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P28073

- PSB6_RAT

UniProt

P28073 - PSB6_RAT

Protein

Proteasome subunit beta type-6

Gene

Psmb6

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (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.

    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_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

    MEROPSiT01.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-6 (EC:3.4.25.1)
    Alternative name(s):
    Macropain delta chain
    Multicatalytic endopeptidase complex delta chain
    Proteasome chain 5
    Proteasome delta chain
    Proteasome subunit Y
    Gene namesi
    Name:Psmb6
    Synonyms:Psmb6l
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi61881. Psmb6.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    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 form1 PublicationPRO_0000026617Add
    BLAST
    Chaini34 – 238205Proteasome subunit beta type-6PRO_0000026618Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation, Zymogen

    Proteomic databases

    PaxDbiP28073.
    PRIDEiP28073.

    2D gel databases

    World-2DPAGE0004:P28073.

    Expressioni

    Gene expression databases

    GenevestigatoriP28073.

    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.

    Protein-protein interaction databases

    BioGridi248287. 1 interaction.
    IntActiP28073. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP28073.
    SMRiP28073. Positions 34-235.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00510000046484.
    HOGENOMiHOG000091079.
    HOVERGENiHBG000123.
    InParanoidiP28073.
    KOiK02738.
    OMAiCIRMCVI.
    OrthoDBiEOG79GT80.
    PhylomeDBiP28073.
    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.

    P28073-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAALAVRGA VSAPAFGPEA LTPDWENREV STGTTIMAVQ FDGGVVLGAD    50
    SRTTTGSYIA NRVTDKLTPI HDHIFCCRSG SAADTQAVAD AVTYQLGFHS 100
    IELNEPPLVH TAASLFKEMC YRYREDLMAG IIIAGWDPQE GGQVYSVPMG 150
    GMMVRQSFAI GGSGSSYIYG YVDATYREGM TKDECLQFTA NALALAMERD 200
    GSSGGVIRLA AIQQSGVERQ VLLGDQIPKV TISTLPPP 238
    Length:238
    Mass (Da):25,290
    Last modified:December 20, 2005 - v3
    Checksum:i4B051AF11D78E49B
    GO

    Sequence cautioni

    The sequence BAA01586.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC058451 mRNA. Translation: AAH58451.1.
    AABR03076595 Genomic DNA. No translation available.
    D10754 mRNA. Translation: BAA01586.1. Different initiation.
    BN000325 mRNA. Translation: CAE48380.1.
    PIRiJX0228.
    S09086.
    RefSeqiNP_476440.2. NM_057099.3.
    UniGeneiRn.8118.

    Genome annotation databases

    EnsembliENSRNOT00000015746; ENSRNOP00000015747; ENSRNOG00000011827.
    ENSRNOT00000026507; ENSRNOP00000026507; ENSRNOG00000019551.
    GeneIDi29666.
    KEGGirno:29666.
    UCSCiRGD:61881. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC058451 mRNA. Translation: AAH58451.1 .
    AABR03076595 Genomic DNA. No translation available.
    D10754 mRNA. Translation: BAA01586.1 . Different initiation.
    BN000325 mRNA. Translation: CAE48380.1 .
    PIRi JX0228.
    S09086.
    RefSeqi NP_476440.2. NM_057099.3.
    UniGenei Rn.8118.

    3D structure databases

    ProteinModelPortali P28073.
    SMRi P28073. Positions 34-235.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248287. 1 interaction.
    IntActi P28073. 1 interaction.

    Protein family/group databases

    MEROPSi T01.010.

    2D gel databases

    World-2DPAGE 0004:P28073.

    Proteomic databases

    PaxDbi P28073.
    PRIDEi P28073.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000015746 ; ENSRNOP00000015747 ; ENSRNOG00000011827 .
    ENSRNOT00000026507 ; ENSRNOP00000026507 ; ENSRNOG00000019551 .
    GeneIDi 29666.
    KEGGi rno:29666.
    UCSCi RGD:61881. rat.

    Organism-specific databases

    CTDi 5694.
    RGDi 61881. Psmb6.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00510000046484.
    HOGENOMi HOG000091079.
    HOVERGENi HBG000123.
    InParanoidi P28073.
    KOi K02738.
    OMAi CIRMCVI.
    OrthoDBi EOG79GT80.
    PhylomeDBi P28073.
    TreeFami TF106221.

    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 609975.

    Gene expression databases

    Genevestigatori P28073.

    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 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].
      Tissue: Pituitary.
    2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    3. "Molecular cloning of cDNAs for rat proteasomes: deduced primary structures of four other subunits."
      Tamura T., Shimbara N., Aki M., Ishida N., Bey F., Scherrer K., Tanaka K., Ichihara A.
      J. Biochem. 112:530-534(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-238.
    4. "N-terminal sequence similarities between components of the multicatalytic proteinase complex."
      Lilley K.S., Davison M.D., Rivett A.J.
      FEBS Lett. 262:327-329(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-51.
    5. Lubec G., Diao W.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 67-78 AND 209-229, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus.
    6. "A genomic analysis of rat proteases and protease inhibitors."
      Puente X.S., Lopez-Otin C.
      Genome Res. 14:609-622(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiPSB6_RAT
    AccessioniPrimary (citable) accession number: P28073
    Secondary accession number(s): Q6IE68, Q6PDW5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 128 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

    Complete proteome, Direct protein sequencing, 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