Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Heme oxygenase 1  

UniProtKB / Swiss-Prot ID :  HMOX1_HUMAN

Gene Name (Synonyms) : 
HMOX1, HO, HO1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Microsome. Endoplasmic reticulum. 

Protein Function :  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. 

Protein Sequence MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKE...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHCC...
Protein Variant
LocationDescription
7D -> H (in dbSNP:rs2071747). VAR_019165
106P -> L (in dbSNP:rs9282702). VAR_022156
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylmethionine.----MERPQ
----CCCCC
9.95UniProtKB
Link-
18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SEALKEATK
HHHHHHHHH
52.96Phosphositeplus
Link
18N6-acetyllysineSEALKEATK
HHHHHHHHH
52.96Phosphositeplus
Link
39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RNFQKGQVT
HHHHCCCCC
47.36Phosphositeplus
Link
39N6-acetyllysineRNFQKGQVT
HHHHCCCCC
47.36HPRD
Link
39N6-acetyllysineRNFQKGQVT
HHHHCCCCC
47.36Phosphositeplus
Link
39N6-acetyllysine.RNFQKGQVT
HHHHCCCCC
47.36UniProtKB
Link
69Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IERNKESPV
HHHHCCCCC
66.83Phosphositeplus
Link
86Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ELHRKAALE
HHHHHHHHH
27.54Phosphositeplus
Link
137PhosphotyrosineAYTRYLGDL
HHHHHHHHH
13.77HPRD
Link
137PhosphotyrosineAYTRYLGDL
HHHHHHHHH
13.77Phosphositeplus
Link
148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GQVLKKIAQ
HHHHHHHHH
43.19Phosphositeplus
Link
153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KIAQKALDL
HHHHHHHCC
41.73Phosphositeplus
Link
177Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ASATKFKQL
CCHHHHHHH
50.73Phosphositeplus
Link
188PhosphoserineSRMNSLEMT
HHCCCCCCC
19.16Phosphositeplus
Link
188Phosphoserine (AKT1)SRMNSLEMT
HHCCCCCCC
19.16HPRD
Link
192PhosphothreonineSLEMTPAVR
CCCCCHHHH
9.94Phosphositeplus
Link
229PhosphoserineTKDQSPSRA
HCCCCCCCC
34.67HPRD
Link-
229PhosphoserineTKDQSPSRA
HCCCCCCCC
34.67PhosphoELM
Link-
229PhosphoserineTKDQSPSRA
HCCCCCCCC
34.67Phosphositeplus
Link-
229PhosphoserineTKDQSPSRA
HCCCCCCCC
34.67SysPTM
Link-
229Phosphoserine.TKDQSPSRA
HCCCCCCCC
34.67UniProtKB
Link-
231PhosphoserineDQSPSRAPG
CCCCCCCHH
46.45HPRD
Link-
231PhosphoserineDQSPSRAPG
CCCCCCCHH
46.45PhosphoELM
Link-
231PhosphoserineDQSPSRAPG
CCCCCCCHH
46.45Phosphositeplus
Link-
231PhosphoserineDQSPSRAPG
CCCCCCCHH
46.45SysPTM
Link-
243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RASNKVQDS
CCHHHHCCC
38.48Phosphositeplus
Link-
256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TPRGKPPLN
CCCCCCCCH
44.75Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NCPR_HUMANin vitroHPRD:00782HPRD12626517
BLVRB_HUMANin vitroHPRD:00782HPRD12626517
HMOX1_HUMANin vitroHPRD:00782HPRD12500973
USF2_HUMANENSP00000216117STRING
USF2_HUMANENSP00000216117STRING
MK14_HUMANENSP00000216117STRING
IL6_HUMANENSP00000216117STRING
BLVRB_HUMANENSP00000216117STRING
NCPR_HUMANENSP00000216117STRING
BIEA_HUMANENSP00000216117STRING
HEMO_HUMANENSP00000216117STRING
PRL_HUMANENSP00000216117STRING
VEGFA_HUMANENSP00000216117STRING
HIF1A_HUMANENSP00000216117STRING
HIF1A_HUMANENSP00000216117STRING
FGF1_HUMANENSP00000216117STRING
CAV1_HUMANENSP00000216117STRING
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Disease Reference
Kegg disease
OMIM disease
614034Heme oxygenase 1 deficiency (HMOX1D)
Drug Reference
DrugBank
DB00163Vitamin E
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures