445.
UCSCi uc008utr.2. mouse.

Organism-specific databases

CTDi 5690.
MGIi MGI:1347045. Psmb2.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00640000091536.
HOGENOMi HOG000188743.
HOVERGENi HBG000815.
InParanoidi Q9R1P3.
KOi K02734.
OMAi HFVRGEL.
OrthoDBi EOG7N63NQ.
PhylomeDBi Q9R1P3.
TreeFami TF106219.

Enzyme and pathway databases

Reactomei REACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.
REACT_232069. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_232469. Hh ligand biogenesis disease.
REACT_233316. Hedgehog ligand biogenesis.
REACT_234963. Regulation of ornithine decarboxylase (ODC).
REACT_244558. CDT1 association with the CDC6:ORC:origin complex.
REACT_245230. Orc1 removal from chromatin.
REACT_249922. CDK-mediated phosphorylation and removal of Cdc6.
REACT_263467. Ubiquitin-dependent degradation of Cyclin D1.
REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_268705. Degradation of GLI1 by the proteasome.
REACT_270923. Degradation of GLI2 by the proteasome.

Miscellaneous databases

ChiTaRSi Psmb2. mouse.
NextBioi 304537.
PROi Q9R1P3.
SOURCEi Search...

Gene expression databases

Bgeei Q9R1P3.
Genevestigatori Q9R1P3.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: B10.BR.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 71-85; 127-145 AND 171-198, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  4. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
  5. "Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity."
    Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., Groll M.
    Cell 148:727-738(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPSB2_MOUSE
AccessioniPrimary (citable) accession number: Q9R1P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 127 of the entry and version 1 of the sequence. [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

External Data

Dasty 3