HMOX1_HUMAN
ID HMOX1_HUMAN Reviewed; 288 AA.
AC P09601;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Heme oxygenase 1;
DE Short=HO-1;
DE EC=1.14.14.18 {ECO:0000269|PubMed:11121422, ECO:0000269|PubMed:7703255};
DE Contains:
DE RecName: Full=Heme oxygenase 1 soluble form {ECO:0000303|PubMed:7703255};
GN Name=HMOX1; Synonyms=HO, HO1;
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], AND INDUCTION.
RX PubMed=3345742; DOI=10.1111/j.1432-1033.1988.tb13811.x;
RA Yoshida T., Biro P., Cohen T., Mueller R.M., Shibahara S.;
RT "Human heme oxygenase cDNA and induction of its mRNA by hemin.";
RL Eur. J. Biochem. 171:457-461(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-7.
RG SeattleSNPs variation discovery resource;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-103, AND INDUCTION.
RC TISSUE=Foreskin;
RX PubMed=2911585; DOI=10.1073/pnas.86.1.99;
RA Keyse S.M., Tyrrell R.M.;
RT "Heme oxygenase is the major 32-kDa stress protein induced in human skin
RT fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:99-103(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=2537723; DOI=10.1111/j.1432-1033.1989.tb14583.x;
RA Shibahara S., Sato M., Muller R.M., Yoshida T.;
RT "Structural organization of the human heme oxygenase gene and the function
RT of its promoter.";
RL Eur. J. Biochem. 179:557-563(1989).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=7703255; DOI=10.1021/bi00013a034;
RA Wilks A., Black S.M., Miller W.L., Ortiz de Montellano P.R.;
RT "Expression and characterization of truncated human heme oxygenase (hHO-1)
RT and a fusion protein of hHO-1 with human cytochrome P450 reductase.";
RL Biochemistry 34:4421-4427(1995).
RN [8]
RP INVOLVEMENT IN HMOX1D.
RX PubMed=9884342; DOI=10.1172/jci4165;
RA Yachie A., Niida Y., Wada T., Igarashi N., Kaneda H., Toma T., Ohta K.,
RA Kasahara Y., Koizumi S.;
RT "Oxidative stress causes enhanced endothelial cell injury in human heme
RT oxygenase-1 deficiency.";
RL J. Clin. Invest. 103:129-135(1999).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-140, AND SITE.
RX PubMed=11121422; DOI=10.1074/jbc.m010349200;
RA Lightning L.K., Huang H., Moenne-Loccoz P., Loehr T.M., Schuller D.J.,
RA Poulos T.L., de Montellano P.R.;
RT "Disruption of an active site hydrogen bond converts human heme oxygenase-1
RT into a peroxidase.";
RL J. Biol. Chem. 276:10612-10619(2001).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP REVIEW ON ANTIAPOPTOTIC FUNCTION.
RX PubMed=20055707; DOI=10.1146/annurev.pharmtox.010909.105600;
RA Gozzelino R., Jeney V., Soares M.P.;
RT "Mechanisms of cell protection by heme oxygenase-1.";
RL Annu. Rev. Pharmacol. Toxicol. 50:323-354(2010).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=20855888; DOI=10.1074/jbc.m110.170324;
RA Datta D., Banerjee P., Gasser M., Waaga-Gasser A.M., Pal S.;
RT "CXCR3-B can mediate growth-inhibitory signals in human renal cancer cells
RT by down-regulating the expression of heme oxygenase-1.";
RL J. Biol. Chem. 285:36842-36848(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=22419571; DOI=10.3324/haematol.2012.063651;
RA Gottlieb Y., Truman M., Cohen L.A., Leichtmann-Bardoogo Y.,
RA Meyron-Holtz E.G.;
RT "Endoplasmic reticulum anchored heme-oxygenase 1 faces the cytosol.";
RL Haematologica 97:1489-1493(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS).
RX PubMed=10467099; DOI=10.1038/12319;
RA Schuller D.J., Wilks A., Ortiz de Montellano P.R., Poulos T.L.;
RT "Crystal structure of human heme oxygenase-1.";
RL Nat. Struct. Biol. 6:860-867(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-233 OF MUTANT ALA-140,
RP HEME-BINDING SITES, AND MUTAGENESIS OF ASP-140.
RX PubMed=12842469; DOI=10.1016/s0022-2836(03)00578-3;
RA Lad L., Wang J., Li H., Friedman J., Bhaskar B., Ortiz de Montellano P.R.,
RA Poulos T.L.;
RT "Crystal structures of the ferric, ferrous, and ferrous-NO forms of the
RT Asp140Ala mutant of human heme oxygenase-1: catalytic implications.";
RL J. Mol. Biol. 330:527-538(2003).
CC -!- FUNCTION: [Heme oxygenase 1]: 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 (PubMed:7703255, PubMed:11121422). Affords
CC protection against programmed cell death and this cytoprotective effect
CC relies on its ability to catabolize free heme and prevent it from
CC sensitizing cells to undergo apoptosis (PubMed:20055707).
CC {ECO:0000269|PubMed:11121422, ECO:0000269|PubMed:7703255,
CC ECO:0000303|PubMed:20055707}.
CC -!- FUNCTION: [Heme oxygenase 1 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:7703255}.
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:11121422, ECO:0000269|PubMed:7703255};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765;
CC Evidence={ECO:0000305|PubMed:7703255};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Heme oxygenase 1]:
CC Kinetic parameters:
CC KM=6 uM for heme b {ECO:0000269|PubMed:7703255};
CC Vmax=102 nmol/h/mg enzyme for heme b {ECO:0000269|PubMed:7703255};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Heme oxygenase 1 soluble form]:
CC Kinetic parameters:
CC KM=3 uM for heme b {ECO:0000269|PubMed:7703255};
CC Vmax=40 nmol/h/mg enzyme for heme b {ECO:0000269|PubMed:7703255};
CC -!- INTERACTION:
CC P09601; Q13520: AQP6; NbExp=3; IntAct=EBI-2806151, EBI-13059134;
CC P09601; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-2806151, EBI-11343438;
CC P09601; P11912: CD79A; NbExp=3; IntAct=EBI-2806151, EBI-7797864;
CC P09601; O75208: COQ9; NbExp=3; IntAct=EBI-2806151, EBI-724524;
CC P09601; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-2806151, EBI-18013275;
CC P09601; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-2806151, EBI-17233035;
CC P09601; P49447: CYB561; NbExp=3; IntAct=EBI-2806151, EBI-8646596;
CC P09601; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-2806151, EBI-8637742;
CC P09601; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-2806151, EBI-18535450;
CC P09601; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-2806151, EBI-11037623;
CC P09601; Q9H5J4: ELOVL6; NbExp=3; IntAct=EBI-2806151, EBI-12821617;
CC P09601; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2806151, EBI-781551;
CC P09601; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-2806151, EBI-18636064;
CC P09601; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2806151, EBI-18304435;
CC P09601; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-2806151, EBI-18938272;
CC P09601; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2806151, EBI-13345167;
CC P09601; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-2806151, EBI-10266796;
CC P09601; Q15800: MSMO1; NbExp=3; IntAct=EBI-2806151, EBI-949102;
CC P09601; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-2806151, EBI-716063;
CC P09601; Q9NUX5: POT1; NbExp=2; IntAct=EBI-2806151, EBI-752420;
CC P09601; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-2806151, EBI-2855401;
CC P09601; O60669: SLC16A7; NbExp=3; IntAct=EBI-2806151, EBI-3921243;
CC P09601; Q16623: STX1A; NbExp=4; IntAct=EBI-2806151, EBI-712466;
CC P09601; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-2806151, EBI-12947623;
CC P09601; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-2806151, EBI-6448756;
CC P09601; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2806151, EBI-8638294;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22419571}; Single-pass type IV membrane protein
CC {ECO:0000255}; Cytoplasmic side {ECO:0000269|PubMed:22419571}.
CC -!- TISSUE SPECIFICITY: Expressed at higher levels in renal cancer tissue
CC than in normal tissue (at protein level).
CC {ECO:0000269|PubMed:20855888}.
CC -!- INDUCTION: Heme oxygenase 1 activity is highly inducible by its
CC substrate heme and by various non-heme substances such as heavy metals,
CC bromobenzene, endotoxin, oxidizing agents and UVA.
CC {ECO:0000269|PubMed:2911585, ECO:0000269|PubMed:3345742}.
CC -!- PTM: A soluble form arises by proteolytic removal of the membrane
CC anchor. {ECO:0000305|PubMed:7703255}.
CC -!- DISEASE: Heme oxygenase 1 deficiency (HMOX1D) [MIM:614034]: A disease
CC characterized by impaired stress hematopoiesis, resulting in marked
CC erythrocyte fragmentation and intravascular hemolysis, coagulation
CC abnormalities, endothelial damage, and iron deposition in renal and
CC hepatic tissues. Clinical features include persistent hemolytic anemia,
CC asplenia, nephritis, generalized erythematous rash, growth retardation
CC and hepatomegaly. {ECO:0000269|PubMed:9884342}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/hmox1/";
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DR EMBL; X06985; CAA30045.1; -; mRNA.
DR EMBL; CR456505; CAG30391.1; -; mRNA.
DR EMBL; AY460337; AAR23262.1; -; Genomic_DNA.
DR EMBL; Z82244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M23041; AAA50403.1; -; mRNA.
DR EMBL; X14782; CAA32886.1; -; Genomic_DNA.
DR CCDS; CCDS13914.1; -.
DR PIR; S00325; S00325.
DR RefSeq; NP_002124.1; NM_002133.2.
DR PDB; 1N3U; X-ray; 2.58 A; A/B=1-233.
DR PDB; 1N45; X-ray; 1.50 A; A/B=1-233.
DR PDB; 1NI6; X-ray; 2.10 A; A/B/C/D=1-224.
DR PDB; 1OYK; X-ray; 2.59 A; A/B=1-233.
DR PDB; 1OYL; X-ray; 1.59 A; A/B=1-233.
DR PDB; 1OZE; X-ray; 2.19 A; A/B=1-233.
DR PDB; 1OZL; X-ray; 1.58 A; A/B=1-233.
DR PDB; 1OZR; X-ray; 1.74 A; A/B=1-233.
DR PDB; 1OZW; X-ray; 1.55 A; A/B=1-233.
DR PDB; 1S13; X-ray; 2.29 A; A/B=1-233.
DR PDB; 1S8C; X-ray; 2.19 A; A/B/C/D=1-233.
DR PDB; 1T5P; X-ray; 2.11 A; A/B=1-233.
DR PDB; 1TWN; X-ray; 2.20 A; A/B=1-233.
DR PDB; 1TWR; X-ray; 2.10 A; A/B=1-233.
DR PDB; 1XJZ; X-ray; 1.88 A; A/B=1-233.
DR PDB; 1XK0; X-ray; 2.18 A; A/B=1-233.
DR PDB; 1XK1; X-ray; 2.08 A; A/B=1-233.
DR PDB; 1XK2; X-ray; 2.20 A; A/B=1-233.
DR PDB; 1XK3; X-ray; 2.08 A; A/B=1-233.
DR PDB; 3CZY; X-ray; 1.54 A; A/B=1-233.
DR PDB; 3HOK; X-ray; 2.19 A; A/B=1-233.
DR PDB; 3K4F; X-ray; 2.17 A; A/B=1-233.
DR PDB; 3TGM; X-ray; 2.85 A; A/B=1-233.
DR PDB; 4WD4; X-ray; 2.95 A; A/B/C/D=1-288.
DR PDB; 5BTQ; X-ray; 2.08 A; A/B=1-233.
DR PDB; 6EHA; X-ray; 2.00 A; A/B=1-288.
DR PDBsum; 1N3U; -.
DR PDBsum; 1N45; -.
DR PDBsum; 1NI6; -.
DR PDBsum; 1OYK; -.
DR PDBsum; 1OYL; -.
DR PDBsum; 1OZE; -.
DR PDBsum; 1OZL; -.
DR PDBsum; 1OZR; -.
DR PDBsum; 1OZW; -.
DR PDBsum; 1S13; -.
DR PDBsum; 1S8C; -.
DR PDBsum; 1T5P; -.
DR PDBsum; 1TWN; -.
DR PDBsum; 1TWR; -.
DR PDBsum; 1XJZ; -.
DR PDBsum; 1XK0; -.
DR PDBsum; 1XK1; -.
DR PDBsum; 1XK2; -.
DR PDBsum; 1XK3; -.
DR PDBsum; 3CZY; -.
DR PDBsum; 3HOK; -.
DR PDBsum; 3K4F; -.
DR PDBsum; 3TGM; -.
DR PDBsum; 4WD4; -.
DR PDBsum; 5BTQ; -.
DR PDBsum; 6EHA; -.
DR AlphaFoldDB; P09601; -.
DR SMR; P09601; -.
DR BioGRID; 109405; 142.
DR IntAct; P09601; 57.
DR MINT; P09601; -.
DR STRING; 9606.ENSP00000216117; -.
DR BindingDB; P09601; -.
DR ChEMBL; CHEMBL2823; -.
DR DrugBank; DB07342; 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone.
DR DrugBank; DB06914; 1-({2-[2-(4-CHLOROPHENYL)ETHYL]-1,3-DIOXOLAN-2-YL}METHYL)-1H-IMIDAZOLE.
DR DrugBank; DB02468; 12-Phenylheme.
DR DrugBank; DB03906; 2-Phenylheme.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR DrugBank; DB02073; Biliverdine IX Alpha.
DR DrugBank; DB14002; D-alpha-Tocopherol acetate.
DR DrugBank; DB01942; Formic acid.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB09221; Polaprezinc.
DR DrugBank; DB04912; Stannsoporfin.
DR DrugBank; DB04803; Verdoheme.
DR DrugBank; DB00163; Vitamin E.
DR GuidetoPHARMACOLOGY; 1441; -.
DR GlyGen; P09601; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09601; -.
DR PhosphoSitePlus; P09601; -.
DR BioMuta; HMOX1; -.
DR DMDM; 123446; -.
DR EPD; P09601; -.
DR jPOST; P09601; -.
DR MassIVE; P09601; -.
DR PaxDb; P09601; -.
DR PeptideAtlas; P09601; -.
DR PRIDE; P09601; -.
DR ProteomicsDB; 52249; -.
DR Antibodypedia; 266; 1132 antibodies from 45 providers.
DR DNASU; 3162; -.
DR Ensembl; ENST00000216117.9; ENSP00000216117.8; ENSG00000100292.18.
DR GeneID; 3162; -.
DR KEGG; hsa:3162; -.
DR MANE-Select; ENST00000216117.9; ENSP00000216117.8; NM_002133.3; NP_002124.1.
DR CTD; 3162; -.
DR DisGeNET; 3162; -.
DR GeneCards; HMOX1; -.
DR HGNC; HGNC:5013; HMOX1.
DR HPA; ENSG00000100292; Tissue enriched (lymphoid).
DR MalaCards; HMOX1; -.
DR MIM; 141250; gene.
DR MIM; 614034; phenotype.
DR neXtProt; NX_P09601; -.
DR OpenTargets; ENSG00000100292; -.
DR Orphanet; 586; Cystic fibrosis.
DR Orphanet; 562509; Heme oxygenase-1 deficiency.
DR PharmGKB; PA29341; -.
DR VEuPathDB; HostDB:ENSG00000100292; -.
DR eggNOG; KOG4480; Eukaryota.
DR GeneTree; ENSGT00390000017673; -.
DR HOGENOM; CLU_057050_0_0_1; -.
DR InParanoid; P09601; -.
DR OMA; KKSHTMA; -.
DR OrthoDB; 1424194at2759; -.
DR PhylomeDB; P09601; -.
DR TreeFam; TF314786; -.
DR BioCyc; MetaCyc:HS02027-MON; -.
DR BRENDA; 1.14.14.18; 2681.
DR PathwayCommons; P09601; -.
DR Reactome; R-HSA-189483; Heme degradation.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-844456; The NLRP3 inflammasome.
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707587; Regulation of HMOX1 expression and activity.
DR Reactome; R-HSA-9707616; Heme signaling.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SignaLink; P09601; -.
DR SIGNOR; P09601; -.
DR BioGRID-ORCS; 3162; 17 hits in 1088 CRISPR screens.
DR ChiTaRS; HMOX1; human.
DR EvolutionaryTrace; P09601; -.
DR GeneWiki; HMOX1; -.
DR GenomeRNAi; 3162; -.
DR Pharos; P09601; Tchem.
DR PRO; PR:P09601; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P09601; protein.
DR Bgee; ENSG00000100292; Expressed in cartilage tissue and 146 other tissues.
DR ExpressionAtlas; P09601; baseline and differential.
DR Genevisible; P09601; HS.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; TAS:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISS:BHF-UCL.
DR GO; GO:0020037; F:heme binding; IDA:BHF-UCL.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004630; F:phospholipase D activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; TAS:BHF-UCL.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:CACAO.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IEA:Ensembl.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR GO; GO:0072719; P:cellular response to cisplatin; IEA:Ensembl.
DR GO; GO:0034605; P:cellular response to heat; IMP:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
DR GO; GO:0031670; P:cellular response to nutrient; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; TAS:BHF-UCL.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:BHF-UCL.
DR GO; GO:0042167; P:heme catabolic process; IDA:BHF-UCL.
DR GO; GO:0006788; P:heme oxidation; IDA:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:BHF-UCL.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0055072; P:iron ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:BHF-UCL.
DR GO; GO:0016236; P:macroautophagy; IEA:Ensembl.
DR GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
DR GO; GO:0002686; P:negative regulation of leukocyte migration; TAS:BHF-UCL.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IEA:Ensembl.
DR GO; GO:0032764; P:negative regulation of mast cell cytokine production; IEA:Ensembl.
DR GO; GO:0043305; P:negative regulation of mast cell degranulation; IEA:Ensembl.
DR GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:UniProtKB.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:BHF-UCL.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IGI:BHF-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IGI:BHF-UCL.
DR GO; GO:0032722; P:positive regulation of chemokine production; TAS:BHF-UCL.
DR GO; GO:1904037; P:positive regulation of epithelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; TAS:BHF-UCL.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISS:BHF-UCL.
DR GO; GO:0034395; P:regulation of transcription from RNA polymerase II promoter in response to iron; IEA:Ensembl.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; ISS:BHF-UCL.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISS:BHF-UCL.
DR GO; GO:0035094; P:response to nicotine; IDA:BHF-UCL.
DR GO; GO:0006979; P:response to oxidative stress; IMP:BHF-UCL.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0014806; P:smooth muscle hyperplasia; TAS:BHF-UCL.
DR GO; GO:0002246; P:wound healing involved in inflammatory response; IMP:BHF-UCL.
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; Apoptosis; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..288
FT /note="Heme oxygenase 1"
FT /id="PRO_0000209687"
FT CHAIN 1..265
FT /note="Heme oxygenase 1 soluble form"
FT /evidence="ECO:0000305|PubMed:7703255"
FT /id="PRO_0000455621"
FT TOPO_DOM 1..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22419571"
FT TRANSMEM 266..288
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT REGION 223..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:12842469,
FT ECO:0007744|PDB:1OZW"
FT BINDING 25
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:12842469,
FT ECO:0007744|PDB:1OZW"
FT BINDING 134
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:12842469,
FT ECO:0007744|PDB:1OZW"
FT BINDING 183
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:12842469,
FT ECO:0007744|PDB:1OZW"
FT SITE 140
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:11121422"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VARIANT 7
FT /note="D -> H (in dbSNP:rs2071747)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019165"
FT VARIANT 106
FT /note="P -> L (in dbSNP:rs9282702)"
FT /id="VAR_022156"
FT MUTAGEN 140
FT /note="D->A,H,N,F,L: Inactive as a heme oxygenase but
FT active as a peroxidase."
FT /evidence="ECO:0000269|PubMed:11121422,
FT ECO:0000269|PubMed:12842469"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1NI6"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 44..68
FT /evidence="ECO:0007829|PDB:1N45"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 109..124
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 129..155
FT /evidence="ECO:0007829|PDB:1N45"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3CZY"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:1N45"
FT HELIX 193..220
FT /evidence="ECO:0007829|PDB:1N45"
SQ SEQUENCE 288 AA; 32819 MW; AB47827778694064 CRC64;
MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA
LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR WQEVIPYTPA MQRYVKRLHE
VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQ
LYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA
SNKVQDSAPV ETPRGKPPLN TRSQAPLLRW VLTLSFLVAT VAVGLYAM
