DnaJ homolog subfamily B member 1

<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

• ATPase activator 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.13

    "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.
• ATPase binding Source: BHF-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%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
    Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
    J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
• cadherin binding Source: BHF-UCLInferred from high throughput direct assayⁱ
  • "E-cadherin interactome complexity and robustness resolved by quantitative proteomics."
    Guo Z., Neilson L.J., Zhong H., Murray P.S., Zanivan S., Zaidel-Bar R.
    Sci Signal 7:rs7-rs7(2014) [PubMed] [Europe PMC] [Abstract]
• chaperone binding Source: UniProtKBInferred from physical interactionⁱ
  • "The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities."
    Hageman J., van Waarde M.A., Zylicz A., Walerych D., Kampinga H.H.
    Biochem. J. 435:127-142(2011) [PubMed] [Europe PMC] [Abstract]
• Hsp70 protein binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
    Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
    J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
• protein folding chaperone Source: Ensembl
• transcription corepressor activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Molecular chaperones as HSF1-specific transcriptional repressors."
    Shi Y., Mosser D.D., Morimoto R.I.
    Genes Dev. 12:654-666(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH HSF1.
• unfolded protein binding Source: UniProtKBInferred from direct assayⁱ
  • "The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities."
    Hageman J., van Waarde M.A., Zylicz A., Walerych D., Kampinga H.H.
    Biochem. J. 435:127-142(2011) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• chaperone cofactor-dependent protein refolding Source: UniProtKBInferred from direct assayⁱ
  • "Role of the cochaperone Tpr2 in Hsp90 chaperoning."
    Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D.
    Biochemistry 47:8203-8213(2008) [PubMed] [Europe PMC] [Abstract]
• forebrain development Source: Ensembl
• negative regulation of inclusion body assembly Source: UniProtKBInferred from direct assayⁱ
  • "The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities."
    Hageman J., van Waarde M.A., Zylicz A., Walerych D., Kampinga H.H.
    Biochem. J. 435:127-142(2011) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription from RNA polymerase II promoter in response to stress Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Molecular chaperones as HSF1-specific transcriptional repressors."
    Shi Y., Mosser D.D., Morimoto R.I.
    Genes Dev. 12:654-666(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH HSF1.
• positive regulation of ATPase activity Source: BHF-UCLInferred from direct assayⁱ
  • "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
    Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
    J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
• regulation of cellular response to heat Source: Reactome
• response to unfolded protein 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%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.3

    "Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2."
    Hata M., Okumura K., Seto M., Ohtsuka K.
    Genomics 38:446-449(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

<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 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

Miscellaneous 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

2D gel 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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

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%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

        10         20         30         40         50
MGKDYYQTLG LARGASDEEI KRAYRRQALR YHPDKNKEPG AEEKFKEIAE 
        60         70         80         90        100
AYDVLSDPRK REIFDRYGEE GLKGSGPSGG SGGGANGTSF SYTFHGDPHA 
       110        120        130        140        150
MFAEFFGGRN PFDTFFGQRN GEEGMDIDDP FSGFPMGMGG FTNVNFGRSR 
       160        170        180        190        200
SAQEPARKKQ DPPVTHDLRV SLEEIYSGCT KKMKISHKRL NPDGKSIRNE 
       210        220        230        240        250
DKILTIEVKK GWKEGTKITF PKEGDQTSNN IPADIVFVLK DKPHNIFKRD 
       260        270        280        290        300
GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE 
       310        320        330        340
GLPLPKTPEK RGDLIIEFEV IFPERIPQTS RTVLEQVLPI            

        10         20         30         40         50
MFAEFFGGRN PFDTFFGQRN GEEGMDIDDP FSGFPMGMGG FTNVNFGRSR 
        60         70         80         90        100
SAQEPARKKQ DPPVTHDLRV SLEEIYSGCT KKMKISHKRL NPDGKSIRNE 
       110        120        130        140        150
DKILTIEVKK GWKEGTKITF PKEGDQTSNN IPADIVFVLK DKPHNIFKRD 
       160        170        180        190        200
GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE 
       210        220        230        240
GLPLPKTPEK RGDLIIEFEV IFPERIPQTS RTVLEQVLPI