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P35228

- NOS2_HUMAN

UniProt

P35228 - NOS2_HUMAN

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Protein

Nitric oxide synthase, inducible

Gene
NOS2, NOS2A
Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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.

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.

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 – 65432FMN By similarityAdd
BLAST
Nucleotide bindingi767 – 77812FAD By similarityAdd
BLAST
Nucleotide bindingi903 – 91311FAD By similarityAdd
BLAST
Nucleotide bindingi978 – 99619NADP By similarityAdd
BLAST
Nucleotide bindingi1076 – 109116NADP By 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
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.
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
Complete GO annotation...

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 PKA Reviewed prediction
Modified residuei578 – 5781Phosphoserine; by PKA Reviewed prediction
Modified residuei892 – 8921Phosphoserine; by PKA Reviewed prediction

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.

Miscellaneous databases

EvolutionaryTraceiP35228.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini539 – 677139Flavodoxin-likeAdd
BLAST
Domaini730 – 970241FAD-binding FR-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni509 – 52921Calmodulin-binding Reviewed predictionAdd
BLAST

Sequence similaritiesi

Belongs to the NOS family.

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

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. VSP_003582Add
BLAST
Alternative sequencei298 – 31114Missing in isoform 2. VSP_003583Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231D → G in AAA56666. 1 Publication
Sequence conflicti154 – 1541F → L in AAA56666. 1 Publication
Sequence conflicti177 – 1771G → V in AAA56666. 1 Publication
Sequence conflicti266 – 2661R → H in AAC19133. 1 Publication
Sequence conflicti423 – 4231L → I in AAA59171. 1 Publication
Sequence conflicti439 – 4391A → T in AAC19133. 1 Publication
Sequence conflicti552 – 5521A → G in AAI44127. 1 Publication
Sequence conflicti676 – 6761T → I in AAB60366. 1 Publication
Sequence conflicti800 – 8001T → A in AAA56666. 1 Publication
Sequence conflicti805 – 8051A → D in AAA59171. 1 Publication
Sequence conflicti831 – 8322FL → SP in AAA59171. 1 Publication
Sequence conflicti913 – 9131S → P in AAA56666. 1 Publication
Sequence conflicti933 – 9331R → G in AAA59171. 1 Publication
Sequence conflicti933 – 9331R → G in AAB60366. 1 Publication
Sequence conflicti966 – 9661G → A in AAA59171. 1 Publication
Sequence conflicti966 – 9661G → A in AAB60366. 1 Publication
Sequence conflicti987 – 9871A → V in AAA59171. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 174 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

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