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O09061

- PSB1_MOUSE

UniProt

O09061 - PSB1_MOUSE

Protein

Proteasome subunit beta type-1

Gene

Psmb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      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. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. 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

    MEROPSiT01.986.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-1 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C5
    Multicatalytic endopeptidase complex subunit C5
    Proteasome component C5
    Proteasome gamma chain
    Gene namesi
    Name:Psmb1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:104884. Psmb1.

    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
    Propeptidei1 – 2727By similarityPRO_0000259624Add
    BLAST
    Chaini28 – 240213Proteasome subunit beta type-1PRO_0000148031Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Glycosylationi57 – 571O-linked (GlcNAc)1 Publication
    Modified residuei149 – 1491Phosphotyrosine1 Publication
    Modified residuei203 – 2031N6-acetyllysineBy similarity
    Glycosylationi208 – 2081O-linked (GlcNAc)1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiO09061.
    PaxDbiO09061.
    PRIDEiO09061.

    PTM databases

    PhosphoSiteiO09061.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiO09061.
    BgeeiO09061.
    GenevestigatoriO09061.

    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 SERPINB2.2 Publications

    Protein-protein interaction databases

    BioGridi202418. 3 interactions.
    IntActiO09061. 6 interactions.
    MINTiMINT-1856820.

    Structurei

    Secondary structure

    1
    240
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 436
    Beta strandi48 – 536
    Beta strandi56 – 583
    Beta strandi61 – 655
    Beta strandi70 – 723
    Beta strandi74 – 8310
    Helixi85 – 10622
    Helixi112 – 12413
    Turni125 – 1284
    Beta strandi133 – 1408
    Beta strandi142 – 1443
    Beta strandi146 – 1516
    Beta strandi157 – 16610
    Helixi169 – 17911
    Helixi195 – 21218
    Beta strandi213 – 2153
    Beta strandi218 – 2269
    Beta strandi229 – 2368

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNBX-ray2.902/L/Z/n28-240[»]
    3UNEX-ray3.202/L/Z/n28-240[»]
    3UNFX-ray2.90L/Z28-240[»]
    3UNHX-ray3.20L/Z28-240[»]
    ProteinModelPortaliO09061.
    SMRiO09061. Positions 28-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091081.
    HOVERGENiHBG000961.
    InParanoidiO09061.
    KOiK02732.
    OMAiQCRAGGA.
    OrthoDBiEOG7WHHBB.
    PhylomeDBiO09061.
    TreeFamiTF106218.

    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.

    O09061-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSTAAYRDV ERELGMGPHG SAGPVQLRFS PYAFNGGTVL AIAGEDFSIV    50
    ASDTRLSEGF SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK 100
    MYKHSNNKAM TTGAIAAMLS TILYSRRFFP YYVYNIIGGL DEEGKGAVYS 150
    FDPVGSYQRD SFKAGGSASA MLQPLLDNQV GFKNMQNVEH VPLTLDRAMR 200
    LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVPLRKD 240
    Length:240
    Mass (Da):26,372
    Last modified:July 1, 1997 - v1
    Checksum:i22ADBC6ACB3A8D31
    GO

    Sequence cautioni

    The sequence CAA56702.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U60824 mRNA. Translation: AAB37251.1.
    X80686 mRNA. Translation: CAA56701.1.
    X80686 mRNA. Translation: CAA56702.1. Different initiation.
    AK077520 mRNA. Translation: BAC36841.1.
    BC018351 mRNA. Translation: AAH18351.1.
    CCDSiCCDS28411.1.
    RefSeqiNP_035315.1. NM_011185.3.
    UniGeneiMm.32912.

    Genome annotation databases

    EnsembliENSMUST00000014913; ENSMUSP00000014913; ENSMUSG00000014769.
    GeneIDi19170.
    KEGGimmu:19170.
    UCSCiuc008aol.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U60824 mRNA. Translation: AAB37251.1 .
    X80686 mRNA. Translation: CAA56701.1 .
    X80686 mRNA. Translation: CAA56702.1 . Different initiation.
    AK077520 mRNA. Translation: BAC36841.1 .
    BC018351 mRNA. Translation: AAH18351.1 .
    CCDSi CCDS28411.1.
    RefSeqi NP_035315.1. NM_011185.3.
    UniGenei Mm.32912.

    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 2/L/Z/n 28-240 [» ]
    3UNE X-ray 3.20 2/L/Z/n 28-240 [» ]
    3UNF X-ray 2.90 L/Z 28-240 [» ]
    3UNH X-ray 3.20 L/Z 28-240 [» ]
    ProteinModelPortali O09061.
    SMRi O09061. Positions 28-240.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202418. 3 interactions.
    IntActi O09061. 6 interactions.
    MINTi MINT-1856820.

    Protein family/group databases

    MEROPSi T01.986.

    PTM databases

    PhosphoSitei O09061.

    Proteomic databases

    MaxQBi O09061.
    PaxDbi O09061.
    PRIDEi O09061.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000014913 ; ENSMUSP00000014913 ; ENSMUSG00000014769 .
    GeneIDi 19170.
    KEGGi mmu:19170.
    UCSCi uc008aol.1. mouse.

    Organism-specific databases

    CTDi 5689.
    MGIi MGI:104884. Psmb1.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091081.
    HOVERGENi HBG000961.
    InParanoidi O09061.
    KOi K02732.
    OMAi QCRAGGA.
    OrthoDBi EOG7WHHBB.
    PhylomeDBi O09061.
    TreeFami TF106218.

    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 PSMB1. mouse.
    NextBioi 295838.
    PROi O09061.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O09061.
    Bgeei O09061.
    Genevestigatori O09061.

    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. "Cloning and sequencing of a murine cDNA encoding the proteasome component C5."
      Savioz A., Houghton I., Davies R.W.
      DNA Seq. 5:307-309(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/10J.
      Tissue: Brain and Testis.
    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.
    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., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 77-93; 109-126; 146-159; 164-197 AND 204-212, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    5. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
    6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    7. "Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag."
      Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A., Siele D., Kloetzel P.M., Janek K.
      Mol. Cell. Proteomics 11:467-477(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-57 AND SER-208.
      Tissue: Brain and Spleen.
    8. "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 nameiPSB1_MOUSE
    AccessioniPrimary (citable) accession number: O09061
    Secondary accession number(s): Q62038, Q62039
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 125 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