Reviewed, UniProtKB/Swiss-Prot P29474 (NOS3_HUMAN)

Names and origin

Protein names

Recommended name:
    Nitric oxide synthase, endothelial
    EC=1.14.13.39
Alternative name(s):
    Endothelial NOS
      Short name=eNOS
    EC-NOS
    NOS type III
      Short name=NOSIII
    Constitutive NOS
      Short name=cNOS

Gene names

Name:

NOS3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1203 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Catalytic activity	L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+.
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 NOSIP and NOSTRIN. Ref.13 Ref.14
Subunit structure	Homodimer. Interacts with NOSIP and NOSTRIN. Ref.13 Ref.14
Subcellular location	Cell membrane. Membrane › caveola. Cytoplasm › cytoskeleton. Golgi apparatus. Note: Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle; which is favored by interaction with NOSIP and results in a reduced enzymatic activity. Ref.13 Ref.14 Ref.15 Ref.16
Tissue specificity	Platelets, placenta, liver and kidney. Ref.12
Polymorphism	Variation in NOS3 seem to be associated with susceptibility to coronary spasm.
Sequence similarities	Belongs to the NOS family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	Calcium Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP Zinc
Molecular function	Oxidoreductase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Inferred from sequence or structural similarity. Source: UniProtKB arginine catabolic process Ref.1 Inferred from direct assay. Source: UniProtKB blood vessel remodeling Inferred from sequence or structural similarity. Source: UniProtKB endothelial cell migration Inferred from mutant phenotype. Source: UniProtKB mitochondrion organization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of muscle hyperplasia Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of platelet activation Non-traceable author statement. Source: UniProtKB nitric oxide biosynthetic process Ref.1 Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of guanylate cyclase activity Inferred from mutant phenotype. Source: UniProtKB positive regulation of vasodilation Non-traceable author statement. Source: UniProtKB regulation of blood vessel size Non-traceable author statement. Source: UniProtKB regulation of systemic arterial blood pressure by endothelin Inferred from mutant phenotype. Source: UniProtKB response to fluid shear stress Inferred from expression pattern. Source: UniProtKB response to heat Non-traceable author statement. Source: UniProtKB smooth muscle hyperplasia Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	Golgi membrane Ref.13 Inferred from Experiment. Source: Reactome caveola Inferred from direct assay. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from Experiment. Source: Reactome nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	FAD binding Non-traceable author statement. Source: UniProtKB FMN binding Non-traceable author statement. Source: UniProtKB NADP or NADPH binding Non-traceable author statement. Source: UniProtKB actin monomer binding Inferred from physical interaction. Source: UniProtKB arginine binding Inferred from direct assay. Source: UniProtKB cadmium ion binding Non-traceable author statement. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from direct assay. Source: UniProtKB nitric-oxide synthase activity Ref.1 Inferred from direct assay. Source: UniProtKB tetrahydrobiopterin binding Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NOSTRIN	Q8IVI9	4	EBI-1391623,EBI-1391643

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 1203

1202

Nitric oxide synthase, endothelial

PRO_0000170943

Regions

Domain

520 – 703

184

Flavodoxin-like

Domain

756 – 1002

247

FAD-binding FR-type

Nucleotide binding

649 – 680

32

FMN By similarity

Nucleotide binding

793 – 804

12

FAD By similarity

Nucleotide binding

935 – 945

11

FAD By similarity

Nucleotide binding

1010 – 1028

19

NADP By similarity

Nucleotide binding

1108 – 1123

16

NADP By similarity

Region

98 – 486

389

Interaction with NOSIP

Region

491 – 510

20

Calmodulin-binding Potential

Sites

Metal binding

94

1

Zinc

Metal binding

99

1

Zinc

Metal binding

184

1

Iron (heme axial ligand)

Amino acid modifications

Modified residue

81

1

Phosphotyrosine Ref.17

Modified residue

495

1

Phosphothreonine By similarity

Modified residue

633

1

Phosphoserine By similarity

Modified residue

1175

1

Phosphothreonine By similarity

Modified residue

1177

1

Phosphoserine By similarity

Lipidation

2

1

N-myristoyl glycine By similarity

Lipidation

15

1

S-palmitoyl cysteine By similarity

Lipidation

26

1

S-palmitoyl cysteine By similarity

Natural variations

Natural variant

112

1

R → Q: dbSNP rs3918166. Ref.8

VAR_031218

Natural variant

298

1

E → D in susceptibility to coronary spasm. dbSNP rs1799983. Ref.8 Ref.9 Ref.20 Ref.21

VAR_008037

Natural variant

474

1

R → C in a colorectal cancer sample; somatic mutation. Ref.22

VAR_036303

Natural variant

602

1

R → Q in a colorectal cancer sample; somatic mutation. Ref.22

VAR_036304

Natural variant

827

1

V → M: dbSNP rs3918232. Ref.8

VAR_031219

Natural variant

885

1

R → M: dbSNP rs3918201. Ref.8

VAR_031220

Natural variant

982

1

Q → L: dbSNP rs3918234. Ref.8

VAR_031221

Experimental info

Sequence conflict

53

1

S → R in AAA36373. Ref.10

Sequence conflict

489

1

G → S in AAD14336. Ref.11

Sequence conflict

567

1

V → W in CAA53950. Ref.6

Sequence conflict

1150

1

R → RQ in BAA05652. Ref.7

Sequence conflict

1194

1

D → E in CAA53950. Ref.6

Secondary structure

1

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1203

Helix Strand Turn

Details...

Beta strand

70 – 73

4

Turn

74 – 76

3

Beta strand

79 – 81

3

Helix

85 – 87

3

Helix

121 – 137

17

Helix

144 – 160

17

Helix

167 – 179

13

Helix

187 – 192

6

Beta strand

194 – 197

4

Helix

204 – 219

16

Helix

220 – 222

3

Beta strand

227 – 230

4

Beta strand

245 – 249

5

Beta strand

253 – 255

3

Beta strand

261 – 263

3

Helix

265 – 267

3

Helix

268 – 276

9

Beta strand

284 – 286

3

Beta strand

291 – 294

4

Beta strand

301 – 303

3

Helix

307 – 309

3

Beta strand

312 – 314

3

Helix

323 – 326

4

Beta strand

329 – 332

4

Beta strand

340 – 343

4

Beta strand

346 – 349

4

Helix

359 – 363

5

Helix

365 – 368

4

Turn

370 – 373

4

Helix

376 – 382

7

Helix

390 – 392

3

Helix

394 – 412

19

Helix

420 – 437

18

Helix

445 – 448

4

Beta strand

451 – 453

3

Helix

454 – 456

3

Turn

458 – 461

4

Beta strand

470 – 474

5

Sequences

	Sequence		Length	Mass (Da)
	P29474-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CD9E60FA277B22C6	FASTA	1,203	133,289
	10 20 30 40 50 60 MGNLKSVAQE PGPPCGLGLG LGLGLCGKQG PATPAPEPSR APASLLPPAP EHSPPSSPLT 70 80 90 100 110 120 QPPEGPKFPR VKNWEVGSIT YDTLSAQAQQ DGPCTPRRCL GSLVFPRKLQ GRPSPGPPAP 130 140 150 160 170 180 EQLLSQARDF INQYYSSIKR SGSQAHEQRL QEVEAEVAAT GTYQLRESEL VFGAKQAWRN 190 200 210 220 230 240 APRCVGRIQW GKLQVFDARD CRSAQEMFTY ICNHIKYATN RGNLRSAITV FPQRCPGRGD 250 260 270 280 290 300 FRIWNSQLVR YAGYRQQDGS VRGDPANVEI TELCIQHGWT PGNGRFDVLP LLLQAPDEPP 310 320 330 340 350 360 ELFLLPPELV LEVPLEHPTL EWFAALGLRW YALPAVSNML LEIGGLEFPA APFSGWYMST 370 380 390 400 410 420 EIGTRNLCDP HRYNILEDVA VCMDLDTRTT SSLWKDKAAV EINVAVLHSY QLAKVTIVDH 430 440 450 460 470 480 HAATASFMKH LENEQKARGG CPADWAWIVP PISGSLTPVF HQEMVNYFLS PAFRYQPDPW 490 500 510 520 530 540 KGSAAKGTGI TRKKTFKEVA NAVKISASLM GTVMAKRVKA TILYGSETGR AQSYAQQLGR 550 560 570 580 590 600 LFRKAFDPRV LCMDEYDVVS LEHETLVLVV TSTFGNGDPP ENGESFAAAL MEMSGPYNSS 610 620 630 640 650 660 PRPEQHKSYK IRFNSISCSD PLVSSWRRKR KESSNTDSAG ALGTLRFCVF GLGSRAYPHF 670 680 690 700 710 720 CAFARAVDTR LEELGGERLL QLGQGDELCG QEEAFRGWAQ AAFQAACETF CVGEDAKAAA 730 740 750 760 770 780 RDIFSPKRSW KRQRYRLSAQ AEGLQLLPGL IHVHRRKMFQ ATIRSVENLQ SSKSTRATIL 790 800 810 820 830 840 VRLDTGGQEG LQYQPGDHIG VCPPNRPGLV EALLSRVEDP PAPTEPVAVE QLEKGSPGGP 850 860 870 880 890 900 PPGWVRDPRL PPCTLRQALT FFLDITSPPS PQLLRLLSTL AEEPREQQEL EALSQDPRRY 910 920 930 940 950 960 EEWKWFRCPT LLEVLEQFPS VALPAPLLLT QLPLLQPRYY SVSSAPSTHP GEIHLTVAVL 970 980 990 1000 1010 1020 AYRTQDGLGP LHYGVCSTWL SQLKPGDPVP CFIRGAPSFR LPPDPSLPCI LVGPGTGIAP 1030 1040 1050 1060 1070 1080 FRGFWQERLH DIESKGLQPT PMTLVFGCRC SQLDHLYRDE VQNAQQRGVF GRVLTAFSRE 1090 1100 1110 1120 1130 1140 PDNPKTYVQD ILRTELAAEV HRVLCLERGH MFVCGDVTMA TNVLQTVQRI LATEGDMELD 1150 1160 1170 1180 1190 1200 EAGDVIGVLR DQQRYHEDIF GLTLRTQEVT SRIRTQSFSL QERQLRGAVP WAFDPPGSDT NSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase." Janssens S.P., Shimouchi A., Quertermous T., Bloch D.B., Bloch K.D. J. Biol. Chem. 267:14519-14522(1992) [PubMed: 1378832] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Erratum Janssens S.P., Shimouchi A., Quertermous T., Bloch D.B., Bloch K.D. J. Biol. Chem. 267:22694-22694(1992)
[3]	"Molecular cloning and characterization of human endothelial nitric oxide synthase." Marsden P.A., Schappert K.T., Chen H.S., Flowers M., Sundell C.L., Wilcox J.N., Lamas S., Michel T. FEBS Lett. 307:287-293(1992) [PubMed: 1379542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structure and chromosomal localization of the human constitutive endothelial nitric oxide synthase gene." Marsden P.A., Heng H.H.Q., Scherer S.W., Stewart R.J., Hall A.V., Shi X.-M., Tsui L.-C., Schappert K.T. J. Biol. Chem. 268:17478-17488(1993) [PubMed: 7688726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	Liao J.K. Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Umbilical vein.
[6]	"Gene structure, polymorphism and mapping of the human endothelial nitric oxide synthase gene." Nadaud S.A., Bonnardeaux A., Lathrop M., Soubrier F. Biochem. Biophys. Res. Commun. 198:1027-1033(1994) [PubMed: 7509596] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[7]	"Cloning and structural characterization of the human endothelial nitric-oxide-synthase gene." Miyahara K., Kawamoto T., Sase K., Yui Y., Toda K., Yang L.X., Hattori R., Aoyama T., Yamamoto Y., Doi Y., Ogoshi S., Hashimoto K., Kawai C., Sasayama S., Shizuta Y. Eur. J. Biochem. 223:719-726(1994) [PubMed: 7519987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	SeattleSNPs variation discovery resource Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-112; ASP-298; MET-827; MET-885 AND LEU-982.
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-298. Tissue: Placenta.
[10]	"Isolation and chromosomal localization of the human endothelial nitric oxide synthase (NOS3) gene." Robinson L.J., Weremowicz S., Morton C.C., Michel T. Genomics 19:350-357(1994) [PubMed: 7514568] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53. Tissue: Placenta.
[11]	"Expression of constitutive endothelial nitric oxide synthase in human blood platelets." Sase K., Michel T. Life Sci. 57:2049-2055(1995) [PubMed: 7475956] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 411-528. Tissue: Platelet.
[12]	"Purification and characterization of the constitutive nitric oxide synthase from human placenta." Garvey E.P., Tuttle J.V., Covington K., Merrill B.M., Wood E.R., Baylis S.A., Charles I.G. Arch. Biochem. Biophys. 311:235-241(1994) [PubMed: 7515611] [Abstract] Cited for: PROTEIN SEQUENCE OF 167-175; 531-540; 835-845; 876-881; 886-898; 1001-1005 AND 1068-1080, TISSUE SPECIFICITY. Tissue: Placenta.
[13]	"NOSIP, a novel modulator of endothelial nitric oxide synthase activity." Dedio J., Koenig P., Wohlfart P., Schroeder C., Kummer W., Mueller-Esterl W. FASEB J. 15:79-89(2001) [PubMed: 11149895] [Abstract] Cited for: INTERACTION WITH NOSIP, ENZYME REGULATION, SUBCELLULAR LOCATION.
[14]	"NOSTRIN: a protein modulating nitric oxide release and subcellular distribution of endothelial nitric oxide synthase." Zimmermann K., Opitz N., Dedio J., Renne C., Mueller-Esterl W., Oess S. Proc. Natl. Acad. Sci. U.S.A. 99:17167-17172(2002) [PubMed: 12446846] [Abstract] Cited for: INTERACTION WITH NOSTRIN, ENZYME REGULATION, SUBCELLULAR LOCATION.
[15]	"NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS." Icking A., Matt S., Opitz N., Wiesenthal A., Mueller-Esterl W., Schilling K. J. Cell Sci. 118:5059-5069(2005) [PubMed: 16234328] [Abstract] Cited for: SUBCELLULAR LOCATION.
[16]	"Cell cycle-regulated inactivation of endothelial NO synthase through NOSIP-dependent targeting to the cytoskeleton." Schleicher M., Brundin F., Gross S., Mueller-Esterl W., Oess S. Mol. Cell. Biol. 25:8251-8258(2005) [PubMed: 16135813] [Abstract] Cited for: SUBCELLULAR LOCATION.
[17]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-81, MASS SPECTROMETRY.
[18]	"Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation." Fischmann T.O., Hruza A., Niu X.D., Fossetta J.D., Lunn C.A., Dolphin E., Prongay A.J., Reichert P., Lundell D.J., Narula S.K., Weber P.C. Nat. Struct. Biol. 6:233-242(1999) [PubMed: 10074942] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[19]	"Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency." Rosenfeld R.J., Garcin E.D., Panda K., Andersson G., Aberg A., Wallace A.V., Morris G.M., Olson A.J., Stuehr D.J., Tainer J.A., Getzoff E.D. Biochemistry 41:13915-13925(2002) [PubMed: 12437348] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 67-480.
[20]	"A missense Glu298Asp variant in the endothelial nitric oxide synthase gene is associated with coronary spasm in the Japanese." Yoshimura M., Yasue H., Nakayama M., Shimasaki Y., Sumida H., Sugiyama S., Kugiyama K., Ogawa H., Ogawa Y., Saito Y., Miyamoto Y., Nakao K. Hum. Genet. 103:65-69(1998) [PubMed: 9737779] [Abstract] Cited for: VARIANT SUSCEPTIBILITY TO CORONARY SPASM ASP-298.
[21]	"In-vivo effects of Glu298Asp endothelial nitric oxide synthase polymorphism." Sofowora G., Dishy V., Xie H.G., Imamura H., Nishimi Y., Morales C.R., Morrow J.D., Kim R.B., Stein C.M., Wood A.J. Pharmacogenetics 11:809-814(2001) [PubMed: 11740345] [Abstract] Cited for: VARIANT SUSCEPTIBILITY TO CORONARY SPASM ASP-298.
[22]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-474 AND GLN-602.
+	Additional computationally mapped references.

Web resources

Wikipedia

Nitric oxide synthase entry

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
L26914 Genomic DNA. Translation: AAA36374.1.
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.
AF519768 Genomic DNA. Translation: AAM74944.1.
BC063294 mRNA. Translation: AAH63294.1.
BC069465 mRNA. Translation: AAH69465.1.
L23210 Genomic DNA. Translation: AAA36373.1.
S80791 mRNA. Translation: AAD14336.1.

IPI

IPI00218845.

PIR

A47501.

RefSeq

NP_000594.2.
NP_001153581.1.
NP_001153582.1.

UniGene

Hs.647092

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M9J	X-ray	2.43	A/B	67-481	[»]
1M9K	X-ray	2.01	A/B	67-481	[»]
1M9M	X-ray	1.96	A/B	67-481	[»]
1M9Q	X-ray	2.01	A/B	67-481	[»]
1M9R	X-ray	2.56	A/B	67-481	[»]
3EAH	X-ray	2.44	A/B	66-492	[»]
3NOS	X-ray	2.40	A/B	66-492	[»]

SMR

P29474. Positions 65-480.

ModBase

Search...

Protein-protein interaction databases

IntAct

P29474. 1 interaction.

STRING

P29474.

PTM databases

PhosphoSite

P29474.

Proteomic databases

PRIDE

P29474.

Genome annotation databases

Ensembl

ENST00000297494; ENSP00000297494; ENSG00000164867; Homo sapiens. [Genome view]
ENST00000404733; ENSP00000385819; ENSG00000164867; Homo sapiens. [Genome view]

GeneID

4846.

KEGG

hsa:4846.

UCSC

uc003wif.1. human.

Organism-specific databases

CTD

4846.

GeneCards

GC07P150319.

H-InvDB

HIX0033558.

HGNC

HGNC:7876. NOS3.

HPA

CAB002168.

MIM

163729. gene+phenotype.

PharmGKB

PA134867615.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P29474.

HOVERGEN

P29474.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11233.

BRENDA

1.14.13.39. 247.

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
txa2pathway. Thromboxane A2 receptor signaling.
vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_12508. Metabolism of nitric oxide.

Gene expression databases

ArrayExpress

P29474.

Bgee

P29474.

CleanEx

HS_NOS3.

Genevestigator

P29474.

GermOnline

ENSG00000164867. Homo sapiens.

Family and domain databases

InterPro

IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012144. Nitric-oxide_synthase.
IPR004030. NO_synthase_oxygenase_reg.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]

Gene3D

G3DSA:3.90.340.10. NO_synthase_oxygenase_reg. 1 hit.

Pfam

PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]

PIRSF

PIRSF000333. NOS. 1 hit.

PRINTS

PR00369. FLAVODOXIN.
PR00371. FPNCR.

PROSITE

PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00125. L-Arginine.
DB00155. L-Citrulline.
DB01098. Rosuvastatin.
DB00360. Tetrahydrobiopterin.

SOURCE

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Entry information

Entry name

NOS3_HUMAN

Accession

Primary (citable) accession number: P29474
Secondary accession number(s): Q13662 , Q14251, Q14434, Q6GSL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.