OGFD2_HUMAN
ID OGFD2_HUMAN Reviewed; 350 AA.
AC Q6N063; B3KT24; Q4KN13; Q6N023; Q9H8K6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2;
DE EC=1.14.11.-;
GN Name=OGFOD2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Colon endothelium, and Fetal liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC Q6N063-2; P55212: CASP6; NbExp=3; IntAct=EBI-22006224, EBI-718729;
CC Q6N063-2; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-22006224, EBI-745535;
CC Q6N063-2; O00291: HIP1; NbExp=3; IntAct=EBI-22006224, EBI-473886;
CC Q6N063-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-22006224, EBI-21591415;
CC Q6N063-2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-22006224, EBI-5280197;
CC Q6N063-2; P62826: RAN; NbExp=3; IntAct=EBI-22006224, EBI-286642;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6N063-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6N063-2; Sequence=VSP_025856, VSP_025857;
CC Name=3;
CC IsoId=Q6N063-3; Sequence=VSP_025858, VSP_025859;
CC Name=4;
CC IsoId=Q6N063-4; Sequence=VSP_025855;
CC -!- SIMILARITY: Belongs to the OGFOD2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE45849.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=CAE45849.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK023553; BAB14610.1; -; mRNA.
DR EMBL; AK094820; BAG52936.1; -; mRNA.
DR EMBL; CR457316; CAG33597.1; -; mRNA.
DR EMBL; BX640675; CAE45807.1; -; mRNA.
DR EMBL; BX640734; CAE45849.1; ALT_SEQ; mRNA.
DR EMBL; CH471054; EAW98364.1; -; Genomic_DNA.
DR EMBL; BC098119; AAH98119.1; -; mRNA.
DR EMBL; BC098293; AAH98293.1; -; mRNA.
DR EMBL; BC101940; AAI01941.1; -; mRNA.
DR EMBL; BC105637; AAI05638.1; -; mRNA.
DR CCDS; CCDS41855.1; -. [Q6N063-2]
DR CCDS; CCDS76617.1; -. [Q6N063-1]
DR CCDS; CCDS76618.1; -. [Q6N063-4]
DR RefSeq; NP_001291762.1; NM_001304833.1. [Q6N063-1]
DR RefSeq; NP_001291763.1; NM_001304834.1. [Q6N063-4]
DR RefSeq; NP_001291764.1; NM_001304835.1. [Q6N063-4]
DR RefSeq; NP_001291765.1; NM_001304836.1. [Q6N063-4]
DR RefSeq; NP_001291766.1; NM_001304837.1. [Q6N063-4]
DR RefSeq; NP_001291767.1; NM_001304838.1. [Q6N063-4]
DR RefSeq; NP_078899.1; NM_024623.2. [Q6N063-2]
DR AlphaFoldDB; Q6N063; -.
DR SMR; Q6N063; -.
DR BioGRID; 122801; 6.
DR IntAct; Q6N063; 9.
DR STRING; 9606.ENSP00000380544; -.
DR DrugBank; DB00126; Ascorbic acid.
DR iPTMnet; Q6N063; -.
DR PhosphoSitePlus; Q6N063; -.
DR BioMuta; OGFOD2; -.
DR DMDM; 156633666; -.
DR EPD; Q6N063; -.
DR jPOST; Q6N063; -.
DR MassIVE; Q6N063; -.
DR MaxQB; Q6N063; -.
DR PaxDb; Q6N063; -.
DR PeptideAtlas; Q6N063; -.
DR PRIDE; Q6N063; -.
DR ProteomicsDB; 66608; -. [Q6N063-1]
DR ProteomicsDB; 66609; -. [Q6N063-2]
DR ProteomicsDB; 66610; -. [Q6N063-3]
DR ProteomicsDB; 66611; -. [Q6N063-4]
DR Antibodypedia; 31731; 132 antibodies from 26 providers.
DR DNASU; 79676; -.
DR Ensembl; ENST00000228922.11; ENSP00000228922.7; ENSG00000111325.16. [Q6N063-1]
DR Ensembl; ENST00000397389.6; ENSP00000380544.2; ENSG00000111325.16. [Q6N063-2]
DR Ensembl; ENST00000454694.6; ENSP00000394175.2; ENSG00000111325.16. [Q6N063-4]
DR Ensembl; ENST00000536150.5; ENSP00000438327.1; ENSG00000111325.16. [Q6N063-4]
DR Ensembl; ENST00000538628.5; ENSP00000444608.1; ENSG00000111325.16. [Q6N063-4]
DR Ensembl; ENST00000538755.5; ENSP00000442817.1; ENSG00000111325.16. [Q6N063-4]
DR Ensembl; ENST00000540324.5; ENSP00000439667.1; ENSG00000111325.16. [Q6N063-3]
DR Ensembl; ENST00000545317.5; ENSP00000438192.1; ENSG00000111325.16. [Q6N063-4]
DR Ensembl; ENST00000545612.5; ENSP00000444436.1; ENSG00000111325.16. [Q6N063-4]
DR GeneID; 79676; -.
DR KEGG; hsa:79676; -.
DR MANE-Select; ENST00000228922.12; ENSP00000228922.7; NM_001304833.2; NP_001291762.1.
DR UCSC; uc001uds.2; human. [Q6N063-1]
DR CTD; 79676; -.
DR GeneCards; OGFOD2; -.
DR HGNC; HGNC:25823; OGFOD2.
DR HPA; ENSG00000111325; Low tissue specificity.
DR neXtProt; NX_Q6N063; -.
DR OpenTargets; ENSG00000111325; -.
DR PharmGKB; PA143485569; -.
DR VEuPathDB; HostDB:ENSG00000111325; -.
DR eggNOG; KOG1971; Eukaryota.
DR GeneTree; ENSGT00940000153974; -.
DR HOGENOM; CLU_045835_1_0_1; -.
DR InParanoid; Q6N063; -.
DR OMA; FYTCSCF; -.
DR OrthoDB; 756511at2759; -.
DR PhylomeDB; Q6N063; -.
DR TreeFam; TF329650; -.
DR PathwayCommons; Q6N063; -.
DR SignaLink; Q6N063; -.
DR BioGRID-ORCS; 79676; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; OGFOD2; human.
DR GenomeRNAi; 79676; -.
DR Pharos; Q6N063; Tdark.
DR PRO; PR:Q6N063; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6N063; protein.
DR Bgee; ENSG00000111325; Expressed in right uterine tube and 97 other tissues.
DR ExpressionAtlas; Q6N063; baseline and differential.
DR Genevisible; Q6N063; HS.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..350
FT /note="2-oxoglutarate and iron-dependent oxygenase domain-
FT containing protein 2"
FT /id="PRO_0000288978"
FT DOMAIN 215..309
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 290
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 300
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025855"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_025856"
FT VAR_SEQ 61..62
FT /note="LA -> MV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_025857"
FT VAR_SEQ 64
FT /note="L -> WPQEDGRPHLVTTLCHPSLSRRWSGGSGWGRSQQLGKPSSRVPTTRH
FT GLRSTTHCRMQLWPPSSWP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025858"
FT VAR_SEQ 65..350
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025859"
FT CONFLICT 244
FT /note="N -> S (in Ref. 2; CAE45807)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="A -> T (in Ref. 5; AAH98119/AAI01941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38996 MW; 651D0F07A32EBB66 CRC64;
MATVGAPRHF CRCACFCTDN LYVARYGLHV RFRGEQQLRR DYGPILRSRG CVSAKDFQQL
LAELEQEVER RQRLGQESAA RKALIASSYH PARPEVYDSL QDAALAPEFL AVTEYSVSPD
ADLKGLLQRL ETVSEEKRIY RVPVFTAPFC QALLEELEHF EQSDMPKGRP NTMNNYGVLL
HELGLDEPLM TPLRERFLQP LMALLYPDCG GGRLDSHRAF VVKYAPGQDL ELGCHYDNAE
LTLNVALGKV FTGGALYFGG LFQAPTALTE PLEVEHVVGQ GVLHRGGQLH GARPLGTGER
WNLVVWLRAS AVRNSLCPMC CREPDLVDDE GFGDGFTREE PATVDVCALT
