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Protein Page:
iNOS (mouse)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
iNOS Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2. Homodimer. Binds SLC9A3R1. By endotoxins and cytokines. Induced by IFNG/IFN-gamma acting synergistically with bacterial lipopolysaccharides (LPS), TNF or IL1B/interleukin-1 beta. Expressed in the liver, retina, bone cells and airway epithelial cells of the lung. Not expressed in the platelets. Regulated by calcium/calmodulin. Aspirin inhibits expression and function of this enzyme and effects may be exerted at the level of translational/post-translational modification and directly on the catalytic activity. Belongs to the NOS family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Amino Acid Metabolism - arginine and proline; Oxidoreductase; EC 1.14.13.39
Cellular Component: cortical cytoskeleton; extracellular space; perinuclear region of cytoplasm; cytoplasm; peroxisome; vesicle membrane; intracellular; cytosol; nucleus
Molecular Function: protein homodimerization activity; FAD binding; nitric-oxide synthase activity; metal ion binding; beta-catenin binding; cAMP-dependent protein kinase regulator activity; oxidoreductase activity; Hsp90 protein binding; actin binding; protein kinase binding; calmodulin binding; protein binding; NADPH-hemoprotein reductase activity; FMN binding; cadherin binding; iron ion binding; heme binding; nitric-oxide synthase binding; NADP binding; receptor binding
Biological Process: positive regulation of apoptosis; cGMP-mediated signaling; superoxide metabolic process; positive regulation of guanylate cyclase activity; positive regulation of killing of cells of another organism; ovulation from ovarian follicle; signal transduction; positive regulation of vasodilation; regulation of heart contraction; regulation of cell proliferation; regulation of blood pressure; defense response to bacterium; response to hypoxia; peptidyl-cysteine S-nitrosylation; arginine catabolic process; blood vessel remodeling; G-protein signaling, coupled to cGMP nucleotide second messenger; negative regulation of blood pressure; negative regulation of protein catabolic process; inflammatory response; regulation of protein kinase activity; nitric oxide biosynthetic process; nitric oxide mediated signal transduction; regulation of insulin secretion
Reference #:  P29477 (UniProtKB)
Alt. Names/Synonyms: i-NOS; inducible nitric oxide synthase; Inducible NO synthase; Inducible NOS; iNOS; Inosl; MAC-NOS; Macrophage NOS; nitric oxide synthase 2, inducible; nitric oxide synthase 2, inducible, macrophage; Nitric oxide synthase, inducible; NOS type II; Nos-2; NOS-II; Nos2; Nos2a; OTTMUSP00000000202
Gene Symbols: Nos2
Molecular weight: 130,575 Da
Basal Isoelectric point: 7.76  Predict pI for various phosphorylation states
CST Pathways:  Angiogenesis  |  Insulin Receptor Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

iNOS

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.


       mouse

 
2 0 Y145 IEFINQYYGSFKEAK
0 1 K422-m1 AVLHSFQkQNVTIMD
0 1 T561 LFSYAFNTKVVCMDQ
0 1 S708-p QQYRLIQsPEPLDLN
0 1 R716-m1 PEPLDLNrALSSIHA
1 0 S733-p VFTMRLKsQQNLQSE
1 1 S739 KsQQNLQSEKSSRTT
0 1 Y862 ALCQPSEYNDWKFSN
0 2 P886 EFPSLHVPAAFLLSQ
0 2 S892 VPAAFLLSQLPILKP
1 0 S903-p ILKPRYYsISSSQDH
0 1 R1041-m1 QVHTGYSrLPGKPKV
1 5 Y1049-p LPGKPKVyVQDILQK
0 2 Y1117 QLKSQKRYHEDIFGA
0 2 Y1128 IFGAVFSYGAKKGSA
  human

 
Y151-p IEFVNQYyGSFKEAK
K428 AVLHSFQKQNVTIMD
P567 LFSCAFNPKVVCMDK
D714 HHYRLVQDSQPLDLS
K722 SQPLDLSKALSSMHA
S739 VFTMRLKSRQNLQsP
S745-p KSRQNLQsPTSSRAT
Y868-p ALCQPSEySKWKFTN
S892-p EFPSLRVsAGFLLsQ
S898-p VsAGFLLsQLPILKP
S909 ILKPRFYSISSSRDH
R1047 AVHTAYSRLPGKPKV
Y1055-p LPGKPKVyVQDILRQ
Y1123-p QLKSQKRyHEDIFGA
Y1134-p IFGAVFPyEAKKDRV
  rat

 
Y148 IEFINQYYGSFKEAK
K425 AVLHSFQKQNVTIMD
T564-p LFSYAFNtKVVCMEQ
S711 EQYKLTQSPESLDLN
K719 PESLDLNKALSSIHA
S736 VFTMRLKSLQNLQSE
S742 KSLQNLQSEKSSRTT
Y865 ALCQPSEYNDWKFSN
P889 EFPSLRVPAAFLLSQ
S895 VPAAFLLSQLPILKP
S906 ILKPRYYSISSSQDH
R1044 QVHTGYSRLPGKPKV
Y1052-p LPGKPKVyVQDILQK
Y1120 QLKSQKRYHEDIFGA
Y1131 IFGAVFSYGAKKGNT
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