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UniProtKB/Swiss-Prot entry P29474


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NOS3_HUMAN
Primary accession number P29474
Secondary accession numbers Q13662 Q14251 Q14434
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 114)
Name and origin of the protein
Protein name Nitric oxide synthase, endothelial
Synonyms EC 1.14.13.39
Endothelial NOS
eNOS
EC-NOS
NOS type III
NOSIII
Constitutive NOS
cNOS
Gene name
Name: NOS3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1378832 [NCBI, ExPASy, EBI, Israel, Japan]
Janssens S.P., Shimouchi A., Quertermous T., Bloch D.B., Bloch K.D.;
"Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase.";
J. Biol. Chem. 267:14519-14522(1992).
[2]
ERRATUM.
Janssens S.P., Shimouchi A., Quertermous T., Bloch D.B., Bloch K.D.;
J. Biol. Chem. 267:22694-22694(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0014-5793(92)80697-F; PubMed=1379542 [NCBI, ExPASy, EBI, Israel, Japan]
Marsden P.A., Schappert K.T., Chen H.S., Flowers M., Sundell C.L., Wilcox J.N., Lamas S., Michel T.;
"Molecular cloning and characterization of human endothelial nitric oxide synthase.";
FEBS Lett. 307:287-293(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7688726 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Structure and chromosomal localization of the human constitutive endothelial nitric oxide synthase gene.";
J. Biol. Chem. 268:17478-17488(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Umbilical vein;
Liao J.K.;
Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
DOI=10.1006/bbrc.1994.1146; PubMed=7509596 [NCBI, ExPASy, EBI, Israel, Japan]
Nadaud S.A., Bonnardeaux A., Lathrop M., Soubrier F.;
"Gene structure, polymorphism and mapping of the human endothelial nitric oxide synthase gene.";
Biochem. Biophys. Res. Commun. 198:1027-1033(1994).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7519987 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Cloning and structural characterization of the human endothelial nitric-oxide-synthase gene.";
Eur. J. Biochem. 223:719-726(1994).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-112; ASP-298; MET-827; MET-885 AND LEU-982.
SeattleSNPs program for genomic applications;
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
TISSUE=Placenta;
DOI=10.1006/geno.1994.1068; PubMed=7514568 [NCBI, ExPASy, EBI, Israel, Japan]
Robinson L.J., Weremowicz S., Morton C.C., Michel T.;
"Isolation and chromosomal localization of the human endothelial nitric oxide synthase (NOS3) gene.";
Genomics 19:350-357(1994).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 411-528.
TISSUE=Platelet;
DOI=10.1016/0024-3205(95)02191-K; PubMed=7475956 [NCBI, ExPASy, EBI, Israel, Japan]
Sase K., Michel T.;
"Expression of constitutive endothelial nitric oxide synthase in human blood platelets.";
Life Sci. 57:2049-2055(1995).
[12]
PROTEIN SEQUENCE OF 167-175; 531-540; 835-845; 876-881; 886-898; 1001-1005 AND 1068-1080, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
DOI=10.1006/abbi.1994.1232; PubMed=7515611 [NCBI, ExPASy, EBI, Israel, Japan]
Garvey E.P., Tuttle J.V., Covington K., Merrill B.M., Wood E.R., Baylis S.A., Charles I.G.;
"Purification and characterization of the constitutive nitric oxide synthase from human placenta.";
Arch. Biochem. Biophys. 311:235-241(1994).
[13]
INTERACTION WITH NOSIP, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
DOI=10.1096/fj.00-0078com; PubMed=11149895 [NCBI, ExPASy, EBI, Israel, Japan]
Dedio J., Koenig P., Wohlfart P., Schroeder C., Kummer W., Mueller-Esterl W.;
"NOSIP, a novel modulator of endothelial nitric oxide synthase activity.";
FASEB J. 15:79-89(2001).
[14]
INTERACTION WITH NOSTRIN, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
DOI=10.1073/pnas.252345399; PubMed=12446846 [NCBI, ExPASy, EBI, Israel, Japan]
Zimmermann K., Opitz N., Dedio J., Renne C., Mueller-Esterl W., Oess S.;
"NOSTRIN: a protein modulating nitric oxide release and subcellular distribution of endothelial nitric oxide synthase.";
Proc. Natl. Acad. Sci. U.S.A. 99:17167-17172(2002).
[15]
SUBCELLULAR LOCATION.
DOI=10.1242/jcs.02620; PubMed=16234328 [NCBI, ExPASy, EBI, Israel, Japan]
Icking A., Matt S., Opitz N., Wiesenthal A., Mueller-Esterl W., Schilling K.;
"NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS.";
J. Cell Sci. 118:5059-5069(2005).
[16]
SUBCELLULAR LOCATION.
DOI=10.1128/MCB.25.18.8251-8258.2005; PubMed=16135813 [NCBI, ExPASy, EBI, Israel, Japan]
Schleicher M., Brundin F., Gross S., Mueller-Esterl W., Oess S.;
"Cell cycle-regulated inactivation of endothelial NO synthase through NOSIP-dependent targeting to the cytoskeleton.";
Mol. Cell. Biol. 25:8251-8258(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-81, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[18]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1038/6675; PubMed=10074942 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation.";
Nat. Struct. Biol. 6:233-242(1999).
[19]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 67-480.
DOI=10.1021/bi026313j; PubMed=12437348 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency.";
Biochemistry 41:13915-13925(2002).
[20]
VARIANT SUSCEPTIBILITY TO CORONARY SPASM ASP-298.
DOI=10.1007/s004390050785; PubMed=9737779 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshimura M., Yasue H., Nakayama M., Shimasaki Y., Sumida H., Sugiyama S., Kugiyama K., Ogawa H., Ogawa Y., Saito Y., Miyamoto Y., Nakao K.;
"A missense Glu298Asp variant in the endothelial nitric oxide synthase gene is associated with coronary spasm in the Japanese.";
Hum. Genet. 103:65-69(1998).
[21]
VARIANT SUSCEPTIBILITY TO CORONARY SPASM ASP-298.
DOI=10.1097/00008571-200112000-00009; PubMed=11740345 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"In-vivo effects of Glu298Asp endothelial nitric oxide synthase polymorphism.";
Pharmacogenetics 11:809-814(2001).
[22]
VARIANTS [LARGE SCALE ANALYSIS] CYS-474 AND GLN-602.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M93718; AAA36364.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M95296; AAA36372.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10709; AAA36365.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10693; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10694; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10695; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10696; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10697; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10698; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10699; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10700; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10701; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10702; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10703; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10704; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10705; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10706; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10707; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L10708; AAA36365.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L26914; AAA36374.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76303; CAA53950.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76304; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76305; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76306; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76307; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76308; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76309; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76310; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76311; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76312; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76313; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76314; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76315; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76316; CAA53950.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D26607; BAA05652.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF519768; AAM74944.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069465; AAH69465.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L23210; AAA36373.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S80791; AAD14336.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A47501; A47501.
UniGene Hs.699165
3D structure databases
PDB
1M9J; X-ray; 2.43 A; A/B=67-481.[ExPASy / RCSB / EBI]
1M9K; X-ray; 2.01 A; A/B=67-481.[ExPASy / RCSB / EBI]
1M9M; X-ray; 1.96 A; A/B=67-481.[ExPASy / RCSB / EBI]
1M9Q; X-ray; 2.01 A; A/B=67-481.[ExPASy / RCSB / EBI]
1M9R; X-ray; 2.56 A; A/B=67-481.[ExPASy / RCSB / EBI]
3NOS; X-ray; 2.40 A; A/B=66-492.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1M9J; -.
1M9K; -.
1M9M; -.
1M9Q; -.
1M9R; -.
3NOS; -.
SMR P29474; 65-480.
ModBase P29474.
Protein-protein interaction databases
IntAct P29474; -.
PTM databases
PhosphoSite P29474; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-11233; -.
Organism-specific databases
H-InvDB HIX0033558; -.
HGNC HGNC:7876; NOS3.
GenAtlas NOS3.
HPA CAB002168; -.
MIM 163729; gene+phenotype. [NCBI / EBI]
PharmGKB PA134867615; -.
GeneCards P29474.
Gene expression databases
ArrayExpress P29474; -.
CleanEx HS_NOS3; -.
GermOnline ENSG00000164867; Homo sapiens.
Ontologies
GO
GO:0005901; Cellular component: caveola (inferred from direct assay from UniProtKB).
GO:0005856; Cellular component: cytoskeleton (inferred from electronic annotation from UniProtKB-KW).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0000139; Cellular component: Golgi membrane (inferred from experiment from Reactome).
GO:0005634; Cellular component: nucleus (inferred from sequence or structural similarity from UniProtKB).
GO:0003785; Molecular function: actin monomer binding (inferred from physical interaction from UniProtKB).
GO:0034618; Molecular function: arginine binding (inferred from direct assay from UniProtKB).
GO:0046870; Molecular function: cadmium ion binding (non-traceable author statement from UniProtKB).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005516; Molecular function: calmodulin binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0010181; Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004517; Molecular function: nitric-oxide synthase activity (inferred from electronic annotation from InterPro).
GO:0034617; Molecular function: tetrahydrobiopterin binding (inferred from direct assay from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006916; Biological process: anti-apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0006527; Biological process: arginine catabolic process (inferred from direct assay from UniProtKB).
GO:0001974; Biological process: blood vessel remodeling (inferred from sequence or structural similarity from UniProtKB).
GO:0043542; Biological process: endothelial cell migration (inferred from mutant phenotype from UniProtKB).
GO:0007005; Biological process: mitochondrion organization (inferred from sequence or structural similarity from UniProtKB).
GO:0008285; Biological process: negative regulation of cell proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0014740; Biological process: negative regulation of muscle hyperplasia (inferred from sequence or structural similarity from UniProtKB).
GO:0010544; Biological process: negative regulation of platelet activation (non-traceable author statement from UniProtKB).
GO:0006809; Biological process: nitric oxide biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0045766; Biological process: positive regulation of angiogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0031284; Biological process: positive regulation of guanylate cyclase activity (inferred from mutant phenotype from UniProtKB).
GO:0045909; Biological process: positive regulation of vasodilation (non-traceable author statement from UniProtKB).
GO:0003100; Biological process: regulation of systemic arterial blood pressure by endothelin (inferred from mutant phenotype from UniProtKB).
GO:0034405; Biological process: response to fluid shear stress (inferred from expression pattern from UniProtKB).
GO:0009408; Biological process: response to heat (non-traceable author statement from UniProtKB).
GO:0014806; Biological process: smooth muscle hyperplasia (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR003097; FAD-binding_1.
IPR008254; Flavodoxin/NO_synth.
IPR004030; NO_synthase_oxygenase_reg.
IPR012144; NOS.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1.
Pfam PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
PF02898; NO_synthase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000333; NOS; 1.
PROSITE PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PS60001; NOS; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P29474.
ProtoNet P29474.
Genome annotation databases
Ensembl ENSG00000164867; Homo sapiens. [Contig view]
Phylogenomic databases
HOGENOM P29474; -.
HOVERGEN P29474; -.
Other
DrugBank DB00125; L-Arginine.
DB00155; L-Citrulline.
DB01098; Rosuvastatin.
DB00360; Tetrahydrobiopterin.
SOURCE NOS3; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; FAD; FMN; Golgi apparatus; Heme; Iron; Lipoprotein; Membrane; Metal-binding; Myristate; NADP; Oxidoreductase; Palmitate; Phosphoprotein; Polymorphism; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed. 
CHAIN   2   1203  1202     Nitric oxide synthase, endothelial. PRO_0000170943
DOMAIN   520    703  184     Flavodoxin-like. 
DOMAIN   756   1002  247     FAD-binding FR-type. 
NP_BIND   649    680  32     FMN (By similarity). 
NP_BIND   793    804  12     FAD (By similarity). 
NP_BIND   935    945  11     FAD (By similarity). 
NP_BIND   1010   1028  19     NADP (By similarity). 
NP_BIND   1108   1123  16     NADP (By similarity). 
REGION   98    486  389     Interaction with NOSIP. 
REGION   491    510  20     Calmodulin-binding (Potential). 
METAL   94     94        Zinc. 
METAL   99     99        Zinc. 
METAL   184    184        Iron (heme axial ligand). 
MOD_RES   81     81        Phosphotyrosine. 
MOD_RES   495    495        Phosphothreonine (By similarity). 
MOD_RES   633    633        Phosphoserine (By similarity). 
MOD_RES   1175   1175        Phosphothreonine (By similarity). 
MOD_RES   1177   1177        Phosphoserine (By similarity). 
LIPID   2      2        N-myristoyl glycine (By similarity). 
LIPID   15     15        S-palmitoyl cysteine (By similarity). 
LIPID   26     26        S-palmitoyl cysteine (By similarity). 
VARIANT   112    112  1     R -> Q (in dbSNP:rs3918166 [NCBI]). VAR_031218 [3D]
VARIANT   298    298  1     E -> D (in susceptibility to coronary spasm; dbSNP:rs1799983 [NCBI]). VAR_008037 [3D]
VARIANT   474    474  1     R -> C (in a colorectal cancer sample; somatic mutation). VAR_036303 [3D]
VARIANT   602    602  1     R -> Q (in a colorectal cancer sample; somatic mutation). VAR_036304 
VARIANT   827    827  1     V -> M (in dbSNP:rs3918232 [NCBI]). VAR_031219 
VARIANT   885    885  1     R -> M (in dbSNP:rs3918201 [NCBI]). VAR_031220 
VARIANT   982    982  1     Q -> L (in dbSNP:rs3918234 [NCBI]). VAR_031221 
CONFLICT   53     53        S -> R (in Ref. 10; AAA36373). 
CONFLICT   489    489        G -> S (in Ref. 11; AAD14336). 
CONFLICT   567    567        V -> W (in Ref. 6; CAA53950). 
CONFLICT   1150   1150        R -> RQ (in Ref. 7; BAA05652).