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P35228 (NOS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NOS2
Synonyms:NOS2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1153 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Heme group By similarity.

Binds 1 FAD By similarity.

Binds 1 FMN By similarity.

Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme By similarity.

Enzyme regulation

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.

Subunit structure

Homodimer. Binds SLC9A3R1.

Tissue specificity

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

Induction

By endotoxins and cytokines. Induced by IFNG/IFN-gamma acting synergistically with bacterial lipopolysaccharides (LPS), TNF or IL1B/interleukin-1 beta. Ref.14

Polymorphism

Note=Genetic variations in NOS2 are involved in resistance to malaria [MIM:611162].

Sequence similarities

Belongs to the NOS family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandCalcium
Calmodulin-binding
FAD
Flavoprotein
FMN
Heme
Iron
Metal-binding
NADP
Zinc
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine catabolic process

Inferred from direct assay Ref.3. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

cellular response to interferon-gamma

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-negative bacterium

Non-traceable author statement PubMed 18390757. Source: BHF-UCL

defense response to bacterium

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Inferred from Biological aspect of Ancestor. Source: RefGenome

innate immune response in mucosa

Non-traceable author statement PubMed 18390757. Source: BHF-UCL

interaction with host

Traceable author statement. Source: Reactome

negative regulation of blood pressure

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of gene expression

Inferred from genetic interaction PubMed 12085352. Source: UniProtKB

negative regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

nitric oxide biosynthetic process

Inferred from direct assay Ref.2. Source: UniProtKB

nitric oxide mediated signal transduction

Inferred from Biological aspect of Ancestor. Source: RefGenome

peptidyl-cysteine S-nitrosylation

Inferred from sequence or structural similarity. Source: UniProtKB

phagosome maturation

Traceable author statement. Source: Reactome

positive regulation of guanylate cyclase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of killing of cells of other organism

Inferred from mutant phenotype PubMed 7544003. Source: BHF-UCL

positive regulation of leukocyte mediated cytotoxicity

Traceable author statement PubMed 10450191. Source: BHF-UCL

positive regulation of vasodilation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of cellular respiration

Traceable author statement PubMed 10450191. Source: BHF-UCL

regulation of insulin secretion

Inferred from mutant phenotype PubMed 8383325. Source: BHF-UCL

response to bacterium

Non-traceable author statement PubMed 12085352. Source: UniProtKB

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

superoxide metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcortical cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 12085352. Source: UniProtKB

cytosol

Inferred from mutant phenotype Ref.3. Source: BHF-UCL

intracellular

Inferred from direct assay PubMed 7544003. Source: BHF-UCL

nucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

peroxisome

Inferred from direct assay PubMed 12085352. Source: UniProtKB

   Molecular_functionFMN binding

Inferred from sequence or structural similarity. Source: BHF-UCL

NADP binding

Traceable author statement Ref.3. Source: BHF-UCL

NADPH-hemoprotein reductase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

arginine binding

Inferred from sequence or structural similarity. Source: BHF-UCL

flavin adenine dinucleotide binding

Inferred from sequence or structural similarity. Source: BHF-UCL

heme binding

Inferred from sequence or structural similarity. Source: BHF-UCL

iron ion binding

Inferred from electronic annotation. Source: InterPro

nitric-oxide synthase activity

Inferred from direct assay Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12855682. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

tetrahydrobiopterin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35228-1)

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.
Isoform 2 (identifier: P35228-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11531153Nitric oxide synthase, inducible
PRO_0000170930

Regions

Domain539 – 677139Flavodoxin-like
Domain730 – 970241FAD-binding FR-type
Nucleotide binding623 – 65432FMN By similarity
Nucleotide binding767 – 77812FAD By similarity
Nucleotide binding903 – 91311FAD By similarity
Nucleotide binding978 – 99619NADP By similarity
Nucleotide binding1076 – 109116NADP By similarity
Region509 – 52921Calmodulin-binding Potential

Sites

Metal binding1101Zinc
Metal binding1151Zinc
Metal binding2001Iron (heme axial ligand)

Amino acid modifications

Modified residue2341Phosphoserine; by PKA Potential
Modified residue5781Phosphoserine; by PKA Potential
Modified residue8921Phosphoserine; by PKA Potential

Natural variations

Alternative sequence264 – 28825Missing in isoform 2.
VSP_003582
Alternative sequence298 – 31114Missing in isoform 2.
VSP_003583
Natural variant2211R → W. Ref.10
Corresponds to variant rs3730017 [ dbSNP | Ensembl ].
VAR_024548
Natural variant6081S → L. Ref.5 Ref.6 Ref.10
Corresponds to variant rs2297518 [ dbSNP | Ensembl ].
VAR_022127
Natural variant6791A → S in a breast cancer sample; somatic mutation. Ref.21
VAR_036302
Natural variant7471T → A. Ref.10
Corresponds to variant rs28944173 [ dbSNP | Ensembl ].
VAR_025020
Natural variant10091R → C. Ref.10
Corresponds to variant rs28944201 [ dbSNP | Ensembl ].
VAR_025021

Experimental info

Sequence conflict231D → G in AAA56666. Ref.4
Sequence conflict1541F → L in AAA56666. Ref.4
Sequence conflict1771G → V in AAA56666. Ref.4
Sequence conflict2661R → H in AAC19133. Ref.8
Sequence conflict4231L → I in AAA59171. Ref.2
Sequence conflict4391A → T in AAC19133. Ref.8
Sequence conflict5521A → G in AAI44127. Ref.12
Sequence conflict6761T → I in AAB60366. Ref.7
Sequence conflict8001T → A in AAA56666. Ref.4
Sequence conflict8051A → D in AAA59171. Ref.2
Sequence conflict831 – 8322FL → SP in AAA59171. Ref.2
Sequence conflict9131S → P in AAA56666. Ref.4
Sequence conflict9331R → G in AAA59171. Ref.2
Sequence conflict9331R → G in AAB60366. Ref.7
Sequence conflict9661G → A in AAA59171. Ref.2
Sequence conflict9661G → A in AAB60366. Ref.7
Sequence conflict9871A → V in AAA59171. Ref.2

Secondary structure

................................................................................................................. 1153
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 47671E5385CB3A52

FASTA1,153131,117
        10         20         30         40         50         60 
MACPWKFLFK TKFHQYAMNG EKDINNNVEK APCATSSPVT QDDLQYHNLS KQQNESPQPL 

        70         80         90        100        110        120 
VETGKKSPES LVKLDATPLS SPRHVRIKNW GSGMTFQDTL HHKAKGILTC RSKSCLGSIM 

       130        140        150        160        170        180 
TPKSLTRGPR DKPTPPDELL PQAIEFVNQY YGSFKEAKIE EHLARVEAVT KEIETTGTYQ 

       190        200        210        220        230        240 
LTGDELIFAT KQAWRNAPRC IGRIQWSNLQ VFDARSCSTA REMFEHICRH VRYSTNNGNI 

       250        260        270        280        290        300 
RSAITVFPQR SDGKHDFRVW NAQLIRYAGY QMPDGSIRGD PANVEFTQLC IDLGWKPKYG 

       310        320        330        340        350        360 
RFDVVPLVLQ ANGRDPELFE IPPDLVLEVA MEHPKYEWFR ELELKWYALP AVANMLLEVG 

       370        380        390        400        410        420 
GLEFPGCPFN GWYMGTEIGV RDFCDVQRYN ILEEVGRRMG LETHKLASLW KDQAVVEINI 

       430        440        450        460        470        480 
AVLHSFQKQN VTIMDHHSAA ESFMKYMQNE YRSRGGCPAD WIWLVPPMSG SITPVFHQEM 

       490        500        510        520        530        540 
LNYVLSPFYY YQVEAWKTHV WQDEKRRPKR REIPLKVLVK AVLFACMLMR KTMASRVRVT 

       550        560        570        580        590        600 
ILFATETGKS EALAWDLGAL FSCAFNPKVV CMDKYRLSCL EEERLLLVVT STFGNGDCPG 

       610        620        630        640        650        660 
NGEKLKKSLF MLKELNNKFR YAVFGLGSSM YPRFCAFAHD IDQKLSHLGA SQLTPMGEGD 

       670        680        690        700        710        720 
ELSGQEDAFR SWAVQTFKAA CETFDVRGKQ HIQIPKLYTS NVTWDPHHYR LVQDSQPLDL 

       730        740        750        760        770        780 
SKALSSMHAK NVFTMRLKSR QNLQSPTSSR ATILVELSCE DGQGLNYLPG EHLGVCPGNQ 

       790        800        810        820        830        840 
PALVQGILER VVDGPTPHQT VRLEALDESG SYWVSDKRLP PCSLSQALTY FLDITTPPTQ 

       850        860        870        880        890        900 
LLLQKLAQVA TEEPERQRLE ALCQPSEYSK WKFTNSPTFL EVLEEFPSLR VSAGFLLSQL 

       910        920        930        940        950        960 
PILKPRFYSI SSSRDHTPTE IHLTVAVVTY HTRDGQGPLH HGVCSTWLNS LKPQDPVPCF 

       970        980        990       1000       1010       1020 
VRNASGFHLP EDPSHPCILI GPGTGIAPFR SFWQQRLHDS QHKGVRGGRM TLVFGCRRPD 

      1030       1040       1050       1060       1070       1080 
EDHIYQEEML EMAQKGVLHA VHTAYSRLPG KPKVYVQDIL RQQLASEVLR VLHKEPGHLY 

      1090       1100       1110       1120       1130       1140 
VCGDVRMARD VAHTLKQLVA AKLKLNEEQV EDYFFQLKSQ KRYHEDIFGA VFPYEAKKDR 

      1150 
VAVQPSSLEM SAL 

« Hide

Isoform 2 [UniParc].

Checksum: C1F9624774435571
Show »

FASTA1,114126,749

References

« Hide 'large scale' references
[1]"Purification and cDNA sequence of an inducible nitric oxide synthase from a human tumor cell line."
Sherman P.A., Laubach V.E., Reep B.R., Wood E.R.
Biochemistry 32:11600-11605(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon adenocarcinoma.
[2]"Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes."
Geller D.A., Lowenstein C.J., Shapiro R.A., Nussler A.K., di Silvio M., Wang S.C., Nakayama D.K., Simmons R.L., Snyder S.H., Billiar T.R.
Proc. Natl. Acad. Sci. U.S.A. 90:3491-3495(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[3]"Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte."
Charles I.G., Palmer R.M.J., Hickery M.S., Bayliss M.T., Chubb A.P., Hall V.S., Moss D.W., Moncada S.
Proc. Natl. Acad. Sci. U.S.A. 90:11419-11423(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Chondrocyte.
[4]"Inducible nitric oxide synthase from human articular chondrocytes: cDNA cloning and analysis of mRNA expression."
Maier R., Bilbe G., Rediske J., Lotz M.
Biochim. Biophys. Acta 1208:145-150(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Articular chondrocyte.
[5]"Human retina expresses both constitutive and inducible isoforms of nitric oxide synthase mRNA."
Park C.S., Pardhasaradhi K., Gianotti C., Villegas E., Krishna G.
Biochem. Biophys. Res. Commun. 205:85-91(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-608.
Tissue: Retina.
[6]"Cloning and functional expression of human inducible nitric oxide synthase (NOS) cDNA from a glioblastoma cell line A-172."
Hokari A., Zeniya M., Esumi H.
J. Biochem. 116:575-581(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-608.
Tissue: Glioblastoma.
[7]"Continuous nitric oxide synthesis by inducible nitric oxide synthase in normal human airway epithelium in vivo."
Guo F.H., de Raeve R.H., Rice T.W., Stuehr D.J., Thunnissen F.B.J.M., Erzurum S.C.
Proc. Natl. Acad. Sci. U.S.A. 92:7809-7813(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Airway epithelium.
[8]"Dedifferentiated human ventricular cardiac myocytes express inducible nitric oxide synthase mRNA but not protein in response to IL-1, TNF, IFNgamma, and LPS."
Luss H., Li R.-K., Shapiro R.A., Tzeng E., McGowan F.X., Yoneyama T., Hatakayama K., Geller D.A., Mickle D.A.G., Simmons R.L., Billiar T.R.
J. Mol. Cell. Cardiol. 29:1153-1165(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Cardiac myocyte.
[9]"Cloning and characterization of a novel splice valiant of human inducible nitric oxide synthase."
Ogawa Y., Nishijima S., Goto M., Ida M.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[10]NIEHS SNPs program
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-221; LEU-608; ALA-747 AND CYS-1009.
[11]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[13]"Nitric oxide production by human proximal tubular cells: a novel immunomodulatory mechanism?"
McLay J.S., Chatterjee P., Nicolson A.G., Jardine A.G., McKay N.G., Ralston S.H., Grabowski P., Haites N.E., Macleod A.M., Hawksworth G.M.
Kidney Int. 46:1043-1049(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 380-473.
Tissue: Kidney.
[14]"Inducible nitric oxide synthase in a human glioblastoma cell line."
Fujisawa H., Ogura T., Hokari A., Weisz A., Yamashita J., Esumi H.
J. Neurochem. 64:85-91(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 667-831, INDUCTION.
Tissue: Glioblastoma.
[15]"Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B, and NOS2C) colocalize to human chromosome 17."
Bloch K.D., Wolfram J.R., Brown D.M., Roberts J.D. Jr., Zapol D.G., Lepore J.J., Filippov G., Thomas J.E., Jacob H.J., Bloch D.B.
Genomics 27:526-530(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[16]"Inducible nitric oxide synthase in the liver: regulation and function."
Taylor B.S., Alarcon L.H., Billiar T.R.
Biochemistry (Mosc.) 63:766-781(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[17]"Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output."
Glynne P.A., Darling K.E.A., Picot J., Evans T.J.
J. Biol. Chem. 277:33132-33138(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC9A3R1.
[18]"A new NOS2 promoter polymorphism associated with increased nitric oxide production and protection from severe malaria in Tanzanian and Kenyan children."
Hobbs M.R., Udhayakumar V., Levesque M.C., Booth J., Roberts J.M., Tkachuk A.N., Pole A., Coon H., Kariuki S., Nahlen B.L., Mwaikambo E.D., Lal A.L., Granger D.L., Anstey N.M., Weinberg J.B.
Lancet 360:1468-1475(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM, INVOLVEMENT IN RESISTANCE TO MALARIA.
[19]"Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase."
Li H., Raman C.S., Glaser C.B., Blasko E., Young T.A., Parkinson J.F., Whitlow M., Poulos T.L.
J. Biol. Chem. 274:21276-21284(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 74-504.
[20]"Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation."
Fischmann T.O., Hruza A., Niu X.D., Fossetta J.D., Lunn C.A., Dolphin E., Prongay A.J., Reichert P., Lundell D.J., Narula S.K., Weber P.C.
Nat. Struct. Biol. 6:233-242(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 82-528.
[21]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-679.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Nitric oxide synthase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11223.1. [P35228-1]
PIRA49676.
RefSeqNP_000616.3. NM_000625.4. [P35228-1]
UniGeneHs.709191.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
4NOSX-ray2.25A/B/C/D82-508[»]
ProteinModelPortalP35228.
SMRP35228. Positions 83-505, 511-1132.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110906. 148 interactions.
DIPDIP-59359N.

Chemistry

BindingDBP35228.
ChEMBLCHEMBL2111350.
DrugBankDB01234. Dexamethasone.
DB00741. Hydrocortisone.
DB00125. L-Arginine.
DB00155. L-Citrulline.
GuidetoPHARMACOLOGY1250.

PTM databases

PhosphoSiteP35228.

Polymorphism databases

DMDM1352513.

Proteomic databases

PaxDbP35228.
PRIDEP35228.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313735; ENSP00000327251; ENSG00000007171. [P35228-1]
GeneID4843.
KEGGhsa:4843.
UCSCuc002gzu.3. human. [P35228-1]

Organism-specific databases

CTD4843.
GeneCardsGC17M026083.
H-InvDBHIX0027239.
HGNCHGNC:7873. NOS2.
HPACAB002014.
MIM163730. gene.
611162. phenotype.
neXtProtNX_P35228.
PharmGKBPA164724093.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4362.
HOVERGENHBG000159.
InParanoidP35228.
KOK13241.
OMAKFTNSPT.
OrthoDBEOG79SDW7.
PhylomeDBP35228.
TreeFamTF324410.

Enzyme and pathway databases

BioCycMetaCyc:HS00205-MONOMER.
ReactomeREACT_116125. Disease.
REACT_604. Hemostasis.
SignaLinkP35228.

Gene expression databases

ArrayExpressP35228.
BgeeP35228.
CleanExHS_NOS2.
GenevestigatorP35228.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
3.90.340.10. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR004030. NO_synthase_oxygenase_dom.
IPR012144. NOS_euk.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF000333. NOS. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNOS2. human.
EvolutionaryTraceP35228.
GeneWikiNitric_oxide_synthase_2_(inducible).
GenomeRNAi4843.
NextBio18662.
PROP35228.
SOURCESearch...

Entry information

Entry nameNOS2_HUMAN
AccessionPrimary (citable) accession number: P35228
Secondary accession number(s): A1L3U5 expand/collapse secondary AC list , B7ZLY2, O60757, O94994, Q16263, Q16692, Q4TTS5, Q9UD42
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM