Description: Homo sapiens proliferation-associated 2G4, 38kDa (PA2G4), mRNA. RefSeq Summary (NM_006191): This gene encodes an RNA-binding protein that is involved in growth regulation. This protein is present in pre-ribosomal ribonucleoprotein complexes and may be involved in ribosome assembly and the regulation of intermediate and late steps of rRNA processing. This protein can interact with the cytoplasmic domain of the ErbB3 receptor and may contribute to transducing growth regulatory signals. This protein is also a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. This protein has been implicated in growth inhibition and the induction of differentiation of human cancer cells. Six pseudogenes, located on chromosomes 3, 6, 9, 18, 20 and X, have been identified. [provided by RefSeq, Jul 2008]. Transcript (Including UTRs) Position: hg19 chr12:56,498,103-56,507,694 Size: 9,592 Total Exon Count: 13 Strand: + Coding Region Position: hg19 chr12:56,498,522-56,506,672 Size: 8,151 Coding Exon Count: 13
ID:PA2G4_HUMAN DESCRIPTION: RecName: Full=Proliferation-associated protein 2G4; AltName: Full=Cell cycle protein p38-2G4 homolog; Short=hG4-1; AltName: Full=ErbB3-binding protein 1; FUNCTION: May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity). SUBUNIT: Interacts with the cytoplasmic domain of non- phosphorylated ERBB3; the interaction requires PKC activity. Interacts with AR. Treatment with HRG leads to dissociation from ERBB3 and increases association with AR. Interacts with NCL/nucleolin. Component of a ribonucleoprotein complex containing at least PA2G4, NCL, TOP1, PABPC2, RPLP0, acetylated histone H1 (HIST1H1A or H1F1), histone H1 2/4, RPL4, RPL8, RPL15, RPL18, RPL18A, RPL21, RPL11, RPL12, RPL28, RPL27, RPLP2 and RPL24. Interacts with HDAC2. Interacts with RB1; the interaction is enhanced upon PA2G4 dephosphorylation. INTERACTION: P19338:NCL; NbExp=2; IntAct=EBI-924893, EBI-346967; P06400:RB1; NbExp=4; IntAct=EBI-924893, EBI-491274; Q96ST3:SIN3A; NbExp=4; IntAct=EBI-924893, EBI-347218; SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=Tranlocates to the nucleus upon treatment with HRG. TISSUE SPECIFICITY: Expressed in several cell lines tested, including primary and transformed cell lines. PTM: Phosphorylated on serine and threonine residues. Phosphorylation is enhanced by HRG treatment. Basal phosphorylation is PKC-dependent and HRG-induced phosphorylation is predominantly PKC-independent. MISCELLANEOUS: Does not contain metal cofactors and does not have aminopeptidase activity. SIMILARITY: Belongs to the peptidase M24 family. SEQUENCE CAUTION: Sequence=AAD00646.1; Type=Erroneous initiation;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9UQ80
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
