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P33672

- PSB3_BOVIN

UniProt

P33672 - PSB3_BOVIN

Protein

Proteasome subunit beta type-3

Gene

PSMB3

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (13 Jun 2006)
      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.

    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_203965. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_205339. APC/C:Cdc20 mediated degradation of Securin.
    REACT_205897. Activation of NF-kappaB in B cells.
    REACT_206368. CDT1 association with the CDC6:ORC:origin complex.
    REACT_207857. Asymmetric localization of PCP proteins.
    REACT_208116. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_208851. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_208889. degradation of AXIN.
    REACT_211738. ER-Phagosome pathway.
    REACT_212887. Separation of Sister Chromatids.
    REACT_213030. Orc1 removal from chromatin.
    REACT_215163. degradation of DVL.
    REACT_217860. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_218058. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_222557. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_222622. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_223494. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_224434. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_225648. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_226120. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.

    Protein family/group databases

    MEROPSiT01.983.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-3 (EC:3.4.25.1)
    Alternative name(s):
    Proteasome chain 13
    Proteasome component C10-II
    Proteasome theta chain
    Gene namesi
    Name:PSMB3
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 19

    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
    Chaini2 – 205204Proteasome subunit beta type-3PRO_0000148056Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei77 – 771N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP33672.
    PRIDEiP33672.

    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.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 156
    Beta strandi17 – 259
    Beta strandi28 – 303
    Beta strandi33 – 375
    Beta strandi42 – 443
    Beta strandi49 – 524
    Helixi57 – 7721
    Beta strandi78 – 803
    Helixi84 – 9613
    Turni97 – 1004
    Beta strandi108 – 1125
    Beta strandi119 – 1246
    Beta strandi130 – 1323
    Beta strandi134 – 1407
    Helixi143 – 15311
    Helixi160 – 17415
    Helixi175 – 1773
    Beta strandi185 – 20016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IRUX-ray2.75J/X1-205[»]
    ProteinModelPortaliP33672.
    SMRiP33672. Positions 2-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33672.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074820.
    HOGENOMiHOG000090523.
    HOVERGENiHBG004446.
    InParanoidiP33672.
    KOiK02735.
    OMAiMDLIGCP.
    OrthoDBiEOG783MWB.
    TreeFamiTF106216.

    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.

    P33672-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY    50
    IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF 100
    GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCTEQMYGMC 150
    ESLWEPNMDP EHLFETISQA MLNAVDRDAV SGMGVIVHII EKDKITTRTL 200
    KARMD 205
    Length:205
    Mass (Da):22,993
    Last modified:June 13, 2006 - v3
    Checksum:i62551E484D5042FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891S → C AA sequence (PubMed:1510924)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102554 mRNA. Translation: AAI02555.1.
    PIRiA42762.
    B42762.
    C42762.
    D42762.
    G42762.
    RefSeqiNP_001029768.1. NM_001034596.2.
    UniGeneiBt.44351.

    Genome annotation databases

    EnsembliENSBTAT00000004984; ENSBTAP00000004984; ENSBTAG00000003830.
    GeneIDi533874.
    KEGGibta:533874.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102554 mRNA. Translation: AAI02555.1 .
    PIRi A42762.
    B42762.
    C42762.
    D42762.
    G42762.
    RefSeqi NP_001029768.1. NM_001034596.2.
    UniGenei Bt.44351.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IRU X-ray 2.75 J/X 1-205 [» ]
    ProteinModelPortali P33672.
    SMRi P33672. Positions 2-205.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi T01.983.

    Proteomic databases

    PaxDbi P33672.
    PRIDEi P33672.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000004984 ; ENSBTAP00000004984 ; ENSBTAG00000003830 .
    GeneIDi 533874.
    KEGGi bta:533874.

    Organism-specific databases

    CTDi 5691.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074820.
    HOGENOMi HOG000090523.
    HOVERGENi HBG004446.
    InParanoidi P33672.
    KOi K02735.
    OMAi MDLIGCP.
    OrthoDBi EOG783MWB.
    TreeFami TF106216.

    Enzyme and pathway databases

    Reactomei REACT_203965. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_205339. APC/C:Cdc20 mediated degradation of Securin.
    REACT_205897. Activation of NF-kappaB in B cells.
    REACT_206368. CDT1 association with the CDC6:ORC:origin complex.
    REACT_207857. Asymmetric localization of PCP proteins.
    REACT_208116. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_208851. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_208889. degradation of AXIN.
    REACT_211738. ER-Phagosome pathway.
    REACT_212887. Separation of Sister Chromatids.
    REACT_213030. Orc1 removal from chromatin.
    REACT_215163. degradation of DVL.
    REACT_217860. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_218058. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_222557. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_222622. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_223494. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_224434. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_225648. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_226120. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.

    Miscellaneous databases

    EvolutionaryTracei P33672.
    NextBioi 20876178.

    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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Testis.
    2. "Identification and localization of a cysteinyl residue critical for the trypsin-like catalytic activity of the proteasome."
      Dick L.R., Moomaw C.R., Pramanik B.C., DeMartino G.N., Slaughter C.A.
      Biochemistry 31:7347-7355(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 14-79; 89-114; 121-141; 160-170 AND 183-205.
    3. "The structure of the mammalian 20S proteasome at 2.75 A resolution."
      Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., Tsukihara T.
      Structure 10:609-618(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH 20S PROTEASOME.

    Entry informationi

    Entry nameiPSB3_BOVIN
    AccessioniPrimary (citable) accession number: P33672
    Secondary accession number(s): Q3T059
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 121 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3