OGFOD1

Official Symbol: OGFOD1
Official Name: 2-oxoglutarate and iron dependent oxygenase domain containing 1
Aliases and Previous Symbols: N/A
Entrez ID: 55239
UniProt: Q8N543
Interactions: BioGRID
PubMed articles: Open PubMed
OMIM: Open OMIM

Entrez Summary: N/A
UniProt Summary: Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-62' of small ribosomal subunit uS12 (RPS23), thereby regulating protein translation termination efficiency. Involved in stress granule formation. {ECO:0000269|PubMed:20154146, ECO:0000269|PubMed:24550447, ECO:0000269|PubMed:24550462}.

Pfam Domains GO Terms

Compound Hit Most Correlated Genes in Chemogenomics Tissues where Essential in the Avana Dataset (DepMap 20Q1)

Global Fraction of Cell Lines Where Essential: 0/726

Tissue	Fraction Of Cell Lines Where Essential
1290807.0	0/1
909776.0	0/1
bile duct	0/28
blood	0/28
bone	0/25
breast	0/33
central nervous system	0/56
cervix	0/4
colorectal	0/17
esophagus	0/13
fibroblast	0/1
gastric	0/15
kidney	0/21
liver	0/20
lung	0/75
lymphocyte	0/14
ovary	0/26
pancreas	0/24
peripheral nervous system	0/16
plasma cell	0/15
prostate	0/1
skin	0/24
soft tissue	0/7
thyroid	0/2
upper aerodigestive	0/22
urinary tract	0/29
uterus	0/5

Expression Distribution

peptidyl-proline 3-dioxygenase activity
peptidyl-proline dioxygenase activity
regulation of translational termination
peptidyl-proline hydroxylation
stress granule assembly
L-ascorbic acid binding
protein hydroxylation
peptidyl-proline modification
cytoplasmic stress granule
regulation of protein complex disassembly
iron ion binding
ribonucleoprotein complex assembly
ribonucleoprotein complex subunit organization
regulation of translation
regulation of cellular amide metabolic process
ribonucleoprotein complex biogenesis
posttranscriptional regulation of gene expression
cell population proliferation
organelle assembly
cellular protein-containing complex assembly
peptidyl-amino acid modification
oxidation-reduction process
protein-containing complex assembly
protein-containing complex subunit organization