GO page 
GO distribution
Genes by species
Genes by evidence tag
- aly
- Arabidopsis lyrata
- ath
- Arabidopsis thaliana
- bdi
- Brachypodium distachyon
- cpa
- Carica papaya
- cre
- Chlamydomonas reinhardtii
- fve
- Fragaria vesca
- gma
- Glycine max
- lja
- Lotus japonicus
- mdo
- Malus domestica
- mes
- Manihot esculenta
- mtr
- Medicago truncatula
- olu
- Ostreococcus lucimarinus
- osa
- Oryza sativa ssp. japonica
- osaindica
- Oryza sativa ssp. indica
- ota
- Ostreococcus tauri
- ppa
- Physcomitrella patens
- ptr
- Populus trichocarpa
- rco
- Ricinus communis
- sbi
- Sorghum bicolor
- smo
- Selaginella moellendorffii
- tca
- Theobroma cacao
- vca
- Volvox carteri
- vvi
- Vitis vinifera
- zma
- Zea mays
Tandem/block/both gene duplicate percentage within this GO term :
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Index of genes with 1 constraints:
GO term parent-child relationships are used in this table.
- GO term : GO:0000303
GO term parent-child relationships are used in this table.
Page 1 of 7, showing 20 records out of 135 total, starting on record 1, ending on 20
gene_id | species | description | comment | go | evidence |
---|---|---|---|---|---|
AT1G32230 | ath | Encodes a protein belonging to the (ADP-ribosyl)transferase domain-containing subfamily of WWE protein-protein interaction domain protein family. Superoxide radicals are necessary and sufficient to propagate cell death or lesion formation in rcd1 mutants. Without stress treatment, RCD1 is localized in the nucleus. Under high salt or oxidative stress, RCD1 is found not only in the nucleus but also in the cytoplasm.;WWE protein-protein interaction domain protein family | transcript=eq;prot=eq; | GO:0000303 | IMP |
AT4G20380 | ath | LSD1 monitors a superoxide-dependent signal and negatively regulates a plant cell death pathway. contains zinc-finger motifs. LSD1 negatively regulates a basal defense pathway that can act upstream or independently of both NIM1/NPR1 function and SA accumulation following avirulent or virulent pathogen challenge;LSD1 zinc finger family protein | transcript=eq;prot=eq; | GO:0000303 | IMP |
ME00999G00030 | mes | PACid=17968595;RNAname=cassava4.1_003468m;GeneName=cassava4.1_003468m.g;transcript=eq;prot=eq | GO:0000303 | ISO | |
ME04321G00010 | mes | PACid=17990526;RNAname=cassava4.1_025537m;GeneName=cassava4.1_025537m.g;transcript=eq;prot=eq | GO:0000303 | ISO | |
RC30068G01410 | rco | name=30068.m002652;gene=30068.t000142;note=30068.t000142;transcript=eq;prot=eq | GO:0000303 | ISO | |
PT01G01790 | ptr | PACid=17310263;name=POPTR_0001s01980;alias=pt041335m,eugene3.00290239,Pt-CEO1.2; | transcript=eq;prot=eq;protein_id=17310263; | GO:0000303 | ISO |
PT03G08580 | ptr | PACid=17345608;name=POPTR_0003s09530;alias=pt022968m,eugene3.00030694,Pt-CEO1.1; | transcript=eq;prot=eq;protein_id=17345608; | GO:0000303 | ISO |
GM09G34000 | gma | 09 | pid=16277112;transcript=eq;prot=eq;name=Glyma09g34000.1 | GO:0000303 | ISO |
GM01G01900 | gma | 01 | pid=16243088;transcript=eq;prot=eq;name=Glyma01g01900.1 | GO:0000303 | ISO |
LJ0G006150 | lja | prot=eq;transcript=eq;scaffold=LjSGA_005932;name=LjSGA_005932.1 | GO:0000303 | ISO | |
LJ4G012100 | lja | prot=eq;transcript=eq;scaffold=CM0283;name=chr4.CM0283.50.nc | GO:0000303 | ISO | |
LJ0G460370 | lja | prot=eq;transcript=eq;scaffold=LjT41N19;name=LjT41N19.60.nd | GO:0000303 | ISO | |
MT7G011550 | mtr | Unknown Protein (AHRD V1); contains Interpro domain(s) IPR012317 Poly(ADP-ribose) polymerase, catalytic region | transcript=eq;prot=eq;pid=Medtr7g011550.1; | GO:0000303 | ISO |
MT5G032190 | mtr | Unknown Protein (AHRD V1); contains Interpro domain(s) IPR004170 WWE domain | transcript=eq;prot=eq;pid=Medtr5g032190.1; | GO:0000303 | ISO |
MD02G024610 | mdo | transcript=eq;prot=eq;pid=MDP0000232873;tid=MDP0000232873;contig=MDC018041.243 | GO:0000303 | ISO | |
MD07G005090 | mdo | transcript=eq;prot=eq;pid=MDP0000234325;tid=MDP0000234325;contig=MDC006553.299 | GO:0000303 | ISO | |
AT2G35510 | ath | Encodes a WWE domain-containing protein with 76% similarity to RCD1. The protein also contains a PARP signature upstream of the C-terminal protein interaction domain. The PARP signature may bind NAD+ and attach the ADP-ribose-moiety from NAD+ to the target molecule. Its presence suggests a role for the protein in ADP ribosylation.;similar to RCD one 1 | transcript=eq;prot=eq; | GO:0000303 | ISO |
AL4G20880 | aly | name=fgenesh2_kg.4__1571__AT2G35510.1;pid=482511;prot=eq;tid=482511 | GO:0000303 | ISO | |
AL1G33490 | aly | name=fgenesh2_kg.1__3367__AT1G32230.1;pid=473413;prot=eq;tid=473413 | GO:0000303 | ISO | |
TC03G029940 | tca | RNAname=Tc03_t029940;GeneName=Tc03_g029940;transcript=eq;prot=eq | GO:0000303 | ISO |