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P29475 (NOS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NOS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1434 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Heme group.

Binds 1 FAD.

Binds 1 FMN.

Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.

Enzyme regulation

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

Subunit structure

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-terminus domain) with DLG4 (via N-terminus tandem pair of PDZ domains) By similarity.

Subcellular location

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.

Tissue specificity

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.

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the NOS family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandCalmodulin-binding
FAD
Flavoprotein
FMN
Heme
Iron
Metal-binding
NADP
   Molecular functionOxidoreductase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine catabolic process

Inferred by curator PubMed 7545544. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

exogenous drug catabolic process

Inferred from electronic annotation. Source: Ensembl

interaction with host

Traceable author statement. Source: Reactome

multicellular organismal response to stress

Inferred from mutant phenotype PubMed 18391107. Source: BHF-UCL

myoblast fusion

Traceable author statement PubMed 7545544. Source: BHF-UCL

negative regulation of blood pressure

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of calcium ion transport into cytosol

Traceable author statement PubMed 17568574. Source: BHF-UCL

negative regulation of hydrolase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of potassium ion transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of serotonin uptake

Inferred from electronic annotation. Source: Ensembl

neurotransmitter biosynthetic process

Traceable author statement PubMed 7545544. Source: BHF-UCL

nitric oxide biosynthetic process

Inferred from sequence or structural similarity PubMed 7545544. Source: BHF-UCL

nitric oxide mediated signal transduction

Inferred from Biological aspect of Ancestor. Source: RefGenome

peptidyl-cysteine S-nitrosylation

Inferred from sequence or structural similarity. Source: BHF-UCL

phagosome maturation

Traceable author statement. Source: Reactome

positive regulation of guanylate cyclase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of histone acetylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of sodium ion transmembrane transport

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from direct assay PubMed 18048451. Source: BHF-UCL

regulation of cardiac muscle contraction

Traceable author statement PubMed 9892689. Source: BHF-UCL

response to heat

Inferred from direct assay PubMed 18048451. Source: BHF-UCL

response to hypoxia

Inferred from expression pattern PubMed 16276418. Source: BHF-UCL

striated muscle contraction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Traceable author statement PubMed 17892502. Source: BHF-UCL

cytoskeleton

Inferred from sequence or structural similarity PubMed 7545544. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from sequence or structural similarity PubMed 17027776. Source: BHF-UCL

photoreceptor inner segment

Inferred from sequence or structural similarity PubMed 17027776. Source: BHF-UCL

protein complex

Inferred from sequence or structural similarity. Source: BHF-UCL

sarcolemma

Inferred from direct assay PubMed 7545544. Source: BHF-UCL

sarcoplasmic reticulum

Inferred from direct assay PubMed 9892689. Source: BHF-UCL

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionFMN binding

Inferred from sequence or structural similarity. Source: BHF-UCL

NADP binding

Inferred from sequence or structural similarity. Source: BHF-UCL

NADPH-hemoprotein reductase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

arginine binding

Traceable author statement PubMed 17029414. Source: BHF-UCL

cadmium ion binding

Inferred from sequence or structural similarity. Source: BHF-UCL

flavin adenine dinucleotide binding

Inferred from sequence or structural similarity. Source: BHF-UCL

heme binding

Inferred from sequence or structural similarity. Source: BHF-UCL

ion channel binding

Inferred from sequence or structural similarity. Source: BHF-UCL

iron ion binding

Inferred from electronic annotation. Source: InterPro

nitric-oxide synthase activity

Inferred from sequence or structural similarity PubMed 7545544. Source: BHF-UCL

oxidoreductase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

scaffold protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

sodium channel regulator activity

Inferred from sequence or structural similarity. Source: BHF-UCL

tetrahydrobiopterin binding

Non-traceable author statement PubMed 7488039. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VAC14Q08AM65EBI-7164065,EBI-2107455

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

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-terminus truncated protein which possesses enzymatic activity comparable to that of isoform 1. The C-terminal 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.
Isoform 1 (identifier: P29475-1)

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.
Isoform 2 (identifier: P29475-2)

Also known as: N-NOS-2;

The sequence of this isoform differs from the canonical sequence as follows:
     509-613: Missing.
Isoform 3 (identifier: P29475-3)

Also known as: TN-NOS; TN-NOSB;

The sequence of this isoform differs from the canonical sequence as follows:
     1-336: Missing.
Isoform 4 (identifier: P29475-4)

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.
Isoform 5 (identifier: P29475-5)

Also known as: nNOSmu;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14341434Nitric oxide synthase, brain
PRO_0000170921

Regions

Domain17 – 9983PDZ
Domain760 – 940181Flavodoxin-like
Domain995 – 1242248FAD-binding FR-type
Nucleotide binding886 – 91732FMN By similarity
Nucleotide binding1032 – 104312FAD By similarity
Nucleotide binding1175 – 118511FAD By similarity
Nucleotide binding1250 – 126819NADP By similarity
Nucleotide binding1348 – 136316NADP By similarity
Region1 – 205205Interaction with NOSIP By similarity
Region163 – 24583PIN (nNOS-inhibiting protein) binding
Region730 – 75021Calmodulin-binding Potential
Region755 – 77420Tetrahydrobiopterin-binding By similarity

Sites

Metal binding4201Iron (heme axial ligand) By similarity

Natural variations

Alternative sequence1 – 336336Missing in isoform 3.
VSP_003571
Alternative sequence285 – 407123PPTSG…DTELI → MRKLRITEGFGVQRGSHNHP PPQENSPPQRMAAPPSVHAS SRSRTGRLRWFSLTPSTLRA HWKRDALSTSAWAPSCILLS MQGGLKTSAQKDSSSLSPKS LLINTIHQLKDLAPKPTWKG WKR in isoform 4.
VSP_003572
Alternative sequence408 – 14341027Missing in isoform 4.
VSP_003573
Alternative sequence509 – 613105Missing in isoform 2.
VSP_003574
Alternative sequence8441K → KYPEPLRFFPRKGPPLPNGD TEVHGLAAARDSQHR in isoform 5.
VSP_044916
Natural variant2281P → S. Ref.6
Corresponds to variant rs9658279 [ dbSNP | Ensembl ].
VAR_018948
Natural variant3941D → A. Ref.6
Corresponds to variant rs9658356 [ dbSNP | Ensembl ].
VAR_018949
Natural variant7251N → D. Ref.6
Corresponds to variant rs9658403 [ dbSNP | Ensembl ].
VAR_018950
Natural variant8641G → D. Ref.6
Corresponds to variant rs9658445 [ dbSNP | Ensembl ].
VAR_018951
Natural variant10641Q → R. Ref.6
Corresponds to variant rs9658482 [ dbSNP | Ensembl ].
VAR_018952

Experimental info

Sequence conflict1311K → E in AAB49040. Ref.4
Sequence conflict178 – 1847LAPRPPG → WPQAPR Ref.3
Sequence conflict178 – 1847LAPRPPG → WPQAPR Ref.4
Sequence conflict492 – 4932QP → HR in AAA36376. Ref.3
Sequence conflict5491V → L in AAA36376. Ref.3
Sequence conflict5631G → A in AAA36376. Ref.3
Sequence conflict14071Y → I in AAA36376. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (N-NOS-1) [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 99235793B953BF37

FASTA1,434160,970
        10         20         30         40         50         60 
MEDHMFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA 

        70         80         90        100        110        120 
GDIILAVNGR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI 

       130        140        150        160        170        180 
RVTQPLGPPT KAVDLSHQPP AGKEQPLAVD GASGPGNGPQ HAYDDGQEAG SLPHANGLAP 

       190        200        210        220        230        240 
RPPGQDPAKK ATRVSLQGRG ENNELLKEIE PVLSLLTSGS RGVKGGAPAK AEMKDMGIQV 

       250        260        270        280        290        300 
DRDLDGKSHK PLPLGVENDR VFNDLWGKGN VPVVLNNPYS EKEQPPTSGK QSPTKNGSPS 

       310        320        330        340        350        360 
KCPRFLKVKN WETEVVLTDT LHLKSTLETG CTEYICMGSI MHPSQHARRP EDVRTKGQLF 

       370        380        390        400        410        420 
PLAKEFIDQY YSSIKRFGSK AHMERLEEVN KEIDTTSTYQ LKDTELIYGA KHAWRNASRC 

       430        440        450        460        470        480 
VGRIQWSKLQ VFDARDCTTA HGMFNYICNH VKYATNKGNL RSAITIFPQR TDGKHDFRVW 

       490        500        510        520        530        540 
NSQLIRYAGY KQPDGSTLGD PANVQFTEIC IQQGWKPPRG RFDVLPLLLQ ANGNDPELFQ 

       550        560        570        580        590        600 
IPPELVLEVP IRHPKFEWFK DLGLKWYGLP AVSNMLLEIG GLEFSACPFS GWYMGTEIGV 

       610        620        630        640        650        660 
RDYCDNSRYN ILEEVAKKMN LDMRKTSSLW KDQALVEINI AVLYSFQSDK VTIVDHHSAT 

       670        680        690        700        710        720 
ESFIKHMENE YRCRGGCPAD WVWIVPPMSG SITPVFHQEM LNYRLTPSFE YQPDPWNTHV 

       730        740        750        760        770        780 
WKGTNGTPTK RRAIGFKKLA EAVKFSAKLM GQAMAKRVKA TILYATETGK SQAYAKTLCE 

       790        800        810        820        830        840 
IFKHAFDAKV MSMEEYDIVH LEHETLVLVV TSTFGNGDPP ENGEKFGCAL MEMRHPNSVQ 

       850        860        870        880        890        900 
EERKSYKVRF NSVSSYSDSQ KSSGDGPDLR DNFESAGPLA NVRFSVFGLG SRAYPHFCAF 

       910        920        930        940        950        960 
GHAVDTLLEE LGGERILKMR EGDELCGQEE AFRTWAKKVF KAACDVFCVG DDVNIEKANN 

       970        980        990       1000       1010       1020 
SLISNDRSWK RNKFRLTFVA EAPELTQGLS NVHKKRVSAA RLLSRQNLQS PKSSRSTIFV 

      1030       1040       1050       1060       1070       1080 
RLHTNGSQEL QYQPGDHLGV FPGNHEDLVN ALIERLEDAP PVNQMVKVEL LEERNTALGV 

      1090       1100       1110       1120       1130       1140 
ISNWTDELRL PPCTIFQAFK YYLDITTPPT PLQLQQFASL ATSEKEKQRL LVLSKGLQEY 

      1150       1160       1170       1180       1190       1200 
EEWKWGKNPT IVEVLEEFPS IQMPATLLLT QLSLLQPRYY SISSSPDMYP DEVHLTVAIV 

      1210       1220       1230       1240       1250       1260 
SYRTRDGEGP IHHGVCSSWL NRIQADELVP CFVRGAPSFH LPRNPQVPCI LVGPGTGIAP 

      1270       1280       1290       1300       1310       1320 
FRSFWQQRQF DIQHKGMNPC PMVLVFGCRQ SKIDHIYREE TLQAKNKGVF RELYTAYSRE 

      1330       1340       1350       1360       1370       1380 
PDKPKKYVQD ILQEQLAESV YRALKEQGGH IYVCGDVTMA ADVLKAIQRI MTQQGKLSAE 

      1390       1400       1410       1420       1430 
DAGVFISRMR DDNRYHEDIF GVTLRTYEVT NRLRSESIAF IEESKKDTDE VFSS 

« Hide

Isoform 2 (N-NOS-2) [UniParc].

Checksum: DF791B80FDB12302
Show »

FASTA1,329148,919
Isoform 3 (TN-NOS) (TN-NOSB) [UniParc].

Checksum: A1CD5C5012436233
Show »

FASTA1,098125,113
Isoform 4 (TEX2-insertion) [UniParc].

Checksum: 7E9420C658EFACD2
Show »

FASTA40743,838
Isoform 5 (nNOSmu) [UniParc].

Checksum: 95906AC90699A0E2
Show »

FASTA1,468164,779

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Nitric oxide synthase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17327 mRNA. Translation: AAA62405.1.
U17326 expand/collapse EMBL AC list , 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.
PIRG01946.
RefSeqNP_000611.1. NM_000620.4.
NP_001191142.1. NM_001204213.1.
NP_001191143.1. NM_001204214.1.
NP_001191147.1. NM_001204218.1.
UniGeneHs.654410.
Hs.684465.
Hs.684466.
Hs.684467.
Hs.735734.

3D structure databases

ProteinModelPortalP29475.
SMRP29475. Positions 12-126, 303-721, 755-1418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110905. 17 interactions.
IntActP29475. 3 interactions.
MINTMINT-122019.
STRING9606.ENSP00000320758.

Chemistry

BindingDBP29475.
ChEMBLCHEMBL2096621.
DrugBankDB00155. L-Citrulline.
GuidetoPHARMACOLOGY1251.

PTM databases

PhosphoSiteP29475.

Polymorphism databases

DMDM1709333.

Proteomic databases

PaxDbP29475.
PRIDEP29475.

Protocols and materials databases

DNASU4842.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317775; ENSP00000320758; ENSG00000089250. [P29475-1]
ENST00000338101; ENSP00000337459; ENSG00000089250. [P29475-5]
GeneID4842.
KEGGhsa:4842.
UCSCuc001twm.2. human. [P29475-1]

Organism-specific databases

CTD4842.
GeneCardsGC12M117636.
HGNCHGNC:7872. NOS1.
HPACAB002167.
MIM163731. gene.
neXtProtNX_P29475.
PharmGKBPA252.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4362.
HOGENOMHOG000220884.
HOVERGENHBG000159.
KOK13240.
OMANQMVKVE.
OrthoDBEOG79SDW7.
PhylomeDBP29475.
TreeFamTF324410.

Enzyme and pathway databases

BioCycMetaCyc:HS01647-MONOMER.
ReactomeREACT_116125. Disease.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP29475.
BgeeP29475.
CleanExHS_NOS1.
GenevestigatorP29475.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
2.30.42.10. 1 hit.
3.90.340.10. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR004030. NO_synthase_oxygenase_dom.
IPR012144. NOS_euk.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001478. PDZ.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. 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]
PIRSFPIRSF000333. NOS. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SMARTSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNOS1. human.
GeneWikiNOS1.
GenomeRNAi4842.
NextBio18658.
PMAP-CutDBP29475.
PROP29475.
SOURCESearch...

Entry information

Entry nameNOS1_HUMAN
AccessionPrimary (citable) accession number: P29475
Secondary accession number(s): E9PH30, O75713
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM