Protein SET (Protein name
), SET_HUMAN from NCBI database.
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General Annotation
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Gene name:
SET;
Protein name:
Protein SET;
Alternative:
Inhibitor of granzyme A-activated DNase(IGAAD);HLA-DR-associated protein II;Phosphatase 2A inhibitor I2PP2A(I-2PP2A);PHAPII;Template-activating factor I(TAF-I);
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Isoform 1 and isoform 2 interact directly with each other and with ANP32A within the tripartite INHAT (inhibitor of acetyltransferases) complex. Isoform 1 and isoform 2 interact also with histones. Isoform 2 is a component of the SET complex, which also contains ANP32A, APEX1, HMGB2 and NME1, but not NME2. Within this complex, directly interacts with NME1 and with HMGB2. Interacts with SETBP1. Interacts with SGOL1. Interacts with APBB1.
Function:
Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone binding. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher.
Subcellular Location:
Cytoplasm
cytosol
Endoplasmic reticulum
Nucleus
nucleoplasm
In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. Following CTL attack, moves rapidly to the nucleus, where it is found in the nucleoplasm, avoiding the nucleolus. Similar translocation to the nucleus is also observed for lymphocyte-activated killer cells after the addition of calcium. The SET complex is associated with the endoplasmic reticulum.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2);PARTIAL PROTEIN SEQUENCE
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2);PROTEIN SEQUENCE OF 14-35; 40-60; 75-90 AND 155-167;ACTIVATION OF DNA REPLICATION
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
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Cited for: PARTIAL PROTEIN SEQUENCE;CHARACTERIZATION
12.
"A relative factor in human rectum carcinoma." Wang L.C.
,
Chen Y.
Submitted (2007-04) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-241 (ISOFORM 2)
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Cited for: FUNCTION;INTERACTION WITH AN32A;CLEAVAGE AT LYS-189;SUBCELLULAR LOCATION
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Cited for: INTERACTION WITH HMGB2;IDENTIFICATION IN THE SET COMPLEX
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Cited for: FUNCTION IN NME1 INHIBITION;INTERACTION WITH NME1;SUBCELLULAR LOCATION;DESCRIPTION OF THE SET COMPLEX;CLEAVAGE BY GZMA
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: INTERACTION WITH TREX1;IDENTIFICATION IN THE SET COMPLEX;CLEAVAGE BY GZMA;SUBCELLULAR LOCATION
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7;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 LYS-132; LYS-150 AND LYS-172;ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11 (ISOFORM 2);IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7;PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-24 (ISOFORM 2);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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-24 (ISOFORM 2);IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-238;DNA-BINDING;DOMAINS;SUBUNIT