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Protein

Nitric oxide synthase, inducible

Gene

Nos2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body (PubMed:7503239). In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (PubMed:16373578). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (By similarity). Involved in inflammation, enhances the synthesis of proinflammatory mediators such as IL6 and IL8 (By similarity).By similarity2 Publications

Catalytic activityi

2 L-arginine + 3 NADPH + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Not stimulated 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi104Zinc1
Metal bindingi109Zinc1
Metal bindingi194Iron (heme axial ligand)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi617 – 648FMNPROSITE-ProRule annotationAdd BLAST32
Nucleotide bindingi761 – 772FADBy similarityAdd BLAST12
Nucleotide bindingi897 – 907FADBy similarityAdd BLAST11
Nucleotide bindingi972 – 990NADPBy similarityAdd BLAST19
Nucleotide bindingi1070 – 1085NADPBy similarityAdd BLAST16

GO - Molecular functioni

  • arginine binding Source: BHF-UCL
  • calmodulin binding Source: UniProtKB
  • flavin adenine dinucleotide binding Source: BHF-UCL
  • FMN binding Source: BHF-UCL
  • heme binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • nitric-oxide synthase activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • receptor binding Source: MGI
  • tetrahydrobiopterin binding Source: BHF-UCL

GO - Biological processi

  • arginine catabolic process Source: BHF-UCL
  • cellular response to cytokine stimulus Source: MGI
  • cellular response to drug Source: MGI
  • cellular response to interferon-gamma Source: MGI
  • cellular response to lipopolysaccharide Source: MGI
  • cellular response to organic cyclic compound Source: MGI
  • circadian rhythm Source: UniProtKB
  • defense response to bacterium Source: MGI
  • inflammatory response Source: UniProtKB
  • interleukin-6 secretion Source: UniProtKB
  • interleukin-8 secretion Source: UniProtKB
  • negative regulation of blood pressure Source: GO_Central
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of protein catabolic process Source: BHF-UCL
  • nitric oxide biosynthetic process Source: BHF-UCL
  • nitric oxide mediated signal transduction Source: GO_Central
  • peptidyl-cysteine S-nitrosylation Source: UniProtKB
  • positive regulation of guanylate cyclase activity Source: GO_Central
  • positive regulation of killing of cells of other organism Source: MGI
  • positive regulation of vasodilation Source: GO_Central
  • prostaglandin secretion Source: UniProtKB
  • regulation of cell proliferation Source: MGI
  • regulation of cytokine production involved in inflammatory response Source: UniProtKB
  • regulation of insulin secretion Source: MGI
  • response to hypoxia Source: MGI
  • response to lipopolysaccharide Source: UniProtKB
  • superoxide metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calmodulin-binding, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP, Zinc

Enzyme and pathway databases

BRENDAi1.14.13.39. 3474.
ReactomeiR-MMU-1222556. ROS, RNS production in response to bacteria.
R-MMU-392154. Nitric oxide stimulates guanylate cyclase.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitric oxide synthase, inducible (EC:1.14.13.39)
Alternative name(s):
Inducible NO synthase
Short name:
Inducible NOS
Short name:
iNOS
Macrophage NOS
Short name:
MAC-NOS
NOS type II
Peptidyl-cysteine S-nitrosylase NOS2
Gene namesi
Name:Nos2
Synonyms:Inosl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:97361. Nos2.

Subcellular locationi

GO - Cellular componenti

  • cortical cytoskeleton Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • intracellular Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • peroxisome Source: MGI
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001709341 – 1144Nitric oxide synthase, inducibleAdd BLAST1144

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei569PhosphotyrosineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP29477.
PaxDbiP29477.
PRIDEiP29477.

PTM databases

iPTMnetiP29477.
PhosphoSitePlusiP29477.
SwissPalmiP29477.

Expressioni

Tissue specificityi

Macrophages.

Inductioni

By treatment with endotoxins or cytokines. By lipopolysaccharides (LPS) (in vitro). Expression in the liver oscillates in a circadian manner with peak levels occurring during the late night.1 Publication

Gene expression databases

BgeeiENSMUSG00000020826.
CleanExiMM_NOS2.
GenevisibleiP29477. MM.

Interactioni

Subunit structurei

Homodimer. Binds SLC9A3R1 (By similarity). Interacts with GAPDH. Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9 transnitrosylase complex (By similarity).By similarity

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • receptor binding Source: MGI

Protein-protein interaction databases

BioGridi201806. 6 interactors.
DIPiDIP-31080N.
IntActiP29477. 1 interactor.
MINTiMINT-202500.
STRINGi10090.ENSMUSP00000018610.

Chemistry databases

BindingDBiP29477.

Structurei

Secondary structure

11144
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi79 – 83Combined sources5
Turni84 – 86Combined sources3
Beta strandi89 – 92Combined sources4
Helixi94 – 97Combined sources4
Beta strandi103 – 107Combined sources5
Helixi117 – 119Combined sources3
Helixi130 – 146Combined sources17
Turni147 – 150Combined sources4
Helixi153 – 170Combined sources18
Helixi177 – 189Combined sources13
Helixi195 – 199Combined sources5
Beta strandi204 – 207Combined sources4
Helixi208 – 210Combined sources3
Helixi214 – 229Combined sources16
Helixi230 – 232Combined sources3
Beta strandi237 – 240Combined sources4
Beta strandi245 – 249Combined sources5
Beta strandi255 – 259Combined sources5
Beta strandi263 – 265Combined sources3
Beta strandi267 – 269Combined sources3
Beta strandi271 – 273Combined sources3
Helixi275 – 277Combined sources3
Helixi278 – 286Combined sources9
Beta strandi294 – 296Combined sources3
Beta strandi301 – 304Combined sources4
Beta strandi311 – 313Combined sources3
Helixi317 – 319Combined sources3
Beta strandi322 – 324Combined sources3
Helixi332 – 334Combined sources3
Turni335 – 337Combined sources3
Beta strandi339 – 342Combined sources4
Beta strandi350 – 353Combined sources4
Beta strandi356 – 359Combined sources4
Helixi369 – 373Combined sources5
Helixi375 – 378Combined sources4
Turni380 – 383Combined sources4
Helixi386 – 392Combined sources7
Helixi400 – 402Combined sources3
Helixi415 – 422Combined sources8
Helixi430 – 442Combined sources13
Helixi455 – 458Combined sources4
Beta strandi461 – 463Combined sources3
Helixi464 – 466Combined sources3
Helixi468 – 471Combined sources4
Beta strandi480 – 485Combined sources6
Helixi489 – 492Combined sources4
Helixi509 – 517Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DD7X-ray2.25A114-498[»]
1DF1X-ray2.35A/B77-499[»]
1DWVX-ray2.35A/B77-496[»]
1DWWX-ray2.35A/B77-496[»]
1DWXX-ray2.60A/B77-496[»]
1JWJX-ray2.60A/B66-498[»]
1JWKX-ray2.30A/B66-498[»]
1M8DX-ray2.35A/B65-498[»]
1M8EX-ray2.90A/B65-498[»]
1M8HX-ray2.85A/B65-498[»]
1M8IX-ray2.70A/B65-498[»]
1M9TX-ray2.40A/B65-498[»]
1N2NX-ray2.40A/B77-495[»]
1NOCX-ray2.60A115-498[»]
1NODX-ray2.60A/B77-499[»]
1NOSX-ray2.10A115-498[»]
1QOMX-ray2.70A/B65-498[»]
1QW4X-ray2.40A/B77-495[»]
1QW5X-ray2.70A/B77-495[»]
1R35X-ray2.30A/B66-498[»]
1VAFX-ray2.90A/B77-495[»]
2BHJX-ray3.20A77-498[»]
2NODX-ray2.60A/B77-499[»]
2NOSX-ray2.30A115-498[»]
2OROX-ray2.00A114-498[»]
2ORPX-ray1.97A114-498[»]
2ORQX-ray2.10A114-498[»]
2ORRX-ray2.00A114-498[»]
2ORSX-ray2.00A114-498[»]
2ORTX-ray1.87A114-498[»]
2Y37X-ray2.60A/B66-498[»]
3DWJX-ray2.75A/B66-496[»]
3E65X-ray2.05A/B66-498[»]
3E67X-ray2.60A/B66-498[»]
3E68X-ray2.20A/B66-498[»]
3E6LX-ray2.30A/B66-498[»]
3E6NX-ray2.40A/B66-498[»]
3E6OX-ray2.60A/B66-498[»]
3E6TX-ray2.50A/B66-498[»]
3E7IX-ray2.90A/B66-498[»]
3E7MX-ray2.00A/B66-498[»]
3E7TX-ray2.60A/B66-498[»]
3EAIX-ray2.20A/B66-498[»]
3EBDX-ray2.40A/B66-498[»]
3EBFX-ray2.29A/B66-498[»]
3GOFX-ray1.45C/D503-518[»]
3NODX-ray2.70A/B77-499[»]
3NQSX-ray2.20A/B66-498[»]
3NW2X-ray2.80A/B77-499[»]
4JS9X-ray2.78A/B66-496[»]
4UX6X-ray3.00A77-100[»]
B108-496[»]
ProteinModelPortaliP29477.
SMRiP29477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29477.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini533 – 671Flavodoxin-likePROSITE-ProRule annotationAdd BLAST139
Domaini724 – 964FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST241

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni503 – 523Calmodulin-bindingSequence analysisAdd BLAST21

Sequence similaritiesi

Belongs to the NOS family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
COG4362. LUCA.
GeneTreeiENSGT00840000129757.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiP29477.
KOiK13241.
OMAiKFTNSPT.
OrthoDBiEOG091G10Z0.
PhylomeDBiP29477.
TreeFamiTF324410.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
3.90.340.10. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR004030. NOS_N.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29477-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACPWKFLFK VKSYQSDLKE EKDINNNVKK TPCAVLSPTI QDDPKSHQNG
60 70 80 90 100
SPQLLTGTAQ NVPESLDKLH VTSTRPQYVR IKNWGSGEIL HDTLHHKATS
110 120 130 140 150
DFTCKSKSCL GSIMNPKSLT RGPRDKPTPL EELLPHAIEF INQYYGSFKE
160 170 180 190 200
AKIEEHLARL EAVTKEIETT GTYQLTLDEL IFATKMAWRN APRCIGRIQW
210 220 230 240 250
SNLQVFDARN CSTAQEMFQH ICRHILYATN NGNIRSAITV FPQRSDGKHD
260 270 280 290 300
FRLWNSQLIR YAGYQMPDGT IRGDAATLEF TQLCIDLGWK PRYGRFDVLP
310 320 330 340 350
LVLQADGQDP EVFEIPPDLV LEVTMEHPKY EWFQELGLKW YALPAVANML
360 370 380 390 400
LEVGGLEFPA CPFNGWYMGT EIGVRDFCDT QRYNILEEVG RRMGLETHTL
410 420 430 440 450
ASLWKDRAVT EINVAVLHSF QKQNVTIMDH HTASESFMKH MQNEYRARGG
460 470 480 490 500
CPADWIWLVP PVSGSITPVF HQEMLNYVLS PFYYYQIEPW KTHIWQNEKL
510 520 530 540 550
RPRRREIRFR VLVKVVFFAS MLMRKVMASR VRATVLFATE TGKSEALARD
560 570 580 590 600
LATLFSYAFN TKVVCMDQYK ASTLEEEQLL LVVTSTFGNG DCPSNGQTLK
610 620 630 640 650
KSLFMLRELN HTFRYAVFGL GSSMYPQFCA FAHDIDQKLS HLGASQLAPT
660 670 680 690 700
GEGDELSGQE DAFRSWAVQT FRAACETFDV RSKHHIQIPK RFTSNATWEP
710 720 730 740 750
QQYRLIQSPE PLDLNRALSS IHAKNVFTMR LKSQQNLQSE KSSRTTLLVQ
760 770 780 790 800
LTFEGSRGPS YLPGEHLGIF PGNQTALVQG ILERVVDCPT PHQTVCLEVL
810 820 830 840 850
DESGSYWVKD KRLPPCSLSQ ALTYFLDITT PPTQLQLHKL ARFATDETDR
860 870 880 890 900
QRLEALCQPS EYNDWKFSNN PTFLEVLEEF PSLHVPAAFL LSQLPILKPR
910 920 930 940 950
YYSISSSQDH TPSEVHLTVA VVTYRTRDGQ GPLHHGVCST WIRNLKPQDP
960 970 980 990 1000
VPCFVRSVSG FQLPEDPSQP CILIGPGTGI APFRSFWQQR LHDSQHKGLK
1010 1020 1030 1040 1050
GGRMSLVFGC RHPEEDHLYQ EEMQEMVRKR VLFQVHTGYS RLPGKPKVYV
1060 1070 1080 1090 1100
QDILQKQLAN EVLSVLHGEQ GHLYICGDVR MARDVATTLK KLVATKLNLS
1110 1120 1130 1140
EEQVEDYFFQ LKSQKRYHED IFGAVFSYGA KKGSALEEPK ATRL
Length:1,144
Mass (Da):130,575
Last modified:April 1, 1993 - v1
Checksum:i0735BE676113457F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti19K → T in AAC52356 (PubMed:7503239).Curated1
Sequence conflicti72T → TP in AAM11887 (Ref. 7) Curated1
Sequence conflicti72T → TP in AAH62378 (PubMed:15489334).Curated1
Sequence conflicti191A → V in M92649 (PubMed:1379716).Curated1
Sequence conflicti245S → T in AAM11887 (Ref. 7) Curated1
Sequence conflicti245S → T in AAH62378 (PubMed:15489334).Curated1
Sequence conflicti844A → G in M92649 (PubMed:1379716).Curated1
Sequence conflicti1075I → V in AAH62378 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti211C → R in strain: NOD/LtJ. 1 Publication1
Natural varianti967P → L in strain: SJL/J. 1 Publication1
Natural varianti968S → F in strain: BALB/CBYJ. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87039 mRNA. Translation: AAA39315.1.
M92649 mRNA. No translation available.
M84373 mRNA. Translation: AAA39834.1.
U43428 mRNA. Translation: AAC52356.1.
AF065919 mRNA. Translation: AAC17914.1.
AF065920 mRNA. Translation: AAC17915.1.
AF065921 mRNA. Translation: AAC17916.2.
AF065922 mRNA. Translation: AAC17917.2.
AF065923 mRNA. Translation: AAC17918.2.
AF427516 Genomic DNA. Translation: AAL24076.1.
AY090567 mRNA. Translation: AAM11887.1.
AL592185 Genomic DNA. Translation: CAI25275.1.
BC062378 mRNA. Translation: AAH62378.1.
CCDSiCCDS25115.1.
PIRiA43271.
RefSeqiNP_001300850.1. NM_001313921.1.
NP_001300851.1. NM_001313922.1.
NP_035057.1. NM_010927.4.
UniGeneiMm.2893.

Genome annotation databases

EnsembliENSMUST00000018610; ENSMUSP00000018610; ENSMUSG00000020826.
GeneIDi18126.
KEGGimmu:18126.
UCSCiuc007kkc.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87039 mRNA. Translation: AAA39315.1.
M92649 mRNA. No translation available.
M84373 mRNA. Translation: AAA39834.1.
U43428 mRNA. Translation: AAC52356.1.
AF065919 mRNA. Translation: AAC17914.1.
AF065920 mRNA. Translation: AAC17915.1.
AF065921 mRNA. Translation: AAC17916.2.
AF065922 mRNA. Translation: AAC17917.2.
AF065923 mRNA. Translation: AAC17918.2.
AF427516 Genomic DNA. Translation: AAL24076.1.
AY090567 mRNA. Translation: AAM11887.1.
AL592185 Genomic DNA. Translation: CAI25275.1.
BC062378 mRNA. Translation: AAH62378.1.
CCDSiCCDS25115.1.
PIRiA43271.
RefSeqiNP_001300850.1. NM_001313921.1.
NP_001300851.1. NM_001313922.1.
NP_035057.1. NM_010927.4.
UniGeneiMm.2893.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DD7X-ray2.25A114-498[»]
1DF1X-ray2.35A/B77-499[»]
1DWVX-ray2.35A/B77-496[»]
1DWWX-ray2.35A/B77-496[»]
1DWXX-ray2.60A/B77-496[»]
1JWJX-ray2.60A/B66-498[»]
1JWKX-ray2.30A/B66-498[»]
1M8DX-ray2.35A/B65-498[»]
1M8EX-ray2.90A/B65-498[»]
1M8HX-ray2.85A/B65-498[»]
1M8IX-ray2.70A/B65-498[»]
1M9TX-ray2.40A/B65-498[»]
1N2NX-ray2.40A/B77-495[»]
1NOCX-ray2.60A115-498[»]
1NODX-ray2.60A/B77-499[»]
1NOSX-ray2.10A115-498[»]
1QOMX-ray2.70A/B65-498[»]
1QW4X-ray2.40A/B77-495[»]
1QW5X-ray2.70A/B77-495[»]
1R35X-ray2.30A/B66-498[»]
1VAFX-ray2.90A/B77-495[»]
2BHJX-ray3.20A77-498[»]
2NODX-ray2.60A/B77-499[»]
2NOSX-ray2.30A115-498[»]
2OROX-ray2.00A114-498[»]
2ORPX-ray1.97A114-498[»]
2ORQX-ray2.10A114-498[»]
2ORRX-ray2.00A114-498[»]
2ORSX-ray2.00A114-498[»]
2ORTX-ray1.87A114-498[»]
2Y37X-ray2.60A/B66-498[»]
3DWJX-ray2.75A/B66-496[»]
3E65X-ray2.05A/B66-498[»]
3E67X-ray2.60A/B66-498[»]
3E68X-ray2.20A/B66-498[»]
3E6LX-ray2.30A/B66-498[»]
3E6NX-ray2.40A/B66-498[»]
3E6OX-ray2.60A/B66-498[»]
3E6TX-ray2.50A/B66-498[»]
3E7IX-ray2.90A/B66-498[»]
3E7MX-ray2.00A/B66-498[»]
3E7TX-ray2.60A/B66-498[»]
3EAIX-ray2.20A/B66-498[»]
3EBDX-ray2.40A/B66-498[»]
3EBFX-ray2.29A/B66-498[»]
3GOFX-ray1.45C/D503-518[»]
3NODX-ray2.70A/B77-499[»]
3NQSX-ray2.20A/B66-498[»]
3NW2X-ray2.80A/B77-499[»]
4JS9X-ray2.78A/B66-496[»]
4UX6X-ray3.00A77-100[»]
B108-496[»]
ProteinModelPortaliP29477.
SMRiP29477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201806. 6 interactors.
DIPiDIP-31080N.
IntActiP29477. 1 interactor.
MINTiMINT-202500.
STRINGi10090.ENSMUSP00000018610.

Chemistry databases

BindingDBiP29477.
ChEMBLiCHEMBL3464.

PTM databases

iPTMnetiP29477.
PhosphoSitePlusiP29477.
SwissPalmiP29477.

Proteomic databases

MaxQBiP29477.
PaxDbiP29477.
PRIDEiP29477.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018610; ENSMUSP00000018610; ENSMUSG00000020826.
GeneIDi18126.
KEGGimmu:18126.
UCSCiuc007kkc.1. mouse.

Organism-specific databases

CTDi4843.
MGIiMGI:97361. Nos2.

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
COG4362. LUCA.
GeneTreeiENSGT00840000129757.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiP29477.
KOiK13241.
OMAiKFTNSPT.
OrthoDBiEOG091G10Z0.
PhylomeDBiP29477.
TreeFamiTF324410.

Enzyme and pathway databases

BRENDAi1.14.13.39. 3474.
ReactomeiR-MMU-1222556. ROS, RNS production in response to bacteria.
R-MMU-392154. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

EvolutionaryTraceiP29477.
PROiP29477.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020826.
CleanExiMM_NOS2.
GenevisibleiP29477. MM.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
3.90.340.10. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR004030. NOS_N.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNOS2_MOUSE
AccessioniPrimary (citable) accession number: P29477
Secondary accession number(s): O70515
, O70516, Q5SXT3, Q6P6A0, Q8R410
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 2, 2016
This is version 184 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.