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P29474

- NOS3_HUMAN

UniProt

P29474 - NOS3_HUMAN

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Protein

Nitric oxide synthase, endothelial

Gene

NOS3

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi94 – 941Zinc
Metal bindingi99 – 991Zinc
Metal bindingi184 – 1841Iron (heme axial ligand)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi649 – 68032FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi793 – 80412FADBy similarityAdd
BLAST
Nucleotide bindingi935 – 94511FADBy similarityAdd
BLAST
Nucleotide bindingi1010 – 102819NADPBy similarityAdd
BLAST
Nucleotide bindingi1108 – 112316NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. actin monomer binding Source: BHF-UCL
  2. arginine binding Source: BHF-UCL
  3. cadmium ion binding Source: BHF-UCL
  4. flavin adenine dinucleotide binding Source: BHF-UCL
  5. FMN binding Source: BHF-UCL
  6. heme binding Source: BHF-UCL
  7. iron ion binding Source: InterPro
  8. NADP binding Source: BHF-UCL
  9. NADPH-hemoprotein reductase activity Source: RefGenome
  10. nitric-oxide synthase activity Source: BHF-UCL
  11. tetrahydrobiopterin binding Source: BHF-UCL

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. arginine catabolic process Source: BHF-UCL
  3. blood coagulation Source: Reactome
  4. blood vessel remodeling Source: BHF-UCL
  5. endothelial cell migration Source: BHF-UCL
  6. interaction with host Source: Reactome
  7. in utero embryonic development Source: Ensembl
  8. lipopolysaccharide-mediated signaling pathway Source: Ensembl
  9. lung development Source: Ensembl
  10. mitochondrion organization Source: BHF-UCL
  11. negative regulation of blood pressure Source: RefGenome
  12. negative regulation of calcium ion transport Source: Ensembl
  13. negative regulation of cell proliferation Source: BHF-UCL
  14. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  15. negative regulation of hydrolase activity Source: Ensembl
  16. negative regulation of muscle hyperplasia Source: BHF-UCL
  17. negative regulation of platelet activation Source: BHF-UCL
  18. negative regulation of potassium ion transport Source: Ensembl
  19. nitric oxide biosynthetic process Source: BHF-UCL
  20. nitric oxide mediated signal transduction Source: RefGenome
  21. nitric oxide metabolic process Source: Reactome
  22. ovulation from ovarian follicle Source: Ensembl
  23. phagosome maturation Source: Reactome
  24. positive regulation of angiogenesis Source: BHF-UCL
  25. positive regulation of guanylate cyclase activity Source: BHF-UCL
  26. positive regulation of vasodilation Source: BHF-UCL
  27. regulation of blood pressure Source: BHF-UCL
  28. regulation of blood vessel size Source: BHF-UCL
  29. regulation of nitric-oxide synthase activity Source: Reactome
  30. regulation of sodium ion transport Source: Ensembl
  31. regulation of systemic arterial blood pressure by endothelin Source: BHF-UCL
  32. regulation of the force of heart contraction by chemical signal Source: Ensembl
  33. response to fluid shear stress Source: BHF-UCL
  34. response to heat Source: BHF-UCL
  35. small molecule metabolic process Source: Reactome
  36. smooth muscle hyperplasia Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:HS09149-MONOMER.
ReactomeiREACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_12477. eNOS activation.
REACT_12510. NOSIP mediated eNOS trafficking.
REACT_12541. NOSTRIN mediated eNOS trafficking.
REACT_228016. VEGFR2 mediated vascular permeability.
REACT_23862. Nitric oxide stimulates guanylate cyclase.
SignaLinkiP29474.

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
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:7876. NOS3.

Subcellular locationi

Cell membrane. Membranecaveola. Cytoplasmcytoskeleton. 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.

GO - Cellular componenti

  1. caveola Source: BHF-UCL
  2. cytoplasm Source: BHF-UCL
  3. cytoskeleton Source: UniProtKB-KW
  4. cytosol Source: Reactome
  5. endocytic vesicle membrane Source: Reactome
  6. Golgi membrane Source: Reactome
  7. nucleus Source: BHF-UCL
  8. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141S → A: Reduced nitrite (NO) production. 1 Publication

Organism-specific databases

MIMi163729. gene+phenotype.
PharmGKBiPA254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 12031202Nitric oxide synthase, endothelialPRO_0000170943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi15 – 151S-palmitoyl cysteineBy similarity
Lipidationi26 – 261S-palmitoyl cysteineBy similarity
Modified residuei114 – 1141Phosphoserine; by CDK51 Publication
Modified residuei141 – 1411PhosphoserineBy similarity
Modified residuei495 – 4951Phosphothreonine; by AMPK1 Publication
Modified residuei633 – 6331PhosphoserineBy similarity
Modified residuei1175 – 11751PhosphothreonineBy similarity
Modified residuei1177 – 11771Phosphoserine; by AMPK1 Publication

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

MaxQBiP29474.
PaxDbiP29474.
PRIDEiP29474.

PTM databases

PhosphoSiteiP29474.

Expressioni

Tissue specificityi

Platelets, placenta, liver and kidney.1 Publication

Gene expression databases

BgeeiP29474.
CleanExiHS_NOS3.
ExpressionAtlasiP29474. baseline and differential.
GenevestigatoriP29474.

Organism-specific databases

HPAiCAB002168.

Interactioni

Subunit structurei

Homodimer. Interacts with NOSIP and NOSTRIN.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P140793EBI-1391623,EBI-9675698From a different organism.
AKT1P317492EBI-1391623,EBI-296087
CDC37Q165434EBI-1391623,EBI-295634
NOSTRINQ8IVI99EBI-1391623,EBI-1391643
ST13P505023EBI-1391623,EBI-357285

Protein-protein interaction databases

BioGridi110909. 44 interactions.
DIPiDIP-38479N.
IntActiP29474. 29 interactions.
MINTiMINT-106980.

Structurei

Secondary structure

1
1203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi70 – 734Combined sources
Turni74 – 763Combined sources
Beta strandi79 – 813Combined sources
Helixi85 – 873Combined sources
Beta strandi88 – 903Combined sources
Helixi121 – 13717Combined sources
Helixi144 – 16017Combined sources
Helixi167 – 18014Combined sources
Helixi187 – 1893Combined sources
Beta strandi194 – 1974Combined sources
Helixi204 – 21916Combined sources
Helixi220 – 2223Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi261 – 2633Combined sources
Helixi265 – 2673Combined sources
Helixi268 – 2769Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi291 – 2944Combined sources
Beta strandi301 – 3033Combined sources
Helixi307 – 3093Combined sources
Beta strandi312 – 3143Combined sources
Helixi321 – 3266Combined sources
Beta strandi329 – 3324Combined sources
Beta strandi340 – 3434Combined sources
Beta strandi346 – 3494Combined sources
Helixi359 – 3635Combined sources
Helixi365 – 3684Combined sources
Turni370 – 3734Combined sources
Helixi376 – 3827Combined sources
Helixi390 – 3923Combined sources
Helixi394 – 41320Combined sources
Helixi420 – 43819Combined sources
Helixi445 – 4484Combined sources
Beta strandi451 – 4533Combined sources
Helixi454 – 4563Combined sources
Helixi458 – 4614Combined sources
Beta strandi470 – 4745Combined sources
Helixi496 – 50611Combined sources
Helixi507 – 5093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
3EAHX-ray2.44A/B66-492[»]
3NOSX-ray2.40A/B66-492[»]
ProteinModelPortaliP29474.
SMRiP29474. Positions 67-481, 492-1177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29474.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini520 – 703184Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini756 – 1002247FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 486389Interaction with NOSIPAdd
BLAST
Regioni491 – 51020Calmodulin-bindingSequence AnalysisAdd
BLAST

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

Phylogenomic databases

eggNOGiCOG4362.
GeneTreeiENSGT00620000087711.
HOGENOMiHOG000111088.
HOVERGENiHBG000159.
InParanoidiP29474.
KOiK13242.
OrthoDBiEOG79SDW7.
PhylomeDBiP29474.
TreeFamiTF324410.

Family and domain databases

Gene3Di1.20.990.10. 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.
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.
[Graphical view]
PIRSFiPIRSF000333. NOS. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. 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.
[Graphical view]

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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531S → R in AAA36373. (PubMed:7514568)Curated
Sequence conflicti168 – 1681S → G in BAG37648. (PubMed:14702039)Curated
Sequence conflicti414 – 4141K → R in BAF85617. (PubMed:14702039)Curated
Sequence conflicti489 – 4891G → S in AAD14336. (PubMed:7475956)Curated
Sequence conflicti567 – 5671V → W in CAA53950. (PubMed:7509596)Curated
Sequence conflicti1150 – 11501R → RQ in BAA05652. (PubMed:7519987)Curated
Sequence conflicti1194 – 11941D → E in CAA53950. (PubMed:7509596)Curated

Polymorphismi

Variation in NOS3 seem to be associated with susceptibility to coronary spasm.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121R → Q.1 Publication
Corresponds to variant rs3918166 [ dbSNP | Ensembl ].
VAR_031218
Natural varianti298 – 2981E → D in susceptibility to coronary spasm. 6 Publications
Corresponds to variant rs1799983 [ dbSNP | Ensembl ].
VAR_008037
Natural varianti474 – 4741R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036303
Natural varianti602 – 6021R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036304
Natural varianti665 – 6651R → H.
Corresponds to variant rs7792133 [ dbSNP | Ensembl ].
VAR_061377
Natural varianti827 – 8271V → M.1 Publication
Corresponds to variant rs3918232 [ dbSNP | Ensembl ].
VAR_031219
Natural varianti885 – 8851R → M.1 Publication
Corresponds to variant rs3918201 [ dbSNP | Ensembl ].
VAR_031220
Natural varianti982 – 9821Q → L.1 Publication
Corresponds to variant rs3918234 [ dbSNP | Ensembl ].
VAR_031221

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei584 – 62542ESFAA…PLVSS → EGLTLWPRLECSSTITAHCS LNLLDSSNPPTSTSQVVGTT GACHDA in isoform eNOS13C. 1 PublicationVSP_042625Add
BLAST
Alternative sequencei585 – 61430SFAAA…KIRFN → RWGFAMLPRLVSNSWVQAIH LPRPPKVLRL in isoform eNOS13B. 1 PublicationVSP_045495Add
BLAST
Alternative sequencei615 – 1203589Missing in isoform eNOS13B. 1 PublicationVSP_045496Add
BLAST
Alternative sequencei626 – 1203578Missing in isoform eNOS13C. 1 PublicationVSP_042626Add
BLAST

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_006716063.1. XM_006716000.1.
UniGeneiHs.647092.

Genome annotation databases

EnsembliENST00000297494; ENSP00000297494; ENSG00000164867.
ENST00000484524; ENSP00000420215; ENSG00000164867.
GeneIDi4846.
KEGGihsa:4846.
UCSCiuc003wif.3. human. [P29474-1]
uc011kuz.2. human. [P29474-2]

Polymorphism databases

DMDMi266648.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Nitric oxide synthase entry

SeattleSNPs

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 .
CCDSi CCDS55182.1. [P29474-2 ]
CCDS55183.1. [P29474-3 ]
CCDS5912.1. [P29474-1 ]
PIRi A47501.
RefSeqi NP_000594.2. NM_000603.4.
NP_001153581.1. NM_001160109.1.
NP_001153582.1. NM_001160110.1.
NP_001153583.1. NM_001160111.1.
XP_006716063.1. XM_006716000.1.
UniGenei Hs.647092.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
1NIW X-ray 2.05 B/D/F/H 492-511 [» ]
2LL7 NMR - B 493-509 [» ]
2MG5 NMR - B 495-510 [» ]
3EAH X-ray 2.44 A/B 66-492 [» ]
3NOS X-ray 2.40 A/B 66-492 [» ]
ProteinModelPortali P29474.
SMRi P29474. Positions 67-481, 492-1177.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110909. 44 interactions.
DIPi DIP-38479N.
IntActi P29474. 29 interactions.
MINTi MINT-106980.

Chemistry

BindingDBi P29474.
ChEMBLi CHEMBL2111405.
DrugBanki DB00997. Doxorubicin.
DB00125. L-Arginine.
DB00155. L-Citrulline.
DB01110. Miconazole.
DB00360. Tetrahydrobiopterin.

PTM databases

PhosphoSitei P29474.

Polymorphism databases

DMDMi 266648.

Proteomic databases

MaxQBi P29474.
PaxDbi P29474.
PRIDEi P29474.

Protocols and materials databases

DNASUi 4846.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297494 ; ENSP00000297494 ; ENSG00000164867 .
ENST00000484524 ; ENSP00000420215 ; ENSG00000164867 .
GeneIDi 4846.
KEGGi hsa:4846.
UCSCi uc003wif.3. human. [P29474-1 ]
uc011kuz.2. human. [P29474-2 ]

Organism-specific databases

CTDi 4846.
GeneCardsi GC07P150688.
H-InvDB HIX0033558.
HGNCi HGNC:7876. NOS3.
HPAi CAB002168.
MIMi 163729. gene+phenotype.
neXtProti NX_P29474.
PharmGKBi PA254.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4362.
GeneTreei ENSGT00620000087711.
HOGENOMi HOG000111088.
HOVERGENi HBG000159.
InParanoidi P29474.
KOi K13242.
OrthoDBi EOG79SDW7.
PhylomeDBi P29474.
TreeFami TF324410.

Enzyme and pathway databases

BioCyci MetaCyc:HS09149-MONOMER.
Reactomei REACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_12477. eNOS activation.
REACT_12510. NOSIP mediated eNOS trafficking.
REACT_12541. NOSTRIN mediated eNOS trafficking.
REACT_228016. VEGFR2 mediated vascular permeability.
REACT_23862. Nitric oxide stimulates guanylate cyclase.
SignaLinki P29474.

Miscellaneous databases

ChiTaRSi NOS3. human.
EvolutionaryTracei P29474.
GeneWikii Endothelial_NOS.
GenomeRNAii 4846.
NextBioi 18666.
PROi P29474.
SOURCEi Search...

Gene expression databases

Bgeei P29474.
CleanExi HS_NOS3.
ExpressionAtlasi P29474. baseline and differential.
Genevestigatori P29474.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
3.40.50.360. 2 hits.
3.90.340.10. 1 hit.
InterProi IPR003097. 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.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000333. NOS. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Alternative splicing in intron 13 of the human eNOS gene: a potential mechanism for regulating eNOS activity."
    Lorenz M., Hewing B., Hui J., Zepp A., Baumann G., Bindereif A., Stangl V., Stangl K.
    FASEB J. 21:1556-1564(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ENOS13B AND ENOS13C), ALTERNATIVE SPLICING, FUNCTION (ISOFORM ENOS13C), VARIANT ASP-298.
  8. Liao J.K.
    Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Umbilical vein.
  9. "The role of phosphatidylinositol-3-oh kinase in platelet-derived nitric oxide release and platelet disaggregation."
    Zhang Y., Freedman J.E.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Platelet.
  10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-298.
    Tissue: Hippocampus and Trachea.
  11. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Spleen.
  12. 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.
  13. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  14. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  15. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  16. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-298.
    Tissue: Placenta.
  17. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
    Tissue: Placenta.
  18. "Expression of constitutive endothelial nitric oxide synthase in human blood platelets."
    Sase K., Michel T.
    Life Sci. 57:2049-2055(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 411-528 (ISOFORM 1/ENOS13C).
    Tissue: Platelet.
  19. "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] [Europe PMC] [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.
  20. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOSIP, ENZYME REGULATION, SUBCELLULAR LOCATION.
  21. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOSTRIN, ENZYME REGULATION, SUBCELLULAR LOCATION.
  22. "Endothelial thrombomodulin induces Ca2+ signals and nitric oxide synthesis through epidermal growth factor receptor kinase and calmodulin kinase II."
    David-Dufilho M., Millanvoye-Van Brussel E., Topal G., Walch L., Brunet A., Rendu F.
    J. Biol. Chem. 280:35999-36006(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-495 AND SER-1177.
  23. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  24. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  25. "CDK5 phosphorylates eNOS at Ser-113 and regulates NO production."
    Lee C.-H., Wei Y.-W., Huang Y.-T., Lin Y.-T., Lee Y.-C., Lee K.-H., Lu P.-J.
    J. Cell. Biochem. 110:112-117(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-114, MUTAGENESIS OF SER-114.
  26. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  27. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 67-480.
  28. Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 66-492.
  29. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT SUSCEPTIBILITY TO CORONARY SPASM ASP-298.
  30. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT SUSCEPTIBILITY TO CORONARY SPASM ASP-298.
  31. Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-474 AND GLN-602.

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 historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 181 of the entry and version 3 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, 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

External Data

Dasty 3