LIM domain-binding protein 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

• chromatin 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
  • "Differential use of SCL/TAL-1 DNA-binding domain in developmental hematopoiesis."
    Kassouf M.T., Chagraoui H., Vyas P., Porcher C.
    Blood 112:1056-1067(2008) [PubMed] [Europe PMC] [Abstract]
  • "SCL and associated proteins distinguish active from repressive GATA transcription factor complexes."
    Tripic T., Deng W., Cheng Y., Zhang Y., Vakoc C.R., Gregory G.D., Hardison R.C., Blobel G.A.
    Blood 113:2191-2201(2009) [PubMed] [Europe PMC] [Abstract]
• DNA-binding transcription factor binding Source: MGI
• enzyme binding Source: UniProtKB <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.13

    "Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors."
    Ostendorff H.P., Peirano R.I., Peters M.A., Schluter A., Bossenz M., Scheffner M., Bach I.
    Nature 416:99-103(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH RLIM, UBIQUITINATION.
• identical protein binding Source: MGIInferred from physical interactionⁱ
  • "LMO4 controls the balance between excitatory and inhibitory spinal V2 interneurons."
    Joshi K., Lee S., Lee B., Lee J.W., Lee S.K.
    Neuron 61:839-851(2009) [PubMed] [Europe PMC] [Abstract]
• LIM domain binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting protein, is expressed early in neuronal development."
    Jurata L.W., Kenny D.A., Gill G.N.
    Proc. Natl. Acad. Sci. U.S.A. 93:11693-11698(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION.
  • Ref.8

    "Functional analysis of the nuclear LIM domain interactor NLI."
    Jurata L.W., Gill G.N.
    Mol. Cell. Biol. 17:5688-5698(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ISL1; LMO2 AND LMX1A, HOMODIMERIZATION, SUBCELLULAR LOCATION, IDENTIFICATION OF LIM-BINDING DOMAIN.
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Functional analysis of the nuclear LIM domain interactor NLI."
    Jurata L.W., Gill G.N.
    Mol. Cell. Biol. 17:5688-5698(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ISL1; LMO2 AND LMX1A, HOMODIMERIZATION, SUBCELLULAR LOCATION, IDENTIFICATION OF LIM-BINDING DOMAIN.
  • Ref.9

    "Interactions between LIM domains and the LIM domain-binding protein Ldb1."
    Breen J.J., Agulnick A.D., Westphal H., Dawid I.B.
    J. Biol. Chem. 273:4712-4717(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH LHX1, DOMAIN, HOMODIMERIZATION.
• protein self-association Source: MGIInferred from physical interactionⁱ
  • "LMO4 controls the balance between excitatory and inhibitory spinal V2 interneurons."
    Joshi K., Lee S., Lee B., Lee J.W., Lee S.K.
    Neuron 61:839-851(2009) [PubMed] [Europe PMC] [Abstract]
• RNA polymerase II-specific DNA-binding transcription factor binding Source: MGI
• transcription coregulator activity Source: InterPro

GO - Biological processⁱ

• anterior/posterior axis specification 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
  • "Functional ablation of the mouse Ldb1 gene results in severe patterning defects during gastrulation."
    Mukhopadhyay M., Teufel A., Yamashita T., Agulnick A.D., Chen L., Downs K.M., Schindler A., Grinberg A., Huang S.P., Dorward D., Westphal H.
    Development 130:495-505(2003) [PubMed] [Europe PMC] [Abstract]
• cell differentiation Source: MGI <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
  • "Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern anterior mesendoderm, node, and midline development."
    Costello I., Nowotschin S., Sun X., Mould A.W., Hadjantonakis A.K., Bikoff E.K., Robertson E.J.
    Genes Dev 29:2108-2122(2015) [PubMed] [Europe PMC] [Abstract]
• cellular component assembly 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
  • "Co-factors of LIM domains (Clims/Ldb/Nli) regulate corneal homeostasis and maintenance of hair follicle stem cells."
    Xu X., Mannik J., Kudryavtseva E., Lin K.K., Flanagan L.A., Spencer J., Soto A., Wang N., Lu Z., Yu Z., Monuki E.S., Andersen B.
    Dev Biol 312:484-500(2007) [PubMed] [Europe PMC] [Abstract]
• cerebellar Purkinje cell differentiation Source: MGIInferred from mutant phenotypeⁱ
  • "LIM-homeodomain proteins Lhx1 and Lhx5, and their cofactor Ldb1, control Purkinje cell differentiation in the developing cerebellum."
    Zhao Y., Kwan K.M., Mailloux C.M., Lee W.K., Grinberg A., Wurst W., Behringer R.R., Westphal H.
    Proc Natl Acad Sci U S A 104:13182-13186(2007) [PubMed] [Europe PMC] [Abstract]
• cerebellum development Source: MGIInferred from mutant phenotypeⁱ
  • "LIM-homeodomain proteins Lhx1 and Lhx5, and their cofactor Ldb1, control Purkinje cell differentiation in the developing cerebellum."
    Zhao Y., Kwan K.M., Mailloux C.M., Lee W.K., Grinberg A., Wurst W., Behringer R.R., Westphal H.
    Proc Natl Acad Sci U S A 104:13182-13186(2007) [PubMed] [Europe PMC] [Abstract]
• epithelial structure maintenance Source: MGIInferred from genetic interactionⁱ
  • "Co-factors of LIM domains (Clims/Ldb/Nli) regulate corneal homeostasis and maintenance of hair follicle stem cells."
    Xu X., Mannik J., Kudryavtseva E., Lin K.K., Flanagan L.A., Spencer J., Soto A., Wang N., Lu Z., Yu Z., Monuki E.S., Andersen B.
    Dev Biol 312:484-500(2007) [PubMed] [Europe PMC] [Abstract]
• gastrulation with mouth forming second Source: MGIInferred from mutant phenotypeⁱ
  • "Functional ablation of the mouse Ldb1 gene results in severe patterning defects during gastrulation."
    Mukhopadhyay M., Teufel A., Yamashita T., Agulnick A.D., Chen L., Downs K.M., Schindler A., Grinberg A., Huang S.P., Dorward D., Westphal H.
    Development 130:495-505(2003) [PubMed] [Europe PMC] [Abstract]
• hair follicle development Source: MGIInferred from genetic interactionⁱ
  • "Co-factors of LIM domains (Clims/Ldb/Nli) regulate corneal homeostasis and maintenance of hair follicle stem cells."
    Xu X., Mannik J., Kudryavtseva E., Lin K.K., Flanagan L.A., Spencer J., Soto A., Wang N., Lu Z., Yu Z., Monuki E.S., Andersen B.
    Dev Biol 312:484-500(2007) [PubMed] [Europe PMC] [Abstract]
• head development Source: UniProtKBInferred from genetic interactionⁱ
  • "Ssdp1 regulates head morphogenesis of mouse embryos by activating the Lim1-Ldb1 complex."
    Nishioka N., Nagano S., Nakayama R., Kiyonari H., Ijiri T., Taniguchi K., Shawlot W., Hayashizaki Y., Westphal H., Behringer R.R., Matsuda Y., Sakoda S., Kondoh H., Sasaki H.
    Development 132:2535-2546(2005) [PubMed] [Europe PMC] [Abstract]
• histone H3-K4 acetylation Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Multiple functions of Ldb1 required for beta-globin activation during erythroid differentiation."
    Song S.H., Kim A., Ragoczy T., Bender M.A., Groudine M., Dean A.
    Blood 116:2356-2364(2010) [PubMed] [Europe PMC] [Abstract]
• mesendoderm development Source: MGIInferred from mutant phenotypeⁱ
  • "Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern anterior mesendoderm, node, and midline development."
    Costello I., Nowotschin S., Sun X., Mould A.W., Hadjantonakis A.K., Bikoff E.K., Robertson E.J.
    Genes Dev 29:2108-2122(2015) [PubMed] [Europe PMC] [Abstract]
• negative regulation of erythrocyte differentiation Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.4

    "The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative regulators of erythroid differentiation."
    Visvader J.E., Mao X., Fujiwara Y., Hahm K., Orkin S.H.
    Proc. Natl. Acad. Sci. U.S.A. 94:13707-13712(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH LMO2, IDENTIFICATION IN A COMPLEX WITH LMO2 AND TAL1.
• negative regulation of transcription, DNA-templated Source: MGI
• negative regulation of transcription by RNA polymerase II Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• nervous system development Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• neuron differentiation Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • Ref.2

    "Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting protein, is expressed early in neuronal development."
    Jurata L.W., Kenny D.A., Gill G.N.
    Proc. Natl. Acad. Sci. U.S.A. 93:11693-11698(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION.
• positive regulation of cell adhesion Source: MGIInferred from genetic interactionⁱ
  • "Co-factors of LIM domains (Clims/Ldb/Nli) regulate corneal homeostasis and maintenance of hair follicle stem cells."
    Xu X., Mannik J., Kudryavtseva E., Lin K.K., Flanagan L.A., Spencer J., Soto A., Wang N., Lu Z., Yu Z., Monuki E.S., Andersen B.
    Dev Biol 312:484-500(2007) [PubMed] [Europe PMC] [Abstract]
• positive regulation of hemoglobin biosynthetic process Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Multiple functions of Ldb1 required for beta-globin activation during erythroid differentiation."
    Song S.H., Kim A., Ragoczy T., Bender M.A., Groudine M., Dean A.
    Blood 116:2356-2364(2010) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription by RNA polymerase II Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Multiple functions of Ldb1 required for beta-globin activation during erythroid differentiation."
    Song S.H., Kim A., Ragoczy T., Bender M.A., Groudine M., Dean A.
    Blood 116:2356-2364(2010) [PubMed] [Europe PMC] [Abstract]
• primitive erythrocyte differentiation Source: BHF-UCLTraceable author statementⁱ
  • "Multiple functions of Ldb1 required for beta-globin activation during erythroid differentiation."
    Song S.H., Kim A., Ragoczy T., Bender M.A., Groudine M., Dean A.
    Blood 116:2356-2364(2010) [PubMed] [Europe PMC] [Abstract]
• regulation of cell migration Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "The Ldb1 and Ldb2 transcriptional cofactors interact with the Ste20-like kinase SLK and regulate cell migration."
    Storbeck C.J., Wagner S., O'Reilly P., McKay M., Parks R.J., Westphal H., Sabourin L.A.
    Mol. Biol. Cell 20:4174-4182(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH SLK, SUBCELLULAR LOCATION.
• regulation of focal adhesion assembly Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "The Ldb1 and Ldb2 transcriptional cofactors interact with the Ste20-like kinase SLK and regulate cell migration."
    Storbeck C.J., Wagner S., O'Reilly P., McKay M., Parks R.J., Westphal H., Sabourin L.A.
    Mol. Biol. Cell 20:4174-4182(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH SLK, SUBCELLULAR LOCATION.
• regulation of kinase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "The Ldb1 and Ldb2 transcriptional cofactors interact with the Ste20-like kinase SLK and regulate cell migration."
    Storbeck C.J., Wagner S., O'Reilly P., McKay M., Parks R.J., Westphal H., Sabourin L.A.
    Mol. Biol. Cell 20:4174-4182(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH SLK, SUBCELLULAR LOCATION.
• regulation of transcription elongation from RNA polymerase II promoter Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Multiple functions of Ldb1 required for beta-globin activation during erythroid differentiation."
    Song S.H., Kim A., Ragoczy T., Bender M.A., Groudine M., Dean A.
    Blood 116:2356-2364(2010) [PubMed] [Europe PMC] [Abstract]
• somatic stem cell population maintenance Source: MGIInferred from genetic interactionⁱ
  • "Co-factors of LIM domains (Clims/Ldb/Nli) regulate corneal homeostasis and maintenance of hair follicle stem cells."
    Xu X., Mannik J., Kudryavtseva E., Lin K.K., Flanagan L.A., Spencer J., Soto A., Wang N., Lu Z., Yu Z., Monuki E.S., Andersen B.
    Dev Biol 312:484-500(2007) [PubMed] [Europe PMC] [Abstract]
• transcription by RNA polymerase II Source: UniProtKBInferred from direct assayⁱ
  • "Ssdp1 regulates head morphogenesis of mouse embryos by activating the Lim1-Ldb1 complex."
    Nishioka N., Nagano S., Nakayama R., Kiyonari H., Ijiri T., Taniguchi K., Shawlot W., Hayashizaki Y., Westphal H., Behringer R.R., Matsuda Y., Sakoda S., Kondoh H., Sasaki H.
    Development 132:2535-2546(2005) [PubMed] [Europe PMC] [Abstract]
• transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Multiple functions of Ldb1 required for beta-globin activation during erythroid differentiation."
    Song S.H., Kim A., Ragoczy T., Bender M.A., Groudine M., Dean A.
    Blood 116:2356-2364(2010) [PubMed] [Europe PMC] [Abstract]
• Wnt signaling pathway Source: MGIInferred from mutant phenotypeⁱ
  • "Functional ablation of the mouse Ldb1 gene results in severe patterning defects during gastrulation."
    Mukhopadhyay M., Teufel A., Yamashita T., Agulnick A.D., Chen L., Downs K.M., Schindler A., Grinberg A., Huang S.P., Dorward D., Westphal H.
    Development 130:495-505(2003) [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

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

• UniProt annotation
• GO - Cellular component

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

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

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

<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

• DNA-binding transcription factor binding Source: MGI
• enzyme binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.13

    "Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors."
    Ostendorff H.P., Peirano R.I., Peters M.A., Schluter A., Bossenz M., Scheffner M., Bach I.
    Nature 416:99-103(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH RLIM, UBIQUITINATION.
• identical protein binding Source: MGIInferred from physical interactionⁱ
  • "LMO4 controls the balance between excitatory and inhibitory spinal V2 interneurons."
    Joshi K., Lee S., Lee B., Lee J.W., Lee S.K.
    Neuron 61:839-851(2009) [PubMed] [Europe PMC] [Abstract]
• LIM domain binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting protein, is expressed early in neuronal development."
    Jurata L.W., Kenny D.A., Gill G.N.
    Proc. Natl. Acad. Sci. U.S.A. 93:11693-11698(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION.
  • Ref.8

    "Functional analysis of the nuclear LIM domain interactor NLI."
    Jurata L.W., Gill G.N.
    Mol. Cell. Biol. 17:5688-5698(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ISL1; LMO2 AND LMX1A, HOMODIMERIZATION, SUBCELLULAR LOCATION, IDENTIFICATION OF LIM-BINDING DOMAIN.
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Functional analysis of the nuclear LIM domain interactor NLI."
    Jurata L.W., Gill G.N.
    Mol. Cell. Biol. 17:5688-5698(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ISL1; LMO2 AND LMX1A, HOMODIMERIZATION, SUBCELLULAR LOCATION, IDENTIFICATION OF LIM-BINDING DOMAIN.
  • Ref.9

    "Interactions between LIM domains and the LIM domain-binding protein Ldb1."
    Breen J.J., Agulnick A.D., Westphal H., Dawid I.B.
    J. Biol. Chem. 273:4712-4717(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH LHX1, DOMAIN, HOMODIMERIZATION.
• protein self-association Source: MGIInferred from physical interactionⁱ
  • "LMO4 controls the balance between excitatory and inhibitory spinal V2 interneurons."
    Joshi K., Lee S., Lee B., Lee J.W., Lee S.K.
    Neuron 61:839-851(2009) [PubMed] [Europe PMC] [Abstract]
• RNA polymerase II-specific DNA-binding transcription factor binding Source: MGI

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

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

Region

Compositional bias

<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

<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>Sequences (3+)ⁱ

<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.

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MSVGCACPGC SSKSFKLYSP KEPPNGNAFP PFHPGTMLDR DVGPTPMYPP 
        60         70         80         90        100
TYLEPGIGRH TPYGNQTDYR IFELNKRLQN WTEECDNLWW DAFTTEFFED 
       110        120        130        140        150
DAMLTITFCL EDGPKRYTIG RTLIPRYFRS IFEGGATELY YVLKHPKEAF 
       160        170        180        190        200
HSNFVSLDCD QGSMVTQHGK PMFTQVCVEG RLYLEFMFDD MMRIKTWHFS 
       210        220        230        240        250
IRQHRELIPR SILAMHAQDP QMLDQLSKNI TRCGLSNSTL NYLRLCVILE 
       260        270        280        290        300
PMQELMSRHK TYSLSPRDCL KTCLFQKWQR MVAPPAEPAR QQPSKRRKRK 
       310        320        330        340        350
MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF 
       360        370        380        390        400
GDEDERLITR LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES 
       410 
KSENPTSQAS Q                                           

        10         20         30         40         50
MLDRDVGPTP MYPPTYLEPG IGRHTPYGNQ TDYRIFELNK RLQNWTEECD 
        60         70         80         90        100
NLWWDAFTTE FFEDDAMLTI TFCLEDGPKR YTIGRTLIPR YFRSIFEGGA 
       110        120        130        140        150
TELYYVLKHP KEAFHSNFVS LDCDQGSMVT QHGKPMFTQV CVEGRLYLEF 
       160        170        180        190        200
MFDDMMRIKT WHFSIRQHRE LIPRSILAMH AQDPQMLDQL SKNITRCGLS 
       210        220        230        240        250
NSTLNYLRLC VILEPMQELM SRHKTYSLSP RDCLKTCLFQ KWQRMVAPPA 
       260        270        280        290        300
EPARQQPSKR RKRKMSGGST MSSGGGNTNN SNSKKKSPAS TFALSSQVPV 
       310 
SISAFFSSGL PHCSPLTPV                                   

        10         20         30         40         50
MLDRDVGPTP MYPPTYLEPG IGRHTPYGNQ TDYRIFELNK RLQNWTEECD 
        60         70         80         90        100
NLWWDAFTTE FFEDDAMLTI TFCLEDGPKR YTIGRTLIPR YFRSIFEGGA 
       110        120        130        140        150
TELYYVLKHP KEAFHSNFVS LDCDQGSMVT QHGKPMFTQV CVEGRLYLEF 
       160        170        180        190        200
MFDDMMRIKT WHFSIRQHRE LIPRSILAMH AQDPQMLDQL SKNITRCGLS 
       210        220        230        240        250
NSTLNYLRLC VILEPMQELM SRHKTYSLSP RDCLKTCLFQ KWQRMVAPPA 
       260        270        280        290        300
EPARQQPSKR RKRKMSGGST MSSGGGNTNN SNSKKKSPAS TFALSSQVPD 
       310        320        330        340        350
VMVVGEPTLM GGEFGDEDER LITRLENTQF DAANGIDDED SFNNSPALGA 
       360        370 
NSPWNSKPPS SQESKSENPT SQASQ                            

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

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. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
3. SIMILARITY comments
   Index of protein domains and families