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Protein Page:
HMOX1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
HMOX1 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. 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. Expressed at higher levels in renal cancer tissue than in normal tissue. Belongs to the heme oxygenase family. Note: This description may include information from UniProtKB.
Protein type: EC 1.14.99.3; Oxidoreductase; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll
Cellular Component: extracellular space; endoplasmic reticulum membrane; membrane; endoplasmic reticulum; nucleolus; caveola; cytosol; nucleus
Molecular Function: signal transducer activity; protein homodimerization activity; enzyme binding; metal ion binding; phospholipase D activity; heme binding; heme oxygenase (decyclizing) activity
Biological Process: cell death; response to nicotine; cellular iron ion homeostasis; negative regulation of smooth muscle cell proliferation; negative regulation of mast cell degranulation; positive regulation of smooth muscle cell proliferation; positive regulation of vasodilation; excretion; erythrocyte homeostasis; regulation of transcription factor activity; heme catabolic process; small GTPase mediated signal transduction; regulation of blood pressure; porphyrin metabolic process; negative regulation of mast cell cytokine production; angiogenesis; negative regulation of neuron apoptosis; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; transmembrane transport; healing during inflammatory response; protein homooligomerization; positive regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of transcription factor activity; heme oxidation; cellular response to nutrient; regulation of angiogenesis; negative regulation of leukocyte migration; negative regulation of DNA binding; iron ion homeostasis; positive regulation of angiogenesis; positive regulation of chemokine biosynthetic process; DNA damage response, signal transduction resulting in induction of apoptosis; response to hydrogen peroxide; response to estrogen stimulus; endothelial cell proliferation; response to oxidative stress; smooth muscle hyperplasia
Reference #:  P09601 (UniProtKB)
Alt. Names/Synonyms: bK286B10; heme oxygenase (decycling) 1; Heme oxygenase 1; HMOX1; HO; HO-1; HO1; HSP32
Gene Symbols: HMOX1
Molecular weight: 32,819 Da
Basal Isoelectric point: 7.89  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HMOX1

Protein Structure Not Found.


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Sites Implicated In
enzymatic activity, induced: S188‑p
molecular association, regulation: S188‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 1 K18-ac QDLSEALkEATKEVH
0 1 K18-ub QDLSEALkEATKEVH
1 0 K22 EALkEATKEVHTQAE
1 1 K39-ac EFMRNFQkGQVTRDG
0 8 K39-ub EFMRNFQkGQVTRDG
1 0 K48 QVTRDGFKLVMAsLy
0 3 S53-p GFKLVMAsLyHIyVA
0 3 Y55-p KLVMAsLyHIyVALE
0 3 Y58-p MAsLyHIyVALEEEI
1 0 K69 EEEIERNKESPVFAP
0 3 K69-ub EEEIERNkESPVFAP
0 3 K86-ub FPEELHRkAALEQDL
0 1 T108-p WQEVIPYtPAMQRyV
0 1 Y114-p YtPAMQRyVKRLHEV
0 1 Y137-p VAHAYTRyLGDLSGG
0 4 K148-ub LSGGQVLkkIAQkAL
1 0 K149 SGGQVLkKIAQkALD
0 1 K149-ub SGGQVLkkIAQkALD
1 0 K153 VLkkIAQKALDLPSS
0 8 K153-ub VLkkIAQkALDLPSS
0 1 S174 FTFPNIASATkFkQL
0 15 K177-ub PNIASATkFkQLYRS
1 0 K179 IASATkFKQLYRSRM
0 15 K179-ub IASATkFkQLYRSRM
1 3 S188-p LYRSRMNsLEMtPAV
0 1 T192-p RMNsLEMtPAVRQRV
1 0 R196 LEMtPAVRQRVIEEA
0 7 S229-p THDTKDQsPsRAPGL
0 2 S231-p DTKDQsPsRAPGLRQ
0 4 G235 QsPsRAPGLRQRASN
0 13 N242 GLRQRASNkVQDSAP
0 22 K243-ub LRQRASNkVQDSAPV
0 6 T252-p QDSAPVEtPRGkPPL
0 1 K256-ub PVEtPRGkPPLNTRS
0 1 P257 VEtPRGkPPLNTRSQ
0 1 S263 kPPLNTRSQAPLLRW
0 1 Y286-p ATVAVGLyAM_____
  mouse

 
K18 QDLSEALKEATKEVH
K18 QDLSEALKEATKEVH
K22 EALKEATKEVHIQAE
K39 EFMKNFQKGQVSREG
K39 EFMKNFQKGQVSREG
K48 QVSREGFKLVMASLY
S53 GFKLVMASLYHIYTA
Y55 KLVMASLYHIYTALE
Y58 MASLYHIYTALEEEI
K69 EEEIERNKQNPVYAP
K69 EEEIERNKQNPVYAP
R86 FPEELHRRAALEQDM
T108 WQEIIPCTPATQHYV
Y114 CTPATQHYVKRLHEV
Y137 VAHAYTRYLGDLSGG
K148 LSGGQVLKKIAQkAM
K149 SGGQVLKKIAQkAMA
K149 SGGQVLKKIAQkAMA
K153 VLKKIAQKAMALPSS
K153-ub VLKKIAQkAMALPSS
S174-p FTFPNIDsPTkFkQL
K177-ub PNIDsPTkFkQLYRA
K179 IDsPTkFKQLYRARM
K179-ub IDsPTkFkQLYRARM
T188-p LYRARMNtLEMTPEV
T192 RMNtLEMTPEVKHRV
K196 LEMTPEVKHRVTEEA
S229 TEEHKDQSPSQMAsL
S231 EHKDQSPSQMAsLRQ
S235-p QSPSQMAsLRQRPAs
S242-p sLRQRPAsLVQDTAP
L243 LRQRPAsLVQDTAPA
T252 QDTAPAETPRGKPQI
K256 PAETPRGKPQISTSS
P257 AETPRGKPQISTSSS
S263 KPQISTSSSQTPLLQ
Y287 ATVAVGIYAM_____
  rat

 
K18-ac QDLSEALkEATkEVH
K18 QDLSEALKEATkEVH
K22-ac EALkEATkEVHIRAE
K39-ac EFMRNFQkGQVSREG
K39 EFMRNFQKGQVSREG
K48-ac QVSREGFkLVMASLY
S53 GFkLVMASLYHIYTA
Y55 kLVMASLYHIYTALE
Y58 MASLYHIYTALEEEI
K69-ac EEEIERNkQNPVYAP
K69 EEEIERNKQNPVYAP
R86 FPEELHRRAALEQDM
T108 WQEAIPYTPATQHYV
Y114 YTPATQHYVKRLHEV
Y137 VAHAYTRYLGDLSGG
K148 LSGGQVLKkIAQkAM
K149-ac SGGQVLKkIAQkAMA
K149 SGGQVLKKIAQkAMA
K153-ac VLKkIAQkAMALPSS
K153 VLKkIAQKAMALPSS
N174 FTFPSIDNPTKFkQL
K177 PSIDNPTKFkQLYRA
K179-ac IDNPTKFkQLYRARM
K179 IDNPTKFKQLYRARM
T188 LYRARMNTLEMTPEV
T192 RMNTLEMTPEVkHRV
K196-ac LEMTPEVkHRVTEEA
S229-p TEEHKDQsPsQTEFL
S231-p EHKDQsPsQTEFLRQ
F235 QsPsQTEFLRQRPAs
S242-p FLRQRPAsLVQDTTS
L243 LRQRPAsLVQDTTSA
T252 QDTTSAETPRGKsQI
K256 SAETPRGKsQISTSs
S257-p AETPRGKsQISTSsS
S263-p KsQISTSsSQTPLLR
Y287 ATVAVGIYAM_____
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