Proliferation-associated protein 2G4 (Protein name
), PA2G4_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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Gene name:
PA2G4(EBP1);
Protein name:
Proliferation-associated protein 2G4;
Alternative:
ErbB3-binding protein 1;Cell cycle protein p38-2G4 homolog(hG4-1);
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
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.
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).
Subcellular Location:
Cytoplasm
Nucleus
nucleolus
Tranlocates to the nucleus upon treatment with HRG.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2);INTERACTION WITH ERBB3;SUBCELLULAR LOCATION;TISSUE SPECIFICITY
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: PROTEIN SEQUENCE OF 2-20; 23-30; 34-62; 73-101; 156-172; 200-211; 216-236; 264-281 AND 299-364;CLEAVAGE OF INITIATOR METHIONINE;ACETYLATION AT SER-2;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: PROTEIN SEQUENCE OF 34-51; 216-236; 264-271; 299-311; 333-344 AND 377-394;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: INTERACTION WITH ERBB3;PHOSPHORYLATION;PHOSPHORYLATION BY PKC;PHOSPHORYLATION AT THR-366;MUTAGENESIS OF SER-363 AND THR-366
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Cited for: FUNCTION IN TRANSCRIPTION REPRESSION;INTERACTION WITH RB1
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Cited for: FUNCTION IN E2F1-MEDIATED TRANSCRIPTION REPRESSION;INTERACTION WITH HDAC2
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Cited for: FUNCTION IN RRNA PROCESSING;SUBCELLULAR LOCATION;TISSUE SPECIFICITY;RNA-BINDING;IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX;ASSOCIATION WITH RRNA;ASSOCIATION WITH U3 SNORNA;MUTAGENESIS OF 20-LYS--LYS-22 AND 364-ARG-LYS-365
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Cited for: FUNCTION IN TRANSCRIPTION REPRESSION;INTERACTION WITH ERBB3 AND AR
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-386;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2);SUBCELLULAR LOCATION;INTERACTION WITH ERBB3;PHOSPHORYLATION AT SER-361;MUTAGENESIS OF SER-361
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND THR-386;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: POLYUBIQUITINATION;SUBCELLULAR LOCATION;INTERACTION WITH RNF20 AND HUWE1;TISSUE SPECIFICITY;MUTAGENESIS OF SER-361
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2;PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-361 AND THR-386;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2;PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-386;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS);INTERACTION WITH 5S RIBOSOMAL RNA;LACK OF METAL COFACTOR;LACK OF AMINOPEPTIDASE ACTIVITY