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P09601

- HMOX1_HUMAN

UniProt

P09601 - HMOX1_HUMAN

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Protein

Heme oxygenase 1

Gene

HMOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.

Catalytic activityi

Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181Heme
Metal bindingi25 – 251Iron (heme axial ligand)
Binding sitei134 – 1341Heme
Binding sitei183 – 1831Heme

GO - Molecular functioni

  1. enzyme binding Source: BHF-UCL
  2. heme binding Source: BHF-UCL
  3. heme oxygenase (decyclizing) activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. phospholipase D activity Source: Ensembl
  6. protein homodimerization activity Source: UniProtKB
  7. signal transducer activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: BHF-UCL
  2. cell death Source: BHF-UCL
  3. cellular iron ion homeostasis Source: Reactome
  4. cellular response to arsenic-containing substance Source: Ensembl
  5. cellular response to cadmium ion Source: Ensembl
  6. cellular response to hypoxia Source: UniProtKB
  7. cellular response to nutrient Source: Ensembl
  8. endothelial cell proliferation Source: BHF-UCL
  9. erythrocyte homeostasis Source: BHF-UCL
  10. excretion Source: BHF-UCL
  11. heme catabolic process Source: BHF-UCL
  12. heme oxidation Source: BHF-UCL
  13. intracellular signal transduction Source: BHF-UCL
  14. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  15. iron ion homeostasis Source: BHF-UCL
  16. low-density lipoprotein particle clearance Source: BHF-UCL
  17. negative regulation of DNA binding Source: Ensembl
  18. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  19. negative regulation of leukocyte migration Source: BHF-UCL
  20. negative regulation of mast cell cytokine production Source: Ensembl
  21. negative regulation of mast cell degranulation Source: Ensembl
  22. negative regulation of muscle cell apoptotic process Source: Ensembl
  23. negative regulation of neuron apoptotic process Source: Ensembl
  24. negative regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  25. negative regulation of smooth muscle cell proliferation Source: UniProtKB
  26. porphyrin-containing compound metabolic process Source: Reactome
  27. positive regulation of angiogenesis Source: Ensembl
  28. positive regulation of chemokine biosynthetic process Source: BHF-UCL
  29. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  30. positive regulation of smooth muscle cell proliferation Source: UniProtKB
  31. positive regulation of vasodilation Source: BHF-UCL
  32. protein homooligomerization Source: UniProtKB
  33. regulation of angiogenesis Source: BHF-UCL
  34. regulation of blood pressure Source: Ensembl
  35. regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  36. regulation of transcription from RNA polymerase II promoter in response to iron Source: Ensembl
  37. regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: BHF-UCL
  38. response to estrogen Source: Ensembl
  39. response to hydrogen peroxide Source: BHF-UCL
  40. response to nicotine Source: BHF-UCL
  41. response to oxidative stress Source: BHF-UCL
  42. small GTPase mediated signal transduction Source: Ensembl
  43. small molecule metabolic process Source: Reactome
  44. smooth muscle hyperplasia Source: BHF-UCL
  45. transmembrane transport Source: Reactome
  46. wound healing involved in inflammatory response Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS02027-MONOMER.
ReactomeiREACT_22297. Heme degradation.
REACT_25060. Iron uptake and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 1 (EC:1.14.99.3)
Short name:
HO-1
Gene namesi
Name:HMOX1
Synonyms:HO, HO1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:5013. HMOX1.

Subcellular locationi

Microsome 1 Publication. Endoplasmic reticulum membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

GO - Cellular componenti

  1. caveola Source: Ensembl
  2. cytosol Source: Ensembl
  3. endoplasmic reticulum Source: UniProtKB
  4. endoplasmic reticulum membrane Source: Reactome
  5. extracellular space Source: BHF-UCL
  6. membrane Source: ProtInc
  7. nucleolus Source: Ensembl
  8. nucleus Source: BHF-UCL
  9. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Involvement in diseasei

Heme oxygenase 1 deficiency (HMOX1D) [MIM:614034]: A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi140 – 1401D → A: Inactive as a heme oxygenase but active as a peroxidase. 1 Publication

Organism-specific databases

MIMi614034. phenotype.
PharmGKBiPA29341.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Heme oxygenase 1PRO_0000209687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei229 – 2291Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP09601.
PaxDbiP09601.
PRIDEiP09601.

PTM databases

PhosphoSiteiP09601.

Expressioni

Tissue specificityi

Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level).1 Publication

Inductioni

Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA.

Gene expression databases

BgeeiP09601.
CleanExiHS_HMOX1.
ExpressionAtlasiP09601. baseline and differential.
GenevestigatoriP09601.

Organism-specific databases

HPAiCAB017444.
HPA000635.

Interactioni

Protein-protein interaction databases

BioGridi109405. 20 interactions.
IntActiP09601. 8 interactions.
STRINGi9606.ENSP00000216117.

Structurei

Secondary structure

1
288
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 208
Helixi22 – 309
Helixi32 – 387
Helixi44 – 6825
Turni72 – 743
Helixi75 – 773
Helixi80 – 834
Helixi86 – 9712
Helixi101 – 1033
Helixi109 – 12416
Helixi126 – 1283
Helixi129 – 15527
Beta strandi159 – 1613
Helixi165 – 1673
Helixi175 – 18814
Helixi193 – 22028

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N3UX-ray2.58A/B1-233[»]
1N45X-ray1.50A/B1-233[»]
1NI6X-ray2.10A/B/C/D1-224[»]
1OYKX-ray2.59A/B1-233[»]
1OYLX-ray1.59A/B1-233[»]
1OZEX-ray2.19A/B1-233[»]
1OZLX-ray1.58A/B1-233[»]
1OZRX-ray1.74A/B1-233[»]
1OZWX-ray1.55A/B1-233[»]
1S13X-ray2.29A/B1-233[»]
1S8CX-ray2.19A/B/C/D1-233[»]
1T5PX-ray2.11A/B1-233[»]
1TWNX-ray2.20A/B1-233[»]
1TWRX-ray2.10A/B1-233[»]
1XJZX-ray1.88A/B1-233[»]
1XK0X-ray2.18A/B1-233[»]
1XK1X-ray2.08A/B1-233[»]
1XK2X-ray2.20A/B1-233[»]
1XK3X-ray2.08A/B1-233[»]
3CZYX-ray1.54A/B1-233[»]
3HOKX-ray2.19A/B1-233[»]
3K4FX-ray2.17A/B1-233[»]
3TGMX-ray2.85A/B1-233[»]
ProteinModelPortaliP09601.
SMRiP09601. Positions 10-223.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09601.

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Phylogenomic databases

eggNOGiCOG5398.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP09601.
KOiK00510.
OMAiYAPLYFP.
PhylomeDBiP09601.
TreeFamiTF314786.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
InterProiIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERiPTHR10720. PTHR10720. 1 hit.
PfamiPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFiPIRSF000343. Haem_Oase. 1 hit.
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09601-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV
60 70 80 90 100
MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR
110 120 130 140 150
WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI
160 170 180 190 200
AQKALDLPSS GEGLAFFTFP NIASATKFKQ LYRSRMNSLE MTPAVRQRVI
210 220 230 240 250
EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV
260 270 280
ETPRGKPPLN TRSQAPLLRW VLTLSFLVAT VAVGLYAM
Length:288
Mass (Da):32,819
Last modified:July 1, 1989 - v1
Checksum:iAB47827778694064
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71D → H.1 Publication
Corresponds to variant rs2071747 [ dbSNP | Ensembl ].
VAR_019165
Natural varianti106 – 1061P → L.
Corresponds to variant rs9282702 [ dbSNP | Ensembl ].
VAR_022156

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06985 mRNA. Translation: CAA30045.1.
CR456505 mRNA. Translation: CAG30391.1.
AY460337 Genomic DNA. Translation: AAR23262.1.
Z82244 Genomic DNA. Translation: CAB05109.1.
M23041 mRNA. Translation: AAA50403.1.
X14782 Genomic DNA. Translation: CAA32886.1.
CCDSiCCDS13914.1.
PIRiS00325.
RefSeqiNP_002124.1. NM_002133.2.
UniGeneiHs.517581.

Genome annotation databases

EnsembliENST00000216117; ENSP00000216117; ENSG00000100292.
GeneIDi3162.
KEGGihsa:3162.
UCSCiuc003ant.2. human.

Polymorphism databases

DMDMi123446.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06985 mRNA. Translation: CAA30045.1 .
CR456505 mRNA. Translation: CAG30391.1 .
AY460337 Genomic DNA. Translation: AAR23262.1 .
Z82244 Genomic DNA. Translation: CAB05109.1 .
M23041 mRNA. Translation: AAA50403.1 .
X14782 Genomic DNA. Translation: CAA32886.1 .
CCDSi CCDS13914.1.
PIRi S00325.
RefSeqi NP_002124.1. NM_002133.2.
UniGenei Hs.517581.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N3U X-ray 2.58 A/B 1-233 [» ]
1N45 X-ray 1.50 A/B 1-233 [» ]
1NI6 X-ray 2.10 A/B/C/D 1-224 [» ]
1OYK X-ray 2.59 A/B 1-233 [» ]
1OYL X-ray 1.59 A/B 1-233 [» ]
1OZE X-ray 2.19 A/B 1-233 [» ]
1OZL X-ray 1.58 A/B 1-233 [» ]
1OZR X-ray 1.74 A/B 1-233 [» ]
1OZW X-ray 1.55 A/B 1-233 [» ]
1S13 X-ray 2.29 A/B 1-233 [» ]
1S8C X-ray 2.19 A/B/C/D 1-233 [» ]
1T5P X-ray 2.11 A/B 1-233 [» ]
1TWN X-ray 2.20 A/B 1-233 [» ]
1TWR X-ray 2.10 A/B 1-233 [» ]
1XJZ X-ray 1.88 A/B 1-233 [» ]
1XK0 X-ray 2.18 A/B 1-233 [» ]
1XK1 X-ray 2.08 A/B 1-233 [» ]
1XK2 X-ray 2.20 A/B 1-233 [» ]
1XK3 X-ray 2.08 A/B 1-233 [» ]
3CZY X-ray 1.54 A/B 1-233 [» ]
3HOK X-ray 2.19 A/B 1-233 [» ]
3K4F X-ray 2.17 A/B 1-233 [» ]
3TGM X-ray 2.85 A/B 1-233 [» ]
ProteinModelPortali P09601.
SMRi P09601. Positions 10-223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109405. 20 interactions.
IntActi P09601. 8 interactions.
STRINGi 9606.ENSP00000216117.

Chemistry

BindingDBi P09601.
ChEMBLi CHEMBL2823.
DrugBanki DB00163. Vitamin E.

PTM databases

PhosphoSitei P09601.

Polymorphism databases

DMDMi 123446.

Proteomic databases

MaxQBi P09601.
PaxDbi P09601.
PRIDEi P09601.

Protocols and materials databases

DNASUi 3162.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216117 ; ENSP00000216117 ; ENSG00000100292 .
GeneIDi 3162.
KEGGi hsa:3162.
UCSCi uc003ant.2. human.

Organism-specific databases

CTDi 3162.
GeneCardsi GC22P035776.
HGNCi HGNC:5013. HMOX1.
HPAi CAB017444.
HPA000635.
MIMi 141250. gene.
614034. phenotype.
neXtProti NX_P09601.
PharmGKBi PA29341.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5398.
HOGENOMi HOG000233221.
HOVERGENi HBG005982.
InParanoidi P09601.
KOi K00510.
OMAi YAPLYFP.
PhylomeDBi P09601.
TreeFami TF314786.

Enzyme and pathway databases

BioCyci MetaCyc:HS02027-MONOMER.
Reactomei REACT_22297. Heme degradation.
REACT_25060. Iron uptake and transport.

Miscellaneous databases

EvolutionaryTracei P09601.
GeneWikii HMOX1.
GenomeRNAii 3162.
NextBioi 12538.
PROi P09601.
SOURCEi Search...

Gene expression databases

Bgeei P09601.
CleanExi HS_HMOX1.
ExpressionAtlasi P09601. baseline and differential.
Genevestigatori P09601.

Family and domain databases

Gene3Di 1.20.910.10. 1 hit.
InterProi IPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view ]
PANTHERi PTHR10720. PTHR10720. 1 hit.
Pfami PF01126. Heme_oxygenase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000343. Haem_Oase. 1 hit.
PRINTSi PR00088. HAEMOXYGNASE.
SUPFAMi SSF48613. SSF48613. 1 hit.
PROSITEi PS00593. HEME_OXYGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human heme oxygenase cDNA and induction of its mRNA by hemin."
    Yoshida T., Biro P., Cohen T., Mueller R.M., Shibahara S.
    Eur. J. Biochem. 171:457-461(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. SeattleSNPs variation discovery resource
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-7.
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite."
    Keyse S.M., Tyrrell R.M.
    Proc. Natl. Acad. Sci. U.S.A. 86:99-103(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-103.
    Tissue: Foreskin.
  6. "Structural organization of the human heme oxygenase gene and the function of its promoter."
    Shibahara S., Sato M., Muller R.M., Yoshida T.
    Eur. J. Biochem. 179:557-563(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
  7. "Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency."
    Yachie A., Niida Y., Wada T., Igarashi N., Kaneda H., Toma T., Ohta K., Kasahara Y., Koizumi S.
    J. Clin. Invest. 103:129-135(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HMOX1D.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: REVIEW ON ANTIAPOPTOTIC FUNCTION.
  10. "CXCR3-B can mediate growth-inhibitory signals in human renal cancer cells by down-regulating the expression of heme oxygenase-1."
    Datta D., Banerjee P., Gasser M., Waaga-Gasser A.M., Pal S.
    J. Biol. Chem. 285:36842-36848(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Endoplasmic reticulum anchored heme-oxygenase 1 faces the cytosol."
    Gottlieb Y., Truman M., Cohen L.A., Leichtmann-Bardoogo Y., Meyron-Holtz E.G.
    Haematologica 97:1489-1493(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS).
  15. "Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications."
    Lad L., Wang J., Li H., Friedman J., Bhaskar B., Ortiz de Montellano P.R., Poulos T.L.
    J. Mol. Biol. 330:527-538(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-233 OF MUTANT ALA-140, HEME-BINDING SITES, MUTAGENESIS OF ASP-140.

Entry informationi

Entry nameiHMOX1_HUMAN
AccessioniPrimary (citable) accession number: P09601
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3