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P43686

- PRS6B_HUMAN

UniProt

P43686 - PRS6B_HUMAN

Protein

26S protease regulatory subunit 6B

Gene

PSMC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (10 May 2002)
      Previous versions | rss
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    Functioni

    The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi206 – 2138ATPSequence Analysis

    GO - Molecular functioni

    1. ATPase activity Source: ProtInc
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    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. ATP catabolic process Source: GOC
    7. blastocyst development Source: Ensembl
    8. cellular nitrogen compound metabolic process Source: Reactome
    9. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    10. G1/S transition of mitotic cell cycle Source: Reactome
    11. gene expression Source: Reactome
    12. mitotic cell cycle Source: Reactome
    13. mRNA metabolic process Source: Reactome
    14. negative regulation of apoptotic process Source: Reactome
    15. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    16. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    17. protein polyubiquitination Source: Reactome
    18. proteolysis Source: ProtInc
    19. regulation of apoptotic process Source: Reactome
    20. regulation of cellular amino acid metabolic process Source: Reactome
    21. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    22. RNA metabolic process Source: Reactome
    23. small molecule metabolic process Source: Reactome
    24. viral process Source: Reactome

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    26S protease regulatory subunit 6B
    Alternative name(s):
    26S proteasome AAA-ATPase subunit RPT3
    MB67-interacting protein
    MIP224
    Proteasome 26S subunit ATPase 4
    Tat-binding protein 7
    Short name:
    TBP-7
    Gene namesi
    Name:PSMC4
    Synonyms:MIP224, TBP7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9551. PSMC4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. cytosolic proteasome complex Source: Ensembl
    4. inclusion body Source: Ensembl
    5. membrane Source: UniProtKB
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProt
    8. proteasome accessory complex Source: UniProtKB
    9. proteasome complex Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33896.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 41841826S protease regulatory subunit 6BPRO_0000084686Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei21 – 211Phosphoserine1 Publication
    Modified residuei28 – 281Phosphoserine5 Publications
    Modified residuei397 – 3971N6-acetyllysine1 Publication
    Modified residuei401 – 4011N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP43686.
    PaxDbiP43686.
    PRIDEiP43686.

    2D gel databases

    OGPiP43686.

    PTM databases

    PhosphoSiteiP43686.

    Expressioni

    Gene expression databases

    ArrayExpressiP43686.
    BgeeiP43686.
    CleanExiHS_PSMC4.
    GenevestigatoriP43686.

    Organism-specific databases

    HPAiHPA002044.
    HPA005471.

    Interactioni

    Subunit structurei

    Interacts with NR1I3. Interacts with PAAF1. Interacts with TRIM5.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PSMC5P6219511EBI-743997,EBI-357745
    PSMC6P623333EBI-743997,EBI-357669
    PSMD10O758328EBI-743997,EBI-752185

    Protein-protein interaction databases

    BioGridi111677. 83 interactions.
    DIPiDIP-29274N.
    IntActiP43686. 20 interactions.
    MINTiMINT-5004247.
    STRINGi9606.ENSP00000157812.

    Structurei

    Secondary structure

    1
    418
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi338 – 34811
    Turni349 – 3513
    Helixi361 – 3644
    Helixi372 – 38817
    Beta strandi392 – 3943
    Helixi396 – 40611

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DVWX-ray2.30B337-418[»]
    ProteinModelPortaliP43686.
    SMRiP43686. Positions 41-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43686.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Curated

    Phylogenomic databases

    eggNOGiCOG1222.
    HOGENOMiHOG000225143.
    HOVERGENiHBG000109.
    InParanoidiP43686.
    KOiK03063.
    OMAiLYIKYKK.
    OrthoDBiEOG7F24ST.
    PhylomeDBiP43686.
    TreeFamiTF106227.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR005937. 26S_Psome_P45.
    IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
    PROSITEiPS00674. AAA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P43686-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE    50
    LEFLEVQEEY IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT 100
    AIVGSTTGSN YYVRILSTID RELLKPNASV ALHKHSNALV DVLPPEADSS 150
    IMMLTSDQKP DVMYADIGGM DIQKQEVREA VELPLTHFEL YKQIGIDPPR 200
    GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL GEGPRMVRDV 250
    FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD 300
    QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS 350
    KMNLSEEVDL EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE 400
    KAYKTVIKKD EQEHEFYK 418
    Length:418
    Mass (Da):47,366
    Last modified:May 10, 2002 - v2
    Checksum:i80F9523C61B88F0C
    GO
    Isoform 2 (identifier: P43686-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         46-76: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:387
    Mass (Da):43,508
    Checksum:iFA64D44EE00E9A7B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731L → F in AAC32612. 1 PublicationCurated
    Sequence conflicti110 – 1101N → S in AAC32612. 1 PublicationCurated
    Sequence conflicti118 – 1181T → A no nucleotide entry (PubMed:8419915)Curated
    Sequence conflicti157 – 1571D → G in AAC32612. 1 PublicationCurated
    Sequence conflicti185 – 1851L → V in AAC32612. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei46 – 7631Missing in isoform 2. 1 PublicationVSP_000022Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038965 mRNA. Translation: AAC26843.1.
    U27515 mRNA. Translation: AAC99817.1.
    AF020736 mRNA. Translation: AAC32612.1.
    BT007232 mRNA. Translation: AAP35896.1.
    AC007842 Genomic DNA. Translation: AAD39267.1.
    BC000343 mRNA. Translation: AAH00343.1.
    BC010396 mRNA. Translation: AAH10396.1.
    BC014488 mRNA. Translation: AAH14488.1.
    CCDSiCCDS12547.1. [P43686-1]
    CCDS46076.1. [P43686-2]
    RefSeqiNP_006494.1. NM_006503.3. [P43686-1]
    NP_694546.1. NM_153001.2. [P43686-2]
    UniGeneiHs.211594.

    Genome annotation databases

    EnsembliENST00000157812; ENSP00000157812; ENSG00000013275. [P43686-1]
    ENST00000455878; ENSP00000413869; ENSG00000013275. [P43686-2]
    GeneIDi5704.
    KEGGihsa:5704.
    UCSCiuc002omq.4. human. [P43686-1]
    uc002omr.4. human. [P43686-2]

    Polymorphism databases

    DMDMi20532409.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038965 mRNA. Translation: AAC26843.1 .
    U27515 mRNA. Translation: AAC99817.1 .
    AF020736 mRNA. Translation: AAC32612.1 .
    BT007232 mRNA. Translation: AAP35896.1 .
    AC007842 Genomic DNA. Translation: AAD39267.1 .
    BC000343 mRNA. Translation: AAH00343.1 .
    BC010396 mRNA. Translation: AAH10396.1 .
    BC014488 mRNA. Translation: AAH14488.1 .
    CCDSi CCDS12547.1. [P43686-1 ]
    CCDS46076.1. [P43686-2 ]
    RefSeqi NP_006494.1. NM_006503.3. [P43686-1 ]
    NP_694546.1. NM_153001.2. [P43686-2 ]
    UniGenei Hs.211594.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DVW X-ray 2.30 B 337-418 [» ]
    ProteinModelPortali P43686.
    SMRi P43686. Positions 41-418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111677. 83 interactions.
    DIPi DIP-29274N.
    IntActi P43686. 20 interactions.
    MINTi MINT-5004247.
    STRINGi 9606.ENSP00000157812.

    PTM databases

    PhosphoSitei P43686.

    Polymorphism databases

    DMDMi 20532409.

    2D gel databases

    OGPi P43686.

    Proteomic databases

    MaxQBi P43686.
    PaxDbi P43686.
    PRIDEi P43686.

    Protocols and materials databases

    DNASUi 5704.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000157812 ; ENSP00000157812 ; ENSG00000013275 . [P43686-1 ]
    ENST00000455878 ; ENSP00000413869 ; ENSG00000013275 . [P43686-2 ]
    GeneIDi 5704.
    KEGGi hsa:5704.
    UCSCi uc002omq.4. human. [P43686-1 ]
    uc002omr.4. human. [P43686-2 ]

    Organism-specific databases

    CTDi 5704.
    GeneCardsi GC19P040477.
    HGNCi HGNC:9551. PSMC4.
    HPAi HPA002044.
    HPA005471.
    MIMi 602707. gene.
    neXtProti NX_P43686.
    PharmGKBi PA33896.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1222.
    HOGENOMi HOG000225143.
    HOVERGENi HBG000109.
    InParanoidi P43686.
    KOi K03063.
    OMAi LYIKYKK.
    OrthoDBi EOG7F24ST.
    PhylomeDBi P43686.
    TreeFami TF106227.

    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 PSMC4. human.
    EvolutionaryTracei P43686.
    GeneWikii PSMC4.
    GenomeRNAii 5704.
    NextBioi 22160.
    PROi P43686.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43686.
    Bgeei P43686.
    CleanExi HS_PSMC4.
    Genevestigatori P43686.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR005937. 26S_Psome_P45.
    IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01242. 26Sp45. 1 hit.
    PROSITEi PS00674. AAA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes."
      Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R., Rosen C.A.
      Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    3. "A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily."
      Choi H.S., Seol W., Moore D.D.
      J. Steroid Biochem. Mol. Biol. 56:23-30(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH NR1I3.
    4. "Cloning and expression analysis of a novel human gene homologous to mouse proteasomal ATPase (Tat-binding protein 7)."
      Bi A., Yu L., Zheng L.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 2).
      Tissue: Lung, Pancreas and Skin.
    8. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-10; 218-229; 307-313 AND 343-369, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    9. "Tat-binding protein 7 is a subunit of the 26S protease."
      Dubiel W., Ferrell K., Rechsteiner M.
      Biol. Chem. Hoppe-Seyler 375:237-240(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION.
    10. "Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases."
      Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.
      Mol. Cell. Biol. 25:3842-3853(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAAF1.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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-397 AND LYS-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions."
      Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M.
      Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM5.
    20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S proteasome."
      Nakamura Y., Nakano K., Umehara T., Kimura M., Hayashizaki Y., Tanaka A., Horikoshi M., Padmanabhan B., Yokoyama S.
      Structure 15:179-189(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 337-418 IN COMPLEX WITH MOUSE PSMD10.

    Entry informationi

    Entry nameiPRS6B_HUMAN
    AccessioniPrimary (citable) accession number: P43686
    Secondary accession number(s): Q96FV5, Q9UBM3, Q9UEX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: May 10, 2002
    Last modified: October 1, 2014
    This is version 150 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3