Homeobox protein Hox-B1

<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

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

• DNA binding Source: MGI <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
  • "Hox proteins have different affinities for a consensus DNA site that correlate with the positions of their genes on the hox cluster."
    Pellerin I., Schnabel C., Catron K.M., Abate C.
    Mol. Cell. Biol. 14:4532-4545(1994) [PubMed] [Europe PMC] [Abstract]
• DNA-binding transcription activator activity, RNA polymerase II-specific Source: MGI
• protein domain specific binding Source: MGI
• RNA polymerase II proximal promoter sequence-specific DNA binding Source: MGI
• RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
• sequence-specific DNA binding Source: MGI <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-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Rostral hindbrain patterning involves the direct activation of a Krox20 transcriptional enhancer by Hox/Pbx and Meis factors."
    Wassef M.A., Chomette D., Pouilhe M., Stedman A., Havis E., Desmarquet-Trin Dinh C., Schneider-Maunoury S., Gilardi-Hebenstreit P., Charnay P., Ghislain J.
    Development 135:3369-3378(2008) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• anatomical structure formation involved in morphogenesis Source: MGIInferred from genetic interactionⁱ
  • "Mice mutant for both Hoxa1 and Hoxb1 show extensive remodeling of the hindbrain and defects in craniofacial development."
    Rossel M., Capecchi M.R.
    Development 126:5027-5040(1999) [PubMed] [Europe PMC] [Abstract]
• anatomical structure morphogenesis Source: MGIInferred from genetic interactionⁱ
  • "Mice mutant for both Hoxa1 and Hoxb1 show extensive remodeling of the hindbrain and defects in craniofacial development."
    Rossel M., Capecchi M.R.
    Development 126:5027-5040(1999) [PubMed] [Europe PMC] [Abstract]
• anterior/posterior pattern specification Source: MGIInferred from genetic interactionⁱ
  • "Mice mutant for both Hoxa1 and Hoxb1 show extensive remodeling of the hindbrain and defects in craniofacial development."
    Rossel M., Capecchi M.R.
    Development 126:5027-5040(1999) [PubMed] [Europe PMC] [Abstract]
  • "A large targeted deletion of Hoxb1-Hoxb9 produces a series of single-segment anterior homeotic transformations."
    Medina-Martinez O., Bradley A., Ramirez-Solis R.
    Dev. Biol. 222:71-83(2000) [PubMed] [Europe PMC] [Abstract]
• embryonic skeletal system morphogenesis Source: MGIInferred from genetic interactionⁱ
  • "A large targeted deletion of Hoxb1-Hoxb9 produces a series of single-segment anterior homeotic transformations."
    Medina-Martinez O., Bradley A., Ramirez-Solis R.
    Dev. Biol. 222:71-83(2000) [PubMed] [Europe PMC] [Abstract]
• facial nerve structural organization Source: MGI <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
  • "Mice with targeted disruption of Hoxb-1 fail to form the motor nucleus of the VIIth nerve."
    Goddard J.M., Rossel M., Manley N.R., Capecchi M.R.
    Development 122:3217-3228(1996) [PubMed] [Europe PMC] [Abstract]
• facial nucleus development Source: MGIInferred from mutant phenotypeⁱ
  • "Mice with targeted disruption of Hoxb-1 fail to form the motor nucleus of the VIIth nerve."
    Goddard J.M., Rossel M., Manley N.R., Capecchi M.R.
    Development 122:3217-3228(1996) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription by RNA polymerase II Source: MGIInferred from direct assayⁱ
  • "Rostral hindbrain patterning involves the direct activation of a Krox20 transcriptional enhancer by Hox/Pbx and Meis factors."
    Wassef M.A., Chomette D., Pouilhe M., Stedman A., Havis E., Desmarquet-Trin Dinh C., Schneider-Maunoury S., Gilardi-Hebenstreit P., Charnay P., Ghislain J.
    Development 135:3369-3378(2008) [PubMed] [Europe PMC] [Abstract]
• rhombomere 4 development Source: MGIInferred from genetic interactionⁱ
  • "Mice mutant for both Hoxa1 and Hoxb1 show extensive remodeling of the hindbrain and defects in craniofacial development."
    Rossel M., Capecchi M.R.
    Development 126:5027-5040(1999) [PubMed] [Europe PMC] [Abstract]
• rhombomere 5 development Source: MGIInferred from genetic interactionⁱ
  • "Mice mutant for both Hoxa1 and Hoxb1 show extensive remodeling of the hindbrain and defects in craniofacial development."
    Rossel M., Capecchi M.R.
    Development 126:5027-5040(1999) [PubMed] [Europe PMC] [Abstract]
• rhombomere development Source: MGIInferred from direct assayⁱ
  • "Hoxb3 negatively regulates Hoxb1 expression in mouse hindbrain patterning."
    Wong E.Y., Wang X.A., Mak S.S., Sae-Pang J.J., Ling K.W., Fritzsch B., Sham M.H.
    Dev. Biol. 352:382-392(2011) [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

<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

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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stageⁱ

Gene expression 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

GO - Molecular functionⁱ

• protein domain specific binding Source: MGI

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

Motif

<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

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>Sequenceⁱ

<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
MDYNRMSSFL EYPLCNRGPS AYSAPTSFPP CSAPAVDSYA GESRYGGGLP 
        60         70         80         90        100
SSALQQNSGY PVQQPPSSLG VSFPSPAPSG YAPAACNPSY GPSQYYSVGQ 
       110        120        130        140        150
SEGDGSYFHP SSYGAQLGGL PDSYGAGGVG SGPYPPPQPP YGTEQTATFA 
       160        170        180        190        200
SAYDLLSEDK ESPCSSEPST LTPRTFDWMK VKRNPPKTAK VSELGLGAPG 
       210        220        230        240        250
GLRTNFTTRQ LTELEKEFHF NKYLSRARRV EIAATLELNE TQVKIWFQNR 
       260        270        280        290 
RMKQKKRERE GGRMPAGPPG CPKEAAGDAS DQSACTSPEA SPSSITS    

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

• 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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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. SIMILARITY comments
   Index of protein domains and families
2. Vertebrate homeotic Hox proteins
   Nomenclature of vertebrate homeotic Hox proteins and list of entries
3. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot