msh-2
H26D21.2 | MSH (MutS Homolog) family 2
The msh-2 gene encodes a DNA mismatch repair protein homolog that is orthologous to human MSH2 (OMIM:120435); mutation of the human MSH2 gene leads to hereditary non-polyposis colon cancer (OMIM:120436).
Graphics for msh-2
3'UTR Zoom
Locus
see this gene in GBrowse
3'UTR mapped for msh-2
If available, we display here the 3'UTRs sequences we obtained by our analysis (in FASTA format). Putative canonical PAS sites, if found, are highlighted in yellow.1
ID: 2587 -
Tier: 1 -
Name: msh-2 -
Cosmid: H26D21.2 -
WBGeneID: WBGene00003418 -
Length: 72 -
PAS: AATAAA
Cluster Coverage (%): 1887 reads (100.00%)
(See this 3'UTR in GBrowse!) (See this Gene in GBrowse!)
id | Name | Chr | Strand | Start | End | Length | PAS | Coverage |
---|---|---|---|---|---|---|---|---|
2587 | msh-2 | I | - | 3694301 | 3694371 | 72nt | AATAAA (-18nt) | 1887 reads |
This 3'UTR isoform has been detected in the following tissues:
UTRome v31 | Intestine2 | Pharynx2 | Body Muscle2 | Arcade cells2 | GABA neurons2 | NMDA neurons2 | Hypodermis2 | Seam cells2 |
---|---|---|---|---|---|---|---|---|
![]() |
  |
2Blazie et al., 2016 - Alternative polyadenylation directs tissue specific miRNA targeting in Caenorhabditis elegans somatic tissues. - under review (mixed stages & tissue-specific datasets)
>|3'UTR|72nt|I:3694301..3694371|PAS:AATAAA
cucaauuucauauuuuaucuuccuacaauucacguauuuuguuuuaaauugugaauaaaccuauuauuaga
Updated miRanda Targets for msh-2 (Murari et al., submitted)
msh-2 transcript has been predicted to be targeted by the following miRNAs:ID | miRNA | Target Gene | Score | Energy | % Binding (Target) | % Binding (miRNA) |
---|---|---|---|---|---|---|
17673 | cel-miR-70-3p | msh-2 | 148 | -9.87 | 66.67 | 80.00 | 84149 | cel-miR-2207-5p | msh-2 | 146 | -12.80 | 90.91 | 90.91 |
Predicted or Experimental Interactors for msh-2 (WormBase)
msh-2 has been predicted to interact with the following genes (data from WS200):- ani-2 Lee I et al. (2008)
ani-2 encodes one of three C. elegans anillins; ANI-2 activity is required in the syncytial gonad for proper gonad structure and oocyte formation; specifically, ANI-2 appears to be required for maintaining the structure of the rachis, the syncytial compartment of germline cytoplasm that connects developing ooctyes; in the adult gonad, ANI-2 localizes to the surface of the rachis. - apb-3 Lee I et al. (2008)
apb-3 encodes an adaptin, orthologous to the beta3 subunit of adaptor protein complex 3 (AP-3); based on structural similarity, APB-3 is predicted to be involved in the formation of intracellular transport vesicles, and genetic analyses indicate that apb-3 activity is required for biogenesis of lysosome-related gut granules. - ars-1 Lee I et al. (2008)
ars-1 encodes an alanyl tRNA synthetase; on the basis of similarity to S. cerevisiae ALA1p, ARS-1 is probably cytoplasmic. - atm-1 Lee I et al. (2008)
atm-1 encodes an ortholog of human ATM (OMIM:208900) that is required for the checkpoint response to DNA damage; human ATM encodes a phosphatidylinositol-3 kinase homolog that is biochemically activated by cellular irradiation, and mutation of ATM leads to ataxia-telengiectasia. - brd-1 Lee I et al. (2008)
brd-1 encodes an ortholog of the BRCA1-associating protein BARD1 (OMIM:601593), associated with susceptibility to breast cancer; BRD-1 forms a heterodimer with BRC-1, which constitutes an E3 ubiquitin ligase; after irradiation, the DNA checkpoint proteins ATL-1 and MRE-11 are required for BRC-1/BRD-1 heterodimers to associate with the E2 ubiqutin-conjugating enzyme LET-70/Ubc5 and with RAD-51, and to ubiquitylate damaged chromatin; BRD-1 and BRC-1 bind one another, probably through their N-terminal RING domains, in yeast two-hybrid experiments and pull-down assays; BRC-1/BRD-1 heterodimers may interact with RAD-51 and other proteins via mutual binding to UBC-9; brd-1(RNAi) animals have excess chromosomal nondisjunction, abnormally high levels of CEP-1-dependent germ cell apoptosis (both with and without gamma-irradiation) and hypersensitivity to gamma-irradiation (e.g., abnormal sterility after irradiation); BRD-1 autoubiquitylation probably activates the BRC-1/BRD-1 heterodimer; BRD-1 binds SMT-3 (a Sumo homolog) and TAC-1; brd-1 is genetically dispensable for the induction of nuclear ATL-1 foci by gamma-irradiation or hydroxyurea. - car-1 Lee I et al. (2008)
- cbp-1 Lee I et al. (2008)
cbp-1 encodes a homolog of the mammalian transcriptional cofactors CBP (OMIM:600140) and p300 (E1A-BINDING PROTEIN, 300-KD; OMIM:602700) that have been shown to possess histone acetyltransferase activity, and which, when mutated, lead to Rubinstein-Taybi syndrome (OMIM:180849) and colorectal cancer (OMIM:114500); at least one splicing form of CBP-1 exhibits histone acetyltransferase (HAT) activity in vitro and has a glutamine/asparagine-rich domain; CBP-1 is required during embryogenesis for differentiation of all non-neuronal somatic cell types; CBP-1 is expressed very early in embryogenesis, suggesting that it may interact with maternally provided transcription factors, such as SKN-1, to specific developmental fates. - cdc-25.1 Lee I et al. (2008)
cdc-25.1 encodes a CDC25 phosphatase homolog that affects embryonic viability, meiosis, mitosis, proliferation of the intestine (E cell lineage), and germ line proliferation; it is expressed in the developing germline, in the nuclei of oocytes, embryonic nuclei, nuclei of embryonic cortical membranes, and sperm pronuclei, and in the germline precursors Z2 and Z3. - cdc-25.3 Lee I et al. (2008)
cdc-25.3 encodes a tyrosine phosphatase that is a member of the cell division cycle 25 (CDC25) family of cell cycle regulators that includes Schizosaccharomyces pombe CDC25 and Drosophila string; cdc-25.3 is one of four cdc-25 genes in C. elegans and while it is known to be expressed in hermaphrodites, the precise function of cdc-25.3 is not yet clear; cdc-25.3 may function redundantly with cdc-25.2 during embryonic development and redundantly with cdc-25.1, cdc-25.2, and emb-29 during meiosis. - cdt-2 Lee I et al. (2008)
More on msh-2
Related Papers
There are no recent papers related to msh-2.Related msh Genes
![SoLS](/UTRome/images/SOLS_RGB.png)
The APAome Project is currently funded by the School of Life Sciences at Arizona State University