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P28070

- PSB4_HUMAN

UniProt

P28070 - PSB4_HUMAN

Protein

Proteasome subunit beta type-4

Gene

PSMB4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 4 (17 Oct 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. Mediates the lipopolysaccharide-induced signal macrophage proteasome By similarity. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1.By similarity1 Publication

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei46 – 461NucleophileBy similarity

    GO - Molecular functioni

    1. lipopolysaccharide binding Source: Ensembl
    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 inflammatory response to antigenic stimulus Source: Ensembl
    14. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    15. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    16. protein polyubiquitination Source: Reactome
    17. regulation of apoptotic process Source: Reactome
    18. regulation of cellular amino acid metabolic process Source: Reactome
    19. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    20. RNA metabolic process Source: Reactome
    21. small molecule metabolic process Source: Reactome
    22. 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

    MEROPSiT01.987.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-4 (EC:3.4.25.1)
    Alternative name(s):
    26 kDa prosomal protein
    Short name:
    HsBPROS26
    Short name:
    PROS-26
    Macropain beta chain
    Multicatalytic endopeptidase complex beta chain
    Proteasome beta chain
    Proteasome chain 3
    Short name:
    HsN3
    Gene namesi
    Name:PSMB4
    Synonyms:PROS26
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9541. PSMB4.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. proteasome complex Source: ProtInc
    6. proteasome core complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33886.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 45452 PublicationsPRO_0000026579Add
    BLAST
    Chaini46 – 264219Proteasome subunit beta type-4PRO_0000026580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei102 – 1021Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Zymogen

    Proteomic databases

    MaxQBiP28070.
    PaxDbiP28070.
    PeptideAtlasiP28070.
    PRIDEiP28070.

    2D gel databases

    DOSAC-COBS-2DPAGEP28070.
    OGPiP28070.
    REPRODUCTION-2DPAGEIPI00555956.
    SWISS-2DPAGEP28070.

    PTM databases

    PhosphoSiteiP28070.

    Expressioni

    Inductioni

    Up-regulated in fibrolamellar carcinomas.1 Publication

    Gene expression databases

    BgeeiP28070.
    CleanExiHS_PSMB4.
    GenevestigatoriP28070.

    Organism-specific databases

    HPAiHPA006700.

    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 and HIV-1 NEF proteins. Interaction with HTLV-1 TAX protein favors NFKB1 activation. Interacts with bacterial lipopolysaccharide (LPS) By similarity. Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome. Interacts with PRPF19.By similarity6 Publications

    Protein-protein interaction databases

    BioGridi111665. 71 interactions.
    IntActiP28070. 18 interactions.
    MINTiMINT-1192686.
    STRINGi9606.ENSP00000290541.

    Structurei

    3D structure databases

    ProteinModelPortaliP28070.
    SMRiP28070. Positions 46-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000181719.
    HOVERGENiHBG018194.
    InParanoidiP28070.
    KOiK02736.
    OMAiRIMRVND.
    OrthoDBiEOG74FF1D.
    PhylomeDBiP28070.
    TreeFamiTF106220.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR016295. Proteasome_endopept_cplx_B.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
    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.

    P28070-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAFLGSRSG LWAGGPAPGQ FYRIPSTPDS FMDPASALYR GPITRTQNPM    50
    VTGTSVLGVK FEGGVVIAAD MLGSYGSLAR FRNISRIMRV NNSTMLGASG 100
    DYADFQYLKQ VLGQMVIDEE LLGDGHSYSP RAIHSWLTRA MYSRRSKMNP 150
    LWNTMVIGGY ADGESFLGYV DMLGVAYEAP SLATGYGAYL AQPLLREVLE 200
    KQPVLSQTEA RDLVERCMRV LYYRDARSYN RFQIATVTEK GVEIEGPLST 250
    ETNWDIAHMI SGFE 264
    Length:264
    Mass (Da):29,204
    Last modified:October 17, 2006 - v4
    Checksum:iB8701C565069F563
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti264 – 2641E → D in CAG33101. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti95 – 951M → I.
    Corresponds to variant rs1804241 [ dbSNP | Ensembl ].
    VAR_012072
    Natural varianti234 – 2341I → T.5 Publications
    Corresponds to variant rs4603 [ dbSNP | Ensembl ].
    VAR_013115

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26600 mRNA. Translation: BAA05647.1.
    AK313825 mRNA. Translation: BAG36560.1.
    CR456820 mRNA. Translation: CAG33101.1.
    BT006917 mRNA. Translation: AAP35563.1.
    AL589764 Genomic DNA. Translation: CAI16806.1.
    CH471121 Genomic DNA. Translation: EAW53442.1.
    S71381 mRNA. Translation: AAB31085.1.
    CCDSiCCDS996.1.
    PIRiS08186.
    S45719.
    S50147.
    RefSeqiNP_002787.2. NM_002796.2.
    UniGeneiHs.89545.

    Genome annotation databases

    EnsembliENST00000290541; ENSP00000290541; ENSG00000159377.
    GeneIDi5692.
    KEGGihsa:5692.
    UCSCiuc001eyc.1. human.

    Polymorphism databases

    DMDMi116242733.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26600 mRNA. Translation: BAA05647.1 .
    AK313825 mRNA. Translation: BAG36560.1 .
    CR456820 mRNA. Translation: CAG33101.1 .
    BT006917 mRNA. Translation: AAP35563.1 .
    AL589764 Genomic DNA. Translation: CAI16806.1 .
    CH471121 Genomic DNA. Translation: EAW53442.1 .
    S71381 mRNA. Translation: AAB31085.1 .
    CCDSi CCDS996.1.
    PIRi S08186.
    S45719.
    S50147.
    RefSeqi NP_002787.2. NM_002796.2.
    UniGenei Hs.89545.

    3D structure databases

    ProteinModelPortali P28070.
    SMRi P28070. Positions 46-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111665. 71 interactions.
    IntActi P28070. 18 interactions.
    MINTi MINT-1192686.
    STRINGi 9606.ENSP00000290541.

    Chemistry

    ChEMBLi CHEMBL2364701.

    Protein family/group databases

    MEROPSi T01.987.

    PTM databases

    PhosphoSitei P28070.

    Polymorphism databases

    DMDMi 116242733.

    2D gel databases

    DOSAC-COBS-2DPAGE P28070.
    OGPi P28070.
    REPRODUCTION-2DPAGE IPI00555956.
    SWISS-2DPAGE P28070.

    Proteomic databases

    MaxQBi P28070.
    PaxDbi P28070.
    PeptideAtlasi P28070.
    PRIDEi P28070.

    Protocols and materials databases

    DNASUi 5692.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290541 ; ENSP00000290541 ; ENSG00000159377 .
    GeneIDi 5692.
    KEGGi hsa:5692.
    UCSCi uc001eyc.1. human.

    Organism-specific databases

    CTDi 5692.
    GeneCardsi GC01P151372.
    HGNCi HGNC:9541. PSMB4.
    HPAi HPA006700.
    MIMi 602177. gene.
    neXtProti NX_P28070.
    PharmGKBi PA33886.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000181719.
    HOVERGENi HBG018194.
    InParanoidi P28070.
    KOi K02736.
    OMAi RIMRVND.
    OrthoDBi EOG74FF1D.
    PhylomeDBi P28070.
    TreeFami TF106220.

    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 PSMB4. human.
    GeneWikii PSMB4.
    GenomeRNAii 5692.
    NextBioi 22110.
    PROi P28070.
    SOURCEi Search...

    Gene expression databases

    Bgeei P28070.
    CleanExi HS_PSMB4.
    Genevestigatori P28070.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR016295. Proteasome_endopept_cplx_B.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001213. Psome_endopept_beta. 1 hit.
    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 THR-234.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-234.
      Tissue: Brain.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-234.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-234.
    7. "Cloning and expression of a human pro(tea)some beta-subunit cDNA: a homologue of the yeast PRE4-subunit essential for peptidylglutamyl-peptide hydrolase activity."
      Gerards W.L., Hop F.W., Hendriks I.L., Bloemendal H.
      FEBS Lett. 346:151-155(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-264, VARIANT THR-234.
    8. "Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)."
      Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A.
      Biochim. Biophys. Acta 1037:178-185(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 46-73.
    9. Cited for: PROTEIN SEQUENCE OF 46-57.
      Tissue: Liver.
    10. "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 132-139; 220-224 AND 241-259.
    11. "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 232-237 AND 241-253.
      Tissue: Keratinocyte.
    12. "Effects on NF-kappa B1/p105 processing of the interaction between the HTLV-1 transactivator Tax and the proteasome."
      Rousset R., Desbois C., Bantignies F., Jalinot P.
      Nature 381:328-331(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 TAX.
    13. "HsN3 proteasomal subunit as a target for human immunodeficiency virus type 1 Nef protein."
      Rossi F., Evstafieva A., Pedrali-Noy G., Gallina A., Milanesi G.
      Virology 237:33-45(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 NEF.
    14. "Proteasomal degradation of Smad1 induced by bone morphogenetic proteins."
      Gruendler C., Lin Y., Farley J., Wang T.
      J. Biol. Chem. 276:46533-46543(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH SMAD1 AND OAZ1.
    15. "A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs)."
      Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y., Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T.
      BMC Cell Biol. 3:15-15(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH SMAD1 AND OAZ1, FUNCTION.
    16. "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.
    17. "Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome."
      Loescher M., Fortschegger K., Ritter G., Wostry M., Voglauer R., Schmid J.A., Watters S., Rivett A.J., Ajuh P., Lamond A.I., Katinger H., Grillari J.
      Biochem. J. 388:593-603(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRPF19.
    18. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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.
    20. "Fibrolamellar carcinomas show overexpression of genes in the RAS, MAPK, PIK3, and xenobiotic degradation pathways."
      Kannangai R., Vivekanandan P., Martinez-Murillo F., Choti M., Torbenson M.
      Hum. Pathol. 38:639-644(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    21. Cited for: IDENTIFICATION.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPSB4_HUMAN
    AccessioniPrimary (citable) accession number: P28070
    Secondary accession number(s): B2R9L3
    , P31148, Q5SZS5, Q6IBI4, Q969L6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 166 of the entry and version 4 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

    Caution

    A report observed N-glycosylation at Asn-83 (PubMed:19139490). However, as the protein does not localize in an extracellular compartment of the cell, additional evidences are required to confirm this result.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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