26S proteasome regulatory subunit 8 homolog

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ATPase activity Source: SGD <p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • "SUG1, a component of the 26 S proteasome, is an ATPase stimulated by specific RNAs."
    Makino Y., Yamano K., Kanemaki M., Morikawa K., Kishimoto T., Shimbara N., Tanaka K., Tamura T.
    J Biol Chem 272:23201-23205(1997) [PubMed] [Europe PMC] [Abstract]
• ATP binding Source: UniProtKB-KW
• proteasome-activating ATPase activity Source: InterPro
• protein domain specific binding Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein."
    Swaffield J.C., Melcher K., Johnston S.A.
    Nature 374:88-91(1995) [PubMed] [Europe PMC] [Abstract]
• TBP-class protein binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• ubiquitin protein ligase binding Source: SGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.10

    "Physical association of ubiquitin ligases and the 26S proteasome."
    Xie Y., Varshavsky A.
    Proc. Natl. Acad. Sci. U.S.A. 97:2497-2502(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH UBR1.
  • "UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis."
    Xie Y., Varshavsky A.
    Nat Cell Biol 4:1003-1007(2002) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• chromatin remodeling Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Cks1, Cdk1, and the 19S proteasome collaborate to regulate gene induction-dependent nucleosome eviction in yeast."
    Chaves S., Baskerville C., Yu V., Reed S.I.
    Mol Cell Biol 30:5284-5294(2010) [PubMed] [Europe PMC] [Abstract]
• negative regulation of DNA-binding transcription factor activity Source: SGDInferred from mutant phenotypeⁱ
  • "The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters."
    Ferdous A., Sikder D., Gillette T., Nalley K., Kodadek T., Johnston S.A.
    Genes Dev 21:112-123(2007) [PubMed] [Europe PMC] [Abstract]
• nonfunctional rRNA decay Source: SGDInferred from mutant phenotypeⁱ
  • "40S subunit dissociation and proteasome-dependent RNA degradation in nonfunctional 25S rRNA decay."
    Fujii K., Kitabatake M., Sakata T., Ohno M.
    EMBO J 31:2579-2589(2012) [PubMed] [Europe PMC] [Abstract]
• nucleotide-excision repair Source: SGD <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "The 19S complex of the proteasome regulates nucleotide excision repair in yeast."
    Gillette T.G., Huang W., Russell S.J., Reed S.H., Johnston S.A., Friedberg E.C.
    Genes Dev 15:1528-1539(2001) [PubMed] [Europe PMC] [Abstract]
• positive regulation of DNA-binding transcription factor activity Source: SGDInferred from mutant phenotypeⁱ
  • "The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators."
    Lee D., Ezhkova E., Li B., Pattenden S.G., Tansey W.P., Workman J.L.
    Cell 123:423-436(2005) [PubMed] [Europe PMC] [Abstract]
• positive regulation of RNA polymerase II transcription preinitiation complex assembly Source: SGDInferred from mutant phenotypeⁱ
  • "The 19 s proteasome subcomplex establishes a specific protein interaction network at the promoter for stimulated transcriptional initiation in vivo."
    Malik S., Shukla A., Sen P., Bhaumik S.R.
    J Biol Chem 284:35714-35724(2009) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription elongation from RNA polymerase II promoter Source: SGDInferred from mutant phenotypeⁱ
  • "The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II."
    Ferdous A., Gonzalez F., Sun L., Kodadek T., Johnston S.A.
    Mol Cell 7:981-991(2001) [PubMed] [Europe PMC] [Abstract]
• proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGDInferred from physical interactionⁱ
  • Ref.10

    "Physical association of ubiquitin ligases and the 26S proteasome."
    Xie Y., Varshavsky A.
    Proc. Natl. Acad. Sci. U.S.A. 97:2497-2502(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH UBR1.
• proteasome regulatory particle assembly Source: SGDInferred from mutant phenotypeⁱ
  • "Hexameric assembly of the proteasomal ATPases is templated through their C termini."
    Park S., Roelofs J., Kim W., Robert J., Schmidt M., Gygi S.P., Finley D.
    Nature 459:866-870(2009) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• protein domain specific binding Source: SGDInferred from direct assayⁱ
  • "A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein."
    Swaffield J.C., Melcher K., Johnston S.A.
    Nature 374:88-91(1995) [PubMed] [Europe PMC] [Abstract]
• TBP-class protein binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• ubiquitin protein ligase binding Source: SGDInferred from physical interactionⁱ
  • Ref.10

    "Physical association of ubiquitin ligases and the 26S proteasome."
    Xie Y., Varshavsky A.
    Proc. Natl. Acad. Sci. U.S.A. 97:2497-2502(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH UBR1.
  • "UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis."
    Xie Y., Varshavsky A.
    Nat Cell Biol 4:1003-1007(2002) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MTAAVTSSNI VLETHESGIK PYFEQKIQET ELKIRSKTEN VRRLEAQRNA 
        60         70         80         90        100
LNDKVRFIKD ELRLLQEPGS YVGEVIKIVS DKKVLVKVQP EGKYIVDVAK 
       110        120        130        140        150
DINVKDLKAS QRVCLRSDSY MLHKVLENKA DPLVSLMMVE KVPDSTYDMV 
       160        170        180        190        200
GGLTKQIKEI KEVIELPVKH PELFESLGIA QPKGVILYGP PGTGKTLLAR 
       210        220        230        240        250
AVAHHTDCKF IRVSGAELVQ KYIGEGSRMV RELFVMAREH APSIIFMDEI 
       260        270        280        290        300
DSIGSTRVEG SGGGDSEVQR TMLELLNQLD GFETSKNIKI IMATNRLDIL 
       310        320        330        340        350
DPALLRPGRI DRKIEFPPPS VAARAEILRI HSRKMNLTRG INLRKVAEKM 
       360        370        380        390        400
NGCSGADVKG VCTEAGMYAL RERRIHVTQE DFELAVGKVM NKNQETAISV 

AKLFK                                                  

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
2. Yeast chromosome VII
   Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
4. SIMILARITY comments
   Index of protein domains and families