RNA-binding protein with multiple splicing

<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

• mRNA 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]
• poly(A) 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

    "Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS."
    Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q.
    Nucleic Acids Res. 34:6314-6326(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SMAD2; SMAD3; SMAD4 AND TGFBR1, SUBCELLULAR LOCATION, RNA-BINDING.
• protein homodimerization activity 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.8

    "Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS."
    Teplova M., Farazi T.A., Tuschl T., Patel D.J.
    Q. Rev. Biophys. 2015:1-11(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 14-111 OF APOPROTEIN AND IN COMPLEX WITH RNA, FUNCTION IN RNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-27; 36-LYS--ARG-38; PHE-65; GLU-97; LYS-100 AND 103-THR-LYS-104.
• RNA binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS."
    Teplova M., Farazi T.A., Tuschl T., Patel D.J.
    Q. Rev. Biophys. 2015:1-11(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 14-111 OF APOPROTEIN AND IN COMPLEX WITH RNA, FUNCTION IN RNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-27; 36-LYS--ARG-38; PHE-65; GLU-97; LYS-100 AND 103-THR-LYS-104.
• transcription coactivator activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS."
    Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q.
    Nucleic Acids Res. 34:6314-6326(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SMAD2; SMAD3; SMAD4 AND TGFBR1, SUBCELLULAR LOCATION, RNA-BINDING.

GO - Biological processⁱ

• positive regulation of pathway-restricted SMAD protein phosphorylation Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS."
    Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q.
    Nucleic Acids Res. 34:6314-6326(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SMAD2; SMAD3; SMAD4 AND TGFBR1, SUBCELLULAR LOCATION, RNA-BINDING.
• positive regulation of SMAD protein signal transduction Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS."
    Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q.
    Nucleic Acids Res. 34:6314-6326(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH SMAD2; SMAD3; SMAD4 AND TGFBR1, SUBCELLULAR LOCATION, RNA-BINDING.
• response to oxidative stress 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.8

    "Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS."
    Teplova M., Farazi T.A., Tuschl T., Patel D.J.
    Q. Rev. Biophys. 2015:1-11(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 14-111 OF APOPROTEIN AND IN COMPLEX WITH RNA, FUNCTION IN RNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-27; 36-LYS--ARG-38; PHE-65; GLU-97; LYS-100 AND 103-THR-LYS-104.
• RNA processing 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

    "A unique human gene that spans over 230 kb in the human chromosome 8p11-12 and codes multiple family proteins sharing RNA-binding motifs."
    Shimamoto A., Kitao S., Ichikawa K., Suzuki N., Yamabe Y., Imamura O., Tokutake Y., Satoh M., Matsumoto T., Kuromitsu J., Kataoka H., Sugawara K., Sugawara M., Sugimoto M., Goto M., Furuichi Y.
    Proc. Natl. Acad. Sci. U.S.A. 93:10913-10917(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D AND E).

<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

Protein family/group 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

Mutagenesis

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

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

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

Sites

<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

• protein homodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • Ref.8

    "Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS."
    Teplova M., Farazi T.A., Tuschl T., Patel D.J.
    Q. Rev. Biophys. 2015:1-11(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 14-111 OF APOPROTEIN AND IN COMPLEX WITH RNA, FUNCTION IN RNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-27; 36-LYS--ARG-38; PHE-65; GLU-97; LYS-100 AND 103-THR-LYS-104.

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

<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

<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

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 (5+)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 5 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MNNGGKAEKE NTPSEANLQE EEVRTLFVSG LPLDIKPREL YLLFRPFKGY 
        60         70         80         90        100
EGSLIKLTSK QPVGFVSFDS RSEAEAAKNA LNGIRFDPEI PQTLRLEFAK 
       110        120        130        140        150
ANTKMAKNKL VGTPNPSTPL PNTVPQFIAR EPYELTVPAL YPSSPEVWAP 
       160        170        180        190 
YPLYPAELAP ALPPPAFTYP ASLHAQMRWL PPSEATSQGW KSRQFC     

        10         20         30         40         50
MNNGGKAEKE NTPSEANLQE EEVRTLFVSG LPLDIKPREL YLLFRPFKGY 
        60         70         80         90        100
EGSLIKLTSK QPVGFVSFDS RSEAEAAKNA LNGIRFDPEI PQTLRLEFAK 
       110        120        130        140        150
ANTKMAKNKL VGTPNPSTPL PNTVPQFIAR EPYELTVPAL YPSSPEVWAP 
       160        170        180        190        200
YPLYPAELAP ALPPPAFTYP ASLHAQLCEG QTVRRSHPLS APSPDSASLA 

WFPV                                                   

        10         20         30         40         50
MNNGGKAEKE NTPSEANLQE EEVRTLFVSG LPLDIKPREL YLLFRPFKGY 
        60         70         80         90        100
EGSLIKLTSK QPVGFVSFDS RSEAEAAKNA LNGIRFDPEI PQTLRLEFAK 
       110        120        130        140        150
ANTKMAKNKL VGTPNPSTPL PNTVPQFIAR EPYELTVPAL YPSSPEVWAP 
       160        170        180        190        200
YPLYPAELAP ALPPPAFTYP ASLHAQCFSP EAKPNTPVFC PLLQQIRFVS 
       210 
GNVFVTYQPT ADQQRELPC                                   

        10         20         30         40         50
MNNGGKAEKE NTPSEANLQE EEVRTLFVSG LPLDIKPREL YLLFRPFKGY 
        60         70         80         90        100
EGSLIKLTSK QPVGFVSFDS RSEAEAAKNA LNGIRFDPEI PQTLRLEFAK 
       110        120        130        140 
ANTKMAKNKL VGTPNPSTPL PNTVPQFIAR EPLGGANEHG ERQ        

        10         20         30         40         50
MNNGGKAEKE NTPSEANLQE EEVRTLFVSG LPLDIKPREL YLLFRPFKGY 
        60         70         80         90        100
EGSLIKLTSK QPVGFVSFDS RSEAEAAKNA LNGIRFDPEI PQTLRLEFAK 
       110        120        130        140        150
ANTKMAKNKL VGTPNPSTPL PNTVPQFIAR EPMRWLPPSE ATSQGWKSRQ 

FC                                                     

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

Protein family/group 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 8
   Human chromosome 8: entries, gene names and cross-references to MIM
2. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references