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HMOX1 (human)

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: Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; Oxidoreductase; EC 1.14.99.3 Cellular Component: extracellular space; endoplasmic reticulum membrane; membrane; endoplasmic reticulum; nucleolus; caveola; nucleus; cytosol 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; positive regulation of smooth muscle cell proliferation; negative regulation of mast cell degranulation; protein kinase cascade; positive regulation of vasodilation; excretion; erythrocyte homeostasis; regulation of transcription factor activity; heme catabolic process; regulation of blood pressure; small GTPase mediated signal transduction; porphyrin metabolic process; negative regulation of mast cell cytokine production; negative regulation of neuron apoptosis; angiogenesis; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; healing during inflammatory response; transmembrane transport; protein homooligomerization; positive regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of transcription factor activity; heme oxidation; cellular response to nutrient; negative regulation of leukocyte migration; regulation of angiogenesis; 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; negative regulation of apoptosis 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®

Select Structure to View Below HMOX1 1N3U - A/B=1-233 (human) 1N45 - A/B=1-233 (human) 1NI6 - A/B/C/D=1-224 (human) 1OYK - A/B=1-233 (human) 1OYL - A/B=1-233 (human) 1OZE - A/B=1-233 (human) 1OZL - A/B=1-233 (human) 1OZR - A/B=1-233 (human) 1OZW - A/B=1-233 (human) 1S13 - A/B=1-233 (human) 1S8C - A/B/C/D=1-233 (human) 1T5P - A/B=1-233 (human) 1TWN - A/B=1-233 (human) 1TWR - A/B=1-233 (human) 1XJZ - A/B=1-233 (human) 1XK0 - A/B=1-233 (human) 1XK1 - A/B=1-233 (human) 1XK2 - A/B=1-233 (human) 1XK3 - A/B=1-233 (human) 3CZY - A/B=1-233 (human) 3HOK - A/B=1-233 (human) 3K4F - A/B=1-233 (human) 3TGM - A/B=1-233 (human) 1DVE - A=1-267 (rat) 1DVG - A/B=1-267 (rat) 1IRM - A/B/C=1-267 (rat) 1IVJ - A=1-267 (rat) 1IX3 - A=1-267 (rat) 1IX4 - A=1-267 (rat) 1J02 - A=1-267 (rat) 1J2C - A=1-267 (rat) 1UBB - A=1-267 (rat) 1ULX - A=1-267 (rat) 1VGI - A=1-267 (rat) 2DY5 - A=1-267 (rat) 2E7E - A=1-267 (rat) 2ZVU - A=1-267 (rat) 3I9T - A=1-261 (rat) 3I9U - A=1-261 (rat) 4G7L - A=1-267 (rat) 4G7P - A=1-267 (rat) 4G7T - A=1-267 (rat) 4G7U - A=1-267 (rat) 4G8P - A=1-267 (rat) 4G8U - A=1-267 (rat) 4G8W - A=1-267 (rat) 4G98 - A=1-267 (rat) 4G99 - A=1-267 (rat)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1N3U 1N45 1NI6 1OYK 1OYL 1OZE 1OZL 1OZR 1OZW 1S13 1S8C 1T5P 1TWN 1TWR 1XJZ 1XK0 1XK1 1XK2 1XK3 3CZY 3HOK 3K4F 3TGM  |  ENZYME  |  Phospho3D  |  DISEASE 141250 606963  |  InnateDB  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	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

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-a	QDLSEALkEATKEVH
0	1		K18-u	QDLSEALkEATKEVH
1	0		K22	EALkEATKEVHTQAE
1	1		K39-a	EFMRNFQkGQVTRDG
0	8		K39-u	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-u	EEEIERNkESPVFAP
0	3		K86-u	FPEELHRkAALEQDL
0	1		T108-p	WQEVIPYtPAMQRyV
0	1		Y114-p	YtPAMQRyVKRLHEV
0	1		Y137-p	VAHAYTRyLGDLSGG
0	4		K148-u	LSGGQVLkkIAQkAL
1	0		K149	SGGQVLkKIAQkALD
0	1		K149-u	SGGQVLkkIAQkALD
1	0		K153	VLkkIAQKALDLPSS
0	8		K153-u	VLkkIAQkALDLPSS
0	1		S174	FTFPNIASATkFkQL
0	15		K177-u	PNIASATkFkQLYRS
1	0		K179	IASATkFKQLYRSRM
0	15		K179-u	IASATkFkQLYRSRM
1	3		S188-p	LYRSRMNsLEMtPAV
0	1		T192-p	RMNsLEMtPAVRQRV
1	0		R196	LEMtPAVRQRVIEEA
0	4		S229-p	THDTKDQsPsRAPGL
0	2		S231-p	DTKDQsPsRAPGLRQ
0	4		G235	QsPsRAPGLRQRASN
0	12		N242	GLRQRASNkVQDSAP
0	22		K243-u	LRQRASNkVQDSAPV
0	3		T252-p	QDSAPVEtPRGkPPL
0	1		K256-u	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-u	VLKKIAQkAMALPSS
S174-p	FTFPNIDsPTkFkQL
K177-u	PNIDsPTkFkQLYRA
K179	IDsPTkFKQLYRARM
K179-u	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-a	QDLSEALkEATkEVH
K18	QDLSEALKEATkEVH
K22-a	EALkEATkEVHIRAE
K39-a	EFMRNFQkGQVSREG
K39	EFMRNFQKGQVSREG
K48-a	QVSREGFkLVMASLY
S53	GFkLVMASLYHIYTA
Y55	kLVMASLYHIYTALE
Y58	MASLYHIYTALEEEI
K69-a	EEEIERNkQNPVYAP
K69	EEEIERNKQNPVYAP
R86	FPEELHRRAALEQDM
T108	WQEAIPYTPATQHYV
Y114	YTPATQHYVKRLHEV
Y137	VAHAYTRYLGDLSGG
K148	LSGGQVLKkIAQkAM
K149-a	SGGQVLKkIAQkAMA
K149	SGGQVLKKIAQkAMA
K153-a	VLKkIAQkAMALPSS
K153	VLKkIAQKAMALPSS
N174	FTFPSIDNPTKFkQL
K177	PSIDNPTKFkQLYRA
K179-a	IDNPTKFkQLYRARM
K179	IDNPTKFKQLYRARM
T188	LYRARMNTLEMTPEV
T192	RMNTLEMTPEVkHRV
K196-a	LEMTPEVkHRVTEEA
S229	TEEHKDQSPSQTEFL
S231	EHKDQSPSQTEFLRQ
F235	QSPSQTEFLRQRPAS
S242	FLRQRPASLVQDTTS
L243	LRQRPASLVQDTTSA
T252	QDTTSAETPRGKsQI
K256	SAETPRGKsQISTSs
S257-p	AETPRGKsQISTSsS
S263-p	KsQISTSsSQTPLLR
Y287	ATVAVGIYAM_____

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