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P99026

- PSB4_MOUSE

UniProt

P99026 - PSB4_MOUSE

Protein

Proteasome subunit beta type-4

Gene

Psmb4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (15 Dec 1998)
      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. Mediates the lipopolysaccharide-induced signal macrophage proteasome. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1 By similarity.By similarity

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei46 – 461NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. negative regulation of inflammatory response to antigenic stimulus Source: UniProtKB
    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

    MEROPSiT01.987.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-4 (EC:3.4.25.1)
    Alternative name(s):
    Low molecular mass protein 3
    Macropain beta chain
    Multicatalytic endopeptidase complex beta chain
    Proteasome beta chain
    Proteasome chain 3
    Gene namesi
    Name:Psmb4
    Synonyms:Lmp3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1098257. Psmb4.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

    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
    Propeptidei1 – 45452 PublicationsPRO_0000026581Add
    BLAST
    Chaini46 – 264219Proteasome subunit beta type-4PRO_0000026582Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei102 – 1021PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Zymogen

    Proteomic databases

    MaxQBiP99026.
    PaxDbiP99026.
    PRIDEiP99026.

    2D gel databases

    REPRODUCTION-2DPAGEP99026.
    SWISS-2DPAGEP99026.

    PTM databases

    PhosphoSiteiP99026.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Inductioni

    Up-regulated in liver tumor tissues (at protein level).1 Publication

    Gene expression databases

    BgeeiP99026.
    GenevestigatoriP99026.

    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. Interacts with bacterial lipopolysaccharide (LPS). Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome. Interacts with PRPF19.3 Publications

    Protein-protein interaction databases

    BioGridi202420. 4 interactions.
    IntActiP99026. 5 interactions.
    MINTiMINT-1850556.

    Structurei

    Secondary structure

    1
    264
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi51 – 533
    Beta strandi56 – 616
    Beta strandi64 – 707
    Beta strandi73 – 753
    Beta strandi78 – 836
    Beta strandi87 – 893
    Beta strandi91 – 10111
    Helixi102 – 12221
    Helixi130 – 14617
    Beta strandi153 – 1619
    Beta strandi164 – 1707
    Beta strandi172 – 1743
    Beta strandi176 – 1783
    Beta strandi180 – 1834
    Helixi187 – 20115
    Helixi207 – 22418
    Beta strandi232 – 2376
    Beta strandi242 – 2487
    Helixi255 – 2573
    Turni258 – 2603

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNBX-ray2.903/M/a/o46-264[»]
    3UNEX-ray3.203/M/a/o46-264[»]
    3UNFX-ray2.90M/a46-264[»]
    3UNHX-ray3.20M/a46-264[»]
    ProteinModelPortaliP99026.
    SMRiP99026. Positions 46-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00390000000698.
    HOVERGENiHBG018194.
    InParanoidiP99026.
    KOiK02736.
    OMAiRIMRVND.
    OrthoDBiEOG74FF1D.
    PhylomeDBiP99026.
    TreeFamiTF106220.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR016295. Proteasome_endopept_cplx_B.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
    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.

    P99026-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAFWESRAG HWAGGPAPGQ FYRIPATPSG LMDPASAPCE GPITRTQNPM    50
    VTGTSVLGVK FDGGVVIAAD MLGSYGSLAR FRNISRIMRV NDSTMLGASG 100
    DYADFQYLKQ VLGQMVIDEE LLGDGHSYSP RAIHSWLTRA MYSRRSKMNP 150
    LWNTMVIGGY ADGESFLGYV DMLGVAYEAP SLATGYGAYL AQPLLREVLE 200
    KQPVLSQTEA RELVERCMRV LYYRDARSYN RFQIATVTEK GVEIEGPLSA 250
    QTNWDIAHMI SGFE 264
    Length:264
    Mass (Da):29,116
    Last modified:December 15, 1998 - v1
    Checksum:i6B6B42B21DFA2B74
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261A → S in BAE33781. (PubMed:16141072)Curated
    Sequence conflicti26 – 261A → S in AAH08241. (PubMed:15489334)Curated
    Sequence conflicti27 – 271T → A in BAE33781. (PubMed:16141072)Curated
    Sequence conflicti42 – 421P → H in BAE40213. (PubMed:16141072)Curated
    Sequence conflicti215 – 2151E → G in BAE23215. (PubMed:16141072)Curated
    Sequence conflicti224 – 2241R → K in BAC36805. (PubMed:16141072)Curated
    Sequence conflicti234 – 2341I → V in BAE33781. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65636 mRNA. Translation: AAC53263.1.
    AK077448 mRNA. Translation: BAC36805.1.
    AK137044 mRNA. Translation: BAE23215.1.
    AK156624 mRNA. Translation: BAE33781.1.
    AK168265 mRNA. Translation: BAE40213.1.
    AK168340 mRNA. Translation: BAE40277.1.
    BC008241 mRNA. Translation: AAH08241.1.
    M74556 mRNA. Translation: AAA39863.1.
    CCDSiCCDS17597.1.
    RefSeqiNP_032971.2. NM_008945.3.
    UniGeneiMm.368.

    Genome annotation databases

    EnsembliENSMUST00000005923; ENSMUSP00000005923; ENSMUSG00000005779.
    GeneIDi19172.
    KEGGimmu:19172.
    UCSCiuc008qhe.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65636 mRNA. Translation: AAC53263.1 .
    AK077448 mRNA. Translation: BAC36805.1 .
    AK137044 mRNA. Translation: BAE23215.1 .
    AK156624 mRNA. Translation: BAE33781.1 .
    AK168265 mRNA. Translation: BAE40213.1 .
    AK168340 mRNA. Translation: BAE40277.1 .
    BC008241 mRNA. Translation: AAH08241.1 .
    M74556 mRNA. Translation: AAA39863.1 .
    CCDSi CCDS17597.1.
    RefSeqi NP_032971.2. NM_008945.3.
    UniGenei Mm.368.

    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 3/M/a/o 46-264 [» ]
    3UNE X-ray 3.20 3/M/a/o 46-264 [» ]
    3UNF X-ray 2.90 M/a 46-264 [» ]
    3UNH X-ray 3.20 M/a 46-264 [» ]
    ProteinModelPortali P99026.
    SMRi P99026. Positions 46-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202420. 4 interactions.
    IntActi P99026. 5 interactions.
    MINTi MINT-1850556.

    Protein family/group databases

    MEROPSi T01.987.

    PTM databases

    PhosphoSitei P99026.

    2D gel databases

    REPRODUCTION-2DPAGE P99026.
    SWISS-2DPAGE P99026.

    Proteomic databases

    MaxQBi P99026.
    PaxDbi P99026.
    PRIDEi P99026.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005923 ; ENSMUSP00000005923 ; ENSMUSG00000005779 .
    GeneIDi 19172.
    KEGGi mmu:19172.
    UCSCi uc008qhe.2. mouse.

    Organism-specific databases

    CTDi 5692.
    MGIi MGI:1098257. Psmb4.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00390000000698.
    HOVERGENi HBG018194.
    InParanoidi P99026.
    KOi K02736.
    OMAi RIMRVND.
    OrthoDBi EOG74FF1D.
    PhylomeDBi P99026.
    TreeFami TF106220.

    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

    ChiTaRSi PSMB4. mouse.
    NextBioi 295846.
    PROi P99026.
    SOURCEi Search...

    Gene expression databases

    Bgeei P99026.
    Genevestigatori P99026.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR016295. Proteasome_endopept_cplx_B.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001213. Psome_endopept_beta. 1 hit.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of mouse Lmp3 cDNA, encoding a proteasome beta subunit."
      Cruz M., Nandi D., Hendil K.B., Monaco J.J.
      Gene 190:251-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: B10.A.
      Tissue: Macrophage.
    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: BALB/c, C57BL/6J and NOD.
      Tissue: Spleen.
    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: NMRI.
      Tissue: Mammary tumor.
    4. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 46-80; 110-131 AND 232-240, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    5. Cited for: PROTEIN SEQUENCE OF 46-51.
      Tissue: Liver.
    6. Wang B., Hunsperger J., Laib J., Fan D.
      Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 95-112.
      Strain: C57BL/6.
    7. "The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events."
      Qureshi N., Perera P.-Y., Shen J., Zhang G., Lenschat A., Splitter G., Morrison D.C., Vogel S.N.
      J. Immunol. 171:1515-1525(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LPS.
    8. "The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice."
      Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X., Zhang X., Yang X.
      Proteomics 6:498-504(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    9. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
    10. "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 nameiPSB4_MOUSE
    AccessioniPrimary (citable) accession number: P99026
    Secondary accession number(s): Q3THC0
    , Q3THI3, Q3U0S0, Q3UVQ4, Q62008, Q8BK27, Q91VV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 126 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