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Q2TBX6

- PSB1_BOVIN

UniProt

Q2TBX6 - PSB1_BOVIN

Protein

Proteasome subunit beta type-1

Gene

PSMB1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (24 Jan 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 By similarity.By similarity

    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

    Protein family/group databases

    MEROPSiT01.986.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-1 (EC:3.4.25.1)
    Gene namesi
    Name:PSMB1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 2828By similarityPRO_0000259622Add
    BLAST
    Chaini29 – 241213Proteasome subunit beta type-1PRO_0000239853Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Glycosylationi58 – 581O-linked (GlcNAc)By similarity
    Modified residuei150 – 1501PhosphotyrosineBy similarity
    Modified residuei204 – 2041N6-acetyllysineBy similarity
    Glycosylationi209 – 2091O-linked (GlcNAc)By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ2TBX6.
    PRIDEiQ2TBX6.

    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.

    Protein-protein interaction databases

    IntActiQ2TBX6. 1 interaction.
    STRINGi9913.ENSBTAP00000010108.

    Structurei

    Secondary structure

    1
    241
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 457
    Beta strandi48 – 547
    Beta strandi57 – 593
    Beta strandi62 – 665
    Beta strandi71 – 755
    Beta strandi78 – 847
    Helixi86 – 10722
    Helixi113 – 12513
    Turni126 – 1294
    Beta strandi134 – 1418
    Beta strandi147 – 1526
    Beta strandi158 – 16710
    Helixi170 – 18011
    Helixi196 – 21318
    Beta strandi219 – 2279
    Beta strandi230 – 2378

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IRUX-ray2.751/M29-241[»]
    ProteinModelPortaliQ2TBX6.
    SMRiQ2TBX6. Positions 29-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ2TBX6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091081.
    HOVERGENiHBG000961.
    InParanoidiQ2TBX6.
    KOiK02732.

    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.

    Q2TBX6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSSVAAYSG AGRDLAMEPH SSVGPLQLRF SPYAFNGGTV LAIAGEDFSI    50
    VASDTRLSEG FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL 100
    KMYKHSNNKA MTTGAIAAML STILYSRRFF PYYVYNIIGG LDEEGKGAVY 150
    SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ VGFKNMQNVE HVPLSLDRAM 200
    RLVKDVFISA AERDVYTGDA LKVCIVTKEG IRGETVPLRK D 241
    Length:241
    Mass (Da):26,246
    Last modified:January 24, 2006 - v1
    Checksum:i8682655C19CF2ACD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC109494 mRNA. Translation: AAI09495.1.
    RefSeqiNP_001033628.1. NM_001038539.2.
    UniGeneiBt.7040.

    Genome annotation databases

    GeneIDi514237.
    KEGGibta:514237.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC109494 mRNA. Translation: AAI09495.1 .
    RefSeqi NP_001033628.1. NM_001038539.2.
    UniGenei Bt.7040.

    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 1/M 29-241 [» ]
    ProteinModelPortali Q2TBX6.
    SMRi Q2TBX6. Positions 29-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q2TBX6. 1 interaction.
    STRINGi 9913.ENSBTAP00000010108.

    Protein family/group databases

    MEROPSi T01.986.

    Proteomic databases

    PaxDbi Q2TBX6.
    PRIDEi Q2TBX6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 514237.
    KEGGi bta:514237.

    Organism-specific databases

    CTDi 5689.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091081.
    HOVERGENi HBG000961.
    InParanoidi Q2TBX6.
    KOi K02732.

    Miscellaneous databases

    EvolutionaryTracei Q2TBX6.
    NextBioi 20871244.

    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 (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Liver.
    2. "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 29-241 OF COMPLEX WITH 20S PROTEASOME.

    Entry informationi

    Entry nameiPSB1_BOVIN
    AccessioniPrimary (citable) accession number: Q2TBX6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 67 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, 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