CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005788
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nitric oxide synthase, endothelial 
Protein Synonyms/Alias
 Constitutive NOS; cNOS; EC-NOS; Endothelial NOS; eNOS; NOS type III; NOSIII 
Gene Name
 NOS3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Bos taurus (Bovine) 
NCBI Taxa ID
 9913 
Lysine Modification
Position
Peptide
Type
References
609SPRPEQHKSYKIRFNacetylation[1]
Reference
 [1] Histone deacetylase 3 antagonizes aspirin-stimulated endothelial nitric oxide production by reversing aspirin-induced lysine acetylation of endothelial nitric oxide synthase.
 Jung SB, Kim CS, Naqvi A, Yamamori T, Mattagajasingh I, Hoffman TA, Cole MP, Kumar A, Dericco JS, Jeon BH, Irani K.
 Circ Res. 2010 Oct 1;107(7):877-87. [PMID: 20705923] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 522 705 Flavodoxin-like.
 DOMAIN 758 1004 FAD-binding FR-type.
 NP_BIND 651 682 FMN (By similarity).
 NP_BIND 795 806 FAD (By similarity).
 NP_BIND 937 947 FAD (By similarity).
 NP_BIND 1012 1030 NADP (By similarity).
 NP_BIND 1110 1125 NADP (By similarity).
 REGION 100 488 Interaction with NOSIP (By similarity).
 REGION 492 512 Calmodulin-binding (Potential).
 METAL 96 96 Zinc.
 METAL 101 101 Zinc.
 METAL 186 186 Iron (heme axial ligand).
 MOD_RES 116 116 Phosphoserine; by CDK5 (By similarity).
 MOD_RES 143 143 Phosphoserine; by PKA.
 MOD_RES 497 497 Phosphothreonine; by AMPK and PKA.
 MOD_RES 635 635 Phosphoserine.
 MOD_RES 1177 1177 Phosphothreonine (By similarity).
 MOD_RES 1179 1179 Phosphoserine; by AMPK, PDPK1 and PKA.
 LIPID 2 2 N-myristoyl glycine.
 LIPID 15 15 S-palmitoyl cysteine.
 LIPID 26 26 S-palmitoyl cysteine.  
Keyword
 3D-structure; Blood coagulation; Calcium; Calmodulin-binding; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; FAD; FMN; Golgi apparatus; Heme; Hemostasis; Iron; Lipoprotein; Membrane; Metal-binding; Myristate; NADP; Oxidoreductase; Palmitate; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1205 AA 
Protein Sequence
MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSR APAPATPHAP DHSPAPNSPT 60
LTRPPEGPKF PRVKNWELGS ITYDTLCAQS QQDGPCTPRC CLGSLVLPRK LQTRPSPGPP 120
PAEQLLSQAR DFINQYYSSI KRSGSQAHEE RLQEVEAEVA STGTYHLRES ELVFGAKQAW 180
RNAPRCVGRI QWGKLQVFDA RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRAPGR 240
GDFRIWNSQL VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE 300
APELFVLPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF SAAPFSGWYM 360
STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA AVEINLAVLH SFQLAKVTIV 420
DHHAATVSFM KHLDNEQKAR GGCPADWAWI VPPISGSLTP VFHQEMVNYI LSPAFRYQPD 480
PWKGSATKGA GITRKKTFKE VANAVKISAS LMGTLMAKRV KATILYASET GRAQSYAQQL 540
GRLFRKAFDP RVLCMDEYDV VSLEHEALVL VVTSTFGNGD PPENGESFAA ALMEMSGPYN 600
SSPRPEQHKS YKIRFNSVSC SDPLVSSWRR KRKESSNTDS AGALGTLRFC VFGLGSRAYP 660
HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFRGW AKAAFQASCE TFCVGEEAKA 720
AAQDIFSPKR SWKRQRYRLS TQAEGLQLLP GLIHVHRRKM FQATVLSVEN LQSSKSTRAT 780
ILVRLDTAGQ EGLQYQPGDH IGICPPNRPG LVEALLSRVE DPPPPTESVA VEQLEKGSPG 840
GPPPSWVRDP RLPPCTLRQA LTFFLDITSP PSPRLLRLLS TLAEEPSEQQ ELETLSQDPR 900
RYEEWKWFRC PTLLEVLEQF PSVALPAPLL LTQLPLLQPR YYSVSSAPNA HPGEVHLTVA 960
VLAYRTQDGL GPLHYGVCST WLSQLKTGDP VPCFIRGAPS FRLPPDPYVP CILVGPGTGI 1020
APFRGFWQER LHDIESKGLQ PAPMTLVFGC RCSQLDHLYR DEVQDAQERG VFGRVLTAFS 1080
REPDSPKTYV QDILRTELAA EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGDME 1140
LDEAGDVIGV LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWAFDPPGP 1200
DTPGP 1205 
Gene Ontology
 GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0010181; F:FMN binding; IEA:InterPro.
 GO:0020037; F:heme binding; IEA:InterPro.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL.
 GO:0006527; P:arginine catabolic process; IDA:BHF-UCL.
 GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
 GO:0007005; P:mitochondrion organization; IMP:BHF-UCL.
 GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
 GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL.
 GO:0031284; P:positive regulation of guanylate cyclase activity; IMP:BHF-UCL. 
Interpro
 IPR003097; FAD-binding_1.
 IPR017927; Fd_Rdtase_FAD-bd.
 IPR001094; Flavdoxin.
 IPR008254; Flavodoxin/NO_synth.
 IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
 IPR023173; NADPH_Cyt_P450_Rdtase_dom3.
 IPR004030; NO_synthase_oxygenase_dom.
 IPR026009; NOS.
 IPR012144; NOS_met.
 IPR001433; OxRdtase_FAD/NAD-bd.
 IPR017938; Riboflavin_synthase-like_b-brl. 
Pfam
 PF00667; FAD_binding_1
 PF00258; Flavodoxin_1
 PF00175; NAD_binding_1
 PF02898; NO_synthase 
SMART
  
PROSITE
 PS51384; FAD_FR
 PS50902; FLAVODOXIN_LIKE
 PS60001; NOS 
PRINTS
 PR00369; FLAVODOXIN.
 PR00371; FPNCR.