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Protein

Nitric oxide synthase, endothelial

Gene

NOS3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.
Isoform eNOS13C: Lacks eNOS activity, dominant-negative form that may down-regulate eNOS activity by forming heterodimers with isoform 1.

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 NOSIP and NOSTRIN.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi94Zinc1
Metal bindingi99Zinc1
Metal bindingi184Iron (heme axial ligand)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi649 – 680FMNPROSITE-ProRule annotationAdd BLAST32
Nucleotide bindingi793 – 804FADBy similarityAdd BLAST12
Nucleotide bindingi935 – 945FADBy similarityAdd BLAST11
Nucleotide bindingi1010 – 1028NADPBy similarityAdd BLAST19
Nucleotide bindingi1108 – 1123NADPBy similarityAdd BLAST16

GO - Molecular functioni

  • actin monomer binding Source: BHF-UCL
  • arginine binding Source: BHF-UCL
  • cadmium ion binding Source: BHF-UCL
  • calmodulin binding Source: UniProtKB-KW
  • flavin adenine dinucleotide binding Source: BHF-UCL
  • FMN binding Source: BHF-UCL
  • heme binding Source: BHF-UCL
  • NADP binding Source: BHF-UCL
  • NADPH-hemoprotein reductase activity Source: GO_Central
  • nitric-oxide synthase activity Source: BHF-UCL
  • scaffold protein binding Source: Ensembl
  • tetrahydrobiopterin binding Source: BHF-UCL

GO - Biological processi

Keywordsi

Molecular functionCalmodulin-binding, Oxidoreductase
LigandCalcium, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS09149-MONOMER
BRENDAi1.14.13.39 2681
ReactomeiR-HSA-1222556 ROS, RNS production in phagocytes
R-HSA-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-HSA-203615 eNOS activation
R-HSA-203641 NOSTRIN mediated eNOS trafficking
R-HSA-203754 NOSIP mediated eNOS trafficking
R-HSA-392154 Nitric oxide stimulates guanylate cyclase
R-HSA-5218920 VEGFR2 mediated vascular permeability
SignaLinkiP29474
SIGNORiP29474

Names & Taxonomyi

Protein namesi
Recommended name:
Nitric oxide synthase, endothelial (EC:1.14.13.39)
Alternative name(s):
Constitutive NOS
Short name:
cNOS
EC-NOS
Endothelial NOS
Short name:
eNOS
NOS type III
Short name:
NOSIII
Gene namesi
Name:NOS3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000164867.10
HGNCiHGNC:7876 NOS3
MIMi163729 gene+phenotype
neXtProtiNX_P29474

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Variation Asp-298 in NOS3 may be associated with susceptibility to coronary spasm.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi114S → A: Reduced nitrite (NO) production. 1 Publication1

Organism-specific databases

DisGeNETi4846
MalaCardsiNOS3
MIMi163729 gene+phenotype
OpenTargetsiENSG00000164867
PharmGKBiPA254

Chemistry databases

ChEMBLiCHEMBL4803
DrugBankiDB02335 2-Aminothiazoline
DB01997 3-Bromo-7-Nitroindazole
DB04534 5-Nitroindazole
DB03100 6-Nitroindazole
DB02207 7-Nitroindazole
DB03065 7-Nitroindazole-2-Carboxamidine
DB05676 Apremilast
DB00997 Doxorubicin
DB07388 ETHYL 4-[(4-METHYLPYRIDIN-2-YL)AMINO]PIPERIDINE-1-CARBOXYLATE
DB02234 Ethylisothiourea
DB02994 Hydroxydimethylarsine Oxide
DB01833 L-2-Amino-4-(Guanidinooxy)Butyric Acid
DB00125 L-Arginine
DB00155 L-Citrulline
DB03974 L-Homoarginine
DB02077 L-N(Omega)-Nitroarginine-(4r)-Amino-L-Proline Amide
DB01110 Miconazole
DB02044 N-(3-(Aminomethyl)Benzyl)Acetamidine
DB04559 N-(Chlorophenyl)-N'-Hydroxyguanidine
DB03144 N-Omega-Hydroxy-L-Arginine
DB02027 N-{(4s)-4-Amino-5-[(2-Aminoethyl)Amino]Pentyl}-N'-Nitroguanidine
DB03305 N5-Iminoethyl-L-Ornithine
DB04223 Nitroarginine
DB03963 S-(Dimethylarsenic)Cysteine
DB03707 S-Ethyl-N-Phenyl-Isothiourea
DB04018 S-Isopropyl-Isothiourea
DB00360 Sapropterin
DB02589 Se-Ethyl-Isoselenourea
GuidetoPHARMACOLOGYi1249

Polymorphism and mutation databases

BioMutaiNOS3
DMDMi266648

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001709432 – 1203Nitric oxide synthase, endothelialAdd BLAST1202

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Lipidationi15S-palmitoyl cysteineBy similarity1
Lipidationi26S-palmitoyl cysteineBy similarity1
Modified residuei33PhosphothreonineCombined sources1
Modified residuei114Phosphoserine; by CDK51 Publication1
Modified residuei495Phosphothreonine; by AMPK1 Publication1
Modified residuei615PhosphoserineBy similarity1
Modified residuei633PhosphoserineCombined sources1
Modified residuei638PhosphoserineCombined sources1
Modified residuei836PhosphoserineCombined sources1
Modified residuei1175PhosphothreonineBy similarity1
Modified residuei1177Phosphoserine; by AMPKCombined sources1 Publication1
Modified residuei1179PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation by AMPK at Ser-1177 in the presence of Ca2+-calmodulin (CaM) activates activity. In absence of Ca2+-calmodulin, AMPK also phosphorylates Thr-495, resulting in inhibition of activity (By similarity). Phosphorylation of Ser-114 by CDK5 reduces activity.By similarity2 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

EPDiP29474
PaxDbiP29474
PeptideAtlasiP29474
PRIDEiP29474
ProteomicsDBi54576
54577 [P29474-2]

PTM databases

iPTMnetiP29474
PhosphoSitePlusiP29474
SwissPalmiP29474

Expressioni

Tissue specificityi

Platelets, placenta, liver and kidney.1 Publication

Gene expression databases

BgeeiENSG00000164867
CleanExiHS_NOS3
ExpressionAtlasiP29474 baseline and differential
GenevisibleiP29474 HS

Organism-specific databases

HPAiCAB002168

Interactioni

Subunit structurei

Homodimer. Interacts with NOSIP and NOSTRIN. Interacts with HSP90AB1 (PubMed:23585225).3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin monomer binding Source: BHF-UCL
  • calmodulin binding Source: UniProtKB-KW
  • scaffold protein binding Source: Ensembl

Protein-protein interaction databases

BioGridi110909, 46 interactors
CORUMiP29474
DIPiDIP-38479N
IntActiP29474, 39 interactors
MINTiP29474
STRINGi9606.ENSP00000297494

Chemistry databases

BindingDBiP29474

Structurei

Secondary structure

11203
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi70 – 73Combined sources4
Turni74 – 76Combined sources3
Beta strandi79 – 81Combined sources3
Helixi84 – 87Combined sources4
Beta strandi88 – 90Combined sources3
Beta strandi104 – 107Combined sources4
Helixi120 – 137Combined sources18
Helixi144 – 160Combined sources17
Helixi167 – 179Combined sources13
Helixi187 – 189Combined sources3
Beta strandi194 – 197Combined sources4
Helixi204 – 219Combined sources16
Helixi220 – 222Combined sources3
Beta strandi227 – 230Combined sources4
Beta strandi236 – 238Combined sources3
Beta strandi245 – 249Combined sources5
Beta strandi253 – 255Combined sources3
Beta strandi257 – 259Combined sources3
Beta strandi261 – 263Combined sources3
Helixi265 – 267Combined sources3
Helixi268 – 276Combined sources9
Beta strandi284 – 286Combined sources3
Beta strandi291 – 294Combined sources4
Beta strandi296 – 298Combined sources3
Beta strandi301 – 303Combined sources3
Helixi307 – 309Combined sources3
Beta strandi312 – 314Combined sources3
Helixi323 – 326Combined sources4
Beta strandi329 – 332Combined sources4
Beta strandi340 – 343Combined sources4
Beta strandi346 – 349Combined sources4
Helixi359 – 363Combined sources5
Helixi365 – 368Combined sources4
Turni370 – 373Combined sources4
Helixi376 – 382Combined sources7
Helixi390 – 392Combined sources3
Helixi394 – 412Combined sources19
Helixi420 – 438Combined sources19
Helixi445 – 448Combined sources4
Beta strandi451 – 453Combined sources3
Helixi454 – 456Combined sources3
Helixi458 – 461Combined sources4
Beta strandi465 – 467Combined sources3
Beta strandi470 – 474Combined sources5
Helixi496 – 506Combined sources11
Helixi507 – 509Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M9JX-ray2.43A/B67-481[»]
1M9KX-ray2.01A/B67-481[»]
1M9MX-ray1.96A/B67-481[»]
1M9QX-ray2.01A/B67-481[»]
1M9RX-ray2.56A/B67-481[»]
1NIWX-ray2.05B/D/F/H492-511[»]
2LL7NMR-B493-509[»]
2MG5NMR-B495-510[»]
2N8JNMR-B491-512[»]
3EAHX-ray2.44A/B66-492[»]
3NOSX-ray2.40A/B66-492[»]
4D1OX-ray1.82A/B41-480[»]
4D1PX-ray1.73A/B41-480[»]
5UO8X-ray2.18A/B/C/D41-480[»]
5UO9X-ray2.19A/B/C/D41-480[»]
5UOAX-ray2.20A/B41-480[»]
5UOBX-ray2.29A/B/C/D41-480[»]
5UOCX-ray2.20A/B/C/D41-480[»]
5VVBX-ray2.15A/B/C/D41-480[»]
5VVCX-ray2.40A/B/C/D41-480[»]
5VVDX-ray2.25A/B/C/D41-480[»]
5XOFX-ray1.96O/P/Q/R30-36[»]
ProteinModelPortaliP29474
SMRiP29474
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29474

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini520 – 703Flavodoxin-likePROSITE-ProRule annotationAdd BLAST184
Domaini756 – 1002FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST247

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 486Interaction with NOSIP1 PublicationAdd BLAST389
Regioni491 – 510Calmodulin-bindingSequence analysisAdd BLAST20

Sequence similaritiesi

Belongs to the NOS family.Curated

Phylogenomic databases

eggNOGiKOG1158 Eukaryota
COG0369 LUCA
COG4362 LUCA
GeneTreeiENSGT00840000129757
HOGENOMiHOG000111088
HOVERGENiHBG000159
InParanoidiP29474
KOiK13242
OrthoDBiEOG091G10Z0
PhylomeDBiP29474
TreeFamiTF324410

Family and domain databases

Gene3Di1.20.990.10, 1 hit
3.40.50.360, 1 hit
InterProiView protein in InterPro
IPR003097 FAD-binding_1
IPR017927 Fd_Rdtase_FAD-bd
IPR001094 Flavdoxin-like
IPR008254 Flavodoxin/NO_synth
IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase
IPR029039 Flavoprotein-like_sf
IPR023173 NADPH_Cyt_P450_Rdtase_alpha
IPR012144 NOS_euk
IPR004030 NOS_N
IPR036119 NOS_N_sf
IPR001433 OxRdtase_FAD/NAD-bd
IPR017938 Riboflavin_synthase-like_b-brl
PfamiView 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
PIRSFiPIRSF000333 NOS, 1 hit
PRINTSiPR00369 FLAVODOXIN
PR00371 FPNCR
SUPFAMiSSF52218 SSF52218, 1 hit
SSF56512 SSF56512, 1 hit
SSF63380 SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS51384 FAD_FR, 1 hit
PS50902 FLAVODOXIN_LIKE, 1 hit
PS60001 NOS, 1 hit

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P29474-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGNLKSVAQE PGPPCGLGLG LGLGLCGKQG PATPAPEPSR APASLLPPAP
60 70 80 90 100
EHSPPSSPLT QPPEGPKFPR VKNWEVGSIT YDTLSAQAQQ DGPCTPRRCL
110 120 130 140 150
GSLVFPRKLQ GRPSPGPPAP EQLLSQARDF INQYYSSIKR SGSQAHEQRL
160 170 180 190 200
QEVEAEVAAT GTYQLRESEL VFGAKQAWRN APRCVGRIQW GKLQVFDARD
210 220 230 240 250
CRSAQEMFTY ICNHIKYATN RGNLRSAITV FPQRCPGRGD FRIWNSQLVR
260 270 280 290 300
YAGYRQQDGS VRGDPANVEI TELCIQHGWT PGNGRFDVLP LLLQAPDDPP
310 320 330 340 350
ELFLLPPELV LEVPLEHPTL EWFAALGLRW YALPAVSNML LEIGGLEFPA
360 370 380 390 400
APFSGWYMST EIGTRNLCDP HRYNILEDVA VCMDLDTRTT SSLWKDKAAV
410 420 430 440 450
EINVAVLHSY QLAKVTIVDH HAATASFMKH LENEQKARGG CPADWAWIVP
460 470 480 490 500
PISGSLTPVF HQEMVNYFLS PAFRYQPDPW KGSAAKGTGI TRKKTFKEVA
510 520 530 540 550
NAVKISASLM GTVMAKRVKA TILYGSETGR AQSYAQQLGR LFRKAFDPRV
560 570 580 590 600
LCMDEYDVVS LEHETLVLVV TSTFGNGDPP ENGESFAAAL MEMSGPYNSS
610 620 630 640 650
PRPEQHKSYK IRFNSISCSD PLVSSWRRKR KESSNTDSAG ALGTLRFCVF
660 670 680 690 700
GLGSRAYPHF CAFARAVDTR LEELGGERLL QLGQGDELCG QEEAFRGWAQ
710 720 730 740 750
AAFQAACETF CVGEDAKAAA RDIFSPKRSW KRQRYRLSAQ AEGLQLLPGL
760 770 780 790 800
IHVHRRKMFQ ATIRSVENLQ SSKSTRATIL VRLDTGGQEG LQYQPGDHIG
810 820 830 840 850
VCPPNRPGLV EALLSRVEDP PAPTEPVAVE QLEKGSPGGP PPGWVRDPRL
860 870 880 890 900
PPCTLRQALT FFLDITSPPS PQLLRLLSTL AEEPREQQEL EALSQDPRRY
910 920 930 940 950
EEWKWFRCPT LLEVLEQFPS VALPAPLLLT QLPLLQPRYY SVSSAPSTHP
960 970 980 990 1000
GEIHLTVAVL AYRTQDGLGP LHYGVCSTWL SQLKPGDPVP CFIRGAPSFR
1010 1020 1030 1040 1050
LPPDPSLPCI LVGPGTGIAP FRGFWQERLH DIESKGLQPT PMTLVFGCRC
1060 1070 1080 1090 1100
SQLDHLYRDE VQNAQQRGVF GRVLTAFSRE PDNPKTYVQD ILRTELAAEV
1110 1120 1130 1140 1150
HRVLCLERGH MFVCGDVTMA TNVLQTVQRI LATEGDMELD EAGDVIGVLR
1160 1170 1180 1190 1200
DQQRYHEDIF GLTLRTQEVT SRIRTQSFSL QERQLRGAVP WAFDPPGSDT

NSP
Length:1,203
Mass (Da):133,275
Last modified:March 28, 2018 - v4
Checksum:iB761A6D40B1A5649
GO
Isoform eNOS13C (identifier: P29474-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     584-625: ESFAAALMEM...ISCSDPLVSS → EGLTLWPRLE...VGTTGACHDA
     626-1203: Missing.

Note: Lacks eNOS activity.
Show »
Length:629
Mass (Da):68,965
Checksum:iA40D0DFCEB1774E3
GO
Isoform eNOS13B (identifier: P29474-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     585-614: SFAAALMEMSGPYNSSPRPEQHKSYKIRFN → RWGFAMLPRLVSNSWVQAIHLPRPPKVLRL
     615-1203: Missing.

Show »
Length:614
Mass (Da):67,862
Checksum:iCE895E896E61722E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53S → R in AAA36373 (PubMed:7514568).Curated1
Sequence conflicti168S → G in BAG37648 (PubMed:14702039).Curated1
Sequence conflicti414K → R in BAF85617 (PubMed:14702039).Curated1
Sequence conflicti489G → S in AAD14336 (PubMed:7475956).Curated1
Sequence conflicti567V → W in CAA53950 (PubMed:7509596).Curated1
Sequence conflicti1150R → RQ in BAA05652 (PubMed:7519987).Curated1
Sequence conflicti1194D → E in CAA53950 (PubMed:7509596).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031218112R → Q1 PublicationCorresponds to variant dbSNP:rs3918166Ensembl.1
Natural variantiVAR_008037298D → E16 PublicationsCorresponds to variant dbSNP:rs1799983EnsemblClinVar.1
Natural variantiVAR_036303474R → C Found in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs145805216Ensembl.1
Natural variantiVAR_036304602R → Q Found in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs145168353Ensembl.1
Natural variantiVAR_061377665R → H. Corresponds to variant dbSNP:rs7792133Ensembl.1
Natural variantiVAR_031219827V → M1 PublicationCorresponds to variant dbSNP:rs3918232Ensembl.1
Natural variantiVAR_031220885R → M1 PublicationCorresponds to variant dbSNP:rs3918201Ensembl.1
Natural variantiVAR_031221982Q → L1 PublicationCorresponds to variant dbSNP:rs3918234Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_042625584 – 625ESFAA…PLVSS → EGLTLWPRLECSSTITAHCS LNLLDSSNPPTSTSQVVGTT GACHDA in isoform eNOS13C. 1 PublicationAdd BLAST42
Alternative sequenceiVSP_045495585 – 614SFAAA…KIRFN → RWGFAMLPRLVSNSWVQAIH LPRPPKVLRL in isoform eNOS13B. 1 PublicationAdd BLAST30
Alternative sequenceiVSP_045496615 – 1203Missing in isoform eNOS13B. 1 PublicationAdd BLAST589
Alternative sequenceiVSP_042626626 – 1203Missing in isoform eNOS13C. 1 PublicationAdd BLAST578

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93718 mRNA Translation: AAA36364.1
M95296 mRNA Translation: AAA36372.1
L10709
, L10693, L10694, L10695, L10696, L10697, L10698, L10699, L10700, L10701, L10702, L10703, L10704, L10705, L10706, L10707, L10708 Genomic DNA Translation: AAA36365.1
X76303
, X76304, X76305, X76306, X76307, X76308, X76309, X76310, X76311, X76312, X76313, X76314, X76315, X76316 Genomic DNA Translation: CAA53950.1
D26607 Genomic DNA Translation: BAA05652.1
DQ256130 mRNA Translation: ABB79839.1
DQ256131 mRNA Translation: ABB79840.1
L26914 Genomic DNA Translation: AAA36374.1
AF400594 mRNA Translation: AAK83389.1
AK292928 mRNA Translation: BAF85617.1
AK315213 mRNA Translation: BAG37648.1
AK223636 mRNA Translation: BAD97356.1
AF519768 Genomic DNA Translation: AAM74944.1
EU332855 Genomic DNA Translation: ABY87544.1
AC010973 Genomic DNA No translation available.
CH471173 Genomic DNA Translation: EAW54069.1
BC063294 mRNA Translation: AAH63294.1
BC069465 mRNA Translation: AAH69465.1
L23210 Genomic DNA Translation: AAA36373.1
S80791 mRNA Translation: AAD14336.1
CCDSiCCDS55182.1 [P29474-2]
CCDS55183.1 [P29474-3]
CCDS5912.1 [P29474-1]
PIRiA47501
RefSeqiNP_000594.2, NM_000603.4 [P29474-1]
NP_001153581.1, NM_001160109.1
NP_001153582.1, NM_001160110.1 [P29474-3]
NP_001153583.1, NM_001160111.1 [P29474-2]
XP_016867721.1, XM_017012232.1 [P29474-1]
UniGeneiHs.647092

Genome annotation databases

EnsembliENST00000297494; ENSP00000297494; ENSG00000164867 [P29474-1]
ENST00000467517; ENSP00000420551; ENSG00000164867 [P29474-3]
ENST00000484524; ENSP00000420215; ENSG00000164867 [P29474-2]
GeneIDi4846
KEGGihsa:4846
UCSCiuc003wif.4 human [P29474-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiNOS3_HUMAN
AccessioniPrimary (citable) accession number: P29474
Secondary accession number(s): A0S0A7
, A0S0A8, A8KA63, B2RCQ1, E9PFR2, Q13662, Q14251, Q14434, Q548C1, Q6GSL5, Q9UDC6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 28, 2018
Last modified: June 20, 2018
This is version 219 of the entry and version 4 of the sequence. See 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

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