AT-rich interactive domain-containing protein 5A

<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

• androgen receptor binding 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.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• chromatin binding Source: Ensembl
• DNA binding Source: GDB <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
  • "DNA-binding properties of ARID family proteins."
    Patsialou A., Wilsker D., Moran E.
    Nucleic Acids Res. 33:66-80(2005) [PubMed] [Europe PMC] [Abstract]
• estrogen receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• 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
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• retinoid X receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• RNA stem-loop binding Source: Ensembl
• sequence-specific DNA binding Source: NTNU_SBInferred from direct assayⁱ
  • "DNA-binding properties of ARID family proteins."
    Patsialou A., Wilsker D., Moran E.
    Nucleic Acids Res. 33:66-80(2005) [PubMed] [Europe PMC] [Abstract]
• thyroid hormone receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• transcription cis-regulatory region binding 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]
• transcription corepressor activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• transcription factor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.

GO - Biological processⁱ

• cellular response to estrogen stimulus Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• cellular response to lipopolysaccharide Source: Ensembl
• chondrocyte differentiation Source: Ensembl
• innate immune response Source: UniProtKB-KW
• negative regulation of transcription, DNA-templated Source: GDBTraceable author statementⁱ
  • "DNA-binding properties of ARID family proteins."
    Patsialou A., Wilsker D., Moran E.
    Nucleic Acids Res. 33:66-80(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription by RNA polymerase II Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• positive regulation of histone acetylation Source: Ensembl
• positive regulation of interferon-gamma production Source: Ensembl
• positive regulation of interleukin-17 production Source: Ensembl
• positive regulation of interleukin-6 production Source: Ensembl
• positive regulation of T-helper 17 type immune response Source: Ensembl
• positive regulation of T-helper 1 cell cytokine production Source: Ensembl
• positive regulation of transcription by RNA polymerase II Source: Ensembl
• positive regulation of tumor necrosis factor production Source: Ensembl
• regulation of transcription by RNA polymerase II 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]

<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 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

Genetic variation 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

<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

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%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

• androgen receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• estrogen receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• retinoid X receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• thyroid hormone receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.
• transcription factor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha."
    Georgescu S.P., Li J.H., Lu Q., Karas R.H., Brown M., Mendelsohn M.E.
    Mol. Endocrinol. 19:2491-2501(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH ESR1.

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

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

Domains and Repeats

Region

Compositional bias

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 (2+)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.

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

        10         20         30         40         50
MAAPVKGNRK QSTEGDALDP PASPKPAGKQ NGIQNPISLE DSPEAGGERE 
        60         70         80         90        100
EEQEREEEQA FLVSLYKFMK ERHTPIERVP HLGFKQINLW KIYKAVEKLG 
       110        120        130        140        150
AYELVTGRRL WKNVYDELGG SPGSTSAATC TRRHYERLVL PYVRHLKGED 
       160        170        180        190        200
DKPLPTSKPR KQYKMAKENR GDDGATERPK KAKEERRMDQ MMPGKTKADA 
       210        220        230        240        250
ADPAPLPSQE PPRNSTEQQG LASGSSVSFV GASGCPEAYK RLLSSFYCKG 
       260        270        280        290        300
THGIMSPLAK KKLLAQVSKV EALQCQEEGC RHGAEPQASP AVHLPESPQS 
       310        320        330        340        350
PKGLTENSRH RLTPQEGLQA PGGSLREEAQ AGPCPAAPIF KGCFYTHPTE 
       360        370        380        390        400
VLKPVSQHPR DFFSRLKDGV LLGPPGKEGL SVKEPQLVWG GDANRPSAFH 
       410        420        430        440        450
KGGSRKGILY PKPKACWVSP MAKVPAESPT LPPTFPSSPG LGSKRSLEEE 
       460        470        480        490        500
GAAHSGKRLR AVSPFLKEAD AKKCGAKPAG SGLVSCLLGP ALGPVPPEAY 
       510        520        530        540        550
RGTMLHCPLN FTGTPGPLKG QAALPFSPLV IPAFPAHFLA TAGPSPMAAG 
       560        570        580        590 
LMHFPPTSFD SALRHRLCPA SSAWHAPPVT TYAAPHFFHL NTKL       

        10         20         30         40         50
MKERHTPIER VPHLGFKQIN LWKIYKAVEK LGAYELVTGR RLWKNVYDEL 
        60         70         80         90        100
GGSPGSTSAA TCTRRHYERL VLPYVRHLKG EDDKPLPTSK PRKQYKMAKE 
       110        120        130        140        150
NRGDDGATER PKKAKEERRM DQMMPGKTKA DAADPAPLPS QEPPRNSTEQ 
       160        170        180        190        200
QGLASGSSVS FVGASGCPEA YKRLLSSFYC KGTHGIMSPL AKKKLLAQVS 
       210        220        230        240        250
KVEALQCQEE GCRHGAEPQA SPAVHLPESP QSPKGLTENS RHRLTPQEGL 
       260        270        280        290        300
QAPGGSLREE AQAGPCPAAP IFKGCFYTHP TEVLKPVSQH PRDFFSRLKD 
       310        320        330        340        350
GVLLGPPGKE GLSVKEPQLV WGGDANRPSA FHKGGSRKGI LYPKPKACWV 
       360        370        380        390        400
SPMAKVPAES PTLPPTFPSS PGLGSKRSLE EEGAAHSGKR LRAVSPFLKE 
       410        420        430        440        450
ADAKKCGAKP AGSGLVSCLL GPALGPVPPE AYRGTMLHCP LNFTGTPGPL 
       460        470        480        490        500
KGQAALPFSP LVIPAFPAHF LATAGPSPMA AGLMHFPPTS FDSALRHRLC 
       510        520 
PASSAWHAPP VTTYAAPHFF HLNTKL                           

<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

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

• 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

Genetic variation 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. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot