ID HMOX2_HUMAN Reviewed; 316 AA. AC P30519; A8MT35; D3DUD5; I3L430; O60605; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 24-JAN-2024, entry version 214. DE RecName: Full=Heme oxygenase 2; DE Short=HO-2; DE EC=1.14.14.18 {ECO:0000269|PubMed:1575508, ECO:0000269|PubMed:7890772}; DE Contains: DE RecName: Full=Heme oxygenase 2 soluble form {ECO:0000303|PubMed:7890772}; GN Name=HMOX2; Synonyms=HO2; 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 1), PROTEIN SEQUENCE OF 30-49, RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PROTEOLYTIC RP CLEAVAGE. RC TISSUE=Placenta; RX PubMed=7890772; DOI=10.1074/jbc.270.11.6345; RA Ishikawa K.; RT "Heme oxygenase-2. Properties of the heme complex of the purified tryptic RT fragment of recombinant human heme oxygenase-2."; RL J. Biol. Chem. 270:6345-6350(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND RP ACTIVITY REGULATION. RC TISSUE=Kidney; RX PubMed=1575508; DOI=10.1016/0003-9861(92)90481-b; RA McCoubrey W.K. Jr., Ewing J.F., Maines M.D.; RT "Human heme oxygenase-2: characterization and expression of a full-length RT cDNA and evidence suggesting that the two HO-2 transcripts may differ by RT choice of polyadenylation signal."; RL Arch. Biochem. Biophys. 295:13-20(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-137 AND LEU-146. RG NIEHS SNPs program; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-148 (ISOFORM 2). RA Hillier L., Clark N., Dubuque T., Elliston K., Hawkins M., Holman M., RA Hultman M., Kucaba T., Le M., Lennon G., Marra M., Parsons J., Rifkin L., RA Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R., Williamson A., RA Wohldmann P., Wilson R.; RT "The WashU-Merck EST project."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [9] RP PROTEIN SEQUENCE OF 2-17; 30-38; 48-59; 138-168; 206-214 AND 219-246, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=Colon carcinoma, and Ovarian carcinoma; RA Bienvenut W.V., Bilsland A.E., Keith W.N.; RL Submitted (JAN-2010) to UniProtKB. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-166. RC TISSUE=Intestine; RA Follett J., Ahn J.-Y.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-264, AND HEME-BINDING SITES. RX PubMed=17965015; DOI=10.1074/jbc.m707396200; RA Bianchetti C.M., Yi L., Ragsdale S.W., Phillips G.N. Jr.; RT "Comparison of apo- and heme-bound crystal structures of a truncated human RT heme oxygenase-2."; RL J. Biol. Chem. 282:37624-37631(2007). CC -!- FUNCTION: [Heme oxygenase 2]: Catalyzes the oxidative cleavage of heme CC at the alpha-methene bridge carbon, released as carbon monoxide (CO), CC to generate biliverdin IXalpha, while releasing the central heme iron CC chelate as ferrous iron. {ECO:0000269|PubMed:1575508, CC ECO:0000269|PubMed:7890772}. CC -!- FUNCTION: [Heme oxygenase 2 soluble form]: Catalyzes the oxidative CC cleavage of heme at the alpha-methene bridge carbon, released as carbon CC monoxide (CO), to generate biliverdin IXalpha, while releasing the CC central heme iron chelate as ferrous iron. CC {ECO:0000269|PubMed:7890772}. CC -!- CATALYTIC ACTIVITY: CC Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = CC biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, CC ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18; CC Evidence={ECO:0000269|PubMed:1575508, ECO:0000269|PubMed:7890772}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765; CC Evidence={ECO:0000305|PubMed:7890772}; CC -!- ACTIVITY REGULATION: Inhibited by metalloporphyrins such as Sn- and Zn- CC protoporphyrins. {ECO:0000269|PubMed:1575508}. CC -!- INTERACTION: CC P30519; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-712096, EBI-18899653; CC P30519; P05067: APP; NbExp=3; IntAct=EBI-712096, EBI-77613; CC P30519; Q13520: AQP6; NbExp=3; IntAct=EBI-712096, EBI-13059134; CC P30519; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-712096, EBI-11343438; CC P30519; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-712096, EBI-5280499; CC P30519; P07307-3: ASGR2; NbExp=3; IntAct=EBI-712096, EBI-12808270; CC P30519; Q14032: BAAT; NbExp=3; IntAct=EBI-712096, EBI-8994378; CC P30519; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-712096, EBI-747430; CC P30519; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-712096, EBI-10693038; CC P30519; Q9NQ89: C12orf4; NbExp=3; IntAct=EBI-712096, EBI-11090973; CC P30519; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-712096, EBI-18036948; CC P30519; O00257-3: CBX4; NbExp=3; IntAct=EBI-712096, EBI-4392727; CC P30519; P11912: CD79A; NbExp=3; IntAct=EBI-712096, EBI-7797864; CC P30519; Q3SX64: CIMAP1D; NbExp=3; IntAct=EBI-712096, EBI-6660184; CC P30519; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-712096, EBI-25836090; CC P30519; Q96BR5: COA7; NbExp=3; IntAct=EBI-712096, EBI-6269632; CC P30519; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-712096, EBI-17233035; CC P30519; Q9H2U1-3: DHX36; NbExp=3; IntAct=EBI-712096, EBI-25868628; CC P30519; Q15125: EBP; NbExp=3; IntAct=EBI-712096, EBI-3915253; CC P30519; O00472: ELL2; NbExp=3; IntAct=EBI-712096, EBI-395274; CC P30519; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-712096, EBI-18535450; CC P30519; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-712096, EBI-11037623; CC P30519; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-712096, EBI-781551; CC P30519; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-712096, EBI-18304435; CC P30519; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-712096, EBI-18938272; CC P30519; P06241: FYN; NbExp=3; IntAct=EBI-712096, EBI-515315; CC P30519; O00258: GET1; NbExp=3; IntAct=EBI-712096, EBI-18908258; CC P30519; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-712096, EBI-13345167; CC P30519; Q8TED1: GPX8; NbExp=3; IntAct=EBI-712096, EBI-11721746; CC P30519; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-712096, EBI-2868501; CC P30519; P48051: KCNJ6; NbExp=3; IntAct=EBI-712096, EBI-12017638; CC P30519; Q13571: LAPTM5; NbExp=3; IntAct=EBI-712096, EBI-2865663; CC P30519; Q8IYG6: LRRC56; NbExp=3; IntAct=EBI-712096, EBI-14752528; CC P30519; O14880: MGST3; NbExp=3; IntAct=EBI-712096, EBI-724754; CC P30519; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-712096, EBI-25835557; CC P30519; Q6IN84-2: MRM1; NbExp=3; IntAct=EBI-712096, EBI-25835707; CC P30519; P36639-4: NUDT1; NbExp=3; IntAct=EBI-712096, EBI-25834643; CC P30519; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-712096, EBI-741048; CC P30519; P36954: POLR2I; NbExp=3; IntAct=EBI-712096, EBI-395202; CC P30519; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-712096, EBI-10192441; CC P30519; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-712096, EBI-18397230; CC P30519; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-712096, EBI-10248967; CC P30519; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-712096, EBI-3920694; CC P30519; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-712096, EBI-9089805; CC P30519; O95470: SGPL1; NbExp=3; IntAct=EBI-712096, EBI-1046170; CC P30519; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-712096, EBI-10262251; CC P30519; Q13573: SNW1; NbExp=3; IntAct=EBI-712096, EBI-632715; CC P30519; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-712096, EBI-2659201; CC P30519; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-712096, EBI-17280858; CC P30519; P27105: STOM; NbExp=3; IntAct=EBI-712096, EBI-1211440; CC P30519; P21579: SYT1; NbExp=3; IntAct=EBI-712096, EBI-524909; CC P30519; P54274-2: TERF1; NbExp=3; IntAct=EBI-712096, EBI-711018; CC P30519; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-712096, EBI-8638294; CC P30519; Q9Y320: TMX2; NbExp=3; IntAct=EBI-712096, EBI-6447886; CC P30519; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-712096, EBI-11525489; CC P30519; P49459: UBE2A; NbExp=3; IntAct=EBI-712096, EBI-2339348; CC P30519; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-712096, EBI-1055364; CC P30519; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-712096, EBI-14104088; CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305|PubMed:7890772}; CC Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P09601}. Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:P09601}; Single-pass type IV membrane protein CC {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P30519-1; Sequence=Displayed; CC Name=2; CC IsoId=P30519-2; Sequence=VSP_055031; CC -!- PTM: A soluble form arises by proteolytic removal of the membrane CC anchor. {ECO:0000305|PubMed:7890772}. CC -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=W38932; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/hmox2/"; 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; D21243; BAA04789.1; -; mRNA. DR EMBL; S34389; AAB22110.2; -; mRNA. DR EMBL; BT019788; AAV38591.1; -; mRNA. DR EMBL; AY771350; AAV28730.1; -; Genomic_DNA. DR EMBL; AC007606; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471112; EAW85299.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85300.1; -; Genomic_DNA. DR EMBL; BC002396; AAH02396.1; -; mRNA. DR EMBL; W38932; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF051306; AAC05297.1; -; mRNA. DR CCDS; CCDS10517.1; -. [P30519-1] DR CCDS; CCDS66931.1; -. [P30519-2] DR PIR; I60119; I60119. DR PIR; S21700; S21700. DR RefSeq; NP_001120676.1; NM_001127204.1. [P30519-1] DR RefSeq; NP_001120677.1; NM_001127205.1. [P30519-1] DR RefSeq; NP_001120678.1; NM_001127206.2. [P30519-1] DR RefSeq; NP_001273196.1; NM_001286267.1. DR RefSeq; NP_001273197.1; NM_001286268.1. [P30519-1] DR RefSeq; NP_001273198.1; NM_001286269.1. [P30519-1] DR RefSeq; NP_001273199.1; NM_001286270.1. [P30519-1] DR RefSeq; NP_001273200.1; NM_001286271.1. [P30519-2] DR RefSeq; NP_002125.3; NM_002134.3. [P30519-1] DR RefSeq; XP_016878685.1; XM_017023196.1. [P30519-1] DR RefSeq; XP_016878686.1; XM_017023197.1. DR PDB; 2Q32; X-ray; 2.40 A; A/B=1-264. DR PDB; 2QPP; X-ray; 2.61 A; A/B=1-264. DR PDB; 2RGZ; X-ray; 2.61 A; A/B=1-264. DR PDB; 4WMH; X-ray; 2.50 A; A=31-237. DR PDB; 5UC8; X-ray; 2.00 A; A/B/C/D=30-242. DR PDB; 5UC9; X-ray; 1.90 A; A/B/C/D=30-242. DR PDB; 5UCA; X-ray; 2.12 A; A/B/C/D=30-242. DR PDBsum; 2Q32; -. DR PDBsum; 2QPP; -. DR PDBsum; 2RGZ; -. DR PDBsum; 4WMH; -. DR PDBsum; 5UC8; -. DR PDBsum; 5UC9; -. DR PDBsum; 5UCA; -. DR AlphaFoldDB; P30519; -. DR SMR; P30519; -. DR BioGRID; 109406; 317. DR DIP; DIP-53564N; -. DR IntAct; P30519; 142. DR MINT; P30519; -. DR STRING; 9606.ENSP00000477572; -. DR BindingDB; P30519; -. DR ChEMBL; CHEMBL2546; -. DR DrugBank; DB00157; NADH. DR DrugBank; DB04912; Stannsoporfin. DR GlyCosmos; P30519; 2 sites, 1 glycan. DR GlyGen; P30519; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P30519; -. DR MetOSite; P30519; -. DR PhosphoSitePlus; P30519; -. DR SwissPalm; P30519; -. DR BioMuta; HMOX2; -. DR DMDM; 1170328; -. DR EPD; P30519; -. DR jPOST; P30519; -. DR MassIVE; P30519; -. DR MaxQB; P30519; -. DR PaxDb; 9606-ENSP00000477572; -. DR PeptideAtlas; P30519; -. DR ProteomicsDB; 47391; -. DR ProteomicsDB; 54710; -. [P30519-1] DR Pumba; P30519; -. DR Antibodypedia; 11116; 737 antibodies from 40 providers. DR DNASU; 3163; -. DR Ensembl; ENST00000219700.10; ENSP00000219700.6; ENSG00000103415.12. [P30519-1] DR Ensembl; ENST00000398595.7; ENSP00000381595.3; ENSG00000103415.12. [P30519-1] DR Ensembl; ENST00000406590.6; ENSP00000385100.2; ENSG00000103415.12. [P30519-1] DR Ensembl; ENST00000414777.5; ENSP00000391637.1; ENSG00000103415.12. [P30519-1] DR Ensembl; ENST00000458134.7; ENSP00000394103.3; ENSG00000103415.12. [P30519-1] DR Ensembl; ENST00000570646.6; ENSP00000459214.1; ENSG00000103415.12. [P30519-1] DR Ensembl; ENST00000575120.5; ENSP00000460926.1; ENSG00000103415.12. [P30519-2] DR Ensembl; ENST00000612525.4; ENSP00000481295.1; ENSG00000277424.4. [P30519-1] DR Ensembl; ENST00000615778.4; ENSP00000484422.1; ENSG00000277424.4. [P30519-1] DR Ensembl; ENST00000619528.4; ENSP00000484423.1; ENSG00000103415.12. [P30519-1] DR Ensembl; ENST00000619913.4; ENSP00000484467.1; ENSG00000103415.12. [P30519-1] DR Ensembl; ENST00000620445.3; ENSP00000478785.1; ENSG00000277424.4. [P30519-1] DR Ensembl; ENST00000621065.4; ENSP00000481811.1; ENSG00000277424.4. [P30519-1] DR Ensembl; ENST00000622146.4; ENSP00000483319.2; ENSG00000277424.4. [P30519-1] DR Ensembl; ENST00000631540.1; ENSP00000487673.1; ENSG00000277424.4. [P30519-1] DR Ensembl; ENST00000631677.1; ENSP00000488579.1; ENSG00000277424.4. [P30519-1] DR Ensembl; ENST00000632458.1; ENSP00000488880.1; ENSG00000277424.4. [P30519-1] DR Ensembl; ENST00000633319.1; ENSP00000488769.1; ENSG00000277424.4. [P30519-2] DR GeneID; 3163; -. DR KEGG; hsa:3163; -. DR MANE-Select; ENST00000570646.6; ENSP00000459214.1; NM_002134.4; NP_002125.3. DR UCSC; uc002cwq.5; human. [P30519-1] DR AGR; HGNC:5014; -. DR CTD; 3163; -. DR DisGeNET; 3163; -. DR GeneCards; HMOX2; -. DR HGNC; HGNC:5014; HMOX2. DR HPA; ENSG00000103415; Low tissue specificity. DR MIM; 141251; gene. DR neXtProt; NX_P30519; -. DR OpenTargets; ENSG00000103415; -. DR PharmGKB; PA29342; -. DR VEuPathDB; HostDB:ENSG00000103415; -. DR eggNOG; KOG4480; Eukaryota. DR GeneTree; ENSGT00390000017673; -. DR HOGENOM; CLU_057050_0_1_1; -. DR InParanoid; P30519; -. DR OMA; ANRAFEY; -. DR OrthoDB; 1366343at2759; -. DR PhylomeDB; P30519; -. DR TreeFam; TF314786; -. DR BRENDA; 1.14.14.18; 2681. DR PathwayCommons; P30519; -. DR Reactome; R-HSA-189483; Heme degradation. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-917937; Iron uptake and transport. DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1. DR SignaLink; P30519; -. DR SIGNOR; P30519; -. DR BioGRID-ORCS; 3163; 19 hits in 1171 CRISPR screens. DR ChiTaRS; HMOX2; human. DR EvolutionaryTrace; P30519; -. DR GeneWiki; HMOX2; -. DR GenomeRNAi; 3163; -. DR Pharos; P30519; Tchem. DR PRO; PR:P30519; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P30519; Protein. DR Bgee; ENSG00000103415; Expressed in right testis and 97 other cell types or tissues. DR ExpressionAtlas; P30519; baseline and differential. DR Genevisible; P30519; HS. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042167; P:heme catabolic process; IBA:GO_Central. DR GO; GO:0006788; P:heme oxidation; IBA:GO_Central. DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR CDD; cd19165; HemeO; 1. DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1. DR InterPro; IPR002051; Haem_Oase. DR InterPro; IPR016053; Haem_Oase-like. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR018207; Haem_oxygenase_CS. DR PANTHER; PTHR10720; HEME OXYGENASE; 1. DR PANTHER; PTHR10720:SF2; HEME OXYGENASE 2; 1. DR Pfam; PF01126; Heme_oxygenase; 1. DR PIRSF; PIRSF000343; Haem_Oase; 1. DR PRINTS; PR00088; HAEMOXYGNASE. DR SUPFAM; SSF48613; Heme oxygenase-like; 1. DR PROSITE; PS00593; HEME_OXYGENASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:25944712" FT CHAIN 2..316 FT /note="Heme oxygenase 2" FT /id="PRO_0000209691" FT CHAIN 2..295 FT /note="Heme oxygenase 2 soluble form" FT /evidence="ECO:0000305|PubMed:7890772" FT /id="PRO_0000455626" FT TOPO_DOM 2..295 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P09601" FT TRANSMEM 296..316 FT /note="Helical; Anchor for type IV membrane protein" FT /evidence="ECO:0000255" FT REPEAT 264..269 FT /note="HRM 1" FT REPEAT 281..286 FT /note="HRM 2" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..29 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 45 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:17965015, FT ECO:0007744|PDB:2QPP" FT BINDING 154 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:17965015, FT ECO:0007744|PDB:2QPP" FT BINDING 199 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:17965015, FT ECO:0007744|PDB:2QPP" FT BINDING 203 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000269|PubMed:17965015, FT ECO:0007744|PDB:2QPP" FT SITE 160 FT /note="Important for catalytic activity" FT /evidence="ECO:0000250|UniProtKB:P09601" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:25944712" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..29 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.8" FT /id="VSP_055031" FT VARIANT 137 FT /note="R -> Q (in dbSNP:rs17884623)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_021067" FT VARIANT 146 FT /note="P -> L (in dbSNP:rs17880805)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_021068" FT CONFLICT 107 FT /note="E -> T (in Ref. 8; W38932)" FT /evidence="ECO:0000305" FT CONFLICT 165..166 FT /note="QV -> KC (in Ref. 10; AAC05297)" FT /evidence="ECO:0000305" FT CONFLICT 222 FT /note="Missing (in Ref. 2; AAB22110)" FT /evidence="ECO:0000305" FT CONFLICT 276 FT /note="Missing (in Ref. 2; AAB22110)" FT /evidence="ECO:0000305" FT CONFLICT 281..288 FT /note="SCPFRTAM -> LSLPTSY (in Ref. 2; AAB22110)" FT /evidence="ECO:0000305" FT HELIX 33..49 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 52..58 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 64..87 FT /evidence="ECO:0007829|PDB:5UC9" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:5UC9" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 100..103 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 106..117 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 121..124 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 129..144 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 149..175 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 195..207 FT /evidence="ECO:0007829|PDB:5UC9" FT HELIX 213..238 FT /evidence="ECO:0007829|PDB:5UC9" FT TURN 243..247 FT /evidence="ECO:0007829|PDB:2Q32" SQ SEQUENCE 316 AA; 36033 MW; BF4B6A341F1A81AC CRC64; MSAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE DGFPVHDGKG DMRKCPFYAA EQDKGALEGS SCPFRTAMAV LRKPSLQFIL AAGVALAAGL LAWYYM //