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Protein Page:
iNOS (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
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
Chromosomal Location of Human Ortholog: 17q11.2
Cellular Component: cortical cytoskeleton; perinuclear region of cytoplasm; cytoplasm; peroxisome; intracellular; cytosol; nucleus
Molecular Function: calmodulin binding; protein binding; protein homodimerization activity; FAD binding; FMN binding; NADPH-hemoprotein reductase activity; nitric-oxide synthase activity; iron ion binding; heme binding; NADP binding; receptor binding
Biological Process: interaction with host; superoxide metabolic process; positive regulation of guanylate cyclase activity; positive regulation of killing of cells of another organism; defense response to Gram-negative bacterium; positive regulation of vasodilation; regulation of cell proliferation; regulation of cellular respiration; positive regulation of leukocyte mediated cytotoxicity; innate immune response in mucosa; response to bacterium; defense response to bacterium; response to hypoxia; peptidyl-cysteine S-nitrosylation; arginine catabolic process; negative regulation of blood pressure; inflammatory response; negative regulation of protein catabolic process; nitric oxide biosynthetic process; blood coagulation; nitric oxide mediated signal transduction; regulation of insulin secretion
Reference #:  P35228 (UniProtKB)
Alt. Names/Synonyms: HEP-NOS; Hepatocyte NOS; Inducible NO synthase; Inducible NOS; iNOS; nitric oxide synthase 2, inducible; nitric oxide synthase 2A (inducible, hepatocytes); Nitric oxide synthase, inducible; nitric oxide synthase, macrophage; NOS; NOS type II; NOS, type II; NOS2; NOS2A
Gene Symbols: NOS2
Molecular weight: 131,117 Da
Basal Isoelectric point: 8.2  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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Sites Implicated In
enzymatic activity, induced: S745‑p
enzymatic activity, inhibited: Y151‑p
intracellular localization: Y151‑p
protein stabilization: Y1055‑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

 
0 1 S50-p DLQYHNLsKQQNESP
0 1 T126-p IMTPKSLtRGPRDKP
2 0 Y151-p IEFVNQYyGSFKEAK
0 1 Y267-p WNAQLIRyAGyQMPD
0 1 Y270-p QLIRyAGyQMPDGSI
0 1 S425-p INIAVLHsFQKQNVT
0 1 K428 AVLHsFQKQNVTIMD
0 1 Y446-p AAESFMKyMQNEyRs
0 1 Y451-p MKyMQNEyRsRGGCP
0 1 S453-p yMQNEyRsRGGCPAD
0 1 K516-ub KRREIPLkVLVKAVL
0 1 P567 LFSCAFNPKVVCMDK
0 1 Y575-p KVVCMDKyRLSCLEE
0 1 K604-ac DCPGNGEkLKKSLFM
0 1 D714 HHYRLVQDSQPLDLS
0 1 K722 SQPLDLSKALSSMHA
1 0 S739 VFTMRLKSRQNLQsP
1 1 S745-p KSRQNLQsPTSSRAT
0 1 Y868-p ALCQPSEySKWKFTN
0 2 S892-p EFPSLRVsAGFLLsQ
0 2 S898-p VsAGFLLsQLPILKP
1 0 S909 ILKPRFYSISSSRDH
0 1 R1047 AVHTAYSRLPGKPKV
1 5 Y1055-p LPGKPKVyVQDILRQ
0 1 Y1123-p QLKSQKRyHEDIFGA
0 1 Y1134-p IFGAVFPyEAKKDRV
0 1 - gap
  mouse

 
- gap
T120 IMNPKSLTRGPRDKP
Y145 IEFINQYYGSFKEAK
Y261 WNSQLIRYAGYQMPD
Y264 QLIRYAGYQMPDGTI
S419 INVAVLHSFQkQNVT
K422-m1 AVLHSFQkQNVTIMD
H440 ASESFMKHMQNEYRA
Y445 MKHMQNEYRARGGCP
A447 HMQNEYRARGGCPAD
R510 RRREIRFRVLVKVVF
T561 LFSYAFNTKVVCMDQ
Y569 KVVCMDQYKASTLEE
T598 DCPSNGQTLKKSLFM
S708-p QQYRLIQsPEPLDLN
R716-m1 PEPLDLNrALSSIHA
S733-p VFTMRLKsQQNLQSE
S739 KsQQNLQSEKSSRTT
Y862 ALCQPSEYNDWKFSN
P886 EFPSLHVPAAFLLSQ
S892 VPAAFLLSQLPILKP
S903-p ILKPRYYsISSSQDH
R1041-m1 QVHTGYSrLPGKPKV
Y1049-p LPGKPKVyVQDILQK
Y1117 QLKSQKRYHEDIFGA
Y1128 IFGAVFSYGAKKGsA
S1134-p SYGAKKGsALEEPKA
  rat

 
- gap
T123 IMNSKSLTRGPRDKP
Y148 IEFINQYYGSFKEAK
Y264 WNSQLIRYAGYQMPD
Y267 QLIRYAGYQMPDGTI
S422 INAAVLHSFQKQNVT
K425 AVLHSFQKQNVTIMD
H443 ASESFMKHMQNEYRA
Y448 MKHMQNEYRARGGCP
A450 HMQNEYRARGGCPAD
T513 RRREIRFTVLVKAVF
T564-p LFSYAFNtKVVCMEQ
Y572 KVVCMEQYKANTLEE
T601 DCPSNGQTLKKSLFM
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
T1138 YGAKKGNTLEEPKGT
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