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Protein Page:
iNOS (mouse)
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: EC 1.14.13.39; Oxidoreductase; Amino Acid Metabolism - arginine and proline
Cellular Component: cortical cytoskeleton; extracellular space; perinuclear region of cytoplasm; cytoplasm; peroxisome; vesicle membrane; intracellular; nucleus; cytosol
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; FMN binding; NADPH-hemoprotein reductase activity; cadherin binding; iron ion binding; heme binding; NADP binding; nitric-oxide synthase binding; receptor binding
Biological Process: superoxide metabolic process; positive regulation of guanylate cyclase activity; response to lipopolysaccharide; positive regulation of killing of cells of another organism; positive regulation of vasodilation; ovulation from ovarian follicle; regulation of cell proliferation; defense response to bacterium; response to hypoxia; peptidyl-cysteine S-nitrosylation; arginine catabolic process; negative regulation of blood pressure; negative regulation of protein catabolic process; regulation of protein kinase activity; nitric oxide biosynthetic process; inflammatory response; 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

 
0 1 - gap
0 1 T120 IMNPKSLTRGPRDKP
2 0 Y145 IEFINQYYGSFKEAK
0 1 Y261 WNSQLIRYAGYQMPD
0 1 Y264 QLIRYAGYQMPDGTI
0 1 S419 INVAVLHSFQkQNVT
0 1 K422-m1 AVLHSFQkQNVTIMD
0 1 H440 ASESFMKHMQNEYRA
0 1 Y445 MKHMQNEYRARGGCP
0 1 A447 HMQNEYRARGGCPAD
0 1 R510 RRREIRFRVLVKVVF
0 1 T561 LFSYAFNTKVVCMDQ
0 1 Y569 KVVCMDQYKASTLEE
0 1 T598 DCPSNGQTLKKSLFM
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 1 Y1117 QLKSQKRYHEDIFGA
0 1 Y1128 IFGAVFSYGAKKGsA
0 1 S1134-p SYGAKKGsALEEPKA
  human

 
S50-p DLQYHNLsKQQNESP
T126-p IMTPKSLtRGPRDKP
Y151-p IEFVNQYyGSFKEAK
Y267-p WNAQLIRyAGyQMPD
Y270-p QLIRyAGyQMPDGSI
S425-p INIAVLHsFQKQNVT
K428 AVLHsFQKQNVTIMD
Y446-p AAESFMKyMQNEyRs
Y451-p MKyMQNEyRsRGGCP
S453-p yMQNEyRsRGGCPAD
K516-ub KRREIPLkVLVKAVL
P567 LFSCAFNPKVVCMDK
Y575-p KVVCMDKyRLSCLEE
K604-ac DCPGNGEkLKKSLFM
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
- gap
  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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