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HUMAN:OGFD1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) OGFOD1 (synonyms: KIAA1612, TPA1)
Protein Name(s) Prolyl 3-hydroxylase OGFOD1

2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1 Termination and polyadenylation 1 homolog

External Links
UniProt Q8N543
EMBL AB046832
AK001688
AK022130
AK022752
AK024314
AC092140
BC032919
CCDS CCDS10761.2
RefSeq NP_060703.3
UniGene Hs.231883
ProteinModelPortal Q8N543
SMR Q8N543
BioGrid 120532
STRING 9606.ENSP00000337196
DrugBank DB00126
PhosphoSite Q8N543
DMDM 74728942
MaxQB Q8N543
PaxDb Q8N543
PRIDE Q8N543
Ensembl ENST00000566157
GeneID 55239
KEGG hsa:55239
UCSC uc002ejb.3
CTD 55239
GeneCards GC16P056488
HGNC HGNC:25585
HPA HPA003215
MIM 615857
neXtProt NX_Q8N543
PharmGKB PA143485568
eggNOG COG3751
GeneTree ENSGT00390000002349
HOGENOM HOG000007015
HOVERGEN HBG056995
InParanoid Q8N543
OMA FSFVYYE
OrthoDB EOG7FBRHW
PhylomeDB Q8N543
TreeFam TF105920
ChiTaRS OGFOD1
GeneWiki OGFOD1
GenomeRNAi 55239
NextBio 35527560
PRO PR:Q8N543
Proteomes UP000005640
Bgee Q8N543
CleanEx HS_OGFOD1
ExpressionAtlas Q8N543
Genevestigator Q8N543
GO GO:0005737
GO:0010494
GO:0005634
GO:0005506
GO:0031418
GO:0031544
GO:0031543
GO:0008283
GO:0019511
GO:0018126
GO:0006449
GO:0034063
InterPro IPR005123
IPR019601
IPR006620
Pfam PF13640
PF10637
SMART SM00702
PROSITE PS51471

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0043022

ribosome binding

PMID:24550447[1]

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
CACAO 9922

GO:0043022

ribosome binding

PMID:24550447[1]

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

GO:0006449

regulation of translational termination

PMID:24550447[1]

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
CACAO 9923

GO:0019511

peptidyl-proline hydroxylation

PMID:24550447[1]

ECO:0000314

P

Figure S4A shows that OGFOD1 does in vitro hydroxylation of a peptide derived from RPS23, assayed by mass spec.

complete
CACAO 9925

involved_in

GO:0019511

peptidyl-proline hydroxylation

PMID:24550447[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006449

regulation of translational termination

PMID:24550447[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034063

stress granule assembly

PMID:24550447[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0031544

peptidyl-proline 3-dioxygenase activity

PMID:24550462[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0031543

peptidyl-proline dioxygenase activity

PMID:24550447[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0018126

protein hydroxylation

PMID:24550462[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0018126

protein hydroxylation

PMID:24550447[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0010494

cytoplasmic stress granule

PMID:24550447[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0008283

cell population proliferation

PMID:24550447[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006449

regulation of translational termination

PMID:24550447[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0031543

peptidyl-proline dioxygenase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0265189
PANTHER:PTN000251752
PomBase:SPBC6B1.08c
UniProtKB:Q8N543

F

Seeded From UniProt

complete

involved_in

GO:0019511

peptidyl-proline hydroxylation

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0265189
PANTHER:PTN000251752
UniProtKB:Q8N543

P

Seeded From UniProt

complete

involved_in

GO:0006449

regulation of translational termination

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000251752
UniProtKB:Q8N543

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0265189
PANTHER:PTN000251752

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

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

enables

GO:0031418

L-ascorbic acid binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006620
InterPro:IPR019601

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005123
InterPro:IPR006620
InterPro:IPR019601

P

Seeded From UniProt

complete

enables

GO:0005506

iron ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006620
InterPro:IPR019601

F

Seeded From UniProt

complete

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

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

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

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

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

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

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

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

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

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 Singleton, RS et al. (2014) OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation. Proc. Natl. Acad. Sci. U.S.A. 111 4031-6 PubMed GONUTS page
  2. ↑ 2.0 2.1 Loenarz, C et al. (2014) Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy. Proc. Natl. Acad. Sci. U.S.A. 111 4019-24 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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