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Protein

Nitric oxide synthase, inducible

Gene

NOS2

Organism
Homo sapiens (Human)
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:7531687, PubMed:7544004). In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (By similarity). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH on 'Cys-247' implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (PubMed:25417112). Involved in inflammation, enhances the synthesis of proinflammatory mediators such as IL6 and IL8 (PubMed:19688109).By similarity4 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:
  • hemeBy similarity
  • FADBy similarityNote: Binds 1 FAD.By similarity
  • FMNBy similarityNote: Binds 1 FMN.By similarity
  • 5,6,7,8-tetrahydrobiopterinBy similarityNote: Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.By similarity

Enzyme regulationi

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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi110Zinc1
Metal bindingi115Zinc1
Metal bindingi200Iron (heme axial ligand)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi623 – 654FMNPROSITE-ProRule annotationAdd BLAST32
Nucleotide bindingi767 – 778FADBy similarityAdd BLAST12
Nucleotide bindingi903 – 913FADBy similarityAdd BLAST11
Nucleotide bindingi978 – 996NADPBy similarityAdd BLAST19
Nucleotide bindingi1076 – 1091NADPBy similarityAdd BLAST16

GO - Molecular functioni

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

GO - Biological processi

  • arginine catabolic process Source: BHF-UCL
  • cell redox homeostasis Source: Reactome
  • cellular response to drug Source: Ensembl
  • cellular response to interferon-gamma Source: Ensembl
  • cellular response to lipopolysaccharide Source: Ensembl
  • circadian rhythm Source: Ensembl
  • defense response to bacterium Source: UniProtKB
  • defense response to Gram-negative bacterium Source: BHF-UCL
  • innate immune response in mucosa Source: BHF-UCL
  • 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: Ensembl
  • nitric oxide biosynthetic process Source: UniProtKB
  • 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: BHF-UCL
  • positive regulation of leukocyte mediated cytotoxicity Source: BHF-UCL
  • positive regulation of vasodilation Source: GO_Central
  • prostaglandin secretion Source: UniProtKB
  • regulation of cell proliferation Source: Ensembl
  • regulation of cellular respiration Source: BHF-UCL
  • regulation of cytokine production involved in inflammatory response Source: UniProtKB
  • regulation of insulin secretion Source: BHF-UCL
  • response to bacterium Source: UniProtKB
  • response to hypoxia Source: Ensembl
  • superoxide metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:HS00205-MONOMER.
ZFISH:HS00205-MONOMER.
BRENDAi1.14.13.39. 2681.
ReactomeiR-HSA-1222556. ROS, RNS production in response to bacteria.
R-HSA-392154. Nitric oxide stimulates guanylate cyclase.
SignaLinkiP35228.
SIGNORiP35228.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitric oxide synthase, inducible (EC:1.14.13.39)
Alternative name(s):
Hepatocyte NOS
Short name:
HEP-NOS
Inducible NO synthase
Short name:
Inducible NOS
Short name:
iNOS
NOS type II
Peptidyl-cysteine S-nitrosylase NOS2
Gene namesi
Name:NOS2
Synonyms:NOS2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:7873. NOS2.

Subcellular locationi

GO - Cellular componenti

  • cortical cytoskeleton Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: BHF-UCL
  • intracellular Source: BHF-UCL
  • nucleus Source: BHF-UCL
  • perinuclear region of cytoplasm Source: Ensembl
  • peroxisome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi4843.
MalaCardsiNOS2.
MIMi611162. phenotype.
OpenTargetsiENSG00000007171.
PharmGKBiPA164724093.

Chemistry databases

ChEMBLiCHEMBL4481.
DrugBankiDB01234. Dexamethasone.
DB00997. Doxorubicin.
DB00125. L-Arginine.
DB00155. L-Citrulline.
DB01110. Miconazole.
DB08814. Triflusal.
GuidetoPHARMACOLOGYi1250.

Polymorphism and mutation databases

BioMutaiNOS2.
DMDMi1352513.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001709301 – 1153Nitric oxide synthase, inducibleAdd BLAST1153

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei234Phosphoserine; by PKASequence analysis1
Modified residuei575PhosphotyrosineBy similarity1
Modified residuei578Phosphoserine; by PKASequence analysis1
Modified residuei892Phosphoserine; by PKASequence analysis1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP35228.
PeptideAtlasiP35228.
PRIDEiP35228.

PTM databases

iPTMnetiP35228.
PhosphoSitePlusiP35228.
SwissPalmiP35228.

Expressioni

Tissue specificityi

Expressed in the liver, retina, bone cells and airway epithelial cells of the lung. Not expressed in the platelets.

Inductioni

By endotoxins and cytokines. Induced by IFNG/IFN-gamma acting synergistically with bacterial lipopolysaccharides (LPS), TNF or IL1B/interleukin-1 beta (PubMed:7528267). Down-regulated by zinc due to inhibition of NF-kappa-B transactivation activity (PubMed:25180171). By oxidatively-modified low-densitity lipoprotein (LDL(ox)) (PubMed:25417112).3 Publications

Gene expression databases

BgeeiENSG00000007171.
CleanExiHS_NOS2.
GenevisibleiP35228. HS.

Organism-specific databases

HPAiCAB002014.

Interactioni

Subunit structurei

Homodimer. Binds SLC9A3R1. Interacts with GAPDH; induced by oxidatively-modified low-densitity lipoprotein (LDL(ox)). Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9 transnitrosylase complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GAPDHP044068EBI-6662224,EBI-354056

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi110906. 146 interactors.
DIPiDIP-59359N.
IntActiP35228. 4 interactors.
STRINGi9606.ENSP00000327251.

Chemistry databases

BindingDBiP35228.

Structurei

Secondary structure

11153
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi85 – 89Combined sources5
Turni90 – 92Combined sources3
Beta strandi95 – 98Combined sources4
Helixi100 – 103Combined sources4
Beta strandi104 – 106Combined sources3
Helixi123 – 125Combined sources3
Helixi136 – 152Combined sources17
Beta strandi154 – 156Combined sources3
Helixi159 – 175Combined sources17
Helixi183 – 195Combined sources13
Helixi203 – 205Combined sources3
Beta strandi210 – 213Combined sources4
Helixi220 – 235Combined sources16
Helixi236 – 238Combined sources3
Beta strandi243 – 246Combined sources4
Beta strandi251 – 255Combined sources5
Beta strandi261 – 265Combined sources5
Beta strandi269 – 271Combined sources3
Beta strandi277 – 279Combined sources3
Helixi281 – 283Combined sources3
Helixi284 – 292Combined sources9
Beta strandi307 – 310Combined sources4
Beta strandi317 – 319Combined sources3
Helixi323 – 325Combined sources3
Beta strandi328 – 330Combined sources3
Helixi337 – 342Combined sources6
Beta strandi345 – 348Combined sources4
Beta strandi356 – 359Combined sources4
Beta strandi362 – 365Combined sources4
Helixi375 – 379Combined sources5
Helixi381 – 384Combined sources4
Turni386 – 389Combined sources4
Helixi392 – 399Combined sources8
Helixi406 – 408Combined sources3
Helixi410 – 428Combined sources19
Helixi436 – 454Combined sources19
Helixi461 – 464Combined sources4
Beta strandi467 – 469Combined sources3
Helixi470 – 472Combined sources3
Helixi474 – 477Combined sources4
Beta strandi486 – 491Combined sources6
Helixi495 – 498Combined sources4
Helixi515 – 534Combined sources20
Beta strandi538 – 544Combined sources7
Beta strandi546 – 548Combined sources3
Helixi549 – 561Combined sources13
Turni562 – 564Combined sources3
Beta strandi565 – 571Combined sources7
Helixi572 – 574Combined sources3
Helixi577 – 581Combined sources5
Beta strandi584 – 591Combined sources8
Turni594 – 596Combined sources3
Helixi600 – 602Combined sources3
Helixi603 – 611Combined sources9
Beta strandi620 – 627Combined sources8
Beta strandi631 – 633Combined sources3
Helixi636 – 648Combined sources13
Beta strandi651 – 654Combined sources4
Beta strandi657 – 660Combined sources4
Helixi665 – 683Combined sources19
Helixi689 – 691Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NSIX-ray2.55A/B/C/D74-504[»]
2LL6NMR-B515-531[»]
2NSIX-ray3.00A/B/C/D74-504[»]
3E7GX-ray2.20A/B/C/D82-505[»]
3EJ8X-ray2.55A/B/C/D82-505[»]
3HR4X-ray2.50A/C/E/G503-715[»]
4CX7X-ray3.16A/B/C/D74-504[»]
4NOSX-ray2.25A/B/C/D82-508[»]
ProteinModelPortaliP35228.
SMRiP35228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35228.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini539 – 677Flavodoxin-likePROSITE-ProRule annotationAdd BLAST139
Domaini730 – 970FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST241

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni509 – 529Calmodulin-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.
HOVERGENiHBG000159.
InParanoidiP35228.
KOiK13241.
OMAiKFTNSPT.
OrthoDBiEOG091G10Z0.
PhylomeDBiP35228.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35228-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MACPWKFLFK TKFHQYAMNG EKDINNNVEK APCATSSPVT QDDLQYHNLS
60 70 80 90 100
KQQNESPQPL VETGKKSPES LVKLDATPLS SPRHVRIKNW GSGMTFQDTL
110 120 130 140 150
HHKAKGILTC RSKSCLGSIM TPKSLTRGPR DKPTPPDELL PQAIEFVNQY
160 170 180 190 200
YGSFKEAKIE EHLARVEAVT KEIETTGTYQ LTGDELIFAT KQAWRNAPRC
210 220 230 240 250
IGRIQWSNLQ VFDARSCSTA REMFEHICRH VRYSTNNGNI RSAITVFPQR
260 270 280 290 300
SDGKHDFRVW NAQLIRYAGY QMPDGSIRGD PANVEFTQLC IDLGWKPKYG
310 320 330 340 350
RFDVVPLVLQ ANGRDPELFE IPPDLVLEVA MEHPKYEWFR ELELKWYALP
360 370 380 390 400
AVANMLLEVG GLEFPGCPFN GWYMGTEIGV RDFCDVQRYN ILEEVGRRMG
410 420 430 440 450
LETHKLASLW KDQAVVEINI AVLHSFQKQN VTIMDHHSAA ESFMKYMQNE
460 470 480 490 500
YRSRGGCPAD WIWLVPPMSG SITPVFHQEM LNYVLSPFYY YQVEAWKTHV
510 520 530 540 550
WQDEKRRPKR REIPLKVLVK AVLFACMLMR KTMASRVRVT ILFATETGKS
560 570 580 590 600
EALAWDLGAL FSCAFNPKVV CMDKYRLSCL EEERLLLVVT STFGNGDCPG
610 620 630 640 650
NGEKLKKSLF MLKELNNKFR YAVFGLGSSM YPRFCAFAHD IDQKLSHLGA
660 670 680 690 700
SQLTPMGEGD ELSGQEDAFR SWAVQTFKAA CETFDVRGKQ HIQIPKLYTS
710 720 730 740 750
NVTWDPHHYR LVQDSQPLDL SKALSSMHAK NVFTMRLKSR QNLQSPTSSR
760 770 780 790 800
ATILVELSCE DGQGLNYLPG EHLGVCPGNQ PALVQGILER VVDGPTPHQT
810 820 830 840 850
VRLEALDESG SYWVSDKRLP PCSLSQALTY FLDITTPPTQ LLLQKLAQVA
860 870 880 890 900
TEEPERQRLE ALCQPSEYSK WKFTNSPTFL EVLEEFPSLR VSAGFLLSQL
910 920 930 940 950
PILKPRFYSI SSSRDHTPTE IHLTVAVVTY HTRDGQGPLH HGVCSTWLNS
960 970 980 990 1000
LKPQDPVPCF VRNASGFHLP EDPSHPCILI GPGTGIAPFR SFWQQRLHDS
1010 1020 1030 1040 1050
QHKGVRGGRM TLVFGCRRPD EDHIYQEEML EMAQKGVLHA VHTAYSRLPG
1060 1070 1080 1090 1100
KPKVYVQDIL RQQLASEVLR VLHKEPGHLY VCGDVRMARD VAHTLKQLVA
1110 1120 1130 1140 1150
AKLKLNEEQV EDYFFQLKSQ KRYHEDIFGA VFPYEAKKDR VAVQPSSLEM

SAL
Length:1,153
Mass (Da):131,117
Last modified:February 1, 1996 - v2
Checksum:i47671E5385CB3A52
GO
Isoform 2 (identifier: P35228-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     264-288: Missing.
     298-311: Missing.

Show »
Length:1,114
Mass (Da):126,749
Checksum:iC1F9624774435571
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23D → G in AAA56666 (PubMed:7522054).Curated1
Sequence conflicti154F → L in AAA56666 (PubMed:7522054).Curated1
Sequence conflicti177G → V in AAA56666 (PubMed:7522054).Curated1
Sequence conflicti266R → H in AAC19133 (PubMed:9160867).Curated1
Sequence conflicti423L → I in AAA59171 (PubMed:7682706).Curated1
Sequence conflicti439A → T in AAC19133 (PubMed:9160867).Curated1
Sequence conflicti552A → G in AAI44127 (PubMed:15489334).Curated1
Sequence conflicti676T → I in AAB60366 (PubMed:7544004).Curated1
Sequence conflicti800T → A in AAA56666 (PubMed:7522054).Curated1
Sequence conflicti805A → D in AAA59171 (PubMed:7682706).Curated1
Sequence conflicti831 – 832FL → SP in AAA59171 (PubMed:7682706).Curated2
Sequence conflicti913S → P in AAA56666 (PubMed:7522054).Curated1
Sequence conflicti933R → G in AAA59171 (PubMed:7682706).Curated1
Sequence conflicti933R → G in AAB60366 (PubMed:7544004).Curated1
Sequence conflicti966G → A in AAA59171 (PubMed:7682706).Curated1
Sequence conflicti966G → A in AAB60366 (PubMed:7544004).Curated1
Sequence conflicti987A → V in AAA59171 (PubMed:7682706).Curated1

Polymorphismi

Note: Genetic variations in NOS2 are involved in resistance to malaria [MIMi:611162].1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_024548221R → W.1 PublicationCorresponds to variant rs3730017dbSNPEnsembl.1
Natural variantiVAR_022127608S → L Polymorphism; found in patients with very early onset inflammatory bowel disease; increases NOS2 activity. 4 PublicationsCorresponds to variant rs2297518dbSNPEnsembl.1
Natural variantiVAR_036302679A → S in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs769900089dbSNPEnsembl.1
Natural variantiVAR_025020747T → A.1 PublicationCorresponds to variant rs28944173dbSNPEnsembl.1
Natural variantiVAR_0250211009R → C.1 PublicationCorresponds to variant rs28944201dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003582264 – 288Missing in isoform 2. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_003583298 – 311Missing in isoform 2. 1 PublicationAdd BLAST14

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24553 mRNA. Translation: AAA36375.1.
L09210 mRNA. Translation: AAA59171.1.
X73029 mRNA. Translation: CAA51512.1.
U05810 mRNA. Translation: AAA56666.1.
U31511 mRNA. Translation: AAB49041.1.
D26525 mRNA. Translation: BAA05531.1.
U20141 mRNA. Translation: AAB60366.1.
AF068236 mRNA. Translation: AAC19133.1.
AB022318 mRNA. Translation: BAA37123.1.
DQ060518 Genomic DNA. Translation: AAY43131.1.
EU332854 Genomic DNA. Translation: ABY87543.1.
BC130283 mRNA. Translation: AAI30284.1.
BC144126 mRNA. Translation: AAI44127.1.
S75615 mRNA. Translation: AAD14179.1.
CCDSiCCDS11223.1. [P35228-1]
PIRiA49676.
RefSeqiNP_000616.3. NM_000625.4. [P35228-1]
XP_011523161.1. XM_011524859.2. [P35228-1]
UniGeneiHs.709191.

Genome annotation databases

EnsembliENST00000313735; ENSP00000327251; ENSG00000007171. [P35228-1]
ENST00000621962; ENSP00000482291; ENSG00000007171. [P35228-2]
GeneIDi4843.
KEGGihsa:4843.
UCSCiuc002gzu.4. human. [P35228-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Nitric oxide synthase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24553 mRNA. Translation: AAA36375.1.
L09210 mRNA. Translation: AAA59171.1.
X73029 mRNA. Translation: CAA51512.1.
U05810 mRNA. Translation: AAA56666.1.
U31511 mRNA. Translation: AAB49041.1.
D26525 mRNA. Translation: BAA05531.1.
U20141 mRNA. Translation: AAB60366.1.
AF068236 mRNA. Translation: AAC19133.1.
AB022318 mRNA. Translation: BAA37123.1.
DQ060518 Genomic DNA. Translation: AAY43131.1.
EU332854 Genomic DNA. Translation: ABY87543.1.
BC130283 mRNA. Translation: AAI30284.1.
BC144126 mRNA. Translation: AAI44127.1.
S75615 mRNA. Translation: AAD14179.1.
CCDSiCCDS11223.1. [P35228-1]
PIRiA49676.
RefSeqiNP_000616.3. NM_000625.4. [P35228-1]
XP_011523161.1. XM_011524859.2. [P35228-1]
UniGeneiHs.709191.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NSIX-ray2.55A/B/C/D74-504[»]
2LL6NMR-B515-531[»]
2NSIX-ray3.00A/B/C/D74-504[»]
3E7GX-ray2.20A/B/C/D82-505[»]
3EJ8X-ray2.55A/B/C/D82-505[»]
3HR4X-ray2.50A/C/E/G503-715[»]
4CX7X-ray3.16A/B/C/D74-504[»]
4NOSX-ray2.25A/B/C/D82-508[»]
ProteinModelPortaliP35228.
SMRiP35228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110906. 146 interactors.
DIPiDIP-59359N.
IntActiP35228. 4 interactors.
STRINGi9606.ENSP00000327251.

Chemistry databases

BindingDBiP35228.
ChEMBLiCHEMBL4481.
DrugBankiDB01234. Dexamethasone.
DB00997. Doxorubicin.
DB00125. L-Arginine.
DB00155. L-Citrulline.
DB01110. Miconazole.
DB08814. Triflusal.
GuidetoPHARMACOLOGYi1250.

PTM databases

iPTMnetiP35228.
PhosphoSitePlusiP35228.
SwissPalmiP35228.

Polymorphism and mutation databases

BioMutaiNOS2.
DMDMi1352513.

Proteomic databases

PaxDbiP35228.
PeptideAtlasiP35228.
PRIDEiP35228.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313735; ENSP00000327251; ENSG00000007171. [P35228-1]
ENST00000621962; ENSP00000482291; ENSG00000007171. [P35228-2]
GeneIDi4843.
KEGGihsa:4843.
UCSCiuc002gzu.4. human. [P35228-1]

Organism-specific databases

CTDi4843.
DisGeNETi4843.
GeneCardsiNOS2.
H-InvDBHIX0027239.
HGNCiHGNC:7873. NOS2.
HPAiCAB002014.
MalaCardsiNOS2.
MIMi163730. gene.
611162. phenotype.
neXtProtiNX_P35228.
OpenTargetsiENSG00000007171.
PharmGKBiPA164724093.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
COG4362. LUCA.
GeneTreeiENSGT00840000129757.
HOVERGENiHBG000159.
InParanoidiP35228.
KOiK13241.
OMAiKFTNSPT.
OrthoDBiEOG091G10Z0.
PhylomeDBiP35228.
TreeFamiTF324410.

Enzyme and pathway databases

BioCyciMetaCyc:HS00205-MONOMER.
ZFISH:HS00205-MONOMER.
BRENDAi1.14.13.39. 2681.
ReactomeiR-HSA-1222556. ROS, RNS production in response to bacteria.
R-HSA-392154. Nitric oxide stimulates guanylate cyclase.
SignaLinkiP35228.
SIGNORiP35228.

Miscellaneous databases

ChiTaRSiNOS2. human.
EvolutionaryTraceiP35228.
GeneWikiiNitric_oxide_synthase_2_(inducible).
GenomeRNAii4843.
PROiP35228.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000007171.
CleanExiHS_NOS2.
GenevisibleiP35228. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P35228
Secondary accession number(s): A1L3U5
, B7ZLY2, O60757, O94994, Q16263, Q16692, Q4TTS5, Q9UD42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 197 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.