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Protein

Nitric oxide synthase, brain

Gene

Nos1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Stimulated by calcium/calmodulin. Inhibited by n-Nos-inhibiting protein (PIN) which may prevent the dimerization of the protein (By similarity). Inhibited by NOSIP.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi415Iron (heme axial ligand)By similarity1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei588Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi881 – 912FMNPROSITE-ProRule annotationAdd BLAST32
Nucleotide bindingi1027 – 1038FADBy similarityAdd BLAST12
Nucleotide bindingi1170 – 1180FADBy similarityAdd BLAST11
Nucleotide bindingi1245 – 1263NADPBy similarityAdd BLAST19
Nucleotide bindingi1343 – 1358NADPBy similarityAdd BLAST16

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • amino acid binding Source: RGD
  • ATPase binding Source: BHF-UCL
  • cadmium ion binding Source: BHF-UCL
  • calmodulin binding Source: RGD
  • enzyme binding Source: RGD
  • flavin adenine dinucleotide binding Source: BHF-UCL
  • FMN binding Source: BHF-UCL
  • heme binding Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • NADP binding Source: BHF-UCL
  • NADPH-hemoprotein reductase activity Source: GO_Central
  • nitric-oxide synthase activity Source: BHF-UCL
  • oxidoreductase activity Source: GO_Central
  • phosphoprotein binding Source: CAFA
  • protein homodimerization activity Source: RGD
  • scaffold protein binding Source: BHF-UCL
  • sodium channel regulator activity Source: BHF-UCL

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCalmodulin-binding, Oxidoreductase
LigandFAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.13.39 5301

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P29476

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Nitric oxide synthase, brain (EC:1.14.13.39)
Alternative name(s):
BNOS
Constitutive NOS
NC-NOS
NOS type I
Neuronal NOS
Short name:
N-NOS
Short name:
nNOS
Peptidyl-cysteine S-nitrosylase NOS1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Nos1
Synonyms:Bnos
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3184 Nos1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi588Y → F: No decrease in activity. 1 Publication1
Mutagenesisi588Y → H: 50% decrease of activity. 1 Publication1
Mutagenesisi588Y → S: 30% decrease of activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3048

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1251

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001709241 – 1429Nitric oxide synthase, brainAdd BLAST1429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei280PhosphoserineBy similarity1
Modified residuei847PhosphoserineCombined sources1
Modified residuei857PhosphoserineBy similarity1
Modified residuei858PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and Hsp40 (in vitro).1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P29476

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P29476

PRoteomics IDEntifications database

More...
PRIDEi
P29476

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P29476

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P29476

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P29476

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform N-NOS-1 is expressed in brain and colorectum. Found in the Auerbach's plexus of the enteric nervous system. Isoform PNNOS is expressed in the penis, urethra, prostate, and skeletal muscle, and coexists with the cerebellar nnos in the pelvic plexus, bladder and liver, and is detectable in the cerebellum.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Interacts with DLG4; the interaction possibly being prevented by the association between NOS1 and CAPON (By similarity). Forms a ternary complex with CAPON and RASD1. Forms a ternary complex with CAPON and SYN1. Interacts with ZDHHC23. Interacts with NOSIP; which may impair its synaptic location. Interacts with HTR4 (By similarity). Interacts with SLC6A4 (By similarity). Interacts with VAC14. Interacts (via N-terminal domain) with DLG4 (via N-terminal tandem pair of PDZ domains).By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
246738, 13 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P29476

Database of interacting proteins

More...
DIPi
DIP-33272N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P29476

Protein interaction database and analysis system

More...
IntActi
P29476, 9 interactors

Molecular INTeraction database

More...
MINTi
P29476

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000062735

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P29476

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11429
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8QNMR-A11-133[»]
1CMIX-ray2.50C/D225-237[»]
1F20X-ray1.90A963-1397[»]
1K2RX-ray2.15A/B299-717[»]
1K2SX-ray2.55A/B299-717[»]
1K2TX-ray2.20A/B299-717[»]
1K2UX-ray2.20A/B299-717[»]
1LZXX-ray2.00A/B299-717[»]
1LZZX-ray2.05A/B299-717[»]
1M00X-ray2.05A/B299-717[»]
1MMVX-ray2.00A/B299-717[»]
1MMWX-ray2.00A/B299-717[»]
1OM4X-ray1.75A/B297-718[»]
1OM5X-ray2.30A/B297-717[»]
1P6HX-ray1.98A/B297-717[»]
1P6IX-ray1.90A/B297-717[»]
1P6JX-ray2.00A/B297-717[»]
1P6KX-ray1.78A/B297-717[»]
1QAUX-ray1.25A14-125[»]
1QAVX-ray1.90B12-126[»]
1QW6X-ray2.10A298-716[»]
1QWCX-ray2.30A298-716[»]
1RS6X-ray1.95A/B297-717[»]
1RS7X-ray1.95A/B297-717[»]
1TLLX-ray2.30A/B742-1429[»]
1VAGX-ray2.00A298-716[»]
1ZVIX-ray2.00A298-716[»]
1ZVLX-ray2.50A/B298-716[»]
1ZZQX-ray1.90A/B299-718[»]
1ZZRX-ray2.05A/B299-718[»]
1ZZUX-ray1.90A/B299-718[»]
2G6HX-ray2.00A/B299-718[»]
2G6IX-ray1.90A/B299-718[»]
2G6JX-ray2.30A/B299-718[»]
2G6KX-ray2.00A/B299-718[»]
2G6LX-ray2.05A/B299-718[»]
2G6MX-ray1.85A/B299-718[»]
2G6NX-ray1.90A/B299-718[»]
2HX3X-ray2.00A/B297-718[»]
2HX4X-ray2.15A/B297-718[»]
3B3MX-ray1.95A/B297-718[»]
3B3NX-ray1.98A/B297-718[»]
3B3OX-ray2.05A/B297-718[»]
3B3PX-ray2.45A/B297-718[»]
3DQRX-ray2.40A/B297-718[»]
3FC5X-ray2.59A/B297-718[»]
3HSNX-ray1.91A/B297-718[»]
3HSOX-ray2.02A/B297-718[»]
3HSPX-ray2.20A/B297-718[»]
3JT3X-ray2.15A/B297-718[»]
3JT4X-ray1.80A/B297-718[»]
3JT5X-ray2.10A/B297-718[»]
3JT6X-ray2.20A/B297-718[»]
3JT7X-ray2.10A/B297-718[»]
3JT8X-ray1.95A/B297-718[»]
3JT9X-ray2.10A/B297-718[»]
3JTAX-ray2.18A/B297-718[»]
3JWSX-ray1.95A/B297-718[»]
3JWTX-ray2.01A/B297-718[»]
3JWUX-ray1.93A/B297-718[»]
3JWVX-ray1.98A/B297-718[»]
3JX0X-ray2.20A/B297-718[»]
3JX1X-ray2.00A/B297-718[»]
3JX2X-ray2.10A/B297-718[»]
3JX3X-ray1.95A/B297-718[»]
3JX4X-ray2.26A/B297-718[»]
3JX5X-ray2.15A/B297-718[»]
3JX6X-ray2.35A/B297-718[»]
3N2RX-ray1.90A/B297-718[»]
3N5VX-ray2.30A/B297-718[»]
3N5WX-ray1.73A/B297-718[»]
3N5XX-ray1.80A/B297-718[»]
3N5YX-ray2.05A/B297-718[»]
3N5ZX-ray2.18A/B297-718[»]
3N60X-ray1.98A/B297-718[»]
3N61X-ray1.95A/B297-718[»]
3N62X-ray1.95A/B297-718[»]
3N63X-ray2.00A/B297-718[»]
3N64X-ray1.95A/B297-718[»]
3N65X-ray1.80A/B297-718[»]
3N66X-ray1.78A/B297-718[»]
3N67X-ray2.09A/B298-711[»]
3N68X-ray2.53A/B298-711[»]
3N69X-ray2.65A/B298-711[»]
3N6AX-ray2.49A/B298-711[»]
3N6BX-ray3.10A/B298-711[»]
3N6CX-ray3.06A/B298-711[»]
3N6DX-ray3.05A/B298-711[»]
3N6EX-ray2.20A/B298-711[»]
3N6FX-ray2.18A/B298-711[»]
3N6GX-ray2.21A/B298-711[»]
3NLJX-ray2.20A/B297-718[»]
3NLKX-ray2.02A/B297-718[»]
3NLMX-ray1.85A/B297-718[»]
3NLNX-ray2.00A/B297-718[»]
3NLOX-ray2.30A/B297-718[»]
3NLPX-ray2.02A/B297-718[»]
3NLQX-ray2.15A/B297-718[»]
3NLRX-ray2.10A/B297-718[»]
3NLVX-ray2.10A/B297-718[»]
3NLWX-ray2.10A/B297-718[»]
3NLXX-ray1.87A/B297-718[»]
3NLYX-ray1.99A/B297-718[»]
3NLZX-ray1.92A/B297-718[»]
3NM0X-ray1.81A/B297-718[»]
3NNYX-ray2.10A/B297-718[»]
3NNZX-ray1.97A/B297-718[»]
3PNEX-ray1.97A/B297-718[»]
3PNFX-ray1.94A/B297-718[»]
3PNGX-ray1.88A/B297-718[»]
3Q99X-ray2.15A/B297-718[»]
3Q9AX-ray2.24A/B297-718[»]
3RQJX-ray1.84A/B297-718[»]
3RQKX-ray2.21A/B297-718[»]
3RQLX-ray1.93A/B297-718[»]
3RQMX-ray1.95A/B297-718[»]
3RQNX-ray1.95A/B297-718[»]
3SVPX-ray2.05A/B297-718[»]
3SVQX-ray2.18A/B297-718[»]
3TYLX-ray1.90A/B297-718[»]
3TYMX-ray2.00A/B297-718[»]
3TYNX-ray1.97A/B297-718[»]
3TYOX-ray1.93A/B297-718[»]
3UFOX-ray2.17A/B297-718[»]
3UFPX-ray2.10A/B297-718[»]
3UFQX-ray2.06A/B297-718[»]
3UFRX-ray2.10A/B297-718[»]
3UFSX-ray1.97A/B297-718[»]
3UFTX-ray2.08A/B297-718[»]
3UFUX-ray1.89A/B297-718[»]
3UFVX-ray2.08A/B297-718[»]
3UFWX-ray2.00A/B297-718[»]
4C39X-ray1.98A/B297-718[»]
4CAMX-ray1.83A/B297-718[»]
4CANX-ray1.91A/B297-718[»]
4CAOX-ray1.98A/B297-718[»]
4CAPX-ray2.06A/B297-718[»]
4CAQX-ray1.95A/B297-718[»]
4CDTX-ray2.00A/B297-718[»]
4CTPX-ray2.05A/B297-718[»]
4CTQX-ray2.00A/B297-718[»]
4CTRX-ray2.20A/B297-718[»]
4CTTX-ray2.30A/B297-718[»]
4CTUX-ray2.16A/B297-718[»]
4CTVX-ray1.78A/B297-718[»]
4CTWX-ray1.90A/B297-718[»]
4CTXX-ray1.82A/B297-718[»]
4CX3X-ray1.97A/B297-718[»]
4CX4X-ray1.98A/B297-718[»]
4CX5X-ray1.80A/B297-718[»]
4CX6X-ray1.90A/B297-718[»]
4D2YX-ray1.98A/B297-718[»]
4D2ZX-ray1.89A/B297-718[»]
4D30X-ray1.96A/B297-718[»]
4D31X-ray1.95A/B297-718[»]
4D32X-ray2.10A/B297-718[»]
4D3BX-ray1.80A/B297-718[»]
4D7OX-ray1.78A/B297-718[»]
4EUXX-ray2.14A/B297-718[»]
4FVWX-ray1.81A/B297-718[»]
4FVXX-ray2.00A/B297-718[»]
4FVYX-ray1.70A/B297-718[»]
4FVZX-ray1.99A/B297-718[»]
4FW0X-ray1.95A/B297-718[»]
4GQEX-ray1.80A/B297-718[»]
4HOPX-ray2.29B/D/F4-126[»]
4IMSX-ray2.15A/B297-718[»]
4IMTX-ray2.20A/B297-718[»]
4IMUX-ray2.03A/B297-718[»]
4IMWX-ray2.20A/B297-718[»]
4JSEX-ray1.97A/B297-718[»]
4JSFX-ray2.05A/B297-718[»]
4JSGX-ray1.94A/B297-718[»]
4JSHX-ray2.35A/B297-718[»]
4JSIX-ray2.09A/B297-718[»]
4JSJX-ray1.92A/B297-718[»]
4K5DX-ray2.10A/B297-718[»]
4K5EX-ray1.89A/B297-718[»]
4K5FX-ray2.20A/B297-718[»]
4K5GX-ray1.85A/B297-718[»]
4KCHX-ray2.15A/B297-718[»]
4KCIX-ray2.27A/B297-718[»]
4KCJX-ray2.05A/B297-718[»]
4KCKX-ray2.10A/B297-718[»]
4KCLX-ray1.93A/B297-718[»]
4KCMX-ray2.07A/B297-718[»]
4KCNX-ray1.85A/B297-718[»]
4KCOX-ray1.86A/B297-718[»]
4LUXX-ray1.86A/B297-718[»]
4UGZX-ray2.08A/B297-718[»]
4UH0X-ray2.04A/B297-718[»]
4UH1X-ray1.80A/B297-718[»]
4UH2X-ray1.99A/B297-718[»]
4UH3X-ray2.03A/B297-718[»]
4UH4X-ray1.95A/B297-718[»]
4UPMX-ray1.90A/B297-718[»]
4UPNX-ray2.09A/B297-718[»]
4UPOX-ray1.95A/B297-718[»]
4UPPX-ray1.91A/B297-718[»]
4V3VX-ray2.06A/B297-718[»]
4V3WX-ray2.13A/B297-718[»]
4V3XX-ray1.99A/B297-718[»]
4V3YX-ray1.96A/B297-718[»]
4V3ZX-ray2.05A/B297-718[»]
5AD4X-ray1.98A/B297-718[»]
5AD5X-ray1.90A/B297-718[»]
5AD6X-ray2.00A/B297-718[»]
5AD7X-ray1.95A/B297-718[»]
5AD8X-ray1.91A/B297-718[»]
5AD9X-ray2.30A/B297-718[»]
5ADAX-ray1.98A/B297-718[»]
5ADBX-ray2.05A/B297-718[»]
5ADCX-ray2.10A/B297-718[»]
5ADDX-ray2.10A/B297-718[»]
5ADEX-ray2.10A/B297-718[»]
5AGKX-ray2.00A/B297-718[»]
5AGLX-ray1.94A/B297-718[»]
5AGMX-ray1.84A/B297-718[»]
5AGNX-ray1.95A/B297-718[»]
5AGOX-ray1.90A/B297-718[»]
5AGPX-ray2.10A/B297-718[»]
5FVOX-ray2.12A297-718[»]
5FVPX-ray2.10A/B297-718[»]
5FVQX-ray1.95A/B297-718[»]
5FVRX-ray1.84A/B297-718[»]
5FVSX-ray1.95A/B297-718[»]
5FVTX-ray1.83A/B297-718[»]
5FW0X-ray1.80A/B297-718[»]
5G0NX-ray1.94A/B297-718[»]
5G0OX-ray1.85A/B297-718[»]
5G0PX-ray2.10A/B297-718[»]
5UNRX-ray1.95A/B297-718[»]
5UNSX-ray1.90A/B297-718[»]
5UNTX-ray2.05A/B297-718[»]
5UNUX-ray2.05A/B297-718[»]
5UNVX-ray2.00A/B297-718[»]
5UNWX-ray2.04A/B297-718[»]
5UNXX-ray2.03A/B297-718[»]
5UNYX-ray1.82A/B297-718[»]
5UNZX-ray1.95A/B297-718[»]
5UO0X-ray1.97A/B297-718[»]
5VUIX-ray2.06A/B297-718[»]
5VUJX-ray1.95A/B297-718[»]
5VUKX-ray1.95A/B297-718[»]
5VULX-ray2.00A/B297-718[»]
5VUMX-ray2.10A/B297-718[»]
5VUNX-ray1.75A/B297-718[»]
5VUOX-ray1.80A/B297-718[»]
5VUPX-ray1.94A/B297-718[»]
5VUQX-ray2.00A/B297-718[»]
5VURX-ray1.97A/B297-718[»]
5VUSX-ray1.95A/B297-718[»]
5VUTX-ray2.00A/B297-718[»]
5VUUX-ray1.96A/B297-718[»]
6AUQX-ray1.95A/B297-718[»]
6AURX-ray1.75A/B297-718[»]
6AUSX-ray1.70A/B297-718[»]
6AUTX-ray1.90A/B297-718[»]
6AUUX-ray1.85A/B297-718[»]
6AUVX-ray1.76A/B297-718[»]
6AUWX-ray1.70A/B297-718[»]
6AUXX-ray1.90A/B297-718[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P29476

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P29476

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P29476

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini17 – 99PDZPROSITE-ProRule annotationAdd BLAST83
Domaini755 – 935Flavodoxin-likePROSITE-ProRule annotationAdd BLAST181
Domaini990 – 1237FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST248

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 200Interaction with NOSIP1 PublicationAdd BLAST200
Regioni163 – 240PIN (nNOS-inhibiting protein) bindingBy similarityAdd BLAST78
Regioni725 – 745Calmodulin-bindingSequence analysisAdd BLAST21
Regioni750 – 769Tetrahydrobiopterin-bindingAdd BLAST20

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PDZ domain in the N-terminal part of the neuronal isoform participates in protein-protein interaction, and is responsible for targeting nNos to synaptic membranes in muscles (By similarity). Mediates interaction with VAC14.By similarity1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NOS family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1158 Eukaryota
COG0369 LUCA
COG4362 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000220884

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000159

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P29476

KEGG Orthology (KO)

More...
KOi
K13240

Database of Orthologous Groups

More...
OrthoDBi
90349at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P29476

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.990.10, 1 hit
3.40.50.360, 1 hit
3.40.50.80, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003097 CysJ-like_FAD-binding
IPR017927 FAD-bd_FR_type
IPR001094 Flavdoxin-like
IPR008254 Flavodoxin/NO_synth
IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase
IPR029039 Flavoprotein-like_sf
IPR039261 FNR_nucleotide-bd
IPR023173 NADPH_Cyt_P450_Rdtase_alpha
IPR012144 NOS_euk
IPR004030 NOS_N
IPR036119 NOS_N_sf
IPR001433 OxRdtase_FAD/NAD-bd
IPR001478 PDZ
IPR036034 PDZ_sf
IPR017938 Riboflavin_synthase-like_b-brl

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00667 FAD_binding_1, 1 hit
PF00258 Flavodoxin_1, 1 hit
PF00175 NAD_binding_1, 1 hit
PF02898 NO_synthase, 1 hit
PF00595 PDZ, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000333 NOS, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00369 FLAVODOXIN
PR00371 FPNCR

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00228 PDZ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50156 SSF50156, 1 hit
SSF52218 SSF52218, 1 hit
SSF52343 SSF52343, 1 hit
SSF56512 SSF56512, 1 hit
SSF63380 SSF63380, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51384 FAD_FR, 1 hit
PS50902 FLAVODOXIN_LIKE, 1 hit
PS60001 NOS, 1 hit
PS50106 PDZ, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform N-NOS-1 (identifier: P29476-1) [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
MEENTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG
60 70 80 90 100
AAEQSGLIQA GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP
110 120 130 140 150
EGFTTHLETT FTGDGTPKTI RVTQPLGPPT KAVDLSHQPS ASKDQSLAVD
160 170 180 190 200
RVTGLGNGPQ HAQGHGQGAG SVSQANGVAI DPTMKSTKAN LQDIGEHDEL
210 220 230 240 250
LKEIEPVLSI LNSGSKATNR GGPAKAEMKD TGIQVDRDLD GKSHKAPPLG
260 270 280 290 300
GDNDRVFNDL WGKDNVPVIL NNPYSEKEQS PTSGKQSPTK NGSPSRCPRF
310 320 330 340 350
LKVKNWETDV VLTDTLHLKS TLETGCTEHI CMGSIMLPSQ HTRKPEDVRT
360 370 380 390 400
KDQLFPLAKE FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE
410 420 430 440 450
LIYGAKHAWR NASRCVGRIQ WSKLQVFDAR DCTTAHGMFN YICNHVKYAT
460 470 480 490 500
NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI RYAGYKQPDG STLGDPANVQ
510 520 530 540 550
FTEICIQQGW KAPRGRFDVL PLLLQANGND PELFQIPPEL VLEVPIRHPK
560 570 580 590 600
FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD
610 620 630 640 650
NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD
660 670 680 690 700
HHSATESFIK HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL
710 720 730 740 750
TPSFEYQPDP WNTHVWKGTN GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA
760 770 780 790 800
KRVKATILYA TETGKSQAYA KTLCEIFKHA FDAKAMSMEE YDIVHLEHEA
810 820 830 840 850
LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS YKVRFNSVSS
860 870 880 890 900
YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD
910 920 930 940 950
TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI
960 970 980 990 1000
EKPNNSLISN DRSWKRNKFR LTYVAEAPDL TQGLSNVHKK RVSAARLLSR
1010 1020 1030 1040 1050
QNLQSPKFSR STIFVRLHTN GNQELQYQPG DHLGVFPGNH EDLVNALIER
1060 1070 1080 1090 1100
LEDAPPANHV VKVEMLEERN TALGVISNWK DESRLPPCTI FQAFKYYLDI
1110 1120 1130 1140 1150
TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW GKNPTMVEVL
1160 1170 1180 1190 1200
EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR
1210 1220 1230 1240 1250
DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG
1260 1270 1280 1290 1300
TGIAPFRSFW QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK
1310 1320 1330 1340 1350
NKGVFRELYT AYSREPDRPK KYVQDVLQEQ LAESVYRALK EQGGHIYVCG
1360 1370 1380 1390 1400
DVTMAADVLK AIQRIMTQQG KLSEEDAGVF ISRLRDDNRY HEDIFGVTLR
1410 1420
TYEVTNRLRS ESIAFIEESK KDADEVFSS
Length:1,429
Mass (Da):160,559
Last modified:April 1, 1993 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7255C5AE165200F5
GO
Isoform N-NOS-2 (identifier: P29476-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     504-608: Missing.

Show »
Length:1,324
Mass (Da):148,548
Checksum:i2B527386DF5B4160
GO
Isoform PNNOS (identifier: P29476-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     839-839: K → KYPEPLRFFPRKGPSLSHVDSEAHSLVAARDSQHR

Show »
Length:1,463
Mass (Da):164,430
Checksum:iA0522B26817B6705
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3ZEW7D3ZEW7_RAT
Nitric oxide synthase, brain
Nos1
1,463Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F1LQL1F1LQL1_RAT
Nitric oxide synthase
Nos1
1,429Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti269I → V in AAC52782 (PubMed:8806605).Curated1
Sequence conflicti269I → V AA sequence (PubMed:7520037).Curated1
Sequence conflicti953P → A in AAC52782 (PubMed:8806605).Curated1
Sequence conflicti953P → A AA sequence (PubMed:7520037).Curated1
Sequence conflicti1008F → S in AAC52782 (PubMed:8806605).Curated1
Sequence conflicti1311A → V in AAC52782 (PubMed:8806605).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_003580504 – 608Missing in isoform N-NOS-2. CuratedAdd BLAST105
Alternative sequenceiVSP_003581839K → KYPEPLRFFPRKGPSLSHVD SEAHSLVAARDSQHR in isoform PNNOS. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X59949 mRNA Translation: CAA42574.1
U67309 mRNA Translation: AAC52782.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S16233

NCBI Reference Sequences

More...
RefSeqi
NP_434686.1, NM_052799.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.10573
Rn.214189
Rn.214216

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24598

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24598

UCSC genome browser

More...
UCSCi
RGD:3184 rat [P29476-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59949 mRNA Translation: CAA42574.1
U67309 mRNA Translation: AAC52782.1
PIRiS16233
RefSeqiNP_434686.1, NM_052799.1
UniGeneiRn.10573
Rn.214189
Rn.214216

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8QNMR-A11-133[»]
1CMIX-ray2.50C/D225-237[»]
1F20X-ray1.90A963-1397[»]
1K2RX-ray2.15A/B299-717[»]
1K2SX-ray2.55A/B299-717[»]
1K2TX-ray2.20A/B299-717[»]
1K2UX-ray2.20A/B299-717[»]
1LZXX-ray2.00A/B299-717[»]
1LZZX-ray2.05A/B299-717[»]
1M00X-ray2.05A/B299-717[»]
1MMVX-ray2.00A/B299-717[»]
1MMWX-ray2.00A/B299-717[»]
1OM4X-ray1.75A/B297-718[»]
1OM5X-ray2.30A/B297-717[»]
1P6HX-ray1.98A/B297-717[»]
1P6IX-ray1.90A/B297-717[»]
1P6JX-ray2.00A/B297-717[»]
1P6KX-ray1.78A/B297-717[»]
1QAUX-ray1.25A14-125[»]
1QAVX-ray1.90B12-126[»]
1QW6X-ray2.10A298-716[»]
1QWCX-ray2.30A298-716[»]
1RS6X-ray1.95A/B297-717[»]
1RS7X-ray1.95A/B297-717[»]
1TLLX-ray2.30A/B742-1429[»]
1VAGX-ray2.00A298-716[»]
1ZVIX-ray2.00A298-716[»]
1ZVLX-ray2.50A/B298-716[»]
1ZZQX-ray1.90A/B299-718[»]
1ZZRX-ray2.05A/B299-718[»]
1ZZUX-ray1.90A/B299-718[»]
2G6HX-ray2.00A/B299-718[»]
2G6IX-ray1.90A/B299-718[»]
2G6JX-ray2.30A/B299-718[»]
2G6KX-ray2.00A/B299-718[»]
2G6LX-ray2.05A/B299-718[»]
2G6MX-ray1.85A/B299-718[»]
2G6NX-ray1.90A/B299-718[»]
2HX3X-ray2.00A/B297-718[»]
2HX4X-ray2.15A/B297-718[»]
3B3MX-ray1.95A/B297-718[»]
3B3NX-ray1.98A/B297-718[»]
3B3OX-ray2.05A/B297-718[»]
3B3PX-ray2.45A/B297-718[»]
3DQRX-ray2.40A/B297-718[»]
3FC5X-ray2.59A/B297-718[»]
3HSNX-ray1.91A/B297-718[»]
3HSOX-ray2.02A/B297-718[»]
3HSPX-ray2.20A/B297-718[»]
3JT3X-ray2.15A/B297-718[»]
3JT4X-ray1.80A/B297-718[»]
3JT5X-ray2.10A/B297-718[»]
3JT6X-ray2.20A/B297-718[»]
3JT7X-ray2.10A/B297-718[»]
3JT8X-ray1.95A/B297-718[»]
3JT9X-ray2.10A/B297-718[»]
3JTAX-ray2.18A/B297-718[»]
3JWSX-ray1.95A/B297-718[»]
3JWTX-ray2.01A/B297-718[»]
3JWUX-ray1.93A/B297-718[»]
3JWVX-ray1.98A/B297-718[»]
3JX0X-ray2.20A/B297-718[»]
3JX1X-ray2.00A/B297-718[»]
3JX2X-ray2.10A/B297-718[»]
3JX3X-ray1.95A/B297-718[»]
3JX4X-ray2.26A/B297-718[»]
3JX5X-ray2.15A/B297-718[»]
3JX6X-ray2.35A/B297-718[»]
3N2RX-ray1.90A/B297-718[»]
3N5VX-ray2.30A/B297-718[»]
3N5WX-ray1.73A/B297-718[»]
3N5XX-ray1.80A/B297-718[»]
3N5YX-ray2.05A/B297-718[»]
3N5ZX-ray2.18A/B297-718[»]
3N60X-ray1.98A/B297-718[»]
3N61X-ray1.95A/B297-718[»]
3N62X-ray1.95A/B297-718[»]
3N63X-ray2.00A/B297-718[»]
3N64X-ray1.95A/B297-718[»]
3N65X-ray1.80A/B297-718[»]
3N66X-ray1.78A/B297-718[»]
3N67X-ray2.09A/B298-711[»]
3N68X-ray2.53A/B298-711[»]
3N69X-ray2.65A/B298-711[»]
3N6AX-ray2.49A/B298-711[»]
3N6BX-ray3.10A/B298-711[»]
3N6CX-ray3.06A/B298-711[»]
3N6DX-ray3.05A/B298-711[»]
3N6EX-ray2.20A/B298-711[»]
3N6FX-ray2.18A/B298-711[»]
3N6GX-ray2.21A/B298-711[»]
3NLJX-ray2.20A/B297-718[»]
3NLKX-ray2.02A/B297-718[»]
3NLMX-ray1.85A/B297-718[»]
3NLNX-ray2.00A/B297-718[»]
3NLOX-ray2.30A/B297-718[»]
3NLPX-ray2.02A/B297-718[»]
3NLQX-ray2.15A/B297-718[»]
3NLRX-ray2.10A/B297-718[»]
3NLVX-ray2.10A/B297-718[»]
3NLWX-ray2.10A/B297-718[»]
3NLXX-ray1.87A/B297-718[»]
3NLYX-ray1.99A/B297-718[»]
3NLZX-ray1.92A/B297-718[»]
3NM0X-ray1.81A/B297-718[»]
3NNYX-ray2.10A/B297-718[»]
3NNZX-ray1.97A/B297-718[»]
3PNEX-ray1.97A/B297-718[»]
3PNFX-ray1.94A/B297-718[»]
3PNGX-ray1.88A/B297-718[»]
3Q99X-ray2.15A/B297-718[»]
3Q9AX-ray2.24A/B297-718[»]
3RQJX-ray1.84A/B297-718[»]
3RQKX-ray2.21A/B297-718[»]
3RQLX-ray1.93A/B297-718[»]
3RQMX-ray1.95A/B297-718[»]
3RQNX-ray1.95A/B297-718[»]
3SVPX-ray2.05A/B297-718[»]
3SVQX-ray2.18A/B297-718[»]
3TYLX-ray1.90A/B297-718[»]
3TYMX-ray2.00A/B297-718[»]
3TYNX-ray1.97A/B297-718[»]
3TYOX-ray1.93A/B297-718[»]
3UFOX-ray2.17A/B297-718[»]
3UFPX-ray2.10A/B297-718[»]
3UFQX-ray2.06A/B297-718[»]
3UFRX-ray2.10A/B297-718[»]
3UFSX-ray1.97A/B297-718[»]
3UFTX-ray2.08A/B297-718[»]
3UFUX-ray1.89A/B297-718[»]
3UFVX-ray2.08A/B297-718[»]
3UFWX-ray2.00A/B297-718[»]
4C39X-ray1.98A/B297-718[»]
4CAMX-ray1.83A/B297-718[»]
4CANX-ray1.91A/B297-718[»]
4CAOX-ray1.98A/B297-718[»]
4CAPX-ray2.06A/B297-718[»]
4CAQX-ray1.95A/B297-718[»]
4CDTX-ray2.00A/B297-718[»]
4CTPX-ray2.05A/B297-718[»]
4CTQX-ray2.00A/B297-718[»]
4CTRX-ray2.20A/B297-718[»]
4CTTX-ray2.30A/B297-718[»]
4CTUX-ray2.16A/B297-718[»]
4CTVX-ray1.78A/B297-718[»]
4CTWX-ray1.90A/B297-718[»]
4CTXX-ray1.82A/B297-718[»]
4CX3X-ray1.97A/B297-718[»]
4CX4X-ray1.98A/B297-718[»]
4CX5X-ray1.80A/B297-718[»]
4CX6X-ray1.90A/B297-718[»]
4D2YX-ray1.98A/B297-718[»]
4D2ZX-ray1.89A/B297-718[»]
4D30X-ray1.96A/B297-718[»]
4D31X-ray1.95A/B297-718[»]
4D32X-ray2.10A/B297-718[»]
4D3BX-ray1.80A/B297-718[»]
4D7OX-ray1.78A/B297-718[»]
4EUXX-ray2.14A/B297-718[»]
4FVWX-ray1.81A/B297-718[»]
4FVXX-ray2.00A/B297-718[»]
4FVYX-ray1.70A/B297-718[»]
4FVZX-ray1.99A/B297-718[»]
4FW0X-ray1.95A/B297-718[»]
4GQEX-ray1.80A/B297-718[»]
4HOPX-ray2.29B/D/F4-126[»]
4IMSX-ray2.15A/B297-718[»]
4IMTX-ray2.20A/B297-718[»]
4IMUX-ray2.03A/B297-718[»]
4IMWX-ray2.20A/B297-718[»]
4JSEX-ray1.97A/B297-718[»]
4JSFX-ray2.05A/B297-718[»]
4JSGX-ray1.94A/B297-718[»]
4JSHX-ray2.35A/B297-718[»]
4JSIX-ray2.09A/B297-718[»]
4JSJX-ray1.92A/B297-718[»]
4K5DX-ray2.10A/B297-718[»]
4K5EX-ray1.89A/B297-718[»]
4K5FX-ray2.20A/B297-718[»]
4K5GX-ray1.85A/B297-718[»]
4KCHX-ray2.15A/B297-718[»]
4KCIX-ray2.27A/B297-718[»]
4KCJX-ray2.05A/B297-718[»]
4KCKX-ray2.10A/B297-718[»]
4KCLX-ray1.93A/B297-718[»]
4KCMX-ray2.07A/B297-718[»]
4KCNX-ray1.85A/B297-718[»]
4KCOX-ray1.86A/B297-718[»]
4LUXX-ray1.86A/B297-718[»]
4UGZX-ray2.08A/B297-718[»]
4UH0X-ray2.04A/B297-718[»]
4UH1X-ray1.80A/B297-718[»]
4UH2X-ray1.99A/B297-718[»]
4UH3X-ray2.03A/B297-718[»]
4UH4X-ray1.95A/B297-718[»]
4UPMX-ray1.90A/B297-718[»]
4UPNX-ray2.09A/B297-718[»]
4UPOX-ray1.95A/B297-718[»]
4UPPX-ray1.91A/B297-718[»]
4V3VX-ray2.06A/B297-718[»]
4V3WX-ray2.13A/B297-718[»]
4V3XX-ray1.99A/B297-718[»]
4V3YX-ray1.96A/B297-718[»]
4V3ZX-ray2.05A/B297-718[»]
5AD4X-ray1.98A/B297-718[»]
5AD5X-ray1.90A/B297-718[»]
5AD6X-ray2.00A/B297-718[»]
5AD7X-ray1.95A/B297-718[»]
5AD8X-ray1.91A/B297-718[»]
5AD9X-ray2.30A/B297-718[»]
5ADAX-ray1.98A/B297-718[»]
5ADBX-ray2.05A/B297-718[»]
5ADCX-ray2.10A/B297-718[»]
5ADDX-ray2.10A/B297-718[»]
5ADEX-ray2.10A/B297-718[»]
5AGKX-ray2.00A/B297-718[»]
5AGLX-ray1.94A/B297-718[»]
5AGMX-ray1.84A/B297-718[»]
5AGNX-ray1.95A/B297-718[»]
5AGOX-ray1.90A/B297-718[»]
5AGPX-ray2.10A/B297-718[»]
5FVOX-ray2.12A297-718[»]
5FVPX-ray2.10A/B297-718[»]
5FVQX-ray1.95A/B297-718[»]
5FVRX-ray1.84A/B297-718[»]
5FVSX-ray1.95A/B297-718[»]
5FVTX-ray1.83A/B297-718[»]
5FW0X-ray1.80A/B297-718[»]
5G0NX-ray1.94A/B297-718[»]
5G0OX-ray1.85A/B297-718[»]
5G0PX-ray2.10A/B297-718[»]
5UNRX-ray1.95A/B297-718[»]
5UNSX-ray1.90A/B297-718[»]
5UNTX-ray2.05A/B297-718[»]
5UNUX-ray2.05A/B297-718[»]
5UNVX-ray2.00A/B297-718[»]
5UNWX-ray2.04A/B297-718[»]
5UNXX-ray2.03A/B297-718[»]
5UNYX-ray1.82A/B297-718[»]
5UNZX-ray1.95A/B297-718[»]
5UO0X-ray1.97A/B297-718[»]
5VUIX-ray2.06A/B297-718[»]
5VUJX-ray1.95A/B297-718[»]
5VUKX-ray1.95A/B297-718[»]
5VULX-ray2.00A/B297-718[»]
5VUMX-ray2.10A/B297-718[»]
5VUNX-ray1.75A/B297-718[»]
5VUOX-ray1.80A/B297-718[»]
5VUPX-ray1.94A/B297-718[»]
5VUQX-ray2.00A/B297-718[»]
5VURX-ray1.97A/B297-718[»]
5VUSX-ray1.95A/B297-718[»]
5VUTX-ray2.00A/B297-718[»]
5VUUX-ray1.96A/B297-718[»]
6AUQX-ray1.95A/B297-718[»]
6AURX-ray1.75A/B297-718[»]
6AUSX-ray1.70A/B297-718[»]
6AUTX-ray1.90A/B297-718[»]
6AUUX-ray1.85A/B297-718[»]
6AUVX-ray1.76A/B297-718[»]
6AUWX-ray1.70A/B297-718[»]
6AUXX-ray1.90A/B297-718[»]
ProteinModelPortaliP29476
SMRiP29476
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246738, 13 interactors
CORUMiP29476
DIPiDIP-33272N
ELMiP29476
IntActiP29476, 9 interactors
MINTiP29476
STRINGi10116.ENSRNOP00000062735

Chemistry databases

BindingDBiP29476
ChEMBLiCHEMBL3048
GuidetoPHARMACOLOGYi1251

PTM databases

CarbonylDBiP29476
iPTMnetiP29476
PhosphoSitePlusiP29476

Proteomic databases

jPOSTiP29476
PaxDbiP29476
PRIDEiP29476

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24598
KEGGirno:24598
UCSCiRGD:3184 rat [P29476-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4842
RGDi3184 Nos1

Phylogenomic databases

eggNOGiKOG1158 Eukaryota
COG0369 LUCA
COG4362 LUCA
HOGENOMiHOG000220884
HOVERGENiHBG000159
InParanoidiP29476
KOiK13240
OrthoDBi90349at2759
PhylomeDBiP29476

Enzyme and pathway databases

BRENDAi1.14.13.39 5301
SABIO-RKiP29476

Miscellaneous databases

EvolutionaryTraceiP29476

Protein Ontology

More...
PROi
PR:P29476

Family and domain databases

Gene3Di1.20.990.10, 1 hit
3.40.50.360, 1 hit
3.40.50.80, 1 hit
InterProiView protein in InterPro
IPR003097 CysJ-like_FAD-binding
IPR017927 FAD-bd_FR_type
IPR001094 Flavdoxin-like
IPR008254 Flavodoxin/NO_synth
IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase
IPR029039 Flavoprotein-like_sf
IPR039261 FNR_nucleotide-bd
IPR023173 NADPH_Cyt_P450_Rdtase_alpha
IPR012144 NOS_euk
IPR004030 NOS_N
IPR036119 NOS_N_sf
IPR001433 OxRdtase_FAD/NAD-bd
IPR001478 PDZ
IPR036034 PDZ_sf
IPR017938 Riboflavin_synthase-like_b-brl
PfamiView protein in Pfam
PF00667 FAD_binding_1, 1 hit
PF00258 Flavodoxin_1, 1 hit
PF00175 NAD_binding_1, 1 hit
PF02898 NO_synthase, 1 hit
PF00595 PDZ, 1 hit
PIRSFiPIRSF000333 NOS, 1 hit
PRINTSiPR00369 FLAVODOXIN
PR00371 FPNCR
SMARTiView protein in SMART
SM00228 PDZ, 1 hit
SUPFAMiSSF50156 SSF50156, 1 hit
SSF52218 SSF52218, 1 hit
SSF52343 SSF52343, 1 hit
SSF56512 SSF56512, 1 hit
SSF63380 SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS51384 FAD_FR, 1 hit
PS50902 FLAVODOXIN_LIKE, 1 hit
PS60001 NOS, 1 hit
PS50106 PDZ, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNOS1_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P29476
Secondary accession number(s): P70594
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: January 16, 2019
This is version 214 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
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