UniProtKB - P29475 (NOS1_HUMAN)
Nitric oxide synthase, brain
NOS1
Functioni
Catalytic activityi
- EC:1.14.13.39
Cofactori
Protein has several cofactor binding sites:- heme
- FADNote: Binds 1 FAD.
- FMNNote: Binds 1 FMN.
- (6R)-L-erythro-5,6,7,8-tetrahydrobiopterinNote: Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 420 | Iron (heme axial ligand)By similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 886 – 917 | FMNPROSITE-ProRule annotationAdd BLAST | 32 | |
Nucleotide bindingi | 1032 – 1043 | FADBy similarityAdd BLAST | 12 | |
Nucleotide bindingi | 1175 – 1185 | FADBy similarityAdd BLAST | 11 | |
Nucleotide bindingi | 1250 – 1268 | NADPBy similarityAdd BLAST | 19 | |
Nucleotide bindingi | 1348 – 1363 | NADPBy similarityAdd BLAST | 16 |
GO - Molecular functioni
- arginine binding Source: BHF-UCL
- cadmium ion binding Source: BHF-UCL
- calcium-dependent protein binding Source: ARUK-UCL
- calmodulin binding Source: UniProtKB-KW
- flavin adenine dinucleotide binding Source: BHF-UCL
- FMN binding Source: BHF-UCL
- heme binding Source: BHF-UCL
- ion channel binding Source: BHF-UCL
- NADP binding Source: BHF-UCL
- NADPH-hemoprotein reductase activity Source: GO_Central
- nitric-oxide synthase activity Source: CACAO
- oxidoreductase activity Source: GO_Central
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Source: GO_Central
- scaffold protein binding Source: BHF-UCL
- sodium channel regulator activity Source: BHF-UCL
- tetrahydrobiopterin binding Source: BHF-UCL
GO - Biological processi
- arginine catabolic process Source: GO_Central
- cell redox homeostasis Source: Reactome
- cellular response to growth factor stimulus Source: BHF-UCL
- exogenous drug catabolic process Source: BHF-UCL
- multicellular organismal response to stress Source: BHF-UCL
- muscle contraction Source: GO_Central
- myoblast fusion Source: BHF-UCL
- negative regulation of blood pressure Source: GO_Central
- negative regulation of calcium ion transport Source: BHF-UCL
- negative regulation of calcium ion transport into cytosol Source: BHF-UCL
- negative regulation of hydrolase activity Source: BHF-UCL
- negative regulation of potassium ion transport Source: BHF-UCL
- negative regulation of serotonin uptake Source: BHF-UCL
- neurotransmitter biosynthetic process Source: BHF-UCL
- nitric oxide biosynthetic process Source: BHF-UCL
- nitric oxide mediated signal transduction Source: GO_Central
- peptidyl-cysteine S-nitrosylation Source: BHF-UCL
- positive regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process Source: Ensembl
- positive regulation of guanylate cyclase activity Source: GO_Central
- positive regulation of histone acetylation Source: BHF-UCL
- positive regulation of peptidyl-serine phosphorylation Source: ARUK-UCL
- positive regulation of sodium ion transmembrane transport Source: BHF-UCL
- positive regulation of the force of heart contraction Source: BHF-UCL
- positive regulation of transcription, DNA-templated Source: BHF-UCL
- positive regulation of transcription by RNA polymerase II Source: BHF-UCL
- regulation of calcium ion transmembrane transport via high voltage-gated calcium channel Source: BHF-UCL
- regulation of cardiac conduction Source: Reactome
- regulation of cardiac muscle contraction Source: BHF-UCL
- regulation of neurogenesis Source: Ensembl
- regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
- regulation of sodium ion transport Source: BHF-UCL
- response to heat Source: BHF-UCL
- response to hormone Source: GO_Central
- response to hypoxia Source: BHF-UCL
- response to lipopolysaccharide Source: GO_Central
- retrograde trans-synaptic signaling by nitric oxide Source: GO_Central
- striated muscle contraction Source: BHF-UCL
- vasodilation Source: BHF-UCL
Keywordsi
Molecular function | Calmodulin-binding, Oxidoreductase |
Ligand | FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP |
Enzyme and pathway databases
BioCyci | MetaCyc:HS01647-MONOMER |
BRENDAi | 1.14.13.39, 2681 |
PathwayCommonsi | P29475 |
Reactomei | R-HSA-1222556, ROS and RNS production in phagocytes R-HSA-392154, Nitric oxide stimulates guanylate cyclase R-HSA-5578775, Ion homeostasis |
SIGNORi | P29475 |
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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:7872, NOS1 |
MIMi | 163731, gene |
neXtProti | NX_P29475 |
VEuPathDBi | HostDB:ENSG00000089250.18 |
Subcellular locationi
Plasma membrane
Other locations
- dendritic 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
Cytoskeleton
- cytoskeleton Source: BHF-UCL
Cytosol
- cytosol Source: GO_Central
Endoplasmic reticulum
- sarcoplasmic reticulum Source: BHF-UCL
- sarcoplasmic reticulum membrane Source: Ensembl
Mitochondrion
- mitochondrion Source: BHF-UCL
Nucleus
- nucleoplasm Source: HPA
- nucleus Source: GO_Central
Plasma Membrane
- caveola Source: Ensembl
- plasma membrane Source: HPA
- sarcolemma Source: BHF-UCL
- T-tubule Source: Ensembl
Other locations
- calyx of Held Source: Ensembl
- cell periphery Source: ARUK-UCL
- cytoplasm Source: ARUK-UCL
- dendritic spine Source: UniProtKB-SubCell
- membrane raft Source: BHF-UCL
- perinuclear region of cytoplasm Source: BHF-UCL
- photoreceptor inner segment Source: BHF-UCL
- postsynaptic density Source: GO_Central
- protein-containing complex Source: BHF-UCL
- synapse Source: BHF-UCL
- vesicle membrane Source: GO_Central
- Z disc Source: Ensembl
Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, Membrane, SynapsePathology & Biotechi
Organism-specific databases
DisGeNETi | 4842 |
MalaCardsi | NOS1 |
OpenTargetsi | ENSG00000089250 |
Orphaneti | 930, Idiopathic achalasia |
PharmGKBi | PA252 |
Miscellaneous databases
Pharosi | P29475, Tchem |
Chemistry databases
ChEMBLi | CHEMBL3568 |
DrugBanki | DB02143, 1-hydroxy-2-isopropylguanidine DB02727, 2-butyl-1-hydroxyguanidine DB01997, 3-Bromo-7-Nitroindazole DB03892, 5-N-Allyl-arginine DB03710, [(1S)-4-(1-Aminobutylideneamino)-1-carboxybutyl]azanium DB00155, Citrulline DB00843, Donepezil DB00997, Doxorubicin DB03147, Flavin adenine dinucleotide DB03247, Flavin mononucleotide DB01942, Formic acid DB01221, Ketamine DB02077, L-N(omega)-nitroarginine-(4R)-amino-L-proline amide DB01821, L-N(omega)-Nitroarginine-2,4-L-diaminobutyric amide DB09241, Methylene blue DB03144, N(5)-[(hydroxyamino)(imino)methyl]-L-ornithine DB03449, N-(4-{2-[(3-chlorobenzyl)amino]ethyl}phenyl)thiophene-2-carboximidamide DB02044, N-[3-(aminomethyl)benzyl]acetamidine DB02644, N-omega-propyl-L-arginine DB08019, N-{(3R,4S)-4-[(6-amino-4-methylpyridin-2-yl)methyl]pyrrolidin-3-yl}-N'-(3-chlorobenzyl)ethane-1,2-diamine DB08018, N-{(3S,4S)-4-[(6-AMINO-4-METHYLPYRIDIN-2-YL)METHYL]PYRROLIDIN-3-YL}-N'-(4-CHLOROBENZYL)ETHANE-1,2-DIAMINE DB02027, N-{(4S)-4-Amino-5-[(2-aminoethyl)amino]pentyl}-N'-nitroguanidine DB03461, Nicotinamide adenine dinucleotide phosphate DB04223, Nitroarginine DB06096, NXN-188 DB02991, S-Ethyl-N-[4-(Trifluoromethyl)Phenyl]Isothiourea DB03707, S-Ethyl-N-Phenyl-Isothiourea |
DrugCentrali | P29475 |
GuidetoPHARMACOLOGYi | 1251 |
Genetic variation databases
BioMutai | NOS1 |
DMDMi | 1709333 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000170921 | 1 – 1434 | Nitric oxide synthase, brainAdd BLAST | 1434 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 852 | PhosphoserineBy similarity | 1 | |
Modified residuei | 862 | PhosphoserineBy similarity | 1 | |
Modified residuei | 863 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Phosphoprotein, Ubl conjugationProteomic databases
jPOSTi | P29475 |
MassIVEi | P29475 |
MaxQBi | P29475 |
PaxDbi | P29475 |
PeptideAtlasi | P29475 |
PRIDEi | P29475 |
ProteomicsDBi | 20446 50171 54578 [P29475-1] 54579 [P29475-2] 54580 [P29475-3] 54581 [P29475-4] |
PTM databases
iPTMneti | P29475 |
PhosphoSitePlusi | P29475 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000089250, Expressed in vastus lateralis and 134 other tissues |
ExpressionAtlasi | P29475, baseline and differential |
Genevisiblei | P29475, HS |
Organism-specific databases
HPAi | ENSG00000089250, Group enriched (brain, skeletal muscle) |
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 similarityBinary interactionsi
P29475
With | #Exp. | IntAct |
---|---|---|
VAC14 [Q08AM6] | 5 | EBI-7164065,EBI-2107455 |
GO - Molecular functioni
- calcium-dependent protein binding Source: ARUK-UCL
- calmodulin binding Source: UniProtKB-KW
- ion channel binding Source: BHF-UCL
- scaffold protein binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 110905, 18 interactors |
CORUMi | P29475 |
DIPi | DIP-40999N |
IntActi | P29475, 5 interactors |
MINTi | P29475 |
STRINGi | 9606.ENSP00000477999 |
Chemistry databases
BindingDBi | P29475 |
Miscellaneous databases
RNActi | P29475, protein |
Structurei
Secondary structure
3D structure databases
BMRBi | P29475 |
SMRi | P29475 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 17 – 99 | PDZPROSITE-ProRule annotationAdd BLAST | 83 | |
Domaini | 760 – 940 | Flavodoxin-likePROSITE-ProRule annotationAdd BLAST | 181 | |
Domaini | 995 – 1242 | FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST | 248 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 205 | Interaction with NOSIPBy similarityAdd BLAST | 205 | |
Regioni | 163 – 245 | PIN (nNOS-inhibiting protein) bindingAdd BLAST | 83 | |
Regioni | 730 – 750 | Calmodulin-bindingSequence analysisAdd BLAST | 21 | |
Regioni | 755 – 774 | Tetrahydrobiopterin-bindingBy similarityAdd BLAST | 20 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG1158, Eukaryota |
GeneTreei | ENSGT00940000159357 |
HOGENOMi | CLU_001570_16_0_1 |
InParanoidi | P29475 |
OMAi | ERGHFYV |
PhylomeDBi | P29475 |
TreeFami | TF324410 |
Family and domain databases
Gene3Di | 1.20.990.10, 1 hit 2.30.42.10, 1 hit 3.40.50.360, 1 hit 3.40.50.80, 1 hit |
InterProi | View protein in InterPro IPR003097, CysJ-like_FAD-binding IPR017927, FAD-bd_FR_type IPR001094, Flavdoxin-like IPR008254, Flavodoxin/NO_synth IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase IPR029039, Flavoprotein-like_sf IPR039261, FNR_nucleotide-bd IPR023173, NADPH_Cyt_P450_Rdtase_alpha IPR012144, NOS_euk IPR004030, NOS_N IPR036119, NOS_N_sf IPR001433, OxRdtase_FAD/NAD-bd IPR001478, PDZ IPR036034, PDZ_sf IPR017938, Riboflavin_synthase-like_b-brl |
Pfami | View protein in Pfam 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 |
PIRSFi | PIRSF000333, NOS, 1 hit |
PRINTSi | PR00369, FLAVODOXIN PR00371, FPNCR |
SMARTi | View protein in SMART SM00228, PDZ, 1 hit |
SUPFAMi | SSF50156, SSF50156, 1 hit SSF52218, SSF52218, 1 hit SSF52343, SSF52343, 1 hit SSF56512, SSF56512, 1 hit SSF63380, SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS51384, FAD_FR, 1 hit PS50902, FLAVODOXIN_LIKE, 1 hit PS60001, NOS, 1 hit PS50106, PDZ, 1 hit |
s (5+)i Sequence
Sequence statusi: Complete.
This entry describes 5 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 5 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketC9J5P6 | C9J5P6_HUMAN | Nitric oxide synthase | NOS1 | 1,433 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 131 | K → E in AAB49040 (PubMed:8879752).Curated | 1 | |
Sequence conflicti | 178 – 184 | LAPRPPG → WPQAPR (PubMed:7678401).Curated | 7 | |
Sequence conflicti | 178 – 184 | LAPRPPG → WPQAPR (PubMed:8879752).Curated | 7 | |
Sequence conflicti | 492 – 493 | QP → HR in AAA36376 (PubMed:7678401).Curated | 2 | |
Sequence conflicti | 549 | V → L in AAA36376 (PubMed:7678401).Curated | 1 | |
Sequence conflicti | 563 | G → A in AAA36376 (PubMed:7678401).Curated | 1 | |
Sequence conflicti | 1407 | Y → I in AAA36376 (PubMed:7678401).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_018948 | 228 | P → S1 PublicationCorresponds to variant dbSNP:rs9658279Ensembl. | 1 | |
Natural variantiVAR_018949 | 394 | D → A1 PublicationCorresponds to variant dbSNP:rs9658356EnsemblClinVar. | 1 | |
Natural variantiVAR_018950 | 725 | N → D1 PublicationCorresponds to variant dbSNP:rs9658403EnsemblClinVar. | 1 | |
Natural variantiVAR_018951 | 864 | G → D1 PublicationCorresponds to variant dbSNP:rs9658445EnsemblClinVar. | 1 | |
Natural variantiVAR_018952 | 1064 | Q → R1 PublicationCorresponds to variant dbSNP:rs9658482Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_003571 | 1 – 336 | Missing in isoform 3. CuratedAdd BLAST | 336 | |
Alternative sequenceiVSP_003572 | 285 – 407 | PPTSG…DTELI → MRKLRITEGFGVQRGSHNHP PPQENSPPQRMAAPPSVHAS SRSRTGRLRWFSLTPSTLRA HWKRDALSTSAWAPSCILLS MQGGLKTSAQKDSSSLSPKS LLINTIHQLKDLAPKPTWKG WKR in isoform 4. CuratedAdd BLAST | 123 | |
Alternative sequenceiVSP_003573 | 408 – 1434 | Missing in isoform 4. CuratedAdd BLAST | 1027 | |
Alternative sequenceiVSP_003574 | 509 – 613 | Missing in isoform 2. 2 PublicationsAdd BLAST | 105 | |
Alternative sequenceiVSP_044916 | 844 | K → KYPEPLRFFPRKGPPLPNGD TEVHGLAAARDSQHR in isoform 5. 1 Publication | 1 |
Sequence databases
Genome annotation databases
Ensembli | ENST00000317775; ENSP00000320758; ENSG00000089250 [P29475-1] ENST00000338101; ENSP00000337459; ENSG00000089250 [P29475-5] ENST00000618760; ENSP00000477999; ENSG00000089250 [P29475-5] |
GeneIDi | 4842 |
KEGGi | hsa:4842 |
UCSCi | uc001twm.3, human [P29475-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
NIEHS-SNPs |
Wikipedia Nitric oxide synthase entry |
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4D1N | X-ray | 2.03 | A/B/C/D | 302-721 | [»] | |
4UCH | X-ray | 2.20 | A/B | 302-723 | [»] | |
4UH5 | X-ray | 1.98 | A/B | 302-722 | [»] | |
4UH6 | X-ray | 1.98 | A/B | 302-722 | [»] | |
4V3U | X-ray | 2.30 | A/B/C/D | 302-721 | [»] | |
5ADF | X-ray | 1.97 | A/B | 302-722 | [»] | |
5ADG | X-ray | 1.98 | A/B | 302-722 | [»] | |
5ADI | X-ray | 2.20 | A/B | 302-722 | [»] | |
5FVU | X-ray | 2.22 | A/B | 302-722 | [»] | |
5FVV | X-ray | 2.05 | A/B | 302-722 | [»] | |
5FVW | X-ray | 2.20 | A/B | 302-722 | [»] | |
5FVX | X-ray | 2.30 | A/B | 302-722 | [»] | |
5UO1 | X-ray | 1.90 | A/B | 302-722 | [»] | |
5UO2 | X-ray | 1.95 | A/B | 302-722 | [»] | |
5UO3 | X-ray | 2.20 | A/B | 302-722 | [»] | |
5UO4 | X-ray | 2.00 | A/B | 302-722 | [»] | |
5UO5 | X-ray | 2.00 | A/B | 302-722 | [»] | |
5UO6 | X-ray | 1.96 | A/B | 302-722 | [»] | |
5UO7 | X-ray | 2.06 | A/B | 302-722 | [»] | |
5VUV | X-ray | 1.98 | A/B | 302-722 | [»] | |
5VUW | X-ray | 2.03 | A/B | 302-722 | [»] | |
5VUX | X-ray | 2.30 | A/B | 302-722 | [»] | |
5VUY | X-ray | 2.15 | A/B | 302-722 | [»] | |
5VUZ | X-ray | 1.97 | A/B | 302-722 | [»] | |
5VV0 | X-ray | 1.80 | A/B | 302-722 | [»] | |
5VV1 | X-ray | 1.95 | A/B | 302-722 | [»] | |
5VV2 | X-ray | 2.00 | A/B | 302-722 | [»] | |
5VV3 | X-ray | 2.18 | A/B | 302-722 | [»] | |
5VV4 | X-ray | 2.10 | A/B | 302-722 | [»] | |
5VV5 | X-ray | 2.15 | A/B | 302-722 | [»] | |
6AUY | X-ray | 1.92 | A/B | 302-722 | [»] | |
6AUZ | X-ray | 2.00 | A/B | 302-722 | [»] | |
6AV0 | X-ray | 2.00 | A/B | 302-722 | [»] | |
6AV1 | X-ray | 2.45 | A/B | 302-722 | [»] | |
6AV2 | X-ray | 2.10 | A/B | 302-722 | [»] | |
6AV3 | X-ray | 1.95 | A/B | 302-722 | [»] | |
6AV4 | X-ray | 1.87 | A/B | 302-722 | [»] | |
6AV5 | X-ray | 1.90 | A/B | 302-722 | [»] | |
6CIC | X-ray | 1.75 | A/B | 302-722 | [»] | |
6CID | X-ray | 1.75 | A/B | 302-722 | [»] | |
6NG1 | X-ray | 2.15 | A/B | 302-722 | [»] | |
6NG2 | X-ray | 1.93 | A/B | 302-722 | [»] | |
6NG4 | X-ray | 1.78 | A/B | 302-722 | [»] | |
6NG5 | X-ray | 1.96 | A/B | 302-722 | [»] | |
6NG6 | X-ray | 2.04 | A/B | 302-722 | [»] | |
6NG7 | X-ray | 2.00 | A/B | 302-722 | [»] | |
6NG8 | X-ray | 1.90 | A/B | 302-722 | [»] | |
6NGA | X-ray | 1.98 | A/B | 302-722 | [»] | |
6NGB | X-ray | 1.90 | A/B | 302-722 | [»] | |
6NGC | X-ray | 2.00 | A/B | 302-722 | [»] | |
6NGD | X-ray | 1.80 | A/B | 302-722 | [»] | |
6NGE | X-ray | 2.10 | A/B | 302-722 | [»] | |
6NGF | X-ray | 1.99 | A/B | 302-722 | [»] | |
6NGH | X-ray | 2.00 | A/B | 302-722 | [»] | |
6NGI | X-ray | 1.80 | A/B | 302-722 | [»] | |
6NHB | X-ray | 2.03 | A/B | 302-722 | [»] | |
6NHC | X-ray | 2.16 | A/B | 302-722 | [»] | |
6PNA | X-ray | 1.95 | A/B | 302-722 | [»] | |
6PNB | X-ray | 2.05 | A/B | 302-722 | [»] | |
6PNC | X-ray | 2.15 | A/B | 302-722 | [»] | |
6PND | X-ray | 2.40 | A/B | 302-722 | [»] | |
6PNE | X-ray | 2.10 | A/B | 302-722 | [»] | |
6PNF | X-ray | 2.10 | A/B | 302-722 | [»] | |
6PNG | X-ray | 1.77 | A/B | 302-722 | [»] | |
6PNH | X-ray | 1.85 | A/B | 302-722 | [»] | |
6PO5 | X-ray | 1.82 | A/B | 302-722 | [»] | |
6PO7 | X-ray | 1.95 | A/B | 302-722 | [»] | |
6PO8 | X-ray | 1.90 | A/B | 302-722 | [»] | |
6PO9 | X-ray | 1.81 | A/B | 302-722 | [»] | |
6POA | X-ray | 1.81 | A/B | 302-722 | [»] | |
6POB | X-ray | 1.95 | A/B | 302-722 | [»] | |
6POC | X-ray | 2.00 | A/B | 302-722 | [»] | |
6POT | X-ray | 2.30 | A/B | 302-722 | [»] | |
BMRBi | P29475 | |||||
SMRi | P29475 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 110905, 18 interactors |
CORUMi | P29475 |
DIPi | DIP-40999N |
IntActi | P29475, 5 interactors |
MINTi | P29475 |
STRINGi | 9606.ENSP00000477999 |
Chemistry databases
BindingDBi | P29475 |
ChEMBLi | CHEMBL3568 |
DrugBanki | DB02143, 1-hydroxy-2-isopropylguanidine DB02727, 2-butyl-1-hydroxyguanidine DB01997, 3-Bromo-7-Nitroindazole DB03892, 5-N-Allyl-arginine DB03710, [(1S)-4-(1-Aminobutylideneamino)-1-carboxybutyl]azanium DB00155, Citrulline DB00843, Donepezil DB00997, Doxorubicin DB03147, Flavin adenine dinucleotide DB03247, Flavin mononucleotide DB01942, Formic acid DB01221, Ketamine DB02077, L-N(omega)-nitroarginine-(4R)-amino-L-proline amide DB01821, L-N(omega)-Nitroarginine-2,4-L-diaminobutyric amide DB09241, Methylene blue DB03144, N(5)-[(hydroxyamino)(imino)methyl]-L-ornithine DB03449, N-(4-{2-[(3-chlorobenzyl)amino]ethyl}phenyl)thiophene-2-carboximidamide DB02044, N-[3-(aminomethyl)benzyl]acetamidine DB02644, N-omega-propyl-L-arginine DB08019, N-{(3R,4S)-4-[(6-amino-4-methylpyridin-2-yl)methyl]pyrrolidin-3-yl}-N'-(3-chlorobenzyl)ethane-1,2-diamine DB08018, N-{(3S,4S)-4-[(6-AMINO-4-METHYLPYRIDIN-2-YL)METHYL]PYRROLIDIN-3-YL}-N'-(4-CHLOROBENZYL)ETHANE-1,2-DIAMINE DB02027, N-{(4S)-4-Amino-5-[(2-aminoethyl)amino]pentyl}-N'-nitroguanidine DB03461, Nicotinamide adenine dinucleotide phosphate DB04223, Nitroarginine DB06096, NXN-188 DB02991, S-Ethyl-N-[4-(Trifluoromethyl)Phenyl]Isothiourea DB03707, S-Ethyl-N-Phenyl-Isothiourea |
DrugCentrali | P29475 |
GuidetoPHARMACOLOGYi | 1251 |
PTM databases
iPTMneti | P29475 |
PhosphoSitePlusi | P29475 |
Genetic variation databases
BioMutai | NOS1 |
DMDMi | 1709333 |
Proteomic databases
jPOSTi | P29475 |
MassIVEi | P29475 |
MaxQBi | P29475 |
PaxDbi | P29475 |
PeptideAtlasi | P29475 |
PRIDEi | P29475 |
ProteomicsDBi | 20446 50171 54578 [P29475-1] 54579 [P29475-2] 54580 [P29475-3] 54581 [P29475-4] |
Protocols and materials databases
ABCDi | P29475, 2 sequenced antibodies |
Antibodypediai | 3691, 908 antibodies |
DNASUi | 4842 |
Genome annotation databases
Ensembli | ENST00000317775; ENSP00000320758; ENSG00000089250 [P29475-1] ENST00000338101; ENSP00000337459; ENSG00000089250 [P29475-5] ENST00000618760; ENSP00000477999; ENSG00000089250 [P29475-5] |
GeneIDi | 4842 |
KEGGi | hsa:4842 |
UCSCi | uc001twm.3, human [P29475-1] |
Organism-specific databases
CTDi | 4842 |
DisGeNETi | 4842 |
GeneCardsi | NOS1 |
HGNCi | HGNC:7872, NOS1 |
HPAi | ENSG00000089250, Group enriched (brain, skeletal muscle) |
MalaCardsi | NOS1 |
MIMi | 163731, gene |
neXtProti | NX_P29475 |
OpenTargetsi | ENSG00000089250 |
Orphaneti | 930, Idiopathic achalasia |
PharmGKBi | PA252 |
VEuPathDBi | HostDB:ENSG00000089250.18 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1158, Eukaryota |
GeneTreei | ENSGT00940000159357 |
HOGENOMi | CLU_001570_16_0_1 |
InParanoidi | P29475 |
OMAi | ERGHFYV |
PhylomeDBi | P29475 |
TreeFami | TF324410 |
Enzyme and pathway databases
BioCyci | MetaCyc:HS01647-MONOMER |
BRENDAi | 1.14.13.39, 2681 |
PathwayCommonsi | P29475 |
Reactomei | R-HSA-1222556, ROS and RNS production in phagocytes R-HSA-392154, Nitric oxide stimulates guanylate cyclase R-HSA-5578775, Ion homeostasis |
SIGNORi | P29475 |
Miscellaneous databases
BioGRID-ORCSi | 4842, 4 hits in 875 CRISPR screens |
ChiTaRSi | NOS1, human |
GeneWikii | NOS1 |
GenomeRNAii | 4842 |
Pharosi | P29475, Tchem |
PROi | PR:P29475 |
RNActi | P29475, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000089250, Expressed in vastus lateralis and 134 other tissues |
ExpressionAtlasi | P29475, baseline and differential |
Genevisiblei | P29475, HS |
Family and domain databases
Gene3Di | 1.20.990.10, 1 hit 2.30.42.10, 1 hit 3.40.50.360, 1 hit 3.40.50.80, 1 hit |
InterProi | View protein in InterPro IPR003097, CysJ-like_FAD-binding IPR017927, FAD-bd_FR_type IPR001094, Flavdoxin-like IPR008254, Flavodoxin/NO_synth IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase IPR029039, Flavoprotein-like_sf IPR039261, FNR_nucleotide-bd IPR023173, NADPH_Cyt_P450_Rdtase_alpha IPR012144, NOS_euk IPR004030, NOS_N IPR036119, NOS_N_sf IPR001433, OxRdtase_FAD/NAD-bd IPR001478, PDZ IPR036034, PDZ_sf IPR017938, Riboflavin_synthase-like_b-brl |
Pfami | View protein in Pfam 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 |
PIRSFi | PIRSF000333, NOS, 1 hit |
PRINTSi | PR00369, FLAVODOXIN PR00371, FPNCR |
SMARTi | View protein in SMART SM00228, PDZ, 1 hit |
SUPFAMi | SSF50156, SSF50156, 1 hit SSF52218, SSF52218, 1 hit SSF52343, SSF52343, 1 hit SSF56512, SSF56512, 1 hit SSF63380, SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS51384, FAD_FR, 1 hit PS50902, FLAVODOXIN_LIKE, 1 hit PS60001, NOS, 1 hit PS50106, PDZ, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NOS1_HUMAN | |
Accessioni | P29475Primary (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: | February 10, 2021 | |
This is version 227 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families