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P28064

- PSB8_RAT

UniProt

P28064 - PSB8_RAT

Protein

Proteasome subunit beta type-8

Gene

Psmb8

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (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. This subunit is involved in antigen processing to generate class I binding peptides. Required for adipocyte differentiation By similarity.By similarity

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei72 – 732Cleavage; by autocatalysisBy similarity
    Active sitei73 – 731NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. antigen processing and presentation Source: RGD
    2. fat cell differentiation Source: UniProtKB
    3. proteolysis involved in cellular protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Differentiation, Immunity

    Enzyme and pathway databases

    ReactomeiREACT_194781. Separation of Sister Chromatids.
    REACT_196424. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_198391. Asymmetric localization of PCP proteins.
    REACT_199194. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_199197. ER-Phagosome pathway.
    REACT_199247. Activation of NF-kappaB in B cells.
    REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_204983. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_206488. degradation of DVL.
    REACT_206997. CDT1 association with the CDC6:ORC:origin complex.
    REACT_211117. Orc1 removal from chromatin.
    REACT_212486. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_220232. Regulation of ornithine decarboxylase (ODC).
    REACT_227706. degradation of AXIN.

    Protein family/group databases

    MEROPSiT01.015.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-8 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C13
    Multicatalytic endopeptidase complex subunit C13
    Proteasome component C13
    Proteasome subunit beta-5i
    Gene namesi
    Name:Psmb8
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 20

    Organism-specific databases

    RGDi3426. Psmb8.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome core complex Source: UniProtKB
    4. spermatoproteasome complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 7272Removed in mature formBy similarityPRO_0000026601Add
    BLAST
    Chaini73 – 276204Proteasome subunit beta type-8PRO_0000026602Add
    BLAST

    Post-translational modificationi

    Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity By similarity.By similarity

    Keywords - PTMi

    Zymogen

    Proteomic databases

    PaxDbiP28064.
    PRIDEiP28064.

    Expressioni

    Inductioni

    Up-regulated by interferon gamma (at protein level). Down-regulated by theophylline (THP), a reprotoxic agent thought to induce infertility.1 Publication

    Gene expression databases

    GenevestigatoriP28064.

    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. Component of the immunoproteasome, where it displaces the equivalent housekeeping subunit PSMB5. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP By similarity. Interacts with TAP1 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000000528.

    Structurei

    3D structure databases

    ProteinModelPortaliP28064.
    SMRiP28064. Positions 73-271.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00510000046395.
    HOGENOMiHOG000091082.
    HOVERGENiHBG108297.
    InParanoidiP28064.
    KOiK02740.
    OMAiSDLMHQY.
    OrthoDBiEOG7FNC86.
    PhylomeDBiP28064.
    TreeFamiTF106223.

    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.

    P28064-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALLDLCGAP RGQRPEWAAV DAGSGLRSDP GHYSFSVQAP ELALPRGMQP    50
    TEFLRSFGDD QERKVQIEMA HGTTTLAFKF QHGVIVAVDS RASAGSYIAT 100
    IRVNKVIEIN PYLLGTMSGC AADCQYWERL LAKECRLYYL RNGERISVSA 150
    ASKLLSNMML QYRGMGLSMG SMICGWDKKG PGLYYVDDNG TRLSGQMFST 200
    GSGNTYAYGV MDSGYRQDLS PEEAYDLARR AIVYATHRDS YSGGVVNMYH 250
    MKKDGWVKVE STDVSDLLHK YREATL 276
    Length:276
    Mass (Da):30,570
    Last modified:December 20, 2005 - v3
    Checksum:i0955C80D2F969A97
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61L → S(PubMed:1451788)Curated
    Sequence conflicti16 – 249EWAAVDAGS → SGLAVDAE(PubMed:1451788)Curated
    Sequence conflicti54 – 541L → S(PubMed:1451788)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX883043 Genomic DNA. Translation: CAE83942.1.
    D10729 mRNA. Translation: BAA01572.1.
    PIRiS21126.
    RefSeqiNP_542945.2. NM_080767.2.
    UniGeneiRn.203098.

    Genome annotation databases

    EnsembliENSRNOT00000000528; ENSRNOP00000000528; ENSRNOG00000000456.
    GeneIDi24968.
    KEGGirno:24968.
    UCSCiRGD:3426. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX883043 Genomic DNA. Translation: CAE83942.1 .
    D10729 mRNA. Translation: BAA01572.1 .
    PIRi S21126.
    RefSeqi NP_542945.2. NM_080767.2.
    UniGenei Rn.203098.

    3D structure databases

    ProteinModelPortali P28064.
    SMRi P28064. Positions 73-271.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000000528.

    Protein family/group databases

    MEROPSi T01.015.

    Proteomic databases

    PaxDbi P28064.
    PRIDEi P28064.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000000528 ; ENSRNOP00000000528 ; ENSRNOG00000000456 .
    GeneIDi 24968.
    KEGGi rno:24968.
    UCSCi RGD:3426. rat.

    Organism-specific databases

    CTDi 5696.
    RGDi 3426. Psmb8.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00510000046395.
    HOGENOMi HOG000091082.
    HOVERGENi HBG108297.
    InParanoidi P28064.
    KOi K02740.
    OMAi SDLMHQY.
    OrthoDBi EOG7FNC86.
    PhylomeDBi P28064.
    TreeFami TF106223.

    Enzyme and pathway databases

    Reactomei REACT_194781. Separation of Sister Chromatids.
    REACT_196424. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_198391. Asymmetric localization of PCP proteins.
    REACT_199194. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_199197. ER-Phagosome pathway.
    REACT_199247. Activation of NF-kappaB in B cells.
    REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_204983. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_206488. degradation of DVL.
    REACT_206997. CDT1 association with the CDC6:ORC:origin complex.
    REACT_211117. Orc1 removal from chromatin.
    REACT_212486. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_220232. Regulation of ornithine decarboxylase (ODC).
    REACT_227706. degradation of AXIN.

    Miscellaneous databases

    NextBioi 605008.
    PROi P28064.

    Gene expression databases

    Genevestigatori P28064.

    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. "The genomic sequence and comparative analysis of the rat major histocompatibility complex."
      Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.
      Genome Res. 14:631-639(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "cDNA cloning of rat proteasome subunit RC1, a homologue of RING10 located in the human MHC class II region."
      Aki M., Tamura T., Fuminori T., Iwanaga S., Kawamura Y., Shimbara N., Kagawa S., Tanaka K., Ichihara A.
      FEBS Lett. 301:65-68(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-276.
    3. "Differential expression of genes encoding constitutive and inducible 20S proteasomal core subunits in the testis and epididymis of theophylline- or 1,3-dinitrobenzene-exposed rats."
      Tengowski M.W., Feng D., Sutovsky M., Sutovsky P.
      Biol. Reprod. 76:149-163(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY THP AND DNB.

    Entry informationi

    Entry nameiPSB8_RAT
    AccessioniPrimary (citable) accession number: P28064
    Secondary accession number(s): Q6MGA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Encoded in the MHC class II region.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3