pgk-1
T03F1.3 | PhosphoGlycerate Kinase 1
T03F1.3 is orthologous to the human gene PHOSPHOGLYCERETE KINASE 1 (PGK1; OMIM:311800), which when mutated leads to hemolytic anemia and neurologic disturbances.
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3'UTR Zoom
Locus
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Operon Information
This gene is part of the operon CEOP1124 (I:3870066..3867543)CEOP1124 contains 2 genes in the following order:
Blumenthal et al., Nature 417, 851-854
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3'UTR mapped for pgk-1
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: 19654 -
Tier: 1 -
Name: pgk-1 -
Cosmid: T03F1.3 -
WBGeneID: WBGene00020185 -
Length: 154 -
PAS: tataaa
Cluster Coverage (%): 3600 reads (100.00%)
(See this 3'UTR in GBrowse!) (See this Gene in GBrowse!)
id | Name | Chr | Strand | Start | End | Length | PAS | Coverage |
---|---|---|---|---|---|---|---|---|
19654 | pgk-1 | I | + | 3868957 | 3869110 | 154nt | tataaa (-23nt) | 3600 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 |
---|---|---|---|---|---|---|---|---|
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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|154nt|I:3868957..3869110|PAS:tataaa
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Updated miRanda Targets for pgk-1 (Murari et al., submitted)
pgk-1 transcript has been predicted to be targeted by the following miRNAs:ID | miRNA | Target Gene | Score | Energy | % Binding (Target) | % Binding (miRNA) |
---|---|---|---|---|---|---|
125576 | cel-miR-5549-5p | pgk-1 | 162 | -13.17 | 76.47 | 82.35 | 1095 | cel-miR-1-5p | pgk-1 | 159 | -13.73 | 82.35 | 82.35 | 66382 | cel-miR-792-3p | pgk-1 | 155 | -12.43 | 72.73 | 72.73 | 102752 | cel-miR-4811-5p | pgk-1 | 149 | -8.10 | 66.67 | 77.78 | 42802 | cel-miR-247-5p | pgk-1 | 146 | -7.54 | 63.64 | 72.73 | 101161 | cel-miR-4809-3p | pgk-1 | 144 | -15.78 | 81.82 | 81.82 | 10367 | cel-miR-51-3p | pgk-1 | 141 | -16.99 | 75.00 | 75.00 |
Predicted or Experimental Interactors for pgk-1 (WormBase)
pgk-1 has been predicted to interact with the following genes (data from WS200):- act-1 Lee I et al. (2008)
act-1 encodes an actin isoform that is required for proper body wall muscle and pharyngeal muscle structures and the motility of animals; actins have highly similar amino acid sequences; ACT-1 is identical to ACT-3; act-1 functions redundantly with two other actin isoforms, act-2 and act-3, to control cytoplasmic microfilament function in the early embryo. - act-2 Lee I et al. (2008)
act-2 encodes an invertebrate actin that may function specifically in the pharynx. - act-3 Lee I et al. (2008)
act-3 encodes an invertebrate actin, highly similar to ACT-1, ACT-2, and ACT-4, that functions in body wall muscle; act-3 functions with two other action isoforms, act-1 and act-2, to control cytoplasmic microfilament function in the early embryo. - act-5 Lee I et al. (2008)
an ortholog of human cytoplasmic actin; and is expressed only in microvillous intestinal cells and excretory cell. - alh-4 Lee I et al. (2008)
none available - asp-2 Lee I et al. (2008)
asp-2 encodes aspartic protease. - cts-1 Lee I et al. (2008)
cts-1 encodes a citrate synthase, predicted to be mitochondrial, that is required for embryonic development. - cyn-7 Lee I et al. (2008)
cyn-7 encodes a cyclophilin A isoform; while not tested for peptidyl-prolyl isomerase activity in vitro, it is very similar to CYN-3 and closely resembles the prototypical CypA, and is therefore likely to be a member of the cytosolic CsA-binding cyclophilin subfamily; CYN-7 was required for embryonic viability in one set of mass RNAi assays. - dhod-1 Lee I et al. (2008)
- enol-1 Lee I et al. (2008)
T21B10.2 is orthologous to human ENOLASE 1 (also CRYSTALLIN, TAU; ENO1; OMIM:172430), which when mutated leads to spherocytic red cell enolase deficiency.
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Related Papers
There are no recent papers related to pgk-1.Related pgk Genes
The APAome Project is currently funded by the School of Life Sciences at Arizona State University