Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
HMOX1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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: Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; EC 1.14.99.3; Oxidoreductase
Chromosomal Location of Human Ortholog: 22q13.1
Cellular Component: caveola; cytosol; endoplasmic reticulum; endoplasmic reticulum membrane; extracellular space; membrane; nucleolus; nucleus; perinuclear region of cytoplasm
Molecular Function: enzyme binding; heme binding; heme oxygenase (decyclizing) activity; metal ion binding; phospholipase D activity; protein binding; protein homodimerization activity; signal transducer activity
Biological Process: angiogenesis; cell death; cellular iron ion homeostasis; cellular response to nutrient; DNA damage response, signal transduction resulting in induction of apoptosis; endothelial cell proliferation; erythrocyte homeostasis; excretion; healing during inflammatory response; heme catabolic process; heme oxidation; iron ion homeostasis; negative regulation of DNA binding; negative regulation of leukocyte migration; negative regulation of mast cell cytokine production; negative regulation of mast cell degranulation; negative regulation of neuron apoptosis; negative regulation of smooth muscle cell proliferation; negative regulation of transcription factor activity; positive regulation of angiogenesis; positive regulation of chemokine biosynthetic process; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of smooth muscle cell proliferation; positive regulation of vasodilation; protein homooligomerization; regulation of angiogenesis; regulation of blood pressure; regulation of transcription factor activity; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; response to estrogen stimulus; response to hydrogen peroxide; response to nicotine; response to oxidative stress; small GTPase mediated signal transduction; smooth muscle hyperplasia
Disease: Heme Oxygenase 1 Deficiency; Pulmonary Disease, Chronic Obstructive
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.
Download PyMol Script
Download ChimeraX Script


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB


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


 LTP 

LTP: 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.


 HTP 

HTP: 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 S160‑p kALDLPSsGEGLAFF
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 16 S229‑p THDTKDQsPsRAPGL
0 5 S231‑p DTKDQsPsRAPGLRQ
0 4 G235 QsPsRAPGLRQRASN
0 19 N242 GLRQRASNkVQDSAP
0 22 K243‑ub LRQRASNkVQDSAPV
0 10 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
S160 kAMALPSSGEGLAFF
S174‑p FTFPNIDsPTkFkQL
K177‑ub PNIDsPTkFkQLYRA
K179 IDsPTkFKQLYRARM
K179‑ub IDsPTkFkQLYRARM
T188‑p LYRARMNtLEMTPEV
T192 RMNtLEMTPEVKHRV
K196 LEMTPEVKHRVTEEA
S229‑p TEEHKDQsPSQMAsL
S231 EHKDQsPSQMAsLRQ
S235‑p QsPSQMAsLRQRPAs
S242‑p sLRQRPAsLVQDTAP
L243 LRQRPAsLVQDTAPA
T252‑p 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
S160 kAMALPSSGEGLAFF
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‑p QDTTSAEtPRGKsQI
K256 SAEtPRGKsQISTSs
S257‑p AEtPRGKsQISTSsS
S263‑p KsQISTSsSQTPLLR
Y287 ATVAVGIYAM_____
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.