Gene ID | Os03g0113800 |
Gene name | |
Homology with Arabidopsis | Similar to At5g41950: binding (HF=6e-11) |
Module size | 8 genes |
NF | 0.53 |
%ile | 70.7 |
VF | %ile | CC | Gene ID | Repr. ID | Gene name | Func. | Ev | AGI code | Arabidopsis gene name | O.I. | H.G. | S.X. | Other DB |
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
0.52 | 69.6 | 0.97 | Os03g0113800 | AK065925.1 | - | ARM repeat fold domain containing protein | 6e-11 | At5g41950 | binding | O.I. | H.G. | S.X. | |
0.75 | 91.9 | 0.97 | Os09g0541900 | AB031299.1 | - | Proteasome component region PCI domain containingprotein | 1e-24 | At1g20200 | EMB2719 (EMBRYO DEFECTIVE 2719) | O.I. | H.G. | S.X. | |
0.61 | 81.2 | 0.98 | Os05g0301500 | AK067027.1 | - | Ribophorin I (Fragment) | 7e-5 | At1g76400 | ribophorin I family protein | O.I. | H.G. | S.X. | |
0.55 | 73.7 | 0.98 | Os07g0209000 | AK058399.1 | - | Dolichyl-di-phosphooligosaccharide-proteinglycotransferase (Oligosaccharyltransferase)-like | 1e-24 | At5g66680 | DGL1 | O.I. | H.G. | S.X. | |
0.55 | 73.7 | 0.98 | Os05g0147400 | AK062146.1 | - | T-complex protein 1, zeta subunit (TCP-1-zeta)(CCT-zeta) (CCT-zeta- 1) | 6e-67 | At5g16070 | chaperonin, putative | O.I. | H.G. | S.X. | |
0.40 | 51.1 | 0.97 | Os06g0538000 | AK069949.1 | - | Chaperonin Cpn60/TCP-1 family protein | 5e-83 | At5g26360 | chaperonin, putative | O.I. | H.G. | S.X. | |
0.37 | 45.0 | 0.97 | Os01g0911200 | AK101333.1 | - | Ribophorin II family protein | 1e-6 | At4g21150 | HAP6 (HAPLESS 6) | O.I. | H.G. | S.X. | |
0.33 | 38.8 | 0.98 | Os06g0143900 | AK111584.1 | - | Coatomer protein complex, beta prime | 6e-99 | At1g52360 | coatomer protein complex, subunit beta 2 (beta prime), putative | O.I. | H.G. | S.X. |
Std2 GX | %ile | GSM ID | Assay name | GSE ID | Experiment title | Link to GEO |
---|---|---|---|---|---|---|
12.0 | 98.3 | GSM422676 | Control | GSE16865 | Heterologous microarrays for the study of drought stress in Musa | ![]() |
6.4 | 97.2 | GSM377073 | Genomic DNA - 45 day old leaf sample - mutant d2943 | GSE15071 | Detection of genomic deletions in rice by genomic DNA hybridization to oligonucleotide microarrays | ![]() |
6.2 | 97.1 | GSM377085 | Genomic DNA - 45 day old leaf sample - mutant f2045 | GSE15071 | Detection of genomic deletions in rice by genomic DNA hybridization to oligonucleotide microarrays | ![]() |
6.1 | 97.1 | GSM377075 | Genomic DNA - 45 day old leaf sample - mutant g650 | GSE15071 | Detection of genomic deletions in rice by genomic DNA hybridization to oligonucleotide microarrays | ![]() |
5.9 | 97.0 | GSM377070 | Genomic DNA - 45 day old leaf sample - mutant d1 | GSE15071 | Detection of genomic deletions in rice by genomic DNA hybridization to oligonucleotide microarrays | ![]() |
5.2 | 96.7 | GSM377084 | Genomic DNA - 45 day old leaf sample - mutant f1856 | GSE15071 | Detection of genomic deletions in rice by genomic DNA hybridization to oligonucleotide microarrays | ![]() |
5.0 | 96.6 | GSM377074 | Genomic DNA - 45 day old leaf sample - mutant g282 | GSE15071 | Detection of genomic deletions in rice by genomic DNA hybridization to oligonucleotide microarrays | ![]() |
5.0 | 96.6 | GSM377081 | Genomic DNA - 45 day old leaf sample - mutant g7534 | GSE15071 | Detection of genomic deletions in rice by genomic DNA hybridization to oligonucleotide microarrays | ![]() |
5.0 | 96.6 | GSM377076 | Genomic DNA - 45 day old leaf sample - mutant g6485 | GSE15071 | Detection of genomic deletions in rice by genomic DNA hybridization to oligonucleotide microarrays | ![]() |
5.0 | 96.6 | GSM377080 | Genomic DNA - 45 day old leaf sample - mutant g6728 | GSE15071 | Detection of genomic deletions in rice by genomic DNA hybridization to oligonucleotide microarrays | ![]() |
SF | Genes | GO ID | Process Name | Link to AmiGO |
---|---|---|---|---|
0.222 | 1 | GO:0018279 | The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification. | ![]() |
0.024 | 1 | GO:0006457 | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. | ![]() |
Arabidopsis_thaliana |
Glycine_max |
Hordeum_vulgare |
Populus_trichocarpa |
Triticum_aestivum |
Vitis_vinifera |
Zea_mays |
Back to the CoP portal site
Back to the KAGIANA project homepage