ID P4HA2_HUMAN Reviewed; 535 AA. AC O15460; D3DQ85; D3DQ86; Q8WWN0; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 10-JUN-2026, entry version 223. DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-2; DE Short=4-PH alpha-2; DE EC=1.14.11.2 {ECO:0000269|PubMed:9211872}; DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2; DE Flags: Precursor; GN Name=P4HA2; ORFNames=UNQ290/PRO330; 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 [MRNA] (ISOFORM IIB), FUNCTION, CATALYTIC ACTIVITY, RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, AND RP TISSUE SPECIFICITY. RC TISSUE=Lung; RX PubMed=9211872; DOI=10.1074/jbc.272.28.17342; RA Annunen P., Helaakoski T., Myllyharju J., Veijola J., Pihlajaniemi T., RA Kivirikko K.I.; RT "Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) RT and characterization of the type II enzyme tetramer. The alpha(I) and RT alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer."; RL J. Biol. Chem. 272:17342-17348(1997). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORMS IIA AND IIB). RX PubMed=11606192; DOI=10.1046/j.0014-2956.2001.02464.x; RA Nokelainen M., Nissi R., Kukkola L., Helaakoski T., Myllyharju J.; RT "Characterization of the human and mouse genes for the alpha subunit of RT type II prolyl 4-hydroxylase. Identification of a previously unknown RT alternatively spliced exon and its expression in various tissues."; RL Eur. J. Biochem. 268:5300-5309(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIA). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIA). RC TISSUE=Brain; 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). RN [6] RP INTERACTION WITH P4HB. RX PubMed=7753822; DOI=10.1073/pnas.92.10.4427; RA Helaakoski T., Annunen P., Vuori K., Macneil I.A., Pihlajaniemi T., RA Kivirikko K.I.; RT "Cloning, baculovirus expression, and characterization of a second mouse RT prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 RT tetramer with the protein disulfide-isomerase/beta subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 92:4427-4431(1995). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP INVOLVEMENT IN MYP25, VARIANTS IN MYP25 ARG-140; VAL-150 AND LYS-291, AND RP CHARACTERIZATION OF VARIANT MYP25 LYS-291. RX PubMed=25741866; DOI=10.1038/gim.2015.28; RA Guo H., Tong P., Liu Y., Xia L., Wang T., Tian Q., Li Y., Hu Y., Zheng Y., RA Jin X., Li Y., Xiong W., Tang B., Feng Y., Li J., Pan Q., Hu Z., Xia K.; RT "Mutations of P4HA2 encoding prolyl 4-hydroxylase 2 are associated with RT nonsyndromic high myopia."; RL Genet. Med. 17:300-306(2015). CC -!- FUNCTION: Catalyzes the post-translational formation of 4- CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other CC proteins. {ECO:0000269|PubMed:9211872}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-prolyl-[collagen] + 2-oxoglutarate + O2 = trans-4-hydroxy-L- CC prolyl-[collagen] + succinate + CO2; Xref=Rhea:RHEA:18945, Rhea:RHEA- CC COMP:11676, Rhea:RHEA-COMP:11680, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.2; CC Evidence={ECO:0000269|PubMed:9211872}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE- CC 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; CC Evidence={ECO:0000305|PubMed:9211872}; CC -!- ACTIVITY REGULATION: Inhibited by poly(L-proline) only at very high CC concentrations. {ECO:0000269|PubMed:9211872}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=22 uM for 2-oxoglutarate {ECO:0000269|PubMed:9211872}; CC -!- SUBUNIT: Heterotetramer of two alpha-2 chains and two beta chains CC (P4HB) (the beta chain is the multi-functional PDI), where P4HB plays CC the role of a structural subunit; this tetramer catalyzes the formation CC of 4-hydroxyproline in collagen. {ECO:0000269|PubMed:9211872}. CC -!- INTERACTION: CC O15460; Q2M1P5: KIF7; NbExp=3; IntAct=EBI-348033, EBI-2512228; CC O15460; P13674: P4HA1; NbExp=2; IntAct=EBI-348033, EBI-1237386; CC O15460; P07237: P4HB; NbExp=4; IntAct=EBI-348033, EBI-395883; CC O15460-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-10182841, EBI-10968534; CC O15460-2; Q13643: FHL3; NbExp=3; IntAct=EBI-10182841, EBI-741101; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=IIb; CC IsoId=O15460-1; Sequence=Displayed; CC Name=IIa; CC IsoId=O15460-2; Sequence=VSP_004506; CC -!- TISSUE SPECIFICITY: Expressed in the heart, placenta, lung and CC pancreas. {ECO:0000269|PubMed:9211872}. CC -!- DISEASE: Myopia 25, autosomal dominant (MYP25) [MIM:617238]: A CC refractive error of the eye, in which parallel rays from a distant CC object come to focus in front of the retina, vision being better for CC near objects than for far. {ECO:0000269|PubMed:25741866}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the P4HA family. {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; U90441; AAB71339.1; -; mRNA. DR EMBL; AJ314859; CAC85688.1; -; Genomic_DNA. DR EMBL; AJ314859; CAC85689.1; -; Genomic_DNA. DR EMBL; AY358970; AAQ89329.1; -; mRNA. DR EMBL; CH471062; EAW62341.1; -; Genomic_DNA. DR EMBL; CH471062; EAW62342.1; -; Genomic_DNA. DR EMBL; CH471062; EAW62343.1; -; Genomic_DNA. DR EMBL; CH471062; EAW62346.1; -; Genomic_DNA. DR EMBL; BC035813; AAH35813.1; -; mRNA. DR CCDS; CCDS34230.1; -. [O15460-2] DR CCDS; CCDS4151.1; -. [O15460-1] DR RefSeq; NP_001017974.1; NM_001017974.2. [O15460-2] DR RefSeq; NP_001136070.1; NM_001142598.2. [O15460-2] DR RefSeq; NP_001136071.1; NM_001142599.2. [O15460-1] DR RefSeq; NP_001352606.1; NM_001365677.2. [O15460-1] DR RefSeq; NP_001352607.1; NM_001365678.2. [O15460-2] DR RefSeq; NP_001352608.1; NM_001365679.2. [O15460-2] DR RefSeq; NP_001352609.1; NM_001365680.2. [O15460-2] DR RefSeq; NP_004190.1; NM_004199.3. [O15460-1] DR PDB; 6EVL; X-ray; 1.87 A; A=163-257. DR PDB; 6EVM; X-ray; 2.00 A; A=163-257. DR PDB; 6EVN; X-ray; 1.48 A; A=163-257. DR PDB; 6EVO; X-ray; 1.55 A; A=163-257. DR PDB; 6EVP; X-ray; 1.68 A; A=163-257. DR PDB; 7ZSC; X-ray; 3.85 A; A/B=282-535. DR PDB; 9HTD; X-ray; 1.75 A; A=163-257. DR PDBsum; 6EVL; -. DR PDBsum; 6EVM; -. DR PDBsum; 6EVN; -. DR PDBsum; 6EVO; -. DR PDBsum; 6EVP; -. DR PDBsum; 7ZSC; -. DR PDBsum; 9HTD; -. DR AlphaFoldDB; O15460; -. DR SMR; O15460; -. DR BioGRID; 114464; 154. DR FunCoup; O15460; 2728. DR IntAct; O15460; 158. DR MINT; O15460; -. DR NDEx; IQUERY-CP-P4HA2; 9 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000384999; -. DR ChEMBL; CHEMBL5640; -. DR DrugBank; DB00172; Proline. DR DrugBank; DB00139; Succinic acid. DR GlyCosmos; O15460; 3 sites, 2 glycans. DR GlyGen; O15460; 6 sites, 11 N-linked glycans (2 sites), 3 O-linked glycans (4 sites). DR iPTMnet; O15460; -. DR MetOSite; O15460; -. DR PhosphoSitePlus; O15460; -. DR BioMuta; P4HA2; -. DR jPOST; O15460; -. DR MassIVE; O15460; -. DR PaxDb; 9606-ENSP00000384999; -. DR PeptideAtlas; O15460; -. DR ProteomicsDB; 48680; -. [O15460-1] DR ProteomicsDB; 48681; -. [O15460-2] DR Pumba; O15460; -. DR Antibodypedia; 35136; 140 antibodies from 25 providers. DR DNASU; 8974; -. DR Ensembl; ENST00000166534.8; ENSP00000166534.4; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000360568.8; ENSP00000353772.3; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000379086.5; ENSP00000368379.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000379100.7; ENSP00000368394.2; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000379104.7; ENSP00000368398.2; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000401867.5; ENSP00000384999.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889324.1; ENSP00000559383.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889325.1; ENSP00000559384.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889326.1; ENSP00000559385.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889327.1; ENSP00000559386.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889328.1; ENSP00000559387.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889329.1; ENSP00000559388.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889330.1; ENSP00000559389.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889331.1; ENSP00000559390.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889332.1; ENSP00000559391.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889333.1; ENSP00000559392.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889334.1; ENSP00000559393.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889335.1; ENSP00000559394.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889336.1; ENSP00000559395.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889337.1; ENSP00000559396.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889339.1; ENSP00000559398.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889341.1; ENSP00000559400.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889342.1; ENSP00000559401.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889344.1; ENSP00000559403.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889345.1; ENSP00000559404.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889346.1; ENSP00000559405.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889347.1; ENSP00000559406.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889348.1; ENSP00000559407.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889349.1; ENSP00000559408.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889350.1; ENSP00000559409.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889351.1; ENSP00000559410.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889352.1; ENSP00000559411.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889353.1; ENSP00000559412.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889354.1; ENSP00000559413.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889355.1; ENSP00000559414.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000889356.1; ENSP00000559415.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889357.1; ENSP00000559416.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000889358.1; ENSP00000559417.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000944792.1; ENSP00000614851.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000944793.1; ENSP00000614852.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000944794.1; ENSP00000614853.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000944795.1; ENSP00000614854.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000944796.1; ENSP00000614855.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000944800.1; ENSP00000614859.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000944801.1; ENSP00000614860.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000944802.1; ENSP00000614861.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000944803.1; ENSP00000614862.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000944804.1; ENSP00000614863.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000944806.1; ENSP00000614865.1; ENSG00000072682.21. [O15460-1] DR Ensembl; ENST00000944807.1; ENSP00000614866.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000944808.1; ENSP00000614867.1; ENSG00000072682.21. [O15460-2] DR Ensembl; ENST00000944809.1; ENSP00000614868.1; ENSG00000072682.21. [O15460-1] DR GeneID; 8974; -. DR KEGG; hsa:8974; -. DR MANE-Select; ENST00000360568.8; ENSP00000353772.3; NM_001017974.2; NP_001017974.1. [O15460-2] DR UCSC; uc003kwg.4; human. [O15460-1] DR AGR; HGNC:8547; -. DR ClinPGx; PA32875; -. DR CTD; 8974; -. DR DisGeNET; 8974; -. DR GeneCards; P4HA2; -. DR HGNC; HGNC:8547; P4HA2. DR HPA; ENSG00000072682; Low tissue specificity. DR MalaCards; P4HA2; -. DR MIM; 600608; gene. DR MIM; 617238; phenotype. DR OpenTargets; ENSG00000072682; -. DR Orphanet; 397; Giant cell arteritis. DR VEuPathDB; HostDB:ENSG00000072682; -. DR eggNOG; KOG1591; Eukaryota. DR GeneTree; ENSGT00940000157695; -. DR HOGENOM; CLU_024155_1_0_1; -. DR InParanoid; O15460; -. DR OMA; VIWMEEA; -. DR OrthoDB; 420380at2759; -. DR PAN-GO; O15460; 2 GO annotations based on evolutionary models. DR PhylomeDB; O15460; -. DR BRENDA; 1.14.11.2; 2681. DR PathwayCommons; O15460; -. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-9918432; Maturation of DENV proteins. DR SignaLink; O15460; -. DR SIGNOR; O15460; -. DR Agora; ENSG00000072682; -. DR BioGRID-ORCS; 8974; 10 hits in 1153 CRISPR screens. DR ChiTaRS; P4HA2; human. DR GeneWiki; P4HA2; -. DR GenomeRNAi; 8974; -. DR Pharos; O15460; Tbio. DR PRO; PR:O15460; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; O15460; protein. DR Bgee; ENSG00000072682; Expressed in stromal cell of endometrium and 185 other cell types or tissues. DR ExpressionAtlas; O15460; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB. 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:0004656; F:procollagen-proline 4-dioxygenase activity; IDA:UniProtKB. DR FunFam; 1.25.40.10:FF:000006; Prolyl 4-hydroxylase subunit alpha 2; 1. DR FunFam; 2.60.120.620:FF:000001; Prolyl 4-hydroxylase subunit alpha 2; 1. DR Gene3D; 6.10.140.1460; -; 1. DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase_dom. DR InterPro; IPR013547; P4H_N. DR InterPro; IPR045054; P4HA-like. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR059068; TPR_P4H. DR InterPro; IPR019734; TPR_rpt. DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1. DR PANTHER; PTHR10869:SF244; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-2; 1. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR Pfam; PF08336; P4Ha_N; 1. DR Pfam; PF23558; TPR_P4H; 1. DR SMART; SM00702; P4Hc; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS50005; TPR; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Dioxygenase; Disease variant; KW Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; Oxidoreductase; KW Proteomics identification; Reference proteome; Signal; TPR repeat; KW Vitamin C. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..535 FT /note="Prolyl 4-hydroxylase subunit alpha-2" FT /id="PRO_0000022726" FT REPEAT 207..240 FT /note="TPR" FT DOMAIN 412..520 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 430 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 432 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 501 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 511 FT /ligand="2-oxoglutarate" FT /ligand_id="ChEBI:CHEBI:16810" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT MOD_RES 480 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q60716" FT CARBOHYD 115 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 264 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 436..451 FT /note="NDERDTFKHLGTGNRV -> RPFDSGLKTEGNRL (in isoform IIa)" FT /evidence="ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:15489334" FT /id="VSP_004506" FT VARIANT 140 FT /note="Q -> R (in MYP25; dbSNP:rs764211125)" FT /evidence="ECO:0000269|PubMed:25741866" FT /id="VAR_074026" FT VARIANT 150 FT /note="I -> V (in MYP25; uncertain significance; FT dbSNP:rs771208496)" FT /evidence="ECO:0000269|PubMed:25741866" FT /id="VAR_074027" FT VARIANT 291 FT /note="E -> K (in MYP25; decreases protein abundance; FT dbSNP:rs758872875)" FT /evidence="ECO:0000269|PubMed:25741866" FT /id="VAR_074028" FT HELIX 166..178 FT /evidence="ECO:0007829|PDB:6EVN" FT HELIX 182..197 FT /evidence="ECO:0007829|PDB:6EVN" FT HELIX 206..219 FT /evidence="ECO:0007829|PDB:6EVN" FT HELIX 223..236 FT /evidence="ECO:0007829|PDB:6EVN" FT HELIX 241..253 FT /evidence="ECO:0007829|PDB:6EVN" SQ SEQUENCE 535 AA; 60902 MW; FD04467B098F63CF CRC64; MKLWVSALLM AWFGVLSCVQ AEFFTSIGHM TDLIYAEKEL VQSLKEYILV EEAKLSKIKS WANKMEALTS KSAADAEGYL AHPVNAYKLV KRLNTDWPAL EDLVLQDSAA GFIANLSVQR QFFPTDEDEI GAAKALMRLQ DTYRLDPGTI SRGELPGTKY QAMLSVDDCF GMGRSAYNEG DYYHTVLWME QVLKQLDAGE EATTTKSQVL DYLSYAVFQL GDLHRALELT RRLLSLDPSH ERAGGNLRYF EQLLEEEREK TLTNQTEAEL ATPEGIYERP VDYLPERDVY ESLCRGEGVK LTPRRQKRLF CRYHHGNRAP QLLIAPFKEE DEWDSPHIVR YYDVMSDEEI ERIKEIAKPK LARATVRDPK TGVLTVASYR VSKSSWLEED DDPVVARVNR RMQHITGLTV KTAELLQVAN YGVGGQYEPH FDFSRNDERD TFKHLGTGNR VATFLNYMSD VEAGGATVFP DLGAAIWPKK GTAVFWYNLL RSGEGDYRTR HAACPVLVGC KWVSNKWFHE RGQEFLRPCG STEVD //