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Protein

Nitric oxide synthase, brain

Gene

NOS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:HS01647-MONOMER.
BRENDAi1.14.13.39. 2681.
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 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7872. NOS1.

Subcellular locationi

GO - Cellular componenti

  • azurophil granule Source: Ensembl
  • caveola Source: Ensembl
  • cytoplasm Source: BHF-UCL
  • cytoskeleton Source: BHF-UCL
  • cytosol Source: GO_Central
  • dendritic spine Source: UniProtKB-SubCell
  • membrane raft Source: BHF-UCL
  • mitochondrial outer membrane Source: Ensembl
  • mitochondrion Source: BHF-UCL
  • nuclear membrane Source: Ensembl
  • perinuclear region of cytoplasm Source: BHF-UCL
  • photoreceptor inner segment Source: BHF-UCL
  • postsynaptic density Source: Ensembl
  • protein complex Source: BHF-UCL
  • sarcolemma Source: BHF-UCL
  • sarcoplasmic reticulum Source: BHF-UCL
  • sarcoplasmic reticulum membrane Source: Ensembl
  • synapse Source: BHF-UCL
  • T-tubule Source: Ensembl
  • vesicle membrane Source: Ensembl
  • Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA252.

Chemistry

DrugBankiDB00997. Doxorubicin.
DB03147. Flavin adenine dinucleotide.
DB00155. L-Citrulline.

Polymorphism and mutation databases

BioMutaiNOS1.
DMDMi1709333.

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

BgeeiP29475.
CleanExiHS_NOS1.
ExpressionAtlasiP29475. baseline and differential.
GenevisibleiP29475. HS.

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. 14 interactions.
DIPiDIP-40999N.
IntActiP29475. 3 interactions.
MINTiMINT-122019.
STRINGi9606.ENSP00000337459.

Structurei

Secondary structure

1
1434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi306 – 3105Combined sources
Turni311 – 3133Combined sources
Beta strandi316 – 3194Combined sources
Helixi321 – 3244Combined sources
Helixi356 – 37318Combined sources
Helixi380 – 39617Combined sources
Helixi403 – 41513Combined sources
Helixi423 – 4253Combined sources
Beta strandi430 – 4334Combined sources
Helixi440 – 45516Combined sources
Helixi456 – 4583Combined sources
Beta strandi463 – 4664Combined sources
Beta strandi471 – 4755Combined sources
Beta strandi481 – 4855Combined sources
Beta strandi489 – 4913Combined sources
Beta strandi497 – 4993Combined sources
Helixi501 – 5033Combined sources
Helixi504 – 5129Combined sources
Beta strandi520 – 5223Combined sources
Beta strandi527 – 5304Combined sources
Beta strandi537 – 5393Combined sources
Helixi543 – 5453Combined sources
Beta strandi548 – 5503Combined sources
Helixi557 – 5626Combined sources
Beta strandi565 – 5684Combined sources
Beta strandi576 – 5794Combined sources
Beta strandi582 – 5854Combined sources
Helixi595 – 5995Combined sources
Helixi601 – 6044Combined sources
Turni606 – 6094Combined sources
Helixi612 – 6187Combined sources
Helixi626 – 6283Combined sources
Helixi630 – 64819Combined sources
Helixi656 – 67419Combined sources
Helixi681 – 6844Combined sources
Beta strandi687 – 6893Combined sources
Helixi690 – 6923Combined sources
Helixi694 – 6974Combined sources
Beta strandi706 – 7105Combined sources
Helixi715 – 7184Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D1NX-ray2.03A/B/C/D302-721[»]
4UCHX-ray2.20A/B302-723[»]
4V3UX-ray2.30A/B/C/D302-721[»]
ProteinModelPortaliP29475.
SMRiP29475. Positions 12-126, 302-721, 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.
GeneTreeiENSGT00620000087711.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiP29475.
KOiK13240.
OMAiDPANVQF.
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. AlignAdd to basket

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

        10         20         30         40         50
MEDHMFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG
60 70 80 90 100
AAEQSGLIQA GDIILAVNGR PLVDLSYDSA LEVLRGIASE THVVLILRGP
110 120 130 140 150
EGFTTHLETT FTGDGTPKTI RVTQPLGPPT KAVDLSHQPP AGKEQPLAVD
160 170 180 190 200
GASGPGNGPQ HAYDDGQEAG SLPHANGLAP RPPGQDPAKK ATRVSLQGRG
210 220 230 240 250
ENNELLKEIE PVLSLLTSGS RGVKGGAPAK AEMKDMGIQV DRDLDGKSHK
260 270 280 290 300
PLPLGVENDR VFNDLWGKGN VPVVLNNPYS EKEQPPTSGK QSPTKNGSPS
310 320 330 340 350
KCPRFLKVKN WETEVVLTDT LHLKSTLETG CTEYICMGSI MHPSQHARRP
360 370 380 390 400
EDVRTKGQLF PLAKEFIDQY YSSIKRFGSK AHMERLEEVN KEIDTTSTYQ
410 420 430 440 450
LKDTELIYGA KHAWRNASRC VGRIQWSKLQ VFDARDCTTA HGMFNYICNH
460 470 480 490 500
VKYATNKGNL RSAITIFPQR TDGKHDFRVW NSQLIRYAGY KQPDGSTLGD
510 520 530 540 550
PANVQFTEIC IQQGWKPPRG RFDVLPLLLQ ANGNDPELFQ IPPELVLEVP
560 570 580 590 600
IRHPKFEWFK DLGLKWYGLP AVSNMLLEIG GLEFSACPFS GWYMGTEIGV
610 620 630 640 650
RDYCDNSRYN ILEEVAKKMN LDMRKTSSLW KDQALVEINI AVLYSFQSDK
660 670 680 690 700
VTIVDHHSAT ESFIKHMENE YRCRGGCPAD WVWIVPPMSG SITPVFHQEM
710 720 730 740 750
LNYRLTPSFE YQPDPWNTHV WKGTNGTPTK RRAIGFKKLA EAVKFSAKLM
760 770 780 790 800
GQAMAKRVKA TILYATETGK SQAYAKTLCE IFKHAFDAKV MSMEEYDIVH
810 820 830 840 850
LEHETLVLVV TSTFGNGDPP ENGEKFGCAL MEMRHPNSVQ EERKSYKVRF
860 870 880 890 900
NSVSSYSDSQ KSSGDGPDLR DNFESAGPLA NVRFSVFGLG SRAYPHFCAF
910 920 930 940 950
GHAVDTLLEE LGGERILKMR EGDELCGQEE AFRTWAKKVF KAACDVFCVG
960 970 980 990 1000
DDVNIEKANN SLISNDRSWK RNKFRLTFVA EAPELTQGLS NVHKKRVSAA
1010 1020 1030 1040 1050
RLLSRQNLQS PKSSRSTIFV RLHTNGSQEL QYQPGDHLGV FPGNHEDLVN
1060 1070 1080 1090 1100
ALIERLEDAP PVNQMVKVEL LEERNTALGV ISNWTDELRL PPCTIFQAFK
1110 1120 1130 1140 1150
YYLDITTPPT PLQLQQFASL ATSEKEKQRL LVLSKGLQEY EEWKWGKNPT
1160 1170 1180 1190 1200
IVEVLEEFPS IQMPATLLLT QLSLLQPRYY SISSSPDMYP DEVHLTVAIV
1210 1220 1230 1240 1250
SYRTRDGEGP IHHGVCSSWL NRIQADELVP CFVRGAPSFH LPRNPQVPCI
1260 1270 1280 1290 1300
LVGPGTGIAP FRSFWQQRQF DIQHKGMNPC PMVLVFGCRQ SKIDHIYREE
1310 1320 1330 1340 1350
TLQAKNKGVF RELYTAYSRE PDKPKKYVQD ILQEQLAESV YRALKEQGGH
1360 1370 1380 1390 1400
IYVCGDVTMA ADVLKAIQRI MTQQGKLSAE DAGVFISRMR DDNRYHEDIF
1410 1420 1430
GVTLRTYEVT NRLRSESIAF IEESKKDTDE VFSS
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:
EMBLi
GenBanki
DDBJi
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_011536700.1. XM_011538398.1. [P29475-5]
UniGeneiHs.654410.
Hs.684465.
Hs.684466.
Hs.684467.
Hs.735734.

Genome annotation databases

EnsembliENST00000317775; ENSP00000320758; ENSG00000089250.
ENST00000338101; ENSP00000337459; ENSG00000089250. [P29475-5]
ENST00000618760; ENSP00000477999; ENSG00000089250. [P29475-5]
GeneIDi4842.
KEGGihsa:4842.
UCSCiuc001twm.2. human. [P29475-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Nitric oxide synthase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_011536700.1. XM_011538398.1. [P29475-5]
UniGeneiHs.654410.
Hs.684465.
Hs.684466.
Hs.684467.
Hs.735734.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D1NX-ray2.03A/B/C/D302-721[»]
4UCHX-ray2.20A/B302-723[»]
4V3UX-ray2.30A/B/C/D302-721[»]
ProteinModelPortaliP29475.
SMRiP29475. Positions 12-126, 302-721, 755-1418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110905. 14 interactions.
DIPiDIP-40999N.
IntActiP29475. 3 interactions.
MINTiMINT-122019.
STRINGi9606.ENSP00000337459.

Chemistry

BindingDBiP29475.
ChEMBLiCHEMBL2096621.
DrugBankiDB00997. Doxorubicin.
DB03147. Flavin adenine dinucleotide.
DB00155. L-Citrulline.
GuidetoPHARMACOLOGYi1251.

PTM databases

PhosphoSiteiP29475.

Polymorphism and mutation databases

BioMutaiNOS1.
DMDMi1709333.

Proteomic databases

MaxQBiP29475.
PaxDbiP29475.
PRIDEiP29475.

Protocols and materials databases

DNASUi4842.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317775; ENSP00000320758; ENSG00000089250.
ENST00000338101; ENSP00000337459; ENSG00000089250. [P29475-5]
ENST00000618760; ENSP00000477999; ENSG00000089250. [P29475-5]
GeneIDi4842.
KEGGihsa:4842.
UCSCiuc001twm.2. human. [P29475-1]

Organism-specific databases

CTDi4842.
GeneCardsiGC12M117636.
HGNCiHGNC:7872. NOS1.
HPAiCAB002167.
MIMi163731. gene.
neXtProtiNX_P29475.
PharmGKBiPA252.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4362.
GeneTreeiENSGT00620000087711.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiP29475.
KOiK13240.
OMAiDPANVQF.
OrthoDBiEOG79SDW7.
PhylomeDBiP29475.
TreeFamiTF324410.

Enzyme and pathway databases

BioCyciMetaCyc:HS01647-MONOMER.
BRENDAi1.14.13.39. 2681.
ReactomeiREACT_121256. Phagosomal maturation (early endosomal stage).
REACT_23862. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

ChiTaRSiNOS1. human.
GeneWikiiNOS1.
GenomeRNAii4842.
NextBioi18658.
PMAP-CutDBP29475.
PROiP29475.
SOURCEiSearch...

Gene expression databases

BgeeiP29475.
CleanExiHS_NOS1.
ExpressionAtlasiP29475. baseline and differential.
GenevisibleiP29475. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 174 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.