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Q60692

- PSB6_MOUSE

UniProt

Q60692 - PSB6_MOUSE

Protein

Proteasome subunit beta type-6

Gene

Psmb6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (20 Dec 2005)
      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. May catalyze basal processing of intracellular antigens.

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei34 – 341NucleophileBy similarity

    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

    MEROPSiT01.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-6 (EC:3.4.25.1)
    Alternative name(s):
    Low molecular mass protein 19
    Macropain delta chain
    Multicatalytic endopeptidase complex delta chain
    Proteasome delta chain
    Proteasome subunit Y
    Gene namesi
    Name:Psmb6
    Synonyms:Lmp19
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:104880. Psmb6.

    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 – 11RemovedBy similarity
    Propeptidei2 – 3332Removed in mature formBy similarityPRO_0000026615Add
    BLAST
    Chaini34 – 238205Proteasome subunit beta type-6PRO_0000026616Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation, Zymogen

    Proteomic databases

    MaxQBiQ60692.
    PaxDbiQ60692.
    PRIDEiQ60692.

    2D gel databases

    REPRODUCTION-2DPAGEQ60692.

    PTM databases

    PhosphoSiteiQ60692.

    Expressioni

    Inductioni

    Up-regulated by the antioxidant dithiolethione (D3T) in liver, lung and small intestine (at protein level).1 Publication

    Gene expression databases

    BgeeiQ60692.
    GenevestigatoriQ60692.

    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. This subunit can be displaced by the equivalent immune-specific subunit PSMB9.1 Publication

    Protein-protein interaction databases

    BioGridi202423. 2 interactions.
    IntActiQ60692. 9 interactions.
    MINTiMINT-1850570.

    Structurei

    Secondary structure

    1
    238
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 405
    Beta strandi42 – 498
    Beta strandi53 – 553
    Beta strandi58 – 636
    Beta strandi67 – 693
    Beta strandi71 – 8010
    Helixi82 – 10322
    Helixi109 – 12214
    Turni123 – 1264
    Beta strandi129 – 1379
    Turni138 – 1403
    Beta strandi141 – 1477
    Beta strandi157 – 1626
    Helixi163 – 1686
    Helixi169 – 1757
    Helixi182 – 19918
    Beta strandi200 – 2023
    Beta strandi207 – 2137
    Beta strandi216 – 2227
    Helixi224 – 2263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNBX-ray2.904/N/b/p34-238[»]
    3UNEX-ray3.204/N/b/p34-238[»]
    ProteinModelPortaliQ60692.
    SMRiQ60692. Positions 34-235.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00510000046484.
    HOGENOMiHOG000091079.
    HOVERGENiHBG000123.
    InParanoidiQ60692.
    KOiK02738.
    OMAiTSIMAVQ.
    OrthoDBiEOG79GT80.
    PhylomeDBiQ60692.
    TreeFamiTF106221.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PRINTSiPR00141. PROTEASOME.
    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.

    Q60692-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAALAVRRA GSAPAFGPEA LTPDWENREV STGTTIMAVQ FNGGVVLGAD    50
    SRTTTGSYIA NRVTDKLTPI HDHIFCCRSG SAADTQAVAD AVTYQLGFHS 100
    IELNEPPLVH TAASLFKEMC YRYREDLMAG IIIAGWDPQE GGQVYSVPMG 150
    GMMVRQSFAI GGSGSSYIYG YVDATYREGM TKDECLQFTA NALALAMERD 200
    GSSGGVIRLA AIQESGVERQ VLLGDQIPKF TIATLPPP 238
    Length:238
    Mass (Da):25,379
    Last modified:December 20, 2005 - v3
    Checksum:i5A4EB82C4374C6FE
    GO

    Sequence cautioni

    The sequence BAE20959.1 differs from that shown. Reason: Frameshift at position 224.
    The sequence AAA75375.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAA75376.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH13897.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → T(PubMed:7797265)Curated
    Sequence conflicti6 – 61A → S(PubMed:7797265)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381A → T.1 Publication
    Natural varianti89 – 891A → T.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13393 mRNA. Translation: AAA75375.1. Different initiation.
    U13394 Genomic DNA. Translation: AAA75376.1. Different initiation.
    AK078437 mRNA. Translation: BAC37272.1.
    AK132042 mRNA. Translation: BAE20959.1. Frameshift.
    AK167123 mRNA. Translation: BAE39271.1.
    AK167227 mRNA. Translation: BAE39351.1.
    AL592547 Genomic DNA. Translation: CAI24014.1.
    BC013897 mRNA. Translation: AAH13897.1. Different initiation.
    CCDSiCCDS48836.1.
    RefSeqiNP_032972.3. NM_008946.4.
    UniGeneiMm.98.

    Genome annotation databases

    EnsembliENSMUST00000018430; ENSMUSP00000018430; ENSMUSG00000018286.
    GeneIDi19175.
    KEGGimmu:19175.
    UCSCiuc007jve.2. mouse.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13393 mRNA. Translation: AAA75375.1 . Different initiation.
    U13394 Genomic DNA. Translation: AAA75376.1 . Different initiation.
    AK078437 mRNA. Translation: BAC37272.1 .
    AK132042 mRNA. Translation: BAE20959.1 . Frameshift.
    AK167123 mRNA. Translation: BAE39271.1 .
    AK167227 mRNA. Translation: BAE39351.1 .
    AL592547 Genomic DNA. Translation: CAI24014.1 .
    BC013897 mRNA. Translation: AAH13897.1 . Different initiation.
    CCDSi CCDS48836.1.
    RefSeqi NP_032972.3. NM_008946.4.
    UniGenei Mm.98.

    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 4/N/b/p 34-238 [» ]
    3UNE X-ray 3.20 4/N/b/p 34-238 [» ]
    ProteinModelPortali Q60692.
    SMRi Q60692. Positions 34-235.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202423. 2 interactions.
    IntActi Q60692. 9 interactions.
    MINTi MINT-1850570.

    Chemistry

    ChEMBLi CHEMBL1944493.

    Protein family/group databases

    MEROPSi T01.010.

    PTM databases

    PhosphoSitei Q60692.

    2D gel databases

    REPRODUCTION-2DPAGE Q60692.

    Proteomic databases

    MaxQBi Q60692.
    PaxDbi Q60692.
    PRIDEi Q60692.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000018430 ; ENSMUSP00000018430 ; ENSMUSG00000018286 .
    GeneIDi 19175.
    KEGGi mmu:19175.
    UCSCi uc007jve.2. mouse.

    Organism-specific databases

    CTDi 5694.
    MGIi MGI:104880. Psmb6.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00510000046484.
    HOGENOMi HOG000091079.
    HOVERGENi HBG000123.
    InParanoidi Q60692.
    KOi K02738.
    OMAi TSIMAVQ.
    OrthoDBi EOG79GT80.
    PhylomeDBi Q60692.
    TreeFami TF106221.

    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 295856.
    PROi Q60692.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q60692.
    Genevestigatori Q60692.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PRINTSi PR00141. PROTEASOME.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and mapping of the gene encoding mouse proteasome subunit DELTA (Lmp19)."
      Woodward E.C., Monaco J.J.
      Immunogenetics 42:28-34(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS THR-38 AND THR-89.
      Strain: DBA/2J.
      Tissue: Liver.
    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: Hippocampus and Wolffian duct.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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] OF 7-238.
      Strain: FVB/N.
      Tissue: Mammary tumor.
    5. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 209-229, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    6. "Tissue specific increase of the catalytic subunits of the 26S proteasome by indirect antioxidant dithiolethione in mice: enhanced activity for degradation of abnormal protein."
      Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.
      Life Sci. 80:2411-2420(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY DITHIOLETHIONE.
    7. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.

    Entry informationi

    Entry nameiPSB6_MOUSE
    AccessioniPrimary (citable) accession number: Q60692
    Secondary accession number(s): Q3V240
    , Q60693, Q8BJX9, Q91VH5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 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