Rhombotin-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

• bHLH transcription factor 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.
• cofactor binding Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.
• DNA-binding transcription activator activity, RNA polymerase II-specific Source: BHF-UCL <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.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.
• DNA-binding transcription factor activity, RNA polymerase II-specific Source: BHF-UCLInferred from direct assayⁱ
  • Ref.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.
• E-box binding Source: BHF-UCLInferred from direct assayⁱ
  • Ref.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.
• metal ion binding Source: UniProtKB-KW
• RNA polymerase II activating transcription factor binding Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.
• RNA polymerase II regulatory region sequence-specific DNA binding Source: BHF-UCLInferred from direct assayⁱ
  • Ref.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.

GO - Biological processⁱ

• cellular response to thyroid hormone stimulus Source: UniProtKBInferred from direct assayⁱ
  • "GAR22: a novel target gene of thyroid hormone receptor causes growth inhibition in human erythroid cells."
    Gamper I., Koh K.R., Ruau D., Ullrich K., Bartunkova J., Piroth D., Hacker C., Bartunek P., Zenke M.
    Exp. Hematol. 37:539-548.e4(2009) [PubMed] [Europe PMC] [Abstract]
• mRNA transcription by RNA polymerase II Source: BHF-UCLInferred from direct assayⁱ
  • Ref.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.
• multicellular organism development 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

    "TTG-2, a new gene encoding a cysteine-rich protein with the LIM motif, is overexpressed in acute T-cell leukaemia with the t(11;14)(p13;q11)."
    Royer-Pokora B., Loos L., Ludwig W.D.
    Oncogene 6:1887-1893(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INVOLVEMENT IN T-CELL ACUTE LYMPHOBLASTIC LEUKEMIA.
• positive regulation of transcription by RNA polymerase II Source: BHF-UCLInferred from direct assayⁱ
  • Ref.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.
• regulation of hematopoietic stem cell differentiation 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

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Keywords - Diseaseⁱ

Organism-specific databases

Chemistry 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

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

• bHLH transcription factor binding Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.
• RNA polymerase II activating transcription factor binding Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.5

    "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH BEX2.

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

Secondary structure

3D structure databases

Miscellaneous 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

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

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>. 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>Sequences (3)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.

        10         20         30         40         50
MSSAIERKSL DPSEEPVDEV LQIPPSLLTC GGCQQNIGDR YFLKAIDQYW 
        60         70         80         90        100
HEDCLSCDLC GCRLGEVGRR LYYKLGRKLC RRDYLRLFGQ DGLCASCDKR 
       110        120        130        140        150
IRAYEMTMRV KDKVYHLECF KCAACQKHFC VGDRYLLINS DIVCEQDIYE 

WTKINGMI                                               

        10         20         30         40         50
MEGSAVTVLE RGGASSPAER RSKRRRRSGG DGGGGGGARA PEGVRAPAAG 
        60         70         80         90        100
QPRATKGAPP PPGTPPPSPM SSAIERKSLD PSEEPVDEVL QIPPSLLTCG 
       110        120        130        140        150
GCQQNIGDRY FLKAIDQYWH EDCLSCDLCG CRLGEVGRRL YYKLGRKLCR 
       160        170        180        190        200
RDYLRLFGQD GLCASCDKRI RAYEMTMRVK DKVYHLECFK CAACQKHFCV 
       210        220 
GDRYLLINSD IVCEQDIYEW TKINGMI                          

        10         20         30         40         50
MSSAIERKSL DPSESLKGSQ VRCPVWPKTI SDPRCWSHSG EAVPDAWPSL 

QGTSG                                                  

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry 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. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. Human chromosome 11
   Human chromosome 11: entries, gene names and cross-references to MIM
3. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot