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Protein

Nitric oxide synthase, endothelial

Gene

NOS3

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 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
  • iron ion binding Source: InterPro
  • 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.

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 in NOS3 seem to 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.
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.
MaxQBiP29474.
PaxDbiP29474.
PeptideAtlasiP29474.
PRIDEiP29474.

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. 33 interactors.
MINTiMINT-106980.
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
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 strandi261 – 263Combined sources3
Helixi265 – 267Combined sources3
Helixi268 – 276Combined sources9
Beta strandi284 – 286Combined sources3
Beta strandi291 – 294Combined sources4
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 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[»]
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.
HOGENOMiHOG000111088.
HOVERGENiHBG000159.
InParanoidiP29474.
KOiK13242.
OrthoDBiEOG091G10Z0.
PhylomeDBiP29474.
TreeFamiTF324410.

Family and domain databases

Gene3Di3.40.50.360. 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_dom.
IPR012144. NOS_euk.
IPR004030. NOS_N.
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 LLLQAPDEPP
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):133,289
Last modified:January 23, 2007 - v3
Checksum:iCD9E60FA277B22C6
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):68,980
Checksum:i057DDC37143265B6
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):67,876
Checksum:iA567DB899BD1372E
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_008037298E → D Polymorphism; may be associated with susceptibility to coronary spasm. 6 PublicationsCorresponds to variant dbSNP:rs1799983Ensembl.1
Natural variantiVAR_036303474R → C Found in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_036304602R → Q Found in a colorectal cancer sample; somatic mutation. 1 Publication1
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.
NP_001153581.1. NM_001160109.1.
NP_001153582.1. NM_001160110.1.
NP_001153583.1. NM_001160111.1.
XP_016867721.1. XM_017012232.1.
UniGeneiHs.647092.

Genome annotation databases

EnsembliENST00000297494; ENSP00000297494; ENSG00000164867.
ENST00000484524; ENSP00000420215; ENSG00000164867.
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: January 23, 2007
Last modified: September 27, 2017
This is version 210 of the entry and version 3 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