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P29474

- NOS3_HUMAN

UniProt

P29474 - NOS3_HUMAN

Protein

Nitric oxide synthase, endothelial

Gene

NOS3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    Heme group.
    Binds 1 FAD.
    Binds 1 FMN.
    Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.

    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. protein binding Source: UniProtKB
    12. 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

    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_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-SubCell
    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

    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

    ArrayExpressiP29474.
    BgeeiP29474.
    CleanExiHS_NOS3.
    GenevestigatoriP29474.

    Organism-specific databases

    HPAiCAB002168.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with NOSIP and NOSTRIN.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    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. 28 interactions.
    MINTiMINT-106980.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MGNLKSVAQE PGPPCGLGLG LGLGLCGKQG PATPAPEPSR APASLLPPAP     50
    EHSPPSSPLT QPPEGPKFPR VKNWEVGSIT YDTLSAQAQQ DGPCTPRRCL 100
    GSLVFPRKLQ GRPSPGPPAP EQLLSQARDF INQYYSSIKR SGSQAHEQRL 150
    QEVEAEVAAT GTYQLRESEL VFGAKQAWRN APRCVGRIQW GKLQVFDARD 200
    CRSAQEMFTY ICNHIKYATN RGNLRSAITV FPQRCPGRGD FRIWNSQLVR 250
    YAGYRQQDGS VRGDPANVEI TELCIQHGWT PGNGRFDVLP LLLQAPDEPP 300
    ELFLLPPELV LEVPLEHPTL EWFAALGLRW YALPAVSNML LEIGGLEFPA 350
    APFSGWYMST EIGTRNLCDP HRYNILEDVA VCMDLDTRTT SSLWKDKAAV 400
    EINVAVLHSY QLAKVTIVDH HAATASFMKH LENEQKARGG CPADWAWIVP 450
    PISGSLTPVF HQEMVNYFLS PAFRYQPDPW KGSAAKGTGI TRKKTFKEVA 500
    NAVKISASLM GTVMAKRVKA TILYGSETGR AQSYAQQLGR LFRKAFDPRV 550
    LCMDEYDVVS LEHETLVLVV TSTFGNGDPP ENGESFAAAL MEMSGPYNSS 600
    PRPEQHKSYK IRFNSISCSD PLVSSWRRKR KESSNTDSAG ALGTLRFCVF 650
    GLGSRAYPHF CAFARAVDTR LEELGGERLL QLGQGDELCG QEEAFRGWAQ 700
    AAFQAACETF CVGEDAKAAA RDIFSPKRSW KRQRYRLSAQ AEGLQLLPGL 750
    IHVHRRKMFQ ATIRSVENLQ SSKSTRATIL VRLDTGGQEG LQYQPGDHIG 800
    VCPPNRPGLV EALLSRVEDP PAPTEPVAVE QLEKGSPGGP PPGWVRDPRL 850
    PPCTLRQALT FFLDITSPPS PQLLRLLSTL AEEPREQQEL EALSQDPRRY 900
    EEWKWFRCPT LLEVLEQFPS VALPAPLLLT QLPLLQPRYY SVSSAPSTHP 950
    GEIHLTVAVL AYRTQDGLGP LHYGVCSTWL SQLKPGDPVP CFIRGAPSFR 1000
    LPPDPSLPCI LVGPGTGIAP FRGFWQERLH DIESKGLQPT PMTLVFGCRC 1050
    SQLDHLYRDE VQNAQQRGVF GRVLTAFSRE PDNPKTYVQD ILRTELAAEV 1100
    HRVLCLERGH MFVCGDVTMA TNVLQTVQRI LATEGDMELD EAGDVIGVLR 1150
    DQQRYHEDIF GLTLRTQEVT SRIRTQSFSL QERQLRGAVP WAFDPPGSDT 1200
    NSP 1203
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 28 interactions.
    MINTi MINT-106980.

    Chemistry

    BindingDBi P29474.
    ChEMBLi CHEMBL2111350.
    DrugBanki DB00125. L-Arginine.
    DB00155. L-Citrulline.
    DB01098. Rosuvastatin.
    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.
    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_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

    ArrayExpressi P29474.
    Bgeei P29474.
    CleanExi HS_NOS3.
    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

    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: October 1, 2014
    This is version 179 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