Protein BMH1

<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

<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

• DNA replication origin 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
  • "The 14-3-3 protein homologues from Saccharomyces cerevisiae, Bmh1p and Bmh2p, have cruciform DNA-binding activity and associate in vivo with ARS307."
    Callejo M., Alvarez D., Price G.B., Zannis-Hadjopoulos M.
    J Biol Chem 277:38416-38423(2002) [PubMed] [Europe PMC] [Abstract]
• phosphoserine residue binding 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
  • "The 14-3-3 proteins positively regulate rapamycin-sensitive signaling."
    Bertram P.G., Zeng C., Thorson J., Shaw A.S., Zheng X.F.
    Curr Biol 8:1259-1267(1998) [PubMed] [Europe PMC] [Abstract]
• RNA polymerase II activating transcription factor binding Source: SGDInferred from direct assayⁱ
  • "Binding and transcriptional regulation by 14-3-3 (Bmh) proteins requires residues outside of the canonical motif."
    Parua P.K., Young E.T.
    Eukaryot Cell 13:21-30(2014) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• aggresome assembly Source: SGDInferred from mutant phenotypeⁱ
  • "14-3-3 protein targets misfolded chaperone-associated proteins to aggresomes."
    Xu Z., Graham K., Foote M., Liang F., Rizkallah R., Hurt M., Wang Y., Wu Y., Zhou Y.
    J Cell Sci 126:4173-4186(2013) [PubMed] [Europe PMC] [Abstract]
• ascospore formation 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
  • "14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae."
    Roberts R.L., Moesch H.-U., Fink G.R.
    Cell 89:1055-1065(1997) [PubMed] [Europe PMC] [Abstract]
• DNA damage checkpoint Source: SGDInferred from mutant phenotypeⁱ
  • "Functions of Saccharomyces cerevisiae 14-3-3 proteins in response to DNA damage and to DNA replication stress."
    Lottersberger F., Rubert F., Baldo V., Lucchini G., Longhese M.P.
    Genetics 165:1717-1732(2003) [PubMed] [Europe PMC] [Abstract]
• fungal-type cell wall chitin biosynthetic process Source: SGDInferred from genetic interactionⁱ
  • "Proteomic analysis of in vivo 14-3-3 interactions in the yeast Saccharomyces cerevisiae."
    Kakiuchi K., Yamauchi Y., Taoka M., Iwago M., Fujita T., Ito T., Song S.Y., Sakai A., Isobe T., Ichimura T.
    Biochemistry 46:7781-7792(2007) [PubMed] [Europe PMC] [Abstract]
• mitotic spindle orientation checkpoint Source: SGDInferred from genetic interactionⁱ
  • "The 14-3-3 protein Bmh1 functions in the spindle position checkpoint by breaking Bfa1 asymmetry at yeast centrosomes."
    Caydasi A.K., Micoogullari Y., Kurtulmus B., Palani S., Pereira G.
    Mol Biol Cell 25:2143-2151(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of apoptotic process Source: SGDInferred from mutant phenotypeⁱ
  • "14-3-3 protects against stress-induced apoptosis."
    Clapp C., Portt L., Khoury C., Sheibani S., Norman G., Ebner P., Eid R., Vali H., Mandato C.A., Madeo F., Greenwood M.T.
    Cell Death Dis. 3:E348-E348(2012) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription by RNA polymerase II Source: SGDInferred from mutant phenotypeⁱ
  • "Binding and transcriptional regulation by 14-3-3 (Bmh) proteins requires residues outside of the canonical motif."
    Parua P.K., Young E.T.
    Eukaryot Cell 13:21-30(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of ubiquitin protein ligase activity 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
  • "Acm1 is a negative regulator of the CDH1-dependent anaphase-promoting complex/cyclosome in budding yeast."
    Martinez J.S., Jeong D.-E., Choi E., Billings B.M., Hall M.C.
    Mol. Cell. Biol. 26:9162-9176(2006) [PubMed] [Europe PMC] [Abstract]
• pseudohyphal growth Source: SGDInferred from genetic interactionⁱ
  • "14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae."
    Roberts R.L., Moesch H.-U., Fink G.R.
    Cell 89:1055-1065(1997) [PubMed] [Europe PMC] [Abstract]
• Ras protein signal transduction Source: SGDInferred from genetic interactionⁱ
  • "14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae."
    Roberts R.L., Moesch H.-U., Fink G.R.
    Cell 89:1055-1065(1997) [PubMed] [Europe PMC] [Abstract]
• regulation of glycogen metabolic process Source: SGDInferred from genetic interactionⁱ
  • "14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae."
    Roberts R.L., Moesch H.-U., Fink G.R.
    Cell 89:1055-1065(1997) [PubMed] [Europe PMC] [Abstract]
• signal transduction involved in filamentous growth Source: SGDInferred from genetic interactionⁱ
  • "14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae."
    Roberts R.L., Moesch H.-U., Fink G.R.
    Cell 89:1055-1065(1997) [PubMed] [Europe PMC] [Abstract]

<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 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>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>Keywords - PTMⁱ

Proteomic databases

2D gel 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

• phosphoserine residue binding Source: SGDInferred from mutant phenotypeⁱ
  • "The 14-3-3 proteins positively regulate rapamycin-sensitive signaling."
    Bertram P.G., Zeng C., Thorson J., Shaw A.S., Zheng X.F.
    Curr Biol 8:1259-1267(1998) [PubMed] [Europe PMC] [Abstract]
• RNA polymerase II activating transcription factor binding Source: SGDInferred from direct assayⁱ
  • "Binding and transcriptional regulation by 14-3-3 (Bmh) proteins requires residues outside of the canonical motif."
    Parua P.K., Young E.T.
    Eukaryot Cell 13:21-30(2014) [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

Secondary structure

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
MSTSREDSVY LAKLAEQAER YEEMVENMKT VASSGQELSV EERNLLSVAY 
        60         70         80         90        100
KNVIGARRAS WRIVSSIEQK EESKEKSEHQ VELICSYRSK IETELTKISD 
       110        120        130        140        150
DILSVLDSHL IPSATTGESK VFYYKMKGDY HRYLAEFSSG DAREKATNAS 
       160        170        180        190        200
LEAYKTASEI ATTELPPTHP IRLGLALNFS VFYYEIQNSP DKACHLAKQA 
       210        220        230        240        250
FDDAIAELDT LSEESYKDST LIMQLLRDNL TLWTSDMSES GQAEDQQQQQ 
       260 
QHQQQQPPAA AEGEAPK                                     

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

2D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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 V
   Yeast (Saccharomyces cerevisiae) chromosome V: 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