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P35228

- NOS2_HUMAN

UniProt

P35228 - NOS2_HUMAN

Protein

Nitric oxide synthase, inducible

Gene

NOS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Cofactori

    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.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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi110 – 1101Zinc
    Metal bindingi115 – 1151Zinc
    Metal bindingi200 – 2001Iron (heme axial ligand)

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi623 – 65432FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi767 – 77812FADBy similarityAdd
    BLAST
    Nucleotide bindingi903 – 91311FADBy similarityAdd
    BLAST
    Nucleotide bindingi978 – 99619NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1076 – 109116NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. arginine binding Source: BHF-UCL
    2. flavin adenine dinucleotide binding Source: BHF-UCL
    3. FMN binding Source: BHF-UCL
    4. heme binding Source: BHF-UCL
    5. iron ion binding Source: InterPro
    6. NADP binding Source: BHF-UCL
    7. NADPH-hemoprotein reductase activity Source: RefGenome
    8. nitric-oxide synthase activity Source: UniProtKB
    9. protein binding Source: UniProtKB
    10. protein homodimerization activity Source: BHF-UCL
    11. receptor binding Source: UniProtKB
    12. tetrahydrobiopterin binding Source: BHF-UCL

    GO - Biological processi

    1. arginine catabolic process Source: BHF-UCL
    2. blood coagulation Source: Reactome
    3. cellular response to interferon-gamma Source: Ensembl
    4. cellular response to lipopolysaccharide Source: Ensembl
    5. defense response to bacterium Source: UniProtKB
    6. defense response to Gram-negative bacterium Source: BHF-UCL
    7. inflammatory response Source: RefGenome
    8. innate immune response in mucosa Source: BHF-UCL
    9. interaction with host Source: Reactome
    10. negative regulation of blood pressure Source: RefGenome
    11. negative regulation of gene expression Source: UniProtKB
    12. negative regulation of protein catabolic process Source: Ensembl
    13. nitric oxide biosynthetic process Source: UniProtKB
    14. nitric oxide mediated signal transduction Source: RefGenome
    15. peptidyl-cysteine S-nitrosylation Source: UniProtKB
    16. phagosome maturation Source: Reactome
    17. positive regulation of guanylate cyclase activity Source: RefGenome
    18. positive regulation of killing of cells of other organism Source: BHF-UCL
    19. positive regulation of leukocyte mediated cytotoxicity Source: BHF-UCL
    20. positive regulation of vasodilation Source: RefGenome
    21. regulation of cell proliferation Source: Ensembl
    22. regulation of cellular respiration Source: BHF-UCL
    23. regulation of insulin secretion Source: BHF-UCL
    24. response to bacterium Source: UniProtKB
    25. response to hypoxia Source: Ensembl
    26. superoxide metabolic process Source: UniProtKB

    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.
    ReactomeiREACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_23862. Nitric oxide stimulates guanylate cyclase.
    SignaLinkiP35228.

    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
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7873. NOS2.

    Subcellular locationi

    GO - Cellular componenti

    1. cortical cytoskeleton Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: BHF-UCL
    4. intracellular Source: BHF-UCL
    5. nucleus Source: BHF-UCL
    6. perinuclear region of cytoplasm Source: Ensembl
    7. peroxisome Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    MIMi611162. phenotype.
    PharmGKBiPA164724093.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11531153Nitric oxide synthase, induciblePRO_0000170930Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei234 – 2341Phosphoserine; by PKASequence Analysis
    Modified residuei578 – 5781Phosphoserine; by PKASequence Analysis
    Modified residuei892 – 8921Phosphoserine; by PKASequence Analysis

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP35228.
    PRIDEiP35228.

    PTM databases

    PhosphoSiteiP35228.

    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.1 Publication

    Gene expression databases

    ArrayExpressiP35228.
    BgeeiP35228.
    CleanExiHS_NOS2.
    GenevestigatoriP35228.

    Organism-specific databases

    HPAiCAB002014.

    Interactioni

    Subunit structurei

    Homodimer. Binds SLC9A3R1.

    Protein-protein interaction databases

    BioGridi110906. 148 interactions.
    DIPiDIP-59359N.

    Structurei

    Secondary structure

    1
    1153
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi85 – 895
    Turni90 – 923
    Beta strandi95 – 984
    Helixi100 – 1034
    Beta strandi104 – 1063
    Helixi123 – 1253
    Helixi136 – 15217
    Beta strandi154 – 1563
    Helixi159 – 17517
    Helixi183 – 19513
    Helixi203 – 2053
    Beta strandi210 – 2134
    Helixi220 – 23516
    Helixi236 – 2383
    Beta strandi243 – 2464
    Beta strandi251 – 2555
    Beta strandi261 – 2655
    Beta strandi269 – 2713
    Beta strandi277 – 2793
    Helixi281 – 2833
    Helixi284 – 2929
    Beta strandi307 – 3104
    Beta strandi317 – 3193
    Helixi323 – 3253
    Beta strandi328 – 3303
    Helixi337 – 3426
    Beta strandi345 – 3484
    Beta strandi356 – 3594
    Beta strandi362 – 3654
    Helixi375 – 3795
    Helixi381 – 3844
    Turni386 – 3894
    Helixi392 – 3998
    Helixi406 – 4083
    Helixi410 – 42819
    Helixi436 – 45419
    Helixi461 – 4644
    Beta strandi467 – 4693
    Helixi470 – 4723
    Helixi474 – 4774
    Beta strandi486 – 4916
    Helixi495 – 4984
    Helixi515 – 53420
    Beta strandi538 – 5447
    Beta strandi546 – 5483
    Helixi549 – 56113
    Turni562 – 5643
    Beta strandi565 – 5717
    Helixi572 – 5743
    Helixi577 – 5815
    Beta strandi584 – 5918
    Turni594 – 5963
    Helixi600 – 6023
    Helixi603 – 6119
    Beta strandi620 – 6278
    Beta strandi631 – 6333
    Helixi636 – 64813
    Beta strandi651 – 6544
    Beta strandi657 – 6604
    Helixi665 – 68319
    Helixi689 – 6913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP35228.
    SMRiP35228. Positions 83-505, 511-1132.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35228.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini539 – 677139Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini730 – 970241FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni509 – 52921Calmodulin-bindingSequence AnalysisAdd
    BLAST

    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

    eggNOGiCOG4362.
    HOVERGENiHBG000159.
    InParanoidiP35228.
    KOiK13241.
    OMAiKFTNSPT.
    OrthoDBiEOG79SDW7.
    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.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR012144. NOS_euk.
    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]
    PIRSFiPIRSF000333. NOS. 1 hit.
    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. Align

    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

    MACPWKFLFK TKFHQYAMNG EKDINNNVEK APCATSSPVT QDDLQYHNLS     50
    KQQNESPQPL VETGKKSPES LVKLDATPLS SPRHVRIKNW GSGMTFQDTL 100
    HHKAKGILTC RSKSCLGSIM TPKSLTRGPR DKPTPPDELL PQAIEFVNQY 150
    YGSFKEAKIE EHLARVEAVT KEIETTGTYQ LTGDELIFAT KQAWRNAPRC 200
    IGRIQWSNLQ VFDARSCSTA REMFEHICRH VRYSTNNGNI RSAITVFPQR 250
    SDGKHDFRVW NAQLIRYAGY QMPDGSIRGD PANVEFTQLC IDLGWKPKYG 300
    RFDVVPLVLQ ANGRDPELFE IPPDLVLEVA MEHPKYEWFR ELELKWYALP 350
    AVANMLLEVG GLEFPGCPFN GWYMGTEIGV RDFCDVQRYN ILEEVGRRMG 400
    LETHKLASLW KDQAVVEINI AVLHSFQKQN VTIMDHHSAA ESFMKYMQNE 450
    YRSRGGCPAD WIWLVPPMSG SITPVFHQEM LNYVLSPFYY YQVEAWKTHV 500
    WQDEKRRPKR REIPLKVLVK AVLFACMLMR KTMASRVRVT ILFATETGKS 550
    EALAWDLGAL FSCAFNPKVV CMDKYRLSCL EEERLLLVVT STFGNGDCPG 600
    NGEKLKKSLF MLKELNNKFR YAVFGLGSSM YPRFCAFAHD IDQKLSHLGA 650
    SQLTPMGEGD ELSGQEDAFR SWAVQTFKAA CETFDVRGKQ HIQIPKLYTS 700
    NVTWDPHHYR LVQDSQPLDL SKALSSMHAK NVFTMRLKSR QNLQSPTSSR 750
    ATILVELSCE DGQGLNYLPG EHLGVCPGNQ PALVQGILER VVDGPTPHQT 800
    VRLEALDESG SYWVSDKRLP PCSLSQALTY FLDITTPPTQ LLLQKLAQVA 850
    TEEPERQRLE ALCQPSEYSK WKFTNSPTFL EVLEEFPSLR VSAGFLLSQL 900
    PILKPRFYSI SSSRDHTPTE IHLTVAVVTY HTRDGQGPLH HGVCSTWLNS 950
    LKPQDPVPCF VRNASGFHLP EDPSHPCILI GPGTGIAPFR SFWQQRLHDS 1000
    QHKGVRGGRM TLVFGCRRPD EDHIYQEEML EMAQKGVLHA VHTAYSRLPG 1050
    KPKVYVQDIL RQQLASEVLR VLHKEPGHLY VCGDVRMARD VAHTLKQLVA 1100
    AKLKLNEEQV EDYFFQLKSQ KRYHEDIFGA VFPYEAKKDR VAVQPSSLEM 1150
    SAL 1153
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231D → G in AAA56666. (PubMed:7522054)Curated
    Sequence conflicti154 – 1541F → L in AAA56666. (PubMed:7522054)Curated
    Sequence conflicti177 – 1771G → V in AAA56666. (PubMed:7522054)Curated
    Sequence conflicti266 – 2661R → H in AAC19133. (PubMed:9160867)Curated
    Sequence conflicti423 – 4231L → I in AAA59171. (PubMed:7682706)Curated
    Sequence conflicti439 – 4391A → T in AAC19133. (PubMed:9160867)Curated
    Sequence conflicti552 – 5521A → G in AAI44127. (PubMed:15489334)Curated
    Sequence conflicti676 – 6761T → I in AAB60366. (PubMed:7544004)Curated
    Sequence conflicti800 – 8001T → A in AAA56666. (PubMed:7522054)Curated
    Sequence conflicti805 – 8051A → D in AAA59171. (PubMed:7682706)Curated
    Sequence conflicti831 – 8322FL → SP in AAA59171. (PubMed:7682706)Curated
    Sequence conflicti913 – 9131S → P in AAA56666. (PubMed:7522054)Curated
    Sequence conflicti933 – 9331R → G in AAA59171. (PubMed:7682706)Curated
    Sequence conflicti933 – 9331R → G in AAB60366. (PubMed:7544004)Curated
    Sequence conflicti966 – 9661G → A in AAA59171. (PubMed:7682706)Curated
    Sequence conflicti966 – 9661G → A in AAB60366. (PubMed:7544004)Curated
    Sequence conflicti987 – 9871A → V in AAA59171. (PubMed:7682706)Curated

    Polymorphismi

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti221 – 2211R → W.1 Publication
    Corresponds to variant rs3730017 [ dbSNP | Ensembl ].
    VAR_024548
    Natural varianti608 – 6081S → L.3 Publications
    Corresponds to variant rs2297518 [ dbSNP | Ensembl ].
    VAR_022127
    Natural varianti679 – 6791A → S in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036302
    Natural varianti747 – 7471T → A.1 Publication
    Corresponds to variant rs28944173 [ dbSNP | Ensembl ].
    VAR_025020
    Natural varianti1009 – 10091R → C.1 Publication
    Corresponds to variant rs28944201 [ dbSNP | Ensembl ].
    VAR_025021

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei264 – 28825Missing in isoform 2. 1 PublicationVSP_003582Add
    BLAST
    Alternative sequencei298 – 31114Missing in isoform 2. 1 PublicationVSP_003583Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    UniGeneiHs.709191.

    Genome annotation databases

    EnsembliENST00000313735; ENSP00000327251; ENSG00000007171. [P35228-1]
    GeneIDi4843.
    KEGGihsa:4843.
    UCSCiuc002gzu.3. human. [P35228-1]

    Polymorphism databases

    DMDMi1352513.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Nitric oxide synthase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11223.1. [P35228-1 ]
    PIRi A49676.
    RefSeqi NP_000616.3. NM_000625.4. [P35228-1 ]
    UniGenei Hs.709191.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NSI X-ray 2.55 A/B/C/D 74-504 [» ]
    2LL6 NMR - B 515-531 [» ]
    2NSI X-ray 3.00 A/B/C/D 74-504 [» ]
    3E7G X-ray 2.20 A/B/C/D 82-505 [» ]
    3EJ8 X-ray 2.55 A/B/C/D 82-505 [» ]
    3HR4 X-ray 2.50 A/C/E/G 503-715 [» ]
    4NOS X-ray 2.25 A/B/C/D 82-508 [» ]
    ProteinModelPortali P35228.
    SMRi P35228. Positions 83-505, 511-1132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110906. 148 interactions.
    DIPi DIP-59359N.

    Chemistry

    BindingDBi P35228.
    ChEMBLi CHEMBL2111350.
    DrugBanki DB01234. Dexamethasone.
    DB00741. Hydrocortisone.
    DB00125. L-Arginine.
    DB00155. L-Citrulline.
    GuidetoPHARMACOLOGYi 1250.

    PTM databases

    PhosphoSitei P35228.

    Polymorphism databases

    DMDMi 1352513.

    Proteomic databases

    PaxDbi P35228.
    PRIDEi P35228.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313735 ; ENSP00000327251 ; ENSG00000007171 . [P35228-1 ]
    GeneIDi 4843.
    KEGGi hsa:4843.
    UCSCi uc002gzu.3. human. [P35228-1 ]

    Organism-specific databases

    CTDi 4843.
    GeneCardsi GC17M026083.
    H-InvDB HIX0027239.
    HGNCi HGNC:7873. NOS2.
    HPAi CAB002014.
    MIMi 163730. gene.
    611162. phenotype.
    neXtProti NX_P35228.
    PharmGKBi PA164724093.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4362.
    HOVERGENi HBG000159.
    InParanoidi P35228.
    KOi K13241.
    OMAi KFTNSPT.
    OrthoDBi EOG79SDW7.
    PhylomeDBi P35228.
    TreeFami TF324410.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00205-MONOMER.
    Reactomei REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_23862. Nitric oxide stimulates guanylate cyclase.
    SignaLinki P35228.

    Miscellaneous databases

    ChiTaRSi NOS2. human.
    EvolutionaryTracei P35228.
    GeneWikii Nitric_oxide_synthase_2_(inducible).
    GenomeRNAii 4843.
    NextBioi 18662.
    PROi P35228.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35228.
    Bgeei P35228.
    CleanExi HS_NOS2.
    Genevestigatori P35228.

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    3.90.340.10. 1 hit.
    InterProi IPR003097. 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.
    IPR012144. NOS_euk.
    IPR004030. NOS_N.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    PF02898. NO_synthase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000333. NOS. 1 hit.
    PRINTSi PR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMi SSF52218. SSF52218. 1 hit.
    SSF56512. SSF56512. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    PS60001. NOS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-679.

    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: October 1, 2014
    This is version 175 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

    External Data

    Dasty 3