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Integrator complex subunit 3

INTS3, integrator complex subunit 3, SOSS-A
INTS3 is a subunit of the Integrator complex, which associates with the C-terminal domain of RNA polymerase II large subunit (POLR2A; MIM 180660) and mediates 3-prime end processing of small nuclear RNAs U1 (RNU1; MIM 180680) and U2 (RNU2; MIM 180690) (Baillat et al., 2005 [PubMed 16239144]). INTS3 is also a subunit of single-stranded DNA (ssDNA)-binding complexes involved in the maintenance of genome stability (Huang et al., 2009) [PubMed 19683501].[supplied by OMIM, Feb 2010] (from NCBI)
Top mentioned proteins: POLYMERASE, V1a, Histone, Atm, Rad51
Papers on INTS3
RPA70 depletion induces hSSB1/2-INTS3 complex to initiate ATR signaling.
New
Saxena et al., New Delhi, India. In Nucleic Acids Res, Jun 2015
We report that in the absence of RPA, human single-stranded DNA-binding protein 1 (hSSB1) and its partner protein INTS3 form sub-nuclear foci, associate with the ATR-ATRIP complex and recruit it to the sites of genomic stress.
The Integrator complex controls the termination of transcription at diverse classes of gene targets.
New
Pagano et al., New York City, United States. In Cell Res, Mar 2015
Complexes containing INTS3 and either NABP1 or NABP2 were initially characterized in DNA damage responses, but their biochemical function remained unknown.
Subnuclear domain proteins in cancer cells support the functions of RUNX2 in the DNA damage response.
New
Stein et al., Worcester, United States. In J Cell Sci, Mar 2015
We used proteomic analysis to identify RUNX2-dependent protein-protein interactions associated with the nuclear matrix in bone, breast and prostate tumor cell types and found that RUNX2 interacts with three distinct proteins that respond to DNA damage - RUVBL2, INTS3 and BAZ1B.
A core hSSB1-INTS complex participates in the DNA damage response.
Yu et al., Ann Arbor, United States. In J Cell Sci, 2013
It has been shown that the core hSSB1 complex contains hSSB1, INTS3 and C9orf80.
Identification of submicroscopic genetic changes and precise breakpoint mapping in myelofibrosis using high resolution mate-pair sequencing.
Tefferi et al., Rochester, United States. In Am J Hematol, 2013
We describe seven novel deletions/translocations in five patients (including two with normal karyotype) whose breakpoints were PCR-validated and involved MACROD2, CACNA2D4, TET2, SGMS2, LRBA, SH3D19, INTS3, FOP (CHTOP), SCLT1, and PHF17.
Single strand DNA binding proteins 1 and 2 protect newly replicated telomeres.
Chang et al., New Haven, United States. In Cell Res, 2013
Human single-strand (ss) DNA binding proteins 1 and 2 (hSSB1 and 2) are components of the hSSB1/2-INTS3-C9orf80 heterotrimeric protein complex shown to participate in DNA damage response and maintenance of genome stability.
Integrator3, a partner of single-stranded DNA-binding protein 1, participates in the DNA damage response.
GeneRIF
Yu et al., Ann Arbor, United States. In J Biol Chem, 2009
INT3 plays a key role in the DNA damage response
INTS3 controls the hSSB1-mediated DNA damage response.
GeneRIF
Pagano et al., New York City, United States. In J Cell Biol, 2009
INTS3 controls the hSSB1-mediated DNA damage response.
HSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response.
Wang et al., Baltimore, United States. In J Biol Chem, 2009
Notably, hSSB1 and hSSB2 form separate complexes with two identical proteins, INTS3 and hSSBIP1 (C9ORF80).
SOSS complexes participate in the maintenance of genomic stability.
GeneRIF
Chen et al., New Haven, United States. In Mol Cell, 2009
INTS3 is part of an ssDNA-binding heterotrimeric complex, SOSS which is involved in the maintenance of genome stability.
CREB3L4, INTS3, and SNAPAP are targets for the 1q21 amplicon frequently detected in hepatocellular carcinoma.
Okanoue et al., Kyoto, Japan. In Cancer Genet Cytogenet, 2008
Among these, CREB3L4 (cAMP responsive element binding protein 3-like 4), INTS3 (integrator complex subunit 3), and SNAPAP (SNAP-associated protein) were significantly overexpressed in tumors from 18 HCC patients, compared with counterpart nontumorous tissues.
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