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Q9R1P1

- PSB3_MOUSE

UniProt

Q9R1P1 - PSB3_MOUSE

Protein

Proteasome subunit beta type-3

Gene

Psmb3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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.1 Publication

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein catabolic process Source: MGI
    2. proteolysis involved in cellular protein catabolic process Source: InterPro

    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_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.

    Protein family/group databases

    MEROPSiT01.983.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-3 (EC:3.4.25.1)
    Alternative name(s):
    Proteasome chain 13
    Proteasome component C10-II
    Proteasome theta chain
    Gene namesi
    Name:Psmb3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1347014. Psmb3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome core complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 205204Proteasome subunit beta type-3PRO_0000148058Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei77 – 771N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9R1P1.
    PaxDbiQ9R1P1.
    PRIDEiQ9R1P1.

    2D gel databases

    REPRODUCTION-2DPAGEQ9R1P1.
    UCD-2DPAGEQ9R1P1.

    PTM databases

    PhosphoSiteiQ9R1P1.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9R1P1.
    BgeeiQ9R1P1.
    GenevestigatoriQ9R1P1.

    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

    BioGridi204997. 3 interactions.
    IntActiQ9R1P1. 2 interactions.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 74
    Beta strandi10 – 156
    Beta strandi20 – 256
    Beta strandi28 – 303
    Beta strandi33 – 375
    Beta strandi42 – 5514
    Helixi57 – 7721
    Beta strandi78 – 803
    Helixi84 – 9613
    Turni97 – 1004
    Beta strandi104 – 1129
    Turni114 – 1163
    Beta strandi119 – 1235
    Beta strandi130 – 1323
    Beta strandi134 – 1407
    Helixi143 – 15311
    Helixi160 – 17516
    Beta strandi178 – 1814
    Beta strandi185 – 1906
    Beta strandi192 – 2009

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNBX-ray2.90I/W/k/y1-205[»]
    3UNEX-ray3.20I/W/k/y1-205[»]
    3UNFX-ray2.90I/W1-205[»]
    3UNHX-ray3.20I/W1-205[»]
    ProteinModelPortaliQ9R1P1.
    SMRiQ9R1P1. Positions 2-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074820.
    HOGENOMiHOG000090523.
    HOVERGENiHBG004446.
    InParanoidiQ9R1P1.
    KOiK02735.
    OMAiDSTEDCW.
    OrthoDBiEOG783MWB.
    PhylomeDBiQ9R1P1.
    TreeFamiTF106216.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9R1P1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY    50
    IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF 100
    GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCSEQMYGMC 150
    ESLWEPNMDP EHLFETISQA MLNAVDRDAV SGMGVIVHVI EKDKITTRTL 200
    KARMD 205
    Length:205
    Mass (Da):22,965
    Last modified:May 1, 2000 - v1
    Checksum:i743DDA584D5045FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060092 mRNA. Translation: AAD50537.1.
    AK002331 mRNA. Translation: BAB22017.1.
    BC014783 mRNA. Translation: AAH14783.1.
    CCDSiCCDS25328.1.
    RefSeqiNP_036101.1. NM_011971.4.
    UniGeneiMm.21874.

    Genome annotation databases

    EnsembliENSMUST00000103147; ENSMUSP00000099436; ENSMUSG00000069744.
    GeneIDi26446.
    KEGGimmu:26446.
    UCSCiuc007lep.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060092 mRNA. Translation: AAD50537.1 .
    AK002331 mRNA. Translation: BAB22017.1 .
    BC014783 mRNA. Translation: AAH14783.1 .
    CCDSi CCDS25328.1.
    RefSeqi NP_036101.1. NM_011971.4.
    UniGenei Mm.21874.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3UNB X-ray 2.90 I/W/k/y 1-205 [» ]
    3UNE X-ray 3.20 I/W/k/y 1-205 [» ]
    3UNF X-ray 2.90 I/W 1-205 [» ]
    3UNH X-ray 3.20 I/W 1-205 [» ]
    ProteinModelPortali Q9R1P1.
    SMRi Q9R1P1. Positions 2-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204997. 3 interactions.
    IntActi Q9R1P1. 2 interactions.

    Protein family/group databases

    MEROPSi T01.983.

    PTM databases

    PhosphoSitei Q9R1P1.

    2D gel databases

    REPRODUCTION-2DPAGE Q9R1P1.
    UCD-2DPAGE Q9R1P1.

    Proteomic databases

    MaxQBi Q9R1P1.
    PaxDbi Q9R1P1.
    PRIDEi Q9R1P1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000103147 ; ENSMUSP00000099436 ; ENSMUSG00000069744 .
    GeneIDi 26446.
    KEGGi mmu:26446.
    UCSCi uc007lep.1. mouse.

    Organism-specific databases

    CTDi 5691.
    MGIi MGI:1347014. Psmb3.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074820.
    HOGENOMi HOG000090523.
    HOVERGENi HBG004446.
    InParanoidi Q9R1P1.
    KOi K02735.
    OMAi DSTEDCW.
    OrthoDBi EOG783MWB.
    PhylomeDBi Q9R1P1.
    TreeFami TF106216.

    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_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.

    Miscellaneous databases

    NextBioi 304541.
    PROi Q9R1P1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9R1P1.
    Bgeei Q9R1P1.
    Genevestigatori Q9R1P1.

    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

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: B10.BR.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Kidney.
    3. "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: FVB/N.
      Tissue: Mammary gland.
    4. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 6-14; 49-66; 71-77; 100-115 AND 394-403, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    5. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX, ACETYLATION AT SER-2.
    6. "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 nameiPSB3_MOUSE
    AccessioniPrimary (citable) accession number: Q9R1P1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 129 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