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TableEdit
HUMAN:OGFD1
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Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status | |
---|---|---|---|---|---|---|---|---|---|---|---|
public |
GO:0043022 |
ribosome binding |
PMID:24550447 |
ECO:0000314 |
F |
See Figure 3. In A, a 100-kDa species in an immunoprecipitation is consistent with the weight of a hypothetical OGFOD1-RPS23 complex. Other experiments on this figure support this. RPS23 is a ribosomal binding site. |
complete | ||||
public |
GO:0043022 |
ribosome binding |
PMID:24550447 |
ECO:0000314 |
F |
See Figure 3. In A, a 100-kDa species in an immunoprecipitation is consistent with the weight of a hypothetical OGFOD1-RPS23 complex. Other experiments on this figure support this. RPS23 is a ribosomal binding site. |
complete | ||||
public |
GO:0006449 |
regulation of translational termination |
PMID:24550447 |
ECO:0000315 |
P |
Figure 5 shows that OGFOD1 knockouts are less likely to terminate at a nonsense codon. This implies that OGFOD1 modulates translation termination efficiency. A catalytically inactive mutant also terminates earlier, similar to the knockout. This suggests that it is the ribosomal binding function of OGFOD1 that regulates the translational termination. |
complete | ||||
public |
GO:0019511 |
peptidyl-proline hydroxylation |
PMID:24550447 |
ECO:0000314 |
P |
Figure S4A shows that OGFOD1 does in vitro hydroxylation of a peptide derived from RPS23, assayed by mass spec. |
complete | ||||
protected |
involved_in |
GO:0019511 |
peptidyl-proline hydroxylation |
PMID:24550447 |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
protected |
involved_in |
GO:0006449 |
regulation of translational termination |
PMID:24550447 |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
protected |
involved_in |
GO:0034063 |
stress granule assembly |
PMID:24550447 |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
protected |
enables |
GO:0031544 |
peptidyl-proline 3-dioxygenase activity |
PMID:24550462 |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | ||
protected |
enables |
GO:0031543 |
peptidyl-proline dioxygenase activity |
PMID:24550447 |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | ||
protected |
involved_in |
GO:0018126 |
protein hydroxylation |
PMID:24550462 |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
protected |
involved_in |
GO:0018126 |
protein hydroxylation |
PMID:24550447 |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
protected |
part_of |
GO:0010494 |
cytoplasmic stress granule |
PMID:24550447 |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
C |
Seeded From UniProt |
complete | ||
protected |
involved_in |
GO:0008283 |
cell population proliferation |
PMID:24550447 |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
protected |
involved_in |
GO:0006449 |
regulation of translational termination |
PMID:24550447 |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
protected |
enables |
GO:0031543 |
peptidyl-proline dioxygenase activity |
PMID:21873635 |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
FB:FBgn0265189 |
F |
Seeded From UniProt |
complete | |
protected |
involved_in |
GO:0019511 |
peptidyl-proline hydroxylation |
PMID:21873635 |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
FB:FBgn0265189 |
P |
Seeded From UniProt |
complete | |
protected |
involved_in |
GO:0006449 |
regulation of translational termination |
PMID:21873635 |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000251752 |
P |
Seeded From UniProt |
complete | |
protected |
part_of |
GO:0005737 |
cytoplasm |
PMID:21873635 |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
FB:FBgn0265189 |
C |
Seeded From UniProt |
complete | |
protected |
part_of |
GO:0005829 |
cytosol |
GO_REF:0000052 |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | ||
protected |
part_of |
GO:0005634 |
nucleus |
GO_REF:0000052 |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | ||
protected |
enables |
GO:0016706 |
2-oxoglutarate-dependent dioxygenase activity |
GO_REF:0000002 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR019601 |
F |
Seeded From UniProt |
complete | |
protected |
enables |
GO:0031418 |
L-ascorbic acid binding |
GO_REF:0000002 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR006620 |
F |
Seeded From UniProt |
complete | |
protected |
involved_in |
GO:0055114 |
oxidation-reduction process |
GO_REF:0000002 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR005123 |
P |
Seeded From UniProt |
complete | |
protected |
enables |
GO:0005506 |
iron ion binding |
GO_REF:0000002 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR006620 |
F |
Seeded From UniProt |
complete | |
protected |
enables |
GO:0016491 |
oxidoreductase activity |
GO_REF:0000002 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR005123 |
F |
Seeded From UniProt |
complete | |
protected |
enables |
GO:0016705 |
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
GO_REF:0000002 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR006620 |
F |
Seeded From UniProt |
complete | |
protected |
part_of |
GO:0005737 |
cytoplasm |
GO_REF:0000037 |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0963 |
C |
Seeded From UniProt |
complete | |
protected |
enables |
GO:0031418 |
L-ascorbic acid binding |
GO_REF:0000037 |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0847 |
F |
Seeded From UniProt |
complete | |
protected |
part_of |
GO:0005634 |
nucleus |
GO_REF:0000037 |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0539 |
C |
Seeded From UniProt |
complete | |
protected |
involved_in |
GO:0055114 |
oxidation-reduction process |
GO_REF:0000037 |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0560 |
P |
Seeded From UniProt |
complete | |
protected |
enables |
GO:0016491 |
oxidoreductase activity |
GO_REF:0000037 |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0560 |
F |
Seeded From UniProt |
complete | |
protected |
enables |
GO:0051213 |
dioxygenase activity |
GO_REF:0000037 |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0223 |
F |
Seeded From UniProt |
complete | |
protected |
enables |
GO:0046872 |
metal ion binding |
GO_REF:0000037 |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0479 |
F |
Seeded From UniProt |
complete |
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