CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024056
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nitric oxide synthase, brain 
Protein Synonyms/Alias
 Constitutive NOS; NC-NOS; NOS type I; Neuronal NOS; N-NOS; nNOS; Peptidyl-cysteine S-nitrosylase NOS1; bNOS 
Gene Name
 Nos1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
24SVRLFKRKVGGLGFLubiquitination[1]
33GGLGFLVKERVSKPPubiquitination[1]
143SRQPSASKDQPLAVDubiquitination[1]
188DPTMKNTKANLQDSGubiquitination[1]
225VNRGGPAKAEMKDTGubiquitination[1]
229GPAKAEMKDTGIQVDubiquitination[1]
245DLDGKLHKAPPLGGEubiquitination[1]
370DQYYSSIKRFGSKAHubiquitination[1]
386DRLEEVNKEIESTSTubiquitination[1]
743EAVKFSAKLMGQAMAubiquitination[1]
1371RIMTQQGKLSEEDAGubiquitination[1]
Reference
 [1] Ubiquitination of neuronal nitric-oxide synthase in the calmodulin-binding site triggers proteasomal degradation of the protein.
 Clapp KM, Peng HM, Jenkins GJ, Ford MJ, Morishima Y, Lau M, Osawa Y.
 J Biol Chem. 2012 Dec 14;287(51):42601-10. [PMID: 23109339] 
Functional Description
 Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Isoform NNOS Mu may be an effector enzyme for the dystrophin complex. 
Sequence Annotation
 DOMAIN 17 99 PDZ.
 DOMAIN 755 935 Flavodoxin-like.
 DOMAIN 990 1237 FAD-binding FR-type.
 NP_BIND 881 912 FMN (By similarity).
 NP_BIND 1027 1038 FAD (By similarity).
 NP_BIND 1170 1180 FAD (By similarity).
 NP_BIND 1245 1263 NADP (By similarity).
 NP_BIND 1343 1358 NADP (By similarity).
 REGION 1 200 Interaction with NOSIP (By similarity).
 REGION 163 240 PIN (nNOS-inhibiting protein) binding (By
 REGION 725 745 Calmodulin-binding.
 REGION 750 769 Tetrahydrobiopterin-binding (By
 METAL 415 415 Iron (heme axial ligand) (By similarity).  
Keyword
 3D-structure; Alternative splicing; Calmodulin-binding; Cell membrane; Cell projection; Complete proteome; FAD; FMN; Heme; Iron; Membrane; Metal-binding; NADP; Oxidoreductase; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1429 AA 
Protein Sequence
MEEHTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA 60
GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI 120
RVTQPLGTPT KAVDLSRQPS ASKDQPLAVD RVPGPSNGPQ HAQGRGQGAG SVSQANGVAI 180
DPTMKNTKAN LQDSGEQDEL LKEIEPVLSI LTGGGKAVNR GGPAKAEMKD TGIQVDRDLD 240
GKLHKAPPLG GENDRVFNDL WGKGNVPVVL NNPYSENEQS PASGKQSPTK NGSPSRCPRF 300
LKVKNWETDV VLTDTLHLKS TLETGCTEQI CMGSIMLPSH HIRKSEDVRT KDQLFPLAKE 360
FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ 420
WSKLQVFDAR DCTTAHGMFN YICNHVKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI 480
RYAGYKQPDG STLGDPANVE FTEICIQQGW KPPRGRFDVL PLLLQANGND PELFQIPPEL 540
VLEVPIRHPK FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD 600
NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD HHSATESFIK 660
HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL TPSFEYQPDP WNTHVWKGTN 720
GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA KRVKATILYA TETGKSQAYA KTLCEIFKHA 780
FDAKAMSMEE YDIVHLEHEA LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS 840
YKVRFNSVSS YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD 900
TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI EKANNSLISN 960
DRSWKRNKFR LTYVAEAPEL TQGLSNVHKK RVSAARLLSR QNLQSPKSSR STIFVRLHTN 1020
GNQELQYQPG DHLGVFPGNH EDLVNALIER LEDAPPANHV VKVEMLEERN TALGVISNWK 1080
DESRLPPCTI FQAFKYYLDI TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW 1140
GKNPTMVEVL EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR 1200
DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG TGIAPFRSFW 1260
QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK NKGVFRELYT AYSREPDRPK 1320
KYVQDVLQEQ LAESVYRALK EQGGHIYVCG DVTMAADVLK AIQRIMTQQG KLSEEDAGVF 1380
ISRLRDDNRY HEDIFGVTLR TYEVTNRLRS ESIAFIEESK KDTDEVFSS 1429 
Gene Ontology
 GO:0005856; C:cytoskeleton; IDA:BHF-UCL.
 GO:0005829; C:cytosol; IBA:RefGenome.
 GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; ISO:MGI.
 GO:0042383; C:sarcolemma; IDA:BHF-UCL.
 GO:0016529; C:sarcoplasmic reticulum; IEA:Compara.
 GO:0045202; C:synapse; IDA:MGI.
 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:0003958; F:NADPH-hemoprotein reductase activity; IBA:RefGenome.
 GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL.
 GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
 GO:0042738; P:exogenous drug catabolic process; IMP:MGI.
 GO:0033555; P:multicellular organismal response to stress; IEA:Compara.
 GO:0045776; P:negative regulation of blood pressure; IBA:RefGenome.
 GO:0051926; P:negative regulation of calcium ion transport; IMP:MGI.
 GO:0051346; P:negative regulation of hydrolase activity; IMP:MGI.
 GO:0043267; P:negative regulation of potassium ion transport; IMP:MGI.
 GO:0051612; P:negative regulation of serotonin uptake; IDA:UniProtKB.
 GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL.
 GO:0007263; P:nitric oxide mediated signal transduction; IBA:RefGenome.
 GO:0018119; P:peptidyl-cysteine S-nitrosylation; IDA:MGI.
 GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:RefGenome.
 GO:0035066; P:positive regulation of histone acetylation; IMP:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
 GO:0045909; P:positive regulation of vasodilation; IBA:RefGenome.
 GO:0002028; P:regulation of sodium ion transport; IMP:MGI.
 GO:0009408; P:response to heat; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0006941; P:striated muscle contraction; IMP:MGI. 
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.
 IPR001478; PDZ.
 IPR017938; Riboflavin_synthase-like_b-brl. 
Pfam
 PF00667; FAD_binding_1
 PF00258; Flavodoxin_1
 PF00175; NAD_binding_1
 PF02898; NO_synthase
 PF00595; PDZ 
SMART
 SM00228; PDZ 
PROSITE
 PS51384; FAD_FR
 PS50902; FLAVODOXIN_LIKE
 PS60001; NOS
 PS50106; PDZ 
PRINTS
 PR00369; FLAVODOXIN.
 PR00371; FPNCR.