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Q9Z0J4

- NOS1_MOUSE

UniProt

Q9Z0J4 - NOS1_MOUSE

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Protein

Nitric oxide synthase, brain

Gene

Nos1

Organism
Mus musculus (Mouse)
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 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

GO - Biological processi

  1. cellular response to growth factor stimulus Source: BHF-UCL
  2. exogenous drug catabolic process Source: MGI
  3. negative regulation of blood pressure Source: RefGenome
  4. negative regulation of calcium ion transport Source: MGI
  5. negative regulation of hydrolase activity Source: MGI
  6. negative regulation of potassium ion transport Source: MGI
  7. negative regulation of serotonin uptake Source: UniProtKB
  8. nitric oxide biosynthetic process Source: BHF-UCL
  9. nitric oxide mediated signal transduction Source: RefGenome
  10. peptidyl-cysteine S-nitrosylation Source: MGI
  11. positive regulation of guanylate cyclase activity Source: RefGenome
  12. positive regulation of histone acetylation Source: BHF-UCL
  13. positive regulation of the force of heart contraction 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. striated muscle contraction Source: MGI
Complete GO annotation...

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. cell projection Source: UniProtKB-KW
  2. cytoskeleton Source: BHF-UCL
  3. cytosol Source: RefGenome
  4. membrane raft Source: MGI
  5. mitochondrion Source: MGI
  6. sarcolemma Source: BHF-UCL
  7. synapse Source: MGI
Complete GO annotation...

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

BgeeiQ9Z0J4.
CleanExiMM_NOS1.
ExpressionAtlasiQ9Z0J4. baseline and differential.
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. 5 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.
InParanoidiQ9Z0J4.
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

        10         20         30         40         50
MEEHTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG
60 70 80 90 100
AAEQSGLIQA GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP
110 120 130 140 150
EGFTTHLETT FTGDGTPKTI RVTQPLGTPT KAVDLSRQPS ASKDQPLAVD
160 170 180 190 200
RVPGPSNGPQ HAQGRGQGAG SVSQANGVAI DPTMKNTKAN LQDSGEQDEL
210 220 230 240 250
LKEIEPVLSI LTGGGKAVNR GGPAKAEMKD TGIQVDRDLD GKLHKAPPLG
260 270 280 290 300
GENDRVFNDL WGKGNVPVVL NNPYSENEQS PASGKQSPTK NGSPSRCPRF
310 320 330 340 350
LKVKNWETDV VLTDTLHLKS TLETGCTEQI CMGSIMLPSH HIRKSEDVRT
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 STLGDPANVE
510 520 530 540 550
FTEICIQQGW KPPRGRFDVL 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
EKANNSLISN DRSWKRNKFR LTYVAEAPEL TQGLSNVHKK RVSAARLLSR
1010 1020 1030 1040 1050
QNLQSPKSSR 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 KDTDEVFSS
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. 5 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 Q9Z0J4.
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

Bgeei Q9Z0J4.
CleanExi MM_NOS1.
ExpressionAtlasi Q9Z0J4. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 149 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