Four and a half LIM domains protein 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

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

• androgen receptor binding Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • "Negative modulation of androgen receptor transcriptional activity by Daxx."
    Lin D.Y., Fang H.I., Ma A.H., Huang Y.S., Pu Y.S., Jenster G., Kung H.J., Shih H.M.
    Mol. Cell. Biol. 24:10529-10541(2004) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntAct <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
  • "The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes."
    Wixler V., Geerts D., Laplantine E., Westhoff D., Smyth N., Aumailley M., Sonnenberg A., Paulsson M.
    J. Biol. Chem. 275:33669-33678(2000) [PubMed] [Europe PMC] [Abstract]
  • "A protein-protein interaction network of transcription factors acting during liver cell proliferation."
    Gao J., Li W.X., Feng S.Q., Yuan Y.S., Wan D.F., Han W., Yu Y.
    Genomics 91:347-355(2008) [PubMed] [Europe PMC] [Abstract]
• metal ion binding Source: UniProtKB-KW
• transcription coactivator activity Source: UniProtKBNon-traceable author statementⁱ
  • "Negative modulation of androgen receptor transcriptional activity by Daxx."
    Lin D.Y., Fang H.I., Ma A.H., Huang Y.S., Pu Y.S., Jenster G., Kung H.J., Shih H.M.
    Mol. Cell. Biol. 24:10529-10541(2004) [PubMed] [Europe PMC] [Abstract]
• transcription factor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.11

    "Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation."
    Yang Y., Hou H., Haller E.M., Nicosia S.V., Bai W.
    EMBO J. 24:1021-1032(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SIRT1 AND FOXO1.

GO - Biological processⁱ

• androgen receptor signaling pathway Source: UniProtKBNon-traceable author statementⁱ
  • "Negative modulation of androgen receptor transcriptional activity by Daxx."
    Lin D.Y., Fang H.I., Ma A.H., Huang Y.S., Pu Y.S., Jenster G., Kung H.J., Shih H.M.
    Mol. Cell. Biol. 24:10529-10541(2004) [PubMed] [Europe PMC] [Abstract]
• atrial cardiac muscle cell development Source: Ensembl
• heart trabecula formation Source: Ensembl
• negative regulation of apoptotic process 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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.11

    "Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation."
    Yang Y., Hou H., Haller E.M., Nicosia S.V., Bai W.
    EMBO J. 24:1021-1032(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SIRT1 AND FOXO1.
• negative regulation of calcineurin-NFAT signaling cascade Source: UniProtKB <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
  • Ref.16

    "FHL2 binds calcineurin and represses pathological cardiac growth."
    Hojayev B., Rothermel B.A., Gillette T.G., Hill J.A.
    Mol. Cell. Biol. 32:4025-4034(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• negative regulation of transcription by RNA polymerase II Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation."
    Yang Y., Hou H., Haller E.M., Nicosia S.V., Bai W.
    EMBO J. 24:1021-1032(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SIRT1 AND FOXO1.
• osteoblast differentiation Source: Ensembl
• positive regulation of transcription, DNA-templated Source: UniProtKBNon-traceable author statementⁱ
  • "Negative modulation of androgen receptor transcriptional activity by Daxx."
    Lin D.Y., Fang H.I., Ma A.H., Huang Y.S., Pu Y.S., Jenster G., Kung H.J., Shih H.M.
    Mol. Cell. Biol. 24:10529-10541(2004) [PubMed] [Europe PMC] [Abstract]
• regulation of lipid metabolic process Source: Reactome
• response to hormone Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Androgen induction of the androgen receptor coactivator four and a half LIM domain protein-2: evidence for a role for serum response factor in prostate cancer."
    Heemers H.V., Regan K.M., Dehm S.M., Tindall D.J.
    Cancer Res. 67:10592-10599(2007) [PubMed] [Europe PMC] [Abstract]
• ventricular cardiac muscle cell development Source: Ensembl

<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 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

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

• androgen receptor binding Source: UniProtKBNon-traceable author statementⁱ
  • "Negative modulation of androgen receptor transcriptional activity by Daxx."
    Lin D.Y., Fang H.I., Ma A.H., Huang Y.S., Pu Y.S., Jenster G., Kung H.J., Shih H.M.
    Mol. Cell. Biol. 24:10529-10541(2004) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes."
    Wixler V., Geerts D., Laplantine E., Westhoff D., Smyth N., Aumailley M., Sonnenberg A., Paulsson M.
    J. Biol. Chem. 275:33669-33678(2000) [PubMed] [Europe PMC] [Abstract]
  • "A protein-protein interaction network of transcription factors acting during liver cell proliferation."
    Gao J., Li W.X., Feng S.Q., Yuan Y.S., Wan D.F., Han W., Yu Y.
    Genomics 91:347-355(2008) [PubMed] [Europe PMC] [Abstract]
• transcription factor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.11

    "Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation."
    Yang Y., Hou H., Haller E.M., Nicosia S.V., Bai W.
    EMBO J. 24:1021-1032(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SIRT1 AND FOXO1.

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

Zinc finger

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 (2+)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.

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MTERFDCHHC NESLFGKKYI LREESPYCVV CFETLFANTC EECGKPIGCD 
        60         70         80         90        100
CKDLSYKDRH WHEACFHCSQ CRNSLVDKPF AAKEDQLLCT DCYSNEYSSK 
       110        120        130        140        150
CQECKKTIMP GTRKMEYKGS SWHETCFICH RCQQPIGTKS FIPKDNQNFC 
       160        170        180        190        200
VPCYEKQHAM QCVQCKKPIT TGGVTYREQP WHKECFVCTA CRKQLSGQRF 
       210        220        230        240        250
TARDDFAYCL NCFCDLYAKK CAGCTNPISG LGGTKYISFE ERQWHNDCFN 
       260        270 
CKKCSLSLVG RGFLTERDDI LCPDCGKDI                        

        10         20         30         40         50
MTERFDCHHC NESLFGKKYI LREESPYCVV CFETLFANTC EECGKPIGCD 
        60         70         80         90        100
CKVPARWSTR AAAGMRPASS ATAASSQLEP RVSSPKTIRI SVCPAMRNNM 
       110        120        130        140        150
PCSAFSAKSP SPREGSLTGS SPGTRSASCA PPAGSSCLGS ASQLAMTLPT 

A                                                      

Natural variant

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

PTM databases

Polymorphism and mutation databases

2D gel 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. Human chromosome 2
   Human chromosome 2: entries, gene names and cross-references to MIM
2. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
3. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
4. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
5. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations