HMOX2_HUMAN
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 03-AUG-2022, entry version 206.
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 [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210,
CC 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; 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; Q3SX64: ODF3L2; NbExp=3; IntAct=EBI-712096, EBI-6660184;
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. [P30519-1]
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; 307.
DR DIP; DIP-53564N; -.
DR IntAct; P30519; 140.
DR MINT; P30519; -.
DR STRING; 9606.ENSP00000477572; -.
DR BindingDB; P30519; -.
DR ChEMBL; CHEMBL2546; -.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB04912; Stannsoporfin.
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; P30519; -.
DR PeptideAtlas; P30519; -.
DR PRIDE; P30519; -.
DR ProteomicsDB; 47391; -.
DR ProteomicsDB; 54710; -. [P30519-1]
DR Antibodypedia; 11116; 654 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 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; 1424194at2759; -.
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; 18 hits in 1082 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 95 other tissues.
DR ExpressionAtlas; P30519; baseline and differential.
DR Genevisible; P30519; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0055072; P:iron ion homeostasis; 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; -; 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; PTHR10720; 1.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR PIRSF; PIRSF000343; Haem_Oase; 1.
DR PRINTS; PR00088; HAEMOXYGNASE.
DR SUPFAM; SSF48613; SSF48613; 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
