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P70195

- PSB7_MOUSE

UniProt

P70195 - PSB7_MOUSE

Protein

Proteasome subunit beta type-7

Gene

Psmb7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Feb 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. This unit is responsible of the trypsin-like activity of the proteasome By similarity.By similarity

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei44 – 441NucleophileBy 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

    MEROPSiT01.011.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-7 (EC:3.4.25.1)
    Alternative name(s):
    Macropain chain Z
    Multicatalytic endopeptidase complex chain Z
    Proteasome subunit Z
    Gene namesi
    Name:Psmb7
    Synonyms:Mmc14
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:107637. Psmb7.

    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 – 4343Removed in mature formBy similarityPRO_0000026647Add
    BLAST
    Chaini44 – 277234Proteasome subunit beta type-7PRO_0000026648Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    MaxQBiP70195.
    PaxDbiP70195.
    PRIDEiP70195.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00136483.
    P70195.

    PTM databases

    PhosphoSiteiP70195.

    Expressioni

    Inductioni

    Up-regulated by the antioxidant dithiolethione (D3T) in colon (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP70195.
    BgeeiP70195.
    GenevestigatoriP70195.

    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 PSMB10.1 Publication

    Protein-protein interaction databases

    BioGridi202424. 1 interaction.
    IntActiP70195. 5 interactions.
    MINTiMINT-1856747.
    STRINGi10090.ENSMUSP00000028083.

    Structurei

    Secondary structure

    1
    277
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi46 – 505
    Beta strandi52 – 609
    Beta strandi63 – 653
    Beta strandi68 – 736
    Beta strandi77 – 9115
    Helixi92 – 11322
    Helixi119 – 13214
    Turni133 – 1353
    Beta strandi139 – 1468
    Beta strandi151 – 1566
    Beta strandi162 – 1643
    Beta strandi166 – 1716
    Helixi174 – 18411
    Helixi191 – 20818
    Beta strandi216 – 2249
    Beta strandi226 – 2338
    Beta strandi254 – 2618

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNBX-ray2.90H/V/j/x44-277[»]
    3UNEX-ray3.20H/V/j/x44-277[»]
    ProteinModelPortaliP70195.
    SMRiP70195. Positions 44-263.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00510000046533.
    HOGENOMiHOG000182856.
    HOVERGENiHBG093416.
    InParanoidiP70195.
    KOiK02739.
    OMAiQIWCAGA.
    OrthoDBiEOG7CRTQJ.
    PhylomeDBiP70195.
    TreeFamiTF106222.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR024689. Proteasome_bsu_C.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF12465. Pr_beta_C. 1 hit.
    PF00227. 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.

    P70195-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVSVFQPP VGGFSFDNCR RNAVLEADFA KKGFKLPKAR KTGTTIAGVV    50
    YKDGIVLGAD TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ 100
    LISSNLELHS LTTGRLPRVV TANRMLKQML FRYQGYIGAA LVLGGVDVTG 150
    PHLYSIYPHG STDKLPYVTM GSGSLAAMAV FEDKFRPDME EEEAKKLVSE 200
    AIAAGIFNDL GSGSNIDLCV ISKSKLDFLR PFSVPNKKGT RLGRYRCEKG 250
    TTAVLTEKVT PLEIEVLEET VQTMDTS 277
    Length:277
    Mass (Da):29,891
    Last modified:February 1, 1997 - v1
    Checksum:i3B8BA01B1E6392F2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081L → F in BAB28354. (PubMed:16141072)Curated
    Sequence conflicti237 – 2371K → E in BAB22385. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83585 mRNA. Translation: BAA12017.1.
    Y10874 mRNA. Translation: CAA71824.1.
    D85570 Genomic DNA. Translation: BAA22857.1.
    AK002823 mRNA. Translation: BAB22385.1.
    AK012613 mRNA. Translation: BAB28354.1.
    AK013961 mRNA. Translation: BAB29085.1.
    AK075759 mRNA. Translation: BAC35937.1.
    AK088276 mRNA. Translation: BAC40251.1.
    AK088765 mRNA. Translation: BAC40556.1.
    AK168823 mRNA. Translation: BAE40650.1.
    BC057662 mRNA. Translation: AAH57662.1.
    CCDSiCCDS16010.1.
    PIRiJC6122.
    RefSeqiNP_035317.1. NM_011187.1.
    UniGeneiMm.389251.

    Genome annotation databases

    EnsembliENSMUST00000028083; ENSMUSP00000028083; ENSMUSG00000026750.
    GeneIDi19177.
    KEGGimmu:19177.
    UCSCiuc008jnp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83585 mRNA. Translation: BAA12017.1 .
    Y10874 mRNA. Translation: CAA71824.1 .
    D85570 Genomic DNA. Translation: BAA22857.1 .
    AK002823 mRNA. Translation: BAB22385.1 .
    AK012613 mRNA. Translation: BAB28354.1 .
    AK013961 mRNA. Translation: BAB29085.1 .
    AK075759 mRNA. Translation: BAC35937.1 .
    AK088276 mRNA. Translation: BAC40251.1 .
    AK088765 mRNA. Translation: BAC40556.1 .
    AK168823 mRNA. Translation: BAE40650.1 .
    BC057662 mRNA. Translation: AAH57662.1 .
    CCDSi CCDS16010.1.
    PIRi JC6122.
    RefSeqi NP_035317.1. NM_011187.1.
    UniGenei Mm.389251.

    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 H/V/j/x 44-277 [» ]
    3UNE X-ray 3.20 H/V/j/x 44-277 [» ]
    ProteinModelPortali P70195.
    SMRi P70195. Positions 44-263.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202424. 1 interaction.
    IntActi P70195. 5 interactions.
    MINTi MINT-1856747.
    STRINGi 10090.ENSMUSP00000028083.

    Protein family/group databases

    MEROPSi T01.011.

    PTM databases

    PhosphoSitei P70195.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00136483.
    P70195.

    Proteomic databases

    MaxQBi P70195.
    PaxDbi P70195.
    PRIDEi P70195.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028083 ; ENSMUSP00000028083 ; ENSMUSG00000026750 .
    GeneIDi 19177.
    KEGGi mmu:19177.
    UCSCi uc008jnp.1. mouse.

    Organism-specific databases

    CTDi 5695.
    MGIi MGI:107637. Psmb7.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00510000046533.
    HOGENOMi HOG000182856.
    HOVERGENi HBG093416.
    InParanoidi P70195.
    KOi K02739.
    OMAi QIWCAGA.
    OrthoDBi EOG7CRTQJ.
    PhylomeDBi P70195.
    TreeFami TF106222.

    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 295860.
    PROi P70195.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70195.
    Bgeei P70195.
    Genevestigatori P70195.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR024689. Proteasome_bsu_C.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF12465. Pr_beta_C. 1 hit.
    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. "Chromosomal localization of the proteasome Z subunit gene reveals an ancient chromosomal duplication involving the major histocompatibility complex."
      Kasahara M., Hayashi M., Tanaka K., Inoko H., Sugaya K., Ikemura T., Ishibashi T.
      Proc. Natl. Acad. Sci. U.S.A. 93:9096-9101(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
      Tissue: Epididymis.
    2. "Molecular cloning of the mouse proteasome subunits MC14 and MECL-1: reciprocally regulated tisue expression of interferon-gamma-modulated proteasome subunits."
      Stohwasser R., Standera S., Peters I., Kloetzel P.-M., Groettrup M.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: C57BL/6.
      Tissue: Spleen.
    3. "The mouse genes encoding the third pair of beta-type proteasome subunits regulated reciprocally by IFN-gamma: structural comparison, chromosomal localization, and analysis of the promoter."
      Hayashi M., Ishibashi T., Tanaka K., Kasahara M.
      J. Immunol. 159:2760-2770(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
    4. "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 and NOD.
      Tissue: Embryonic head, Heart, Testis and Thymus.
    5. "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.
    6. Lubec G., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 226-237.
      Tissue: Brain.
    7. "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.
    8. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.

    Entry informationi

    Entry nameiPSB7_MOUSE
    AccessioniPrimary (citable) accession number: P70195
    Secondary accession number(s): O09084
    , Q542F7, Q9CZH4, Q9DCF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 137 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