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P49720

- PSB3_HUMAN

UniProt

P49720 - PSB3_HUMAN

Protein

Proteasome subunit beta type-3

Gene

PSMB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (10 May 2002)
      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. protein binding Source: IntAct
    2. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    5. apoptotic process Source: Reactome
    6. cellular nitrogen compound metabolic process Source: Reactome
    7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    8. G1/S transition of mitotic cell cycle Source: Reactome
    9. gene expression Source: Reactome
    10. mitotic cell cycle Source: Reactome
    11. mRNA metabolic process Source: Reactome
    12. negative regulation of apoptotic process Source: Reactome
    13. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    14. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    15. protein polyubiquitination Source: Reactome
    16. regulation of apoptotic process Source: Reactome
    17. regulation of cellular amino acid metabolic process Source: Reactome
    18. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    19. RNA metabolic process Source: Reactome
    20. small molecule metabolic process Source: Reactome
    21. viral process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9540. PSMB3.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. Golgi apparatus Source: HPA
    6. mitochondrion Source: HPA
    7. nucleoplasm Source: Reactome
    8. nucleus Source: UniProt
    9. proteasome complex Source: ProtInc
    10. proteasome core complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33885.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 205204Proteasome subunit beta type-3PRO_0000148057Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei77 – 771N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP49720.
    PaxDbiP49720.
    PeptideAtlasiP49720.
    PRIDEiP49720.

    2D gel databases

    OGPiP49720.
    REPRODUCTION-2DPAGEIPI00028004.

    PTM databases

    PhosphoSiteiP49720.

    Expressioni

    Inductioni

    Up-regulated in asthenozoospermic sperm.1 Publication

    Gene expression databases

    ArrayExpressiP49720.
    BgeeiP49720.
    CleanExiHS_PSMB3.
    GenevestigatoriP49720.

    Organism-specific databases

    HPAiHPA042775.
    HPA048147.

    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. Interacts with HIV-1 TAT protein.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PSMB2P497214EBI-603340,EBI-359335

    Protein-protein interaction databases

    BioGridi111664. 70 interactions.
    IntActiP49720. 21 interactions.
    MINTiMINT-5001041.
    STRINGi9606.ENSP00000225426.

    Structurei

    3D structure databases

    ProteinModelPortaliP49720.
    SMRiP49720. Positions 2-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000090523.
    HOVERGENiHBG004446.
    InParanoidiP49720.
    KOiK02735.
    OMAiMDLIGCP.
    OrthoDBiEOG783MWB.
    PhylomeDBiP49720.
    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.

    P49720-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY    50
    IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF 100
    GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCAEQMYGMC 150
    ESLWEPNMDP DHLFETISQA MLNAVDRDAV SGMGVIVHII EKDKITTRTL 200
    KARMD 205
    Length:205
    Mass (Da):22,949
    Last modified:May 10, 2002 - v2
    Checksum:i624972384C0112FD
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti34 – 341M → L.1 Publication
    Corresponds to variant rs4907 [ dbSNP | Ensembl ].
    VAR_034415

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26598 mRNA. Translation: BAA05645.1.
    BC013008 mRNA. Translation: AAH13008.1.
    CCDSiCCDS11328.1.
    PIRiS55041.
    RefSeqiNP_002786.2. NM_002795.3.
    UniGeneiHs.82793.

    Genome annotation databases

    GeneIDi5691.
    KEGGihsa:5691.
    UCSCiuc002hqr.3. human.

    Polymorphism databases

    DMDMi20532411.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26598 mRNA. Translation: BAA05645.1 .
    BC013008 mRNA. Translation: AAH13008.1 .
    CCDSi CCDS11328.1.
    PIRi S55041.
    RefSeqi NP_002786.2. NM_002795.3.
    UniGenei Hs.82793.

    3D structure databases

    ProteinModelPortali P49720.
    SMRi P49720. Positions 2-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111664. 70 interactions.
    IntActi P49720. 21 interactions.
    MINTi MINT-5001041.
    STRINGi 9606.ENSP00000225426.

    Chemistry

    ChEMBLi CHEMBL2364701.

    Protein family/group databases

    MEROPSi T01.983.

    PTM databases

    PhosphoSitei P49720.

    Polymorphism databases

    DMDMi 20532411.

    2D gel databases

    OGPi P49720.
    REPRODUCTION-2DPAGE IPI00028004.

    Proteomic databases

    MaxQBi P49720.
    PaxDbi P49720.
    PeptideAtlasi P49720.
    PRIDEi P49720.

    Protocols and materials databases

    DNASUi 5691.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5691.
    KEGGi hsa:5691.
    UCSCi uc002hqr.3. human.

    Organism-specific databases

    CTDi 5691.
    GeneCardsi GC17P036909.
    H-InvDB HIX0030292.
    HGNCi HGNC:9540. PSMB3.
    HPAi HPA042775.
    HPA048147.
    MIMi 602176. gene.
    neXtProti NX_P49720.
    PharmGKBi PA33885.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000090523.
    HOVERGENi HBG004446.
    InParanoidi P49720.
    KOi K02735.
    OMAi MDLIGCP.
    OrthoDBi EOG783MWB.
    PhylomeDBi P49720.
    TreeFami TF106216.

    Enzyme and pathway databases

    Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Miscellaneous databases

    ChiTaRSi PSMB3. human.
    GeneWikii PSMB3.
    GenomeRNAii 5691.
    NextBioi 22106.
    PROi P49720.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49720.
    Bgeei P49720.
    CleanExi HS_PSMB3.
    Genevestigatori P49720.

    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. "Sequence analyses and inter-species comparisons of three novel human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential proteolytic active-site residues."
      Nothwang H.G., Tamura T., Tanaka K., Ichihara A.
      Biochim. Biophys. Acta 1219:361-368(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-34.
    2. "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: Muscle.
    3. Bienvenut W.V., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15; 28-41; 49-66; 71-77; 100-115 AND 178-192, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    4. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 29-42; 50-67 AND 101-116, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    5. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 49-66 AND 99-111.
      Tissue: Keratinocyte.
    6. "Human proteasome subunits from 2-dimensional gels identified by partial sequencing."
      Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.
      Biochem. Biophys. Res. Commun. 205:1785-1789(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 100-115.
      Tissue: Placenta.
    7. "Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
      Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
      FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    8. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
      Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
      Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "Identification of proteomic differences in asthenozoospermic sperm samples."
      Martinez-Heredia J., de Mateo S., Vidal-Taboada J.M., Ballesca J.L., Oliva R.
      Hum. Reprod. 23:783-791(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPSB3_HUMAN
    AccessioniPrimary (citable) accession number: P49720
    Secondary accession number(s): P31147, Q0P6J7, Q96E27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 10, 2002
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3