BAG family molecular chaperone regulator 2

<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

<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

• adenyl-nucleotide exchange factor activity Source: UniProtKB <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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.12

    "Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro."
    Rauch J.N., Gestwicki J.E.
    J. Biol. Chem. 289:1402-1414(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH HSPA1A; HSPA1B AND HSPA8.
• chaperone binding Source: ARUK-UCL <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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP."
    Arndt V., Daniel C., Nastainczyk W., Alberti S., Hohfeld J.
    Mol. Biol. Cell 16:5891-5900(2005) [PubMed] [Europe PMC] [Abstract]
• heat shock protein binding Source: Ensembl
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Dynamic protein-protein interaction wiring of the human spliceosome."
    Hegele A., Kamburov A., Grossmann A., Sourlis C., Wowro S., Weimann M., Will C.L., Pena V., Luehrmann R., Stelzl U.
    Mol. Cell 45:567-580(2012) [PubMed] [Europe PMC] [Abstract]
  • "A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways."
    Taipale M., Tucker G., Peng J., Krykbaeva I., Lin Z.Y., Larsen B., Choi H., Berger B., Gingras A.C., Lindquist S.
    Cell 158:434-448(2014) [PubMed] [Europe PMC] [Abstract]
  • "A proteome-scale map of the human interactome network."
    Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M.

    , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
    Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
• ion channel binding Source: ARUK-UCLInferred from physical interactionⁱ
  • "BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP."
    Arndt V., Daniel C., Nastainczyk W., Alberti S., Hohfeld J.
    Mol. Biol. Cell 16:5891-5900(2005) [PubMed] [Europe PMC] [Abstract]
• tau protein binding Source: ARUK-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • "Roles of tau protein in health and disease."
    Guo T., Noble W., Hanger D.P.
    Acta Neuropathol. 133:665-704(2017) [PubMed] [Europe PMC] [Abstract]
• ubiquitin protein ligase binding Source: Ensembl

GO - Biological processⁱ

• negative regulation of protein binding Source: ARUK-UCLInferred from direct assayⁱ
  • "BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP."
    Arndt V., Daniel C., Nastainczyk W., Alberti S., Hohfeld J.
    Mol. Biol. Cell 16:5891-5900(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of protein ubiquitination Source: ARUK-UCLInferred from direct assayⁱ
  • "The BAG2 protein stabilises PINK1 by decreasing its ubiquitination."
    Che X., Tang B., Wang X., Chen D., Yan X., Jiang H., Shen L., Xu Q., Wang G., Guo J.
    Biochem. Biophys. Res. Commun. 441:488-492(2013) [PubMed] [Europe PMC] [Abstract]
  • "The BAG2 and BAG5 proteins inhibit the ubiquitination of pathogenic ataxin3-80Q."
    Che X.Q., Tang B.S., Wang H.F., Yan X.X., Jiang H., Shen L., Xu Q., Wang G.H., Zhang H.N., Wang C.Y., Guo J.F.
    Int. J. Neurosci. 125:390-394(2015) [PubMed] [Europe PMC] [Abstract]
• negative regulation of ubiquitin protein ligase activity Source: ARUK-UCLInferred from direct assayⁱ
  • "BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP."
    Arndt V., Daniel C., Nastainczyk W., Alberti S., Hohfeld J.
    Mol. Biol. Cell 16:5891-5900(2005) [PubMed] [Europe PMC] [Abstract]
• positive regulation of proteasomal protein catabolic process Source: ARUK-UCL <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-go-evidence-codes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • "The cochaperone BAG2 sweeps paired helical filament- insoluble tau from the microtubule."
    Carrettiero D.C., Hernandez I., Neveu P., Papagiannakopoulos T., Kosik K.S.
    J. Neurosci. 29:2151-2161(2009) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein processing Source: ARUK-UCL <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP."
    Arndt V., Daniel C., Nastainczyk W., Alberti S., Hohfeld J.
    Mol. Biol. Cell 16:5891-5900(2005) [PubMed] [Europe PMC] [Abstract]
• protein folding Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.1

    "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators."
    Takayama S., Xie Z., Reed J.C.
    J. Biol. Chem. 274:781-786(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH HSP70/HSC70 CHAPERONES.
• protein metabolic process Source: MGIInferred from direct assayⁱ
  • "Control of glycogen synthesis in cultured human muscle cells."
    Halse R., Rochford J.J., McCormack J.G., Vandenheede J.R., Hemmings B.A., Yeaman S.J.
    J. Biol. Chem. 274:776-780(1999) [PubMed] [Europe PMC] [Abstract]
• protein stabilization Source: ARUK-UCLInferred from direct assayⁱ
  • "BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP."
    Arndt V., Daniel C., Nastainczyk W., Alberti S., Hohfeld J.
    Mol. Biol. Cell 16:5891-5900(2005) [PubMed] [Europe PMC] [Abstract]
  • "The BAG2 protein stabilises PINK1 by decreasing its ubiquitination."
    Che X., Tang B., Wang X., Chen D., Yan X., Jiang H., Shen L., Xu Q., Wang G., Guo J.
    Biochem. Biophys. Res. Commun. 441:488-492(2013) [PubMed] [Europe PMC] [Abstract]
  • "The BAG2 and BAG5 proteins inhibit the ubiquitination of pathogenic ataxin3-80Q."
    Che X.Q., Tang B.S., Wang H.F., Yan X.X., Jiang H., Shen L., Xu Q., Wang G.H., Zhang H.N., Wang C.Y., Guo J.F.
    Int. J. Neurosci. 125:390-394(2015) [PubMed] [Europe PMC] [Abstract]
• regulation of cellular response to heat Source: Reactome

<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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Organism-specific databases

Polymorphism and mutation databases

<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

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

Organism-specific 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_section">'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_section">'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_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• chaperone binding Source: ARUK-UCLInferred from physical interactionⁱ
  • "BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP."
    Arndt V., Daniel C., Nastainczyk W., Alberti S., Hohfeld J.
    Mol. Biol. Cell 16:5891-5900(2005) [PubMed] [Europe PMC] [Abstract]
• heat shock protein binding Source: Ensembl
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Dynamic protein-protein interaction wiring of the human spliceosome."
    Hegele A., Kamburov A., Grossmann A., Sourlis C., Wowro S., Weimann M., Will C.L., Pena V., Luehrmann R., Stelzl U.
    Mol. Cell 45:567-580(2012) [PubMed] [Europe PMC] [Abstract]
  • "A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways."
    Taipale M., Tucker G., Peng J., Krykbaeva I., Lin Z.Y., Larsen B., Choi H., Berger B., Gingras A.C., Lindquist S.
    Cell 158:434-448(2014) [PubMed] [Europe PMC] [Abstract]
  • "A proteome-scale map of the human interactome network."
    Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M.

    , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
    Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
• ion channel binding Source: ARUK-UCLInferred from physical interactionⁱ
  • "BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP."
    Arndt V., Daniel C., Nastainczyk W., Alberti S., Hohfeld J.
    Mol. Biol. Cell 16:5891-5900(2005) [PubMed] [Europe PMC] [Abstract]
• tau protein binding Source: ARUK-UCLNon-traceable author statementⁱ
  • "Roles of tau protein in health and disease."
    Guo T., Noble W., Hanger D.P.
    Acta Neuropathol. 133:665-704(2017) [PubMed] [Europe PMC] [Abstract]
• ubiquitin protein ligase binding Source: Ensembl

Protein-protein interaction 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

Domains and Repeats

Coiled coil

Keywords - Domainⁱ

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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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
MAQAKINAKA NEGRFCRSSS MADRSSRLLE SLDQLELRVE ALREAATAVE 
        60         70         80         90        100
QEKEILLEMI HSIQNSQDMR QISDGEREEL NLTANRLMGR TLTVEVSVET 
       110        120        130        140        150
IRNPQQQESL KHATRIIDEV VNKFLDDLGN AKSHLMSLYS ACSSEVPHGP 
       160        170        180        190        200
VDQKFQSIVI GCALEDQKKI KRRLETLLRN IENSDKAIKL LEHSKGAGSK 
       210 
TLQQNAESRF N                                           

        10         20         30         40         50
MPHMWVEALR EAATAVEQEK EILLEMIHSI QNSQDMRQIS DGEREELNLT 
        60         70         80         90        100
ANRLMGRTLT VEVSVETIRN PQQQESLKHA TRIIDEVVNK FLDDLGNAKS 
       110        120        130        140        150
HLMSLYSACS SEVPHGPVDQ KFQSIVIGCA LEDQKKIKRR LETLLRNIEN 
       160        170 
SDKAIKLLEH SKGAGSKTLQ QNAESRFN                         

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression 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. Human chromosome 6
   Human chromosome 6: entries, gene names and cross-references to MIM
2. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot