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Protein Page:
HMOX2 (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
HMOX2 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 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. Belongs to the heme oxygenase family. Note: This description may include information from UniProtKB.
Protein type: Oxidoreductase; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; EC 1.14.99.3
Cellular Component: endoplasmic reticulum membrane; membrane; plasma membrane
Molecular Function: protein binding; metal ion binding; heme oxygenase (decyclizing) activity
Biological Process: heme catabolic process; cellular iron ion homeostasis; porphyrin metabolic process; response to hypoxia; heme oxidation; response to oxidative stress; transmembrane transport
Reference #:  P30519 (UniProtKB)
Alt. Names/Synonyms: heme oxygenase (decycling) 2; Heme oxygenase 2; HMOX2; HO-2; HO2
Gene Symbols: HMOX2
Molecular weight: 36,033 Da
Basal Isoelectric point: 5.31  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HMOX2

Protein Structure Not Found.


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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

 
0 2 S2-p ______MsAEVETsE
0 1 S8-p MsAEVETsEGVDEsE
0 1 S14-p TsEGVDEsEKKNSGA
0 2 S34-p QMRMADLsELLKEGT
0 1 Y140 KYVERIHYIGQNEPE
0 1 Y157-p VAHAYTRyMGDLSGG
0 10 K199-ub VDNAQQFkQLyRARM
0 1 Y202-p AQQFkQLyRARMNAL
0 1 K214 NALDLNMKTkERIVE
0 1 K216-ac LDLNMKTkERIVEEA
0 1 D251-ca LARETLEdGFPVHDG
0 1 K259 GFPVHDGKGDMRKCP
0 1 Y268-p DMRKCPFyAAEQDKG
0 1 T286-p GSSCPFRtAMAVLRK
0 1 S295-p MAVLRKPsLQFILAA
0 1 Y314-p AAGLLAWyyM_____
0 1 Y315-p AGLLAWyyM______
  mouse

 
S2 ______MSSEVETSE
S8 MSSEVETSEGVDESE
S14 TSEGVDESEKNSMAP
S33 HTKMADLSELLKEGT
Y139-p KYVDRIHyVGQNEPE
Y156 VAHAYTRYMGDLSGG
K198-ub VDNAQQFkQFYRARM
Y201 AQQFkQFYRARMNAL
K213-ub NALDLNLkTKERIVE
K215 LDLNLkTKERIVEEA
D250 LARETLEDGLPVHDG
K258-ub GLPVHDGkGDIRKCP
Y267 DIRKCPFYAAQPDKG
T285 GSNCPFQTTVAVLRK
S294 VAVLRKPSLQLILAA
Y313 VAGLLAWYYM_____
Y314 AGLLAWYYM______
  rat

 
S2 ______MSSEVETSE
S8 MSSEVETSEGVDESE
S14 TSEGVDESENNSTAP
S33 HTKMADLSELLKEGT
Y139 KYVDRIHYVGQNEPE
Y156 VAHAYTRYMGDLSGG
K198 VDNAQQFKQFYRARM
Y201 AQQFKQFYRARMNAL
K213 NALDLSMKTKERIVE
K215 LDLSMKTKERIVEEA
D250 LTKETLEDGLPVHDG
K258 GLPVHDGKGDVRKCP
Y267 DVRKCPFYAAQPDKG
T285 GSNCPFRTAMAVLRK
S294 MAVLRKPSLQLILAA
Y313 VAGLLAWYYM_____
Y314 AGLLAWYYM______
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