Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P29475

- NOS1_HUMAN

UniProt

P29475 - NOS1_HUMAN

Protein

Nitric oxide synthase, brain

Gene

NOS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    Catalytic activityi

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

    Cofactori

    Heme group.
    Binds 1 FAD.
    Binds 1 FMN.
    Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi420 – 4201Iron (heme axial ligand)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi886 – 91732FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi1032 – 104312FADBy similarityAdd
    BLAST
    Nucleotide bindingi1175 – 118511FADBy similarityAdd
    BLAST
    Nucleotide bindingi1250 – 126819NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1348 – 136316NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. arginine binding Source: BHF-UCL
    2. cadmium ion binding Source: BHF-UCL
    3. flavin adenine dinucleotide binding Source: BHF-UCL
    4. FMN binding Source: BHF-UCL
    5. heme binding Source: BHF-UCL
    6. ion channel binding Source: BHF-UCL
    7. iron ion binding Source: InterPro
    8. NADP binding Source: BHF-UCL
    9. NADPH-hemoprotein reductase activity Source: RefGenome
    10. nitric-oxide synthase activity Source: BHF-UCL
    11. oxidoreductase activity Source: RefGenome
    12. protein binding Source: UniProtKB
    13. scaffold protein binding Source: BHF-UCL
    14. sodium channel regulator activity Source: BHF-UCL
    15. tetrahydrobiopterin binding Source: BHF-UCL

    GO - Biological processi

    1. arginine catabolic process Source: BHF-UCL
    2. blood coagulation Source: Reactome
    3. cellular response to growth factor stimulus Source: Ensembl
    4. exogenous drug catabolic process Source: Ensembl
    5. interaction with host Source: Reactome
    6. multicellular organismal response to stress Source: BHF-UCL
    7. myoblast fusion Source: BHF-UCL
    8. negative regulation of blood pressure Source: RefGenome
    9. negative regulation of calcium ion transport into cytosol Source: BHF-UCL
    10. negative regulation of hydrolase activity Source: Ensembl
    11. negative regulation of potassium ion transport Source: Ensembl
    12. negative regulation of serotonin uptake Source: Ensembl
    13. neurotransmitter biosynthetic process Source: BHF-UCL
    14. nitric oxide biosynthetic process Source: BHF-UCL
    15. nitric oxide mediated signal transduction Source: RefGenome
    16. peptidyl-cysteine S-nitrosylation Source: BHF-UCL
    17. phagosome maturation Source: Reactome
    18. positive regulation of guanylate cyclase activity Source: RefGenome
    19. positive regulation of histone acetylation Source: Ensembl
    20. positive regulation of sodium ion transmembrane transport Source: BHF-UCL
    21. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    22. positive regulation of vasodilation Source: BHF-UCL
    23. regulation of cardiac muscle contraction Source: BHF-UCL
    24. response to heat Source: BHF-UCL
    25. response to hypoxia Source: BHF-UCL
    26. striated muscle contraction Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01647-MONOMER.
    ReactomeiREACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_23862. Nitric oxide stimulates guanylate cyclase.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:7872. 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. cytoplasm Source: BHF-UCL
    2. cytoskeleton Source: BHF-UCL
    3. cytosol Source: Reactome
    4. dendritic spine Source: UniProtKB-SubCell
    5. perinuclear region of cytoplasm Source: BHF-UCL
    6. photoreceptor inner segment Source: BHF-UCL
    7. protein complex Source: BHF-UCL
    8. sarcolemma Source: BHF-UCL
    9. sarcoplasmic reticulum Source: BHF-UCL
    10. synapse Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA252.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14341434Nitric oxide synthase, brainPRO_0000170921Add
    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

    MaxQBiP29475.
    PaxDbiP29475.
    PRIDEiP29475.

    PTM databases

    PhosphoSiteiP29475.

    Miscellaneous databases

    PMAP-CutDBP29475.

    Expressioni

    Tissue specificityi

    Isoform 1 is ubiquitously expressed: detected in skeletal muscle and brain, also in testis, lung and kidney, and at low levels in heart, adrenal gland and retina. Not detected in the platelets. Isoform 3 is expressed only in testis. Isoform 4 is detected in testis, skeletal muscle, lung, and kidney, at low levels in the brain, but not in the heart and adrenal gland.

    Gene expression databases

    ArrayExpressiP29475.
    BgeeiP29475.
    CleanExiHS_NOS1.
    GenevestigatoriP29475.

    Organism-specific databases

    HPAiCAB002167.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with DLG4; the interaction possibly being prevented by the association between NOS1 and CAPON. 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 By similarity. Interacts with HTR4. Interacts with VAC14 By similarity. Interacts with SLC6A4 By similarity. Interacts (via N-terminal domain) with DLG4 (via N-terminal tandem pair of PDZ domains) By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    VAC14Q08AM65EBI-7164065,EBI-2107455

    Protein-protein interaction databases

    BioGridi110905. 17 interactions.
    DIPiDIP-40999N.
    IntActiP29475. 3 interactions.
    MINTiMINT-122019.
    STRINGi9606.ENSP00000320758.

    Structurei

    3D structure databases

    ProteinModelPortaliP29475.
    SMRiP29475. Positions 12-126, 303-721, 755-1418.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 9983PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini760 – 940181Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini995 – 1242248FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 205205Interaction with NOSIPBy similarityAdd
    BLAST
    Regioni163 – 24583PIN (nNOS-inhibiting protein) bindingAdd
    BLAST
    Regioni730 – 75021Calmodulin-bindingSequence AnalysisAdd
    BLAST
    Regioni755 – 77420Tetrahydrobiopterin-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.
    HOGENOMiHOG000220884.
    HOVERGENiHBG000159.
    KOiK13240.
    OMAiNQMVKVE.
    OrthoDBiEOG79SDW7.
    PhylomeDBiP29475.
    TreeFamiTF324410.

    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

    Note: Isoform 3 is produced by different alternative splicing events implicating either the untranslated exons TEX1 (TN-NOS) or TEX1B (TN-NOSB) leading to a N-terminally truncated protein which possesses enzymatic activity comparable to that of isoform 1. The C-terminally truncated isoform 4 is produced by insertion of the TEX2 exon between exons 3 and 4 of isoform 1, leading to a frameshift and a premature stop codon.1 Publication

    Isoform 1 (identifier: P29475-1) [UniParc]FASTAAdd to Basket

    Also known as: N-NOS-1

    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

    MEDHMFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG     50
    AAEQSGLIQA GDIILAVNGR PLVDLSYDSA LEVLRGIASE THVVLILRGP 100
    EGFTTHLETT FTGDGTPKTI RVTQPLGPPT KAVDLSHQPP AGKEQPLAVD 150
    GASGPGNGPQ HAYDDGQEAG SLPHANGLAP RPPGQDPAKK ATRVSLQGRG 200
    ENNELLKEIE PVLSLLTSGS RGVKGGAPAK AEMKDMGIQV DRDLDGKSHK 250
    PLPLGVENDR VFNDLWGKGN VPVVLNNPYS EKEQPPTSGK QSPTKNGSPS 300
    KCPRFLKVKN WETEVVLTDT LHLKSTLETG CTEYICMGSI MHPSQHARRP 350
    EDVRTKGQLF PLAKEFIDQY YSSIKRFGSK AHMERLEEVN KEIDTTSTYQ 400
    LKDTELIYGA KHAWRNASRC VGRIQWSKLQ VFDARDCTTA HGMFNYICNH 450
    VKYATNKGNL RSAITIFPQR TDGKHDFRVW NSQLIRYAGY KQPDGSTLGD 500
    PANVQFTEIC IQQGWKPPRG RFDVLPLLLQ ANGNDPELFQ IPPELVLEVP 550
    IRHPKFEWFK DLGLKWYGLP AVSNMLLEIG GLEFSACPFS GWYMGTEIGV 600
    RDYCDNSRYN ILEEVAKKMN LDMRKTSSLW KDQALVEINI AVLYSFQSDK 650
    VTIVDHHSAT ESFIKHMENE YRCRGGCPAD WVWIVPPMSG SITPVFHQEM 700
    LNYRLTPSFE YQPDPWNTHV WKGTNGTPTK RRAIGFKKLA EAVKFSAKLM 750
    GQAMAKRVKA TILYATETGK SQAYAKTLCE IFKHAFDAKV MSMEEYDIVH 800
    LEHETLVLVV TSTFGNGDPP ENGEKFGCAL MEMRHPNSVQ EERKSYKVRF 850
    NSVSSYSDSQ KSSGDGPDLR DNFESAGPLA NVRFSVFGLG SRAYPHFCAF 900
    GHAVDTLLEE LGGERILKMR EGDELCGQEE AFRTWAKKVF KAACDVFCVG 950
    DDVNIEKANN SLISNDRSWK RNKFRLTFVA EAPELTQGLS NVHKKRVSAA 1000
    RLLSRQNLQS PKSSRSTIFV RLHTNGSQEL QYQPGDHLGV FPGNHEDLVN 1050
    ALIERLEDAP PVNQMVKVEL LEERNTALGV ISNWTDELRL PPCTIFQAFK 1100
    YYLDITTPPT PLQLQQFASL ATSEKEKQRL LVLSKGLQEY EEWKWGKNPT 1150
    IVEVLEEFPS IQMPATLLLT QLSLLQPRYY SISSSPDMYP DEVHLTVAIV 1200
    SYRTRDGEGP IHHGVCSSWL NRIQADELVP CFVRGAPSFH LPRNPQVPCI 1250
    LVGPGTGIAP FRSFWQQRQF DIQHKGMNPC PMVLVFGCRQ SKIDHIYREE 1300
    TLQAKNKGVF RELYTAYSRE PDKPKKYVQD ILQEQLAESV YRALKEQGGH 1350
    IYVCGDVTMA ADVLKAIQRI MTQQGKLSAE DAGVFISRMR DDNRYHEDIF 1400
    GVTLRTYEVT NRLRSESIAF IEESKKDTDE VFSS 1434
    Length:1,434
    Mass (Da):160,970
    Last modified:October 1, 1996 - v2
    Checksum:i99235793B953BF37
    GO
    Isoform 2 (identifier: P29475-2) [UniParc]FASTAAdd to Basket

    Also known as: N-NOS-2

    The sequence of this isoform differs from the canonical sequence as follows:
         509-613: Missing.

    Show »
    Length:1,329
    Mass (Da):148,919
    Checksum:iDF791B80FDB12302
    GO
    Isoform 3 (identifier: P29475-3) [UniParc]FASTAAdd to Basket

    Also known as: TN-NOS, TN-NOSB

    The sequence of this isoform differs from the canonical sequence as follows:
         1-336: Missing.

    Show »
    Length:1,098
    Mass (Da):125,113
    Checksum:iA1CD5C5012436233
    GO
    Isoform 4 (identifier: P29475-4) [UniParc]FASTAAdd to Basket

    Also known as: TEX2-insertion

    The sequence of this isoform differs from the canonical sequence as follows:
         285-407: PPTSGKQSPT...TYQLKDTELI → MRKLRITEGF...PKPTWKGWKR
         408-1434: Missing.

    Show »
    Length:407
    Mass (Da):43,838
    Checksum:i7E9420C658EFACD2
    GO
    Isoform 5 (identifier: P29475-5) [UniParc]FASTAAdd to Basket

    Also known as: nNOSmu

    The sequence of this isoform differs from the canonical sequence as follows:
         844-844: K → KYPEPLRFFPRKGPPLPNGDTEVHGLAAARDSQHR

    Show »
    Length:1,468
    Mass (Da):164,779
    Checksum:i95906AC90699A0E2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311K → E in AAB49040. (PubMed:8879752)Curated
    Sequence conflicti178 – 1847LAPRPPG → WPQAPR(PubMed:7678401)Curated
    Sequence conflicti178 – 1847LAPRPPG → WPQAPR(PubMed:8879752)Curated
    Sequence conflicti492 – 4932QP → HR in AAA36376. (PubMed:7678401)Curated
    Sequence conflicti549 – 5491V → L in AAA36376. (PubMed:7678401)Curated
    Sequence conflicti563 – 5631G → A in AAA36376. (PubMed:7678401)Curated
    Sequence conflicti1407 – 14071Y → I in AAA36376. (PubMed:7678401)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti228 – 2281P → S.1 Publication
    Corresponds to variant rs9658279 [ dbSNP | Ensembl ].
    VAR_018948
    Natural varianti394 – 3941D → A.1 Publication
    Corresponds to variant rs9658356 [ dbSNP | Ensembl ].
    VAR_018949
    Natural varianti725 – 7251N → D.1 Publication
    Corresponds to variant rs9658403 [ dbSNP | Ensembl ].
    VAR_018950
    Natural varianti864 – 8641G → D.1 Publication
    Corresponds to variant rs9658445 [ dbSNP | Ensembl ].
    VAR_018951
    Natural varianti1064 – 10641Q → R.1 Publication
    Corresponds to variant rs9658482 [ dbSNP | Ensembl ].
    VAR_018952

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 336336Missing in isoform 3. CuratedVSP_003571Add
    BLAST
    Alternative sequencei285 – 407123PPTSG…DTELI → MRKLRITEGFGVQRGSHNHP PPQENSPPQRMAAPPSVHAS SRSRTGRLRWFSLTPSTLRA HWKRDALSTSAWAPSCILLS MQGGLKTSAQKDSSSLSPKS LLINTIHQLKDLAPKPTWKG WKR in isoform 4. CuratedVSP_003572Add
    BLAST
    Alternative sequencei408 – 14341027Missing in isoform 4. CuratedVSP_003573Add
    BLAST
    Alternative sequencei509 – 613105Missing in isoform 2. 2 PublicationsVSP_003574Add
    BLAST
    Alternative sequencei844 – 8441K → KYPEPLRFFPRKGPPLPNGD TEVHGLAAARDSQHR in isoform 5. 1 PublicationVSP_044916

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17327 mRNA. Translation: AAA62405.1.
    U17326
    , U17299, U17300, U17301, U17302, U17303, U17304, U17305, U17307, U17308, U17309, U17310, U17311, U17312, U17313, U17314, U17315, U17316, U17317, U17318, U17319, U17320, U17321, U17322, U17323, U17324, U17325 Genomic DNA. Translation: AAB60654.1. Sequence problems.
    D16408 mRNA. Translation: BAA03895.1.
    L02881 mRNA. Translation: AAA36376.1.
    U31466 mRNA. Translation: AAB49040.1.
    U66362 Genomic DNA. No translation available.
    AY445095 Genomic DNA. Translation: AAR07069.1.
    AC026364 Genomic DNA. No translation available.
    AC068799 Genomic DNA. No translation available.
    AC073864 Genomic DNA. No translation available.
    AJ004918 mRNA. Translation: CAA06218.1.
    CCDSiCCDS41842.1. [P29475-1]
    CCDS55890.1. [P29475-5]
    PIRiG01946.
    RefSeqiNP_000611.1. NM_000620.4. [P29475-1]
    NP_001191142.1. NM_001204213.1. [P29475-3]
    NP_001191143.1. NM_001204214.1. [P29475-3]
    NP_001191147.1. NM_001204218.1. [P29475-5]
    XP_006719489.1. XM_006719426.1. [P29475-5]
    XP_006719490.1. XM_006719427.1. [P29475-5]
    XP_006719491.1. XM_006719428.1. [P29475-1]
    UniGeneiHs.654410.
    Hs.684465.
    Hs.684466.
    Hs.684467.
    Hs.735734.

    Genome annotation databases

    EnsembliENST00000317775; ENSP00000320758; ENSG00000089250. [P29475-1]
    ENST00000338101; ENSP00000337459; ENSG00000089250. [P29475-5]
    GeneIDi4842.
    KEGGihsa:4842.
    UCSCiuc001twm.2. human. [P29475-1]

    Polymorphism databases

    DMDMi1709333.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Nitric oxide synthase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17327 mRNA. Translation: AAA62405.1 .
    U17326
    , U17299 , U17300 , U17301 , U17302 , U17303 , U17304 , U17305 , U17307 , U17308 , U17309 , U17310 , U17311 , U17312 , U17313 , U17314 , U17315 , U17316 , U17317 , U17318 , U17319 , U17320 , U17321 , U17322 , U17323 , U17324 , U17325 Genomic DNA. Translation: AAB60654.1 . Sequence problems.
    D16408 mRNA. Translation: BAA03895.1 .
    L02881 mRNA. Translation: AAA36376.1 .
    U31466 mRNA. Translation: AAB49040.1 .
    U66362 Genomic DNA. No translation available.
    AY445095 Genomic DNA. Translation: AAR07069.1 .
    AC026364 Genomic DNA. No translation available.
    AC068799 Genomic DNA. No translation available.
    AC073864 Genomic DNA. No translation available.
    AJ004918 mRNA. Translation: CAA06218.1 .
    CCDSi CCDS41842.1. [P29475-1 ]
    CCDS55890.1. [P29475-5 ]
    PIRi G01946.
    RefSeqi NP_000611.1. NM_000620.4. [P29475-1 ]
    NP_001191142.1. NM_001204213.1. [P29475-3 ]
    NP_001191143.1. NM_001204214.1. [P29475-3 ]
    NP_001191147.1. NM_001204218.1. [P29475-5 ]
    XP_006719489.1. XM_006719426.1. [P29475-5 ]
    XP_006719490.1. XM_006719427.1. [P29475-5 ]
    XP_006719491.1. XM_006719428.1. [P29475-1 ]
    UniGenei Hs.654410.
    Hs.684465.
    Hs.684466.
    Hs.684467.
    Hs.735734.

    3D structure databases

    ProteinModelPortali P29475.
    SMRi P29475. Positions 12-126, 303-721, 755-1418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110905. 17 interactions.
    DIPi DIP-40999N.
    IntActi P29475. 3 interactions.
    MINTi MINT-122019.
    STRINGi 9606.ENSP00000320758.

    Chemistry

    BindingDBi P29475.
    ChEMBLi CHEMBL2096621.
    DrugBanki DB00155. L-Citrulline.
    GuidetoPHARMACOLOGYi 1251.

    PTM databases

    PhosphoSitei P29475.

    Polymorphism databases

    DMDMi 1709333.

    Proteomic databases

    MaxQBi P29475.
    PaxDbi P29475.
    PRIDEi P29475.

    Protocols and materials databases

    DNASUi 4842.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317775 ; ENSP00000320758 ; ENSG00000089250 . [P29475-1 ]
    ENST00000338101 ; ENSP00000337459 ; ENSG00000089250 . [P29475-5 ]
    GeneIDi 4842.
    KEGGi hsa:4842.
    UCSCi uc001twm.2. human. [P29475-1 ]

    Organism-specific databases

    CTDi 4842.
    GeneCardsi GC12M117636.
    HGNCi HGNC:7872. NOS1.
    HPAi CAB002167.
    MIMi 163731. gene.
    neXtProti NX_P29475.
    PharmGKBi PA252.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4362.
    HOGENOMi HOG000220884.
    HOVERGENi HBG000159.
    KOi K13240.
    OMAi NQMVKVE.
    OrthoDBi EOG79SDW7.
    PhylomeDBi P29475.
    TreeFami TF324410.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01647-MONOMER.
    Reactomei REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_23862. Nitric oxide stimulates guanylate cyclase.

    Miscellaneous databases

    ChiTaRSi NOS1. human.
    GeneWikii NOS1.
    GenomeRNAii 4842.
    NextBioi 18658.
    PMAP-CutDB P29475.
    PROi P29475.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29475.
    Bgeei P29475.
    CleanExi HS_NOS1.
    Genevestigatori P29475.

    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 organization of the human neuronal nitric oxide synthase gene (NOS1)."
      Hall A.V., Antoniou H., Wang Y., Cheung A.H., Arbus A.M., Olson S.L., Lu W.C., Kau C.-L., Marsden P.A.
      J. Biol. Chem. 269:33082-33090(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    2. "Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines."
      Fujisawa H., Ogura T., Kurashima Y., Yokoyama T., Yamashita J., Esumi H.
      J. Neurochem. 63:140-145(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Cerebellum.
    3. "Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle."
      Nakane M., Schmidt H.H.H.W., Pollock J.S., Foerstermann U., Murad F.
      FEBS Lett. 316:175-180(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    4. "Neuronal isoform of nitric oxide synthase is expressed at low levels in human retina."
      Park C.-S., Gianotti C., Park R., Krishna G.
      Cell. Mol. Neurobiol. 16:499-515(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retina.
    5. "A novel, testis-specific mRNA transcript encoding an NH2-terminal truncated nitric-oxide synthase."
      Wang Y., Goligorsky M.S., Lin M., Wilcox J.N., Marsden P.A.
      J. Biol. Chem. 272:11392-11401(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3 AND 4).
      Tissue: Testis.
    6. NIEHS SNPs program
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-228; ALA-394; ASP-725; ASP-864 AND ARG-1064.
    7. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "Isolation and characterization of a novel, human neuronal nitric oxide synthase cDNA."
      Larsson B., Phillips S.C.
      Biochem. Biophys. Res. Commun. 251:898-902(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 835-901 (ISOFORM 5), ALTERNATIVE SPLICING.
      Tissue: Skeletal muscle.

    Entry informationi

    Entry nameiNOS1_HUMAN
    AccessioniPrimary (citable) accession number: P29475
    Secondary accession number(s): E9PH30, O75713
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 164 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3