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Q9Z0J4

- NOS1_MOUSE

UniProt

Q9Z0J4 - NOS1_MOUSE

Protein

Nitric oxide synthase, brain

Gene

Nos1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    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. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Isoform NNOS Mu may be an effector enzyme for the dystrophin complex.1 Publication

    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

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi415 – 4151Iron (heme axial ligand)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi881 – 91232FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi1027 – 103812FADBy similarityAdd
    BLAST
    Nucleotide bindingi1170 – 118011FADBy similarityAdd
    BLAST
    Nucleotide bindingi1245 – 126319NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1343 – 135816NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to growth factor stimulus Source: BHF-UCL
    2. exogenous drug catabolic process Source: MGI
    3. multicellular organismal response to stress Source: Ensembl
    4. negative regulation of blood pressure Source: RefGenome
    5. negative regulation of calcium ion transport Source: MGI
    6. negative regulation of hydrolase activity Source: MGI
    7. negative regulation of potassium ion transport Source: MGI
    8. negative regulation of serotonin uptake Source: UniProtKB
    9. nitric oxide biosynthetic process Source: BHF-UCL
    10. nitric oxide mediated signal transduction Source: RefGenome
    11. peptidyl-cysteine S-nitrosylation Source: MGI
    12. positive regulation of guanylate cyclase activity Source: RefGenome
    13. positive regulation of histone acetylation Source: BHF-UCL
    14. positive regulation of transcription, DNA-templated Source: BHF-UCL
    15. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    16. positive regulation of vasodilation Source: RefGenome
    17. regulation of sodium ion transport Source: MGI
    18. response to heat Source: Ensembl
    19. response to hypoxia Source: Ensembl
    20. striated muscle contraction Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nitric oxide synthase, brain (EC:1.14.13.39)
    Alternative name(s):
    Constitutive NOS
    NC-NOS
    NOS type I
    Neuronal NOS
    Short name:
    N-NOS
    Short name:
    nNOS
    Peptidyl-cysteine S-nitrosylase NOS1
    bNOS
    Gene namesi
    Name:Nos1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:97360. Nos1.

    Subcellular locationi

    Cell membranesarcolemma; Peripheral membrane protein. Cell projectiondendritic spine By similarity
    Note: In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glycoprotein complex. In neurons, enriched in dendritic spines By similarity.By similarity

    GO - Cellular componenti

    1. cytoskeleton Source: BHF-UCL
    2. cytosol Source: RefGenome
    3. dendritic spine Source: UniProtKB-SubCell
    4. membrane raft Source: MGI
    5. mitochondrion Source: MGI
    6. sarcolemma Source: BHF-UCL
    7. sarcoplasmic reticulum Source: Ensembl
    8. synapse Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    In MDX mice (mouse model of dystrophinopathy) the dystrophin complex is disrupted and nNOS is displaced from sarcolemma and accumulates in the cytosol.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14291429Nitric oxide synthase, brainPRO_0000170922Add
    BLAST

    Post-translational modificationi

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

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ9Z0J4.
    PaxDbiQ9Z0J4.
    PRIDEiQ9Z0J4.

    PTM databases

    PhosphoSiteiQ9Z0J4.

    Expressioni

    Tissue specificityi

    Widely expressed in the nervous system: expressed in cerebrum, olfactory bulb, hippocampus, midbrain, cerebellum, pons, medulla oblongata, and spinal cord. Also found in skeletal muscle, where it is localized beneath the sarcolemma of fast twitch muscle fibers, and in spleen, heart, kidney, and liver. N-NOS-1 and N-NOS-2 are found in all parts of the nervous system. NNOS beta and gamma occur in a region-specific manner in the brain and NNOS beta expression is developmentally regulated. NNOS Mu is only found in mature skeletal and cardiac muscles.

    Inductioni

    By cholinergic agonists acting at inositol phosphate-linked muscarinic receptors in cardiac myocytes.

    Gene expression databases

    ArrayExpressiQ9Z0J4.
    BgeeiQ9Z0J4.
    CleanExiMM_NOS1.
    GenevestigatoriQ9Z0J4.

    Interactioni

    Subunit structurei

    Homodimer. Forms a ternary complex with CAPON and SYN1. Interacts with ZDHHC23. Interacts with NOSIP; which may impair its synaptic location By similarity. Interacts with DLG4; the interaction possibly being prevented by the association between NOS1 and CAPON. Interacts with HTR4. Forms a ternary complex with CAPON and RASD1. Interacts with VAC14 By similarity. Interacts (via N-terminal domain) with DLG4 (via N-terminal tandem pair of PDZ domains) By similarity. Interacts with SLC6A4.By similarity5 Publications

    Protein-protein interaction databases

    BioGridi201805. 5 interactions.
    DIPiDIP-31556N.
    IntActiQ9Z0J4. 4 interactions.

    Structurei

    Secondary structure

    1
    1429
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi731 – 74414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O60X-ray1.55B725-747[»]
    ProteinModelPortaliQ9Z0J4.
    SMRiQ9Z0J4. Positions 12-126, 298-716, 750-1413.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Z0J4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 9983PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini755 – 935181Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini990 – 1237248FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 200200Interaction with NOSIPBy similarityAdd
    BLAST
    Regioni163 – 24078PIN (nNOS-inhibiting protein) bindingBy similarityAdd
    BLAST
    Regioni725 – 74521Calmodulin-bindingAdd
    BLAST
    Regioni750 – 76920Tetrahydrobiopterin-bindingBy similarityAdd
    BLAST

    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. Mediates interaction with VAC14 By similarity.By similarity

    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
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4362.
    GeneTreeiENSGT00620000087711.
    HOGENOMiHOG000220884.
    HOVERGENiHBG000159.
    InParanoidiQ3UR10.
    KOiK13240.
    OrthoDBiEOG79SDW7.
    PhylomeDBiQ9Z0J4.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    2.30.42.10. 1 hit.
    3.40.50.360. 2 hits.
    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.
    IPR001478. PDZ.
    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.
    PF00595. PDZ. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000333. NOS. 1 hit.
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SMARTiSM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    SSF52218. 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.
    PS50106. PDZ. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform N-NOS-1 (identifier: Q9Z0J4-1) [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

    MEEHTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG     50
    AAEQSGLIQA GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP 100
    EGFTTHLETT FTGDGTPKTI RVTQPLGTPT KAVDLSRQPS ASKDQPLAVD 150
    RVPGPSNGPQ HAQGRGQGAG SVSQANGVAI DPTMKNTKAN LQDSGEQDEL 200
    LKEIEPVLSI LTGGGKAVNR GGPAKAEMKD TGIQVDRDLD GKLHKAPPLG 250
    GENDRVFNDL WGKGNVPVVL NNPYSENEQS PASGKQSPTK NGSPSRCPRF 300
    LKVKNWETDV VLTDTLHLKS TLETGCTEQI CMGSIMLPSH HIRKSEDVRT 350
    KDQLFPLAKE FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE 400
    LIYGAKHAWR NASRCVGRIQ WSKLQVFDAR DCTTAHGMFN YICNHVKYAT 450
    NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI RYAGYKQPDG STLGDPANVE 500
    FTEICIQQGW KPPRGRFDVL PLLLQANGND PELFQIPPEL VLEVPIRHPK 550
    FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD 600
    NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD 650
    HHSATESFIK HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL 700
    TPSFEYQPDP WNTHVWKGTN GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA 750
    KRVKATILYA TETGKSQAYA KTLCEIFKHA FDAKAMSMEE YDIVHLEHEA 800
    LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS YKVRFNSVSS 850
    YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD 900
    TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI 950
    EKANNSLISN DRSWKRNKFR LTYVAEAPEL TQGLSNVHKK RVSAARLLSR 1000
    QNLQSPKSSR STIFVRLHTN GNQELQYQPG DHLGVFPGNH EDLVNALIER 1050
    LEDAPPANHV VKVEMLEERN TALGVISNWK DESRLPPCTI FQAFKYYLDI 1100
    TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW GKNPTMVEVL 1150
    EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR 1200
    DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG 1250
    TGIAPFRSFW QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK 1300
    NKGVFRELYT AYSREPDRPK KYVQDVLQEQ LAESVYRALK EQGGHIYVCG 1350
    DVTMAADVLK AIQRIMTQQG KLSEEDAGVF ISRLRDDNRY HEDIFGVTLR 1400
    TYEVTNRLRS ESIAFIEESK KDTDEVFSS 1429
    Length:1,429
    Mass (Da):160,472
    Last modified:May 1, 1999 - v1
    Checksum:i3782848D65B41BFC
    GO
    Isoform N-NOS-2 (identifier: Q9Z0J4-2) [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):148,435
    Checksum:iF8532C1457C09EA4
    GO
    Isoform NNOS beta (identifier: Q9Z0J4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-230: Missing.
         231-236: TGIQVD → MRGLGS

    Show »
    Length:1,199
    Mass (Da):136,243
    Checksum:i4ACB46D2B44CFEEA
    GO
    Isoform NNOS gamma (identifier: Q9Z0J4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-331: Missing.

    Show »
    Length:1,098
    Mass (Da):125,183
    Checksum:i51C8FA95A3865266
    GO
    Isoform NNOS Mu (identifier: Q9Z0J4-5) [UniParc]FASTAAdd to Basket

    Also known as: Muscle-specific

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

    Show »
    Length:1,463
    Mass (Da):164,343
    Checksum:i11689C595839D9A7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1320 – 13201K → Q in BAE24878. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 331331Missing in isoform NNOS gamma. CuratedVSP_003577Add
    BLAST
    Alternative sequencei1 – 230230Missing in isoform NNOS beta. CuratedVSP_003575Add
    BLAST
    Alternative sequencei231 – 2366TGIQVD → MRGLGS in isoform NNOS beta. CuratedVSP_003576
    Alternative sequencei504 – 608105Missing in isoform N-NOS-2. 1 PublicationVSP_003578Add
    BLAST
    Alternative sequencei839 – 8391K → KYPEPLRFFPRKGPSLSHVD SEAHSLVAARDSQHR in isoform NNOS Mu. 1 PublicationVSP_003579

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14552 mRNA. Translation: BAA03415.1.
    S81982 mRNA. Translation: AAB36469.1.
    AK141904 mRNA. Translation: BAE24878.1.
    CCDSiCCDS19606.1. [Q9Z0J4-1]
    PIRiJN0609.
    RefSeqiNP_032738.1. NM_008712.2. [Q9Z0J4-1]
    XP_006530256.1. XM_006530193.1. [Q9Z0J4-1]
    UniGeneiMm.442195.
    Mm.44249.

    Genome annotation databases

    EnsembliENSMUST00000142742; ENSMUSP00000120421; ENSMUSG00000029361. [Q9Z0J4-1]
    ENSMUST00000171055; ENSMUSP00000127432; ENSMUSG00000029361. [Q9Z0J4-1]
    GeneIDi18125.
    KEGGimmu:18125.
    UCSCiuc008zfy.2. mouse. [Q9Z0J4-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14552 mRNA. Translation: BAA03415.1 .
    S81982 mRNA. Translation: AAB36469.1 .
    AK141904 mRNA. Translation: BAE24878.1 .
    CCDSi CCDS19606.1. [Q9Z0J4-1 ]
    PIRi JN0609.
    RefSeqi NP_032738.1. NM_008712.2. [Q9Z0J4-1 ]
    XP_006530256.1. XM_006530193.1. [Q9Z0J4-1 ]
    UniGenei Mm.442195.
    Mm.44249.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2O60 X-ray 1.55 B 725-747 [» ]
    ProteinModelPortali Q9Z0J4.
    SMRi Q9Z0J4. Positions 12-126, 298-716, 750-1413.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201805. 5 interactions.
    DIPi DIP-31556N.
    IntActi Q9Z0J4. 4 interactions.

    Chemistry

    BindingDBi Q9Z0J4.
    ChEMBLi CHEMBL4719.

    PTM databases

    PhosphoSitei Q9Z0J4.

    Proteomic databases

    MaxQBi Q9Z0J4.
    PaxDbi Q9Z0J4.
    PRIDEi Q9Z0J4.

    Protocols and materials databases

    DNASUi 18125.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000142742 ; ENSMUSP00000120421 ; ENSMUSG00000029361 . [Q9Z0J4-1 ]
    ENSMUST00000171055 ; ENSMUSP00000127432 ; ENSMUSG00000029361 . [Q9Z0J4-1 ]
    GeneIDi 18125.
    KEGGi mmu:18125.
    UCSCi uc008zfy.2. mouse. [Q9Z0J4-1 ]

    Organism-specific databases

    CTDi 4842.
    MGIi MGI:97360. Nos1.

    Phylogenomic databases

    eggNOGi COG4362.
    GeneTreei ENSGT00620000087711.
    HOGENOMi HOG000220884.
    HOVERGENi HBG000159.
    InParanoidi Q3UR10.
    KOi K13240.
    OrthoDBi EOG79SDW7.
    PhylomeDBi Q9Z0J4.

    Enzyme and pathway databases

    Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).

    Miscellaneous databases

    EvolutionaryTracei Q9Z0J4.
    NextBioi 293344.
    PROi Q9Z0J4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z0J4.
    Bgeei Q9Z0J4.
    CleanExi MM_NOS1.
    Genevestigatori Q9Z0J4.

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    2.30.42.10. 1 hit.
    3.40.50.360. 2 hits.
    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.
    IPR001478. PDZ.
    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.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000333. NOS. 1 hit.
    PRINTSi PR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SMARTi SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    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.
    PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural diversity of neuronal oxide synthase mRNA in the nervous system."
      Ogura T., Yokoyama T., Fujisawa H., Kurashima Y., Esumi H.
      Biochem. Biophys. Res. Commun. 193:1014-1022(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS N-NOS-1 AND N-NOS-2).
      Strain: BALB/c.
      Tissue: Brain.
    2. "Neuronal nitric-oxide synthase-mu, an alternatively spliced isoform expressed in differentiated skeletal muscle."
      Silvagno F., Xia H., Bredt D.S.
      J. Biol. Chem. 271:11204-11208(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NNOS MU).
      Tissue: Skeletal muscle.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1320-1429.
      Strain: C57BL/6J.
      Tissue: Spinal ganglion.
    4. "Regulation of neuronal nitric oxide synthase through alternative transcripts."
      Brenman J.E., Xia H., Chao D.S., Black S.M., Bredt D.S.
      Dev. Neurosci. 19:224-231(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS NNOS BETA; NNOS GAMMA AND NNOS MU).
    5. "Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95."
      Tochio H., Hung F., Li M., Bredt D.S., Zhang M.
      J. Mol. Biol. 295:225-237(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG4.
    6. "Dexras1: a G protein specifically coupled to neuronal nitric oxide synthase via CAPON."
      Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.
      Neuron 28:183-193(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASD1 AND CAPON.
    7. "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a receptor splice variant: roles in receptor targeting."
      Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W., Marin P., Dumuis A., Bockaert J.
      J. Cell Sci. 117:5367-5379(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTR4.
    8. "Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition of D-serine formation."
      Mustafa A.K., Kumar M., Selvakumar B., Ho G.P., Ehmsen J.T., Barrow R.K., Amzel L.M., Snyder S.H.
      Proc. Natl. Acad. Sci. U.S.A. 104:2950-2955(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS NITROSYLASE.
    9. "Physical interaction between the serotonin transporter and neuronal nitric oxide synthase underlies reciprocal modulation of their activity."
      Chanrion B., Mannoury la Cour C., Bertaso F., Lerner-Natoli M., Freissmuth M., Millan M.J., Bockaert J., Marin P.
      Proc. Natl. Acad. Sci. U.S.A. 104:8119-8124(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC6A4.
    10. "Crystal structure of calmodulin-neuronal nitric oxide synthase complex."
      Valentine K.G., Ng H.L., Schneeweis L., Kranz J.K., Frederick K.K., Alber T., Wand A.J.
      Submitted (DEC-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 725-747 IN COMPLEX WITH CALMODULIN.

    Entry informationi

    Entry nameiNOS1_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z0J4
    Secondary accession number(s): Q3UR10, Q64208
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 148 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3