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Prolyl 3-hydroxylase OGFOD1 (EC 1.14.11.-) (2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1) (Termination and polyadenylation 1 homolog) (uS12 prolyl 3-hydroxylase)

 OGFD1_HUMAN             Reviewed;         542 AA.
Q8N543; H3BUQ2; Q9H7U5; Q9H9J9; Q9HA87; Q9HCG0; Q9NVB6;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Prolyl 3-hydroxylase OGFOD1;
EC=1.14.11.-;
AltName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1;
AltName: Full=Termination and polyadenylation 1 homolog;
AltName: Full=uS12 prolyl 3-hydroxylase {ECO:0000303|PubMed:25728928};
Name=OGFOD1; Synonyms=KIAA1612, TPA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10997877; DOI=10.1093/dnares/7.4.271;
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes.
XVIII. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro.";
DNA Res. 7:273-281(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
SER-173.
TISSUE=Embryo, Ovary, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-155.
PubMed=20579638; DOI=10.1016/j.febslet.2010.06.015;
Saito K., Adachi N., Koyama H., Matsushita M.;
"OGFOD1, a member of the 2-oxoglutarate and iron dependent dioxygenase
family, functions in ischemic signaling.";
FEBS Lett. 584:3340-3347(2010).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20154146; DOI=10.1128/MCB.01350-09;
Wehner K.A., Schutz S., Sarnow P.;
"OGFOD1, a novel modulator of eukaryotic translation initiation factor
2alpha phosphorylation and the cellular response to stress.";
Mol. Cell. Biol. 30:2006-2016(2010).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
SUBCELLULAR LOCATION.
PubMed=22002106; DOI=10.1074/mcp.M111.013680;
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
"Systematic analysis of protein pools, isoforms, and modifications
affecting turnover and subcellular localization.";
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=24550462; DOI=10.1073/pnas.1311750111;
Loenarz C., Sekirnik R., Thalhammer A., Ge W., Spivakovsky E.,
Mackeen M.M., McDonough M.A., Cockman M.E., Kessler B.M.,
Ratcliffe P.J., Wolf A., Schofield C.J.;
"Hydroxylation of the eukaryotic ribosomal decoding center affects
translational accuracy.";
Proc. Natl. Acad. Sci. U.S.A. 111:4019-4024(2014).
[10]
FUNCTION, AND MUTAGENESIS OF ASP-157.
PubMed=24550447; DOI=10.1073/pnas.1314482111;
Singleton R.S., Liu-Yi P., Formenti F., Ge W., Sekirnik R.,
Fischer R., Adam J., Pollard P.J., Wolf A., Thalhammer A., Loenarz C.,
Flashman E., Yamamoto A., Coleman M.L., Kessler B.M., Wappner P.,
Schofield C.J., Ratcliffe P.J., Cockman M.E.;
"OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in
translation control and stress granule formation.";
Proc. Natl. Acad. Sci. U.S.A. 111:4031-4036(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
SUBUNIT.
PubMed=25728928; DOI=10.1016/j.str.2015.01.014;
Horita S., Scotti J.S., Thinnes C., Mottaghi-Taromsari Y.S.,
Thalhammer A., Ge W., Aik W., Loenarz C., Schofield C.J.,
McDonough M.A.;
"Structure of the ribosomal oxygenase OGFOD1 provides insights into
the regio- and stereoselectivity of prolyl hydroxylases.";
Structure 23:639-652(2015).
-!- FUNCTION: 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}.
-!- CATALYTIC ACTIVITY: [ribosomal protein uS12]-L-proline + 2-
oxoglutarate + O2 = [ribosomal protein uS12]-(3S)-3-hydroxy-L-
proline + succinate + CO2. {ECO:0000269|PubMed:24550462,
ECO:0000305|PubMed:25728928}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00805};
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25728928}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus. Note=Mainly
nuclear. A portion relocalizes to cytoplasmic stress granules upon
stress.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8N543-1; Sequence=Displayed;
Name=2;
IsoId=Q8N543-2; Sequence=VSP_025852;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the TPA1 family. {ECO:0000305}.
-!- CAUTION: According to a report, it is incorporated into stress
granules upon arsenite-induced stress and associates with heme-
regulated kinase and eIF-2-alpha (EIF2S1) in regulating eIF-2-
alpha phosphorylation (PubMed:20154146). However, no effect in
eIF-2-alpha phosphorylation have been observed by another study
(PubMed:24550447). {ECO:0000305|PubMed:20154146,
ECO:0000305|PubMed:24550447}.
-!- SEQUENCE CAUTION:
Sequence=BAB13438.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB14880.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB046832; BAB13438.1; ALT_INIT; mRNA.
EMBL; AK001688; BAA91838.1; -; mRNA.
EMBL; AK022130; BAB13967.1; -; mRNA.
EMBL; AK022752; BAB14226.1; -; mRNA.
EMBL; AK024314; BAB14880.1; ALT_INIT; mRNA.
EMBL; AC092140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032919; AAH32919.1; -; mRNA.
CCDS; CCDS10761.2; -. [Q8N543-1]
RefSeq; NP_001311291.1; NM_001324362.1. [Q8N543-2]
RefSeq; NP_060703.3; NM_018233.3.
UniGene; Hs.231883; -.
PDB; 4NHX; X-ray; 2.10 A; A=1-542.
PDB; 4NHY; X-ray; 2.60 A; A/B/C/D=1-542.
PDBsum; 4NHX; -.
PDBsum; 4NHY; -.
ProteinModelPortal; Q8N543; -.
SMR; Q8N543; -.
BioGrid; 120532; 33.
IntAct; Q8N543; 1.
STRING; 9606.ENSP00000457258; -.
DrugBank; DB00126; Vitamin C.
iPTMnet; Q8N543; -.
PhosphoSitePlus; Q8N543; -.
BioMuta; OGFOD1; -.
DMDM; 74728942; -.
EPD; Q8N543; -.
MaxQB; Q8N543; -.
PaxDb; Q8N543; -.
PeptideAtlas; Q8N543; -.
PRIDE; Q8N543; -.
Ensembl; ENST00000566157; ENSP00000457258; ENSG00000087263. [Q8N543-1]
GeneID; 55239; -.
KEGG; hsa:55239; -.
UCSC; uc002ejb.4; human. [Q8N543-1]
CTD; 55239; -.
DisGeNET; 55239; -.
EuPathDB; HostDB:ENSG00000087263.16; -.
GeneCards; OGFOD1; -.
HGNC; HGNC:25585; OGFOD1.
HPA; HPA003215; -.
MIM; 615857; gene.
neXtProt; NX_Q8N543; -.
OpenTargets; ENSG00000087263; -.
PharmGKB; PA143485568; -.
eggNOG; KOG3844; Eukaryota.
eggNOG; COG3751; LUCA.
GeneTree; ENSGT00390000002349; -.
HOGENOM; HOG000007015; -.
HOVERGEN; HBG056995; -.
InParanoid; Q8N543; -.
OMA; FSFVYYE; -.
OrthoDB; EOG091G08PF; -.
PhylomeDB; Q8N543; -.
TreeFam; TF105920; -.
ChiTaRS; OGFOD1; human.
GeneWiki; OGFOD1; -.
GenomeRNAi; 55239; -.
PRO; PR:Q8N543; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000087263; -.
CleanEx; HS_OGFOD1; -.
ExpressionAtlas; Q8N543; baseline and differential.
Genevisible; Q8N543; HS.
GO; GO:0010494; C:cytoplasmic stress granule; IMP:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
GO; GO:0031544; F:peptidyl-proline 3-dioxygenase activity; IDA:UniProtKB.
GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0019511; P:peptidyl-proline hydroxylation; IDA:CACAO.
GO; GO:0018126; P:protein hydroxylation; IDA:UniProtKB.
GO; GO:0006449; P:regulation of translational termination; IMP:UniProtKB.
GO; GO:0034063; P:stress granule assembly; IMP:UniProtKB.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
InterPro; IPR006620; Pro_4_hyd_alph.
Pfam; PF10637; Ofd1_CTDD; 1.
SMART; SM00702; P4Hc; 1.
PROSITE; PS51471; FE2OG_OXY; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
Polymorphism; Reference proteome; Vitamin C.
CHAIN 1 542 Prolyl 3-hydroxylase OGFOD1.
/FTId=PRO_0000288974.
DOMAIN 134 239 Fe2OG dioxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
MOTIF 4 20 Nuclear localization signal.
{ECO:0000305}.
METAL 155 155 Iron; via tele nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00805,
ECO:0000269|PubMed:25728928}.
METAL 157 157 Iron. {ECO:0000255|PROSITE-
ProRule:PRU00805,
ECO:0000269|PubMed:25728928}.
METAL 218 218 Iron; via tele nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00805,
ECO:0000269|PubMed:25728928}.
BINDING 169 169 2-oxoglutarate.
{ECO:0000305|PubMed:25728928}.
BINDING 230 230 2-oxoglutarate. {ECO:0000255|PROSITE-
ProRule:PRU00805,
ECO:0000305|PubMed:25728928}.
VAR_SEQ 1 140 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_025852.
VARIANT 173 173 P -> S (in dbSNP:rs34883368).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_032545.
MUTAGEN 155 155 H->A: Loss of function.
{ECO:0000269|PubMed:20579638}.
MUTAGEN 157 157 D->A: Loss of function.
{ECO:0000269|PubMed:24550447}.
CONFLICT 50 50 S -> G (in Ref. 2; BAB13967).
{ECO:0000305}.
CONFLICT 112 112 I -> V (in Ref. 2; BAB14226).
{ECO:0000305}.
CONFLICT 343 343 E -> G (in Ref. 2; BAB14880).
{ECO:0000305}.
HELIX 28 30 {ECO:0000244|PDB:4NHX}.
HELIX 33 44 {ECO:0000244|PDB:4NHX}.
STRAND 55 57 {ECO:0000244|PDB:4NHX}.
STRAND 59 61 {ECO:0000244|PDB:4NHX}.
STRAND 63 68 {ECO:0000244|PDB:4NHX}.
HELIX 73 84 {ECO:0000244|PDB:4NHX}.
STRAND 88 102 {ECO:0000244|PDB:4NHX}.
HELIX 104 106 {ECO:0000244|PDB:4NHY}.
HELIX 110 120 {ECO:0000244|PDB:4NHX}.
HELIX 122 131 {ECO:0000244|PDB:4NHX}.
STRAND 141 146 {ECO:0000244|PDB:4NHX}.
STRAND 151 155 {ECO:0000244|PDB:4NHX}.
STRAND 162 169 {ECO:0000244|PDB:4NHX}.
HELIX 176 178 {ECO:0000244|PDB:4NHX}.
STRAND 182 187 {ECO:0000244|PDB:4NHX}.
STRAND 193 200 {ECO:0000244|PDB:4NHX}.
STRAND 207 211 {ECO:0000244|PDB:4NHX}.
STRAND 218 220 {ECO:0000244|PDB:4NHX}.
STRAND 230 238 {ECO:0000244|PDB:4NHX}.
HELIX 266 269 {ECO:0000244|PDB:4NHX}.
HELIX 272 275 {ECO:0000244|PDB:4NHX}.
HELIX 277 290 {ECO:0000244|PDB:4NHX}.
STRAND 291 297 {ECO:0000244|PDB:4NHX}.
HELIX 301 313 {ECO:0000244|PDB:4NHX}.
STRAND 318 321 {ECO:0000244|PDB:4NHX}.
TURN 324 326 {ECO:0000244|PDB:4NHX}.
STRAND 327 332 {ECO:0000244|PDB:4NHX}.
HELIX 334 336 {ECO:0000244|PDB:4NHX}.
HELIX 339 349 {ECO:0000244|PDB:4NHX}.
HELIX 351 361 {ECO:0000244|PDB:4NHX}.
STRAND 434 442 {ECO:0000244|PDB:4NHX}.
STRAND 459 467 {ECO:0000244|PDB:4NHX}.
HELIX 473 475 {ECO:0000244|PDB:4NHX}.
STRAND 479 483 {ECO:0000244|PDB:4NHX}.
STRAND 489 493 {ECO:0000244|PDB:4NHX}.
STRAND 500 505 {ECO:0000244|PDB:4NHX}.
STRAND 509 513 {ECO:0000244|PDB:4NHX}.
HELIX 518 525 {ECO:0000244|PDB:4NHX}.
STRAND 532 541 {ECO:0000244|PDB:4NHX}.
SEQUENCE 542 AA; 63246 MW; 8834BB200D5D8D85 CRC64;
MNGKRPAEPG PARVGKKGKK EVMAEFSDAV TEETLKKQVA EAWSRRTPFS HEVIVMDMDP
FLHCVIPNFI QSQDFLEGLQ KELMNLDFHE KYNDLYKFQQ SDDLKKRREP HISTLRKILF
EDFRSWLSDI SKIDLESTID MSCAKYEFTD ALLCHDDELE GRRIAFILYL VPPWDRSMGG
TLDLYSIDEH FQPKQIVKSL IPSWNKLVFF EVSPVSFHQV SEVLSEEKSR LSISGWFHGP
SLTRPPNYFE PPIPRSPHIP QDHEILYDWI NPTYLDMDYQ VQIQEEFEES SEILLKEFLK
PEKFTKVCEA LEHGHVEWSS RGPPNKRFYE KAEESKLPEI LKECMKLFRS EALFLLLSNF
TGLKLHFLAP SEEDEMNDKK EAETTDITEE GTSHSPPEPE NNQMAISNNS QQSNEQTDPE
PEENETKKES SVPMCQGELR HWKTGHYTLI HDHSKAEFAL DLILYCGCEG WEPEYGGFTS
YIAKGEDEEL LTVNPESNSL ALVYRDRETL KFVKHINHRS LEQKKTFPNR TGFWDFSFIY
YE


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EIAAB12621 Egl nine homolog 3,Egln3,HIF-PH3,HIF-prolyl hydroxylase 3,HPH-3,Hypoxia-inducible factor prolyl hydroxylase 3,Mouse,Mus musculus,SM-20
EIAAB12616 Egl nine homolog 1,Egln1,HIF-PH2,HIF-prolyl hydroxylase 2,HPH-2,Hypoxia-inducible factor prolyl hydroxylase 2,Mouse,Mus musculus,SM-20
CSB-EL016309BO Bovine 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1(OGFOD1) ELISA kit 96T
CSB-EL016309HU Human 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1(OGFOD1) ELISA kit 96T
EIAAB28708 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1,Bos taurus,Bovine,OGFOD1
CSB-EL016309MO Mouse 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1(OGFOD1) ELISA kit 96T
CSB-EL016309MO Mouse 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1(OGFOD1) ELISA kit SpeciesMouse 96T
EIAAB28709 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1,Kiaa1612,Mouse,Mus musculus,Ogfod1
CSB-EL016309BO Bovine 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1(OGFOD1) ELISA kit SpeciesBovine 96T
CSB-EL016309HU Human 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1(OGFOD1) ELISA kit SpeciesHuman 96T
OGFD1_BOVIN ELISA Kit FOR 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1; organism: Bovine; gene name: OGFOD1 96T
OGFR OGFOD1 Gene 2-oxoglutarate and iron-dependent oxygenase domain containing 1
CSB-EL016309MO Mouse 2-oxoglutarate and iron-dependent oxygenase domain containing 1 (OGFOD1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL016309HU Human 2-oxoglutarate and iron-dependent oxygenase domain containing 1 (OGFOD1) ELISA kit, Species Human, Sample Type serum, plasma 96T


 

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