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P29475

- NOS1_HUMAN

UniProt

P29475 - NOS1_HUMAN

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Protein
Nitric oxide synthase, brain
Gene
NOS1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

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 n-Nos-inhibiting protein (PIN) which may prevent the dimerization of the protein. Inhibited by NOSIP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi420 – 4201Iron (heme axial ligand) By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi886 – 91732FMN By similarity
Add
BLAST
Nucleotide bindingi1032 – 104312FAD By similarity
Add
BLAST
Nucleotide bindingi1175 – 118511FAD By similarity
Add
BLAST
Nucleotide bindingi1250 – 126819NADP By similarity
Add
BLAST
Nucleotide bindingi1348 – 136316NADP By similarity
Add
BLAST

GO - Molecular functioni

  1. FMN binding Source: BHF-UCL
  2. NADP binding Source: BHF-UCL
  3. NADPH-hemoprotein reductase activity Source: RefGenome
  4. arginine binding Source: BHF-UCL
  5. cadmium ion binding Source: BHF-UCL
  6. flavin adenine dinucleotide binding Source: BHF-UCL
  7. heme binding Source: BHF-UCL
  8. ion channel binding Source: BHF-UCL
  9. iron ion binding Source: InterPro
  10. nitric-oxide synthase activity Source: BHF-UCL
  11. oxidoreductase activity Source: RefGenome
  12. protein binding Source: UniProtKB
  13. scaffold protein binding Source: BHF-UCL
  14. sodium channel regulator activity Source: BHF-UCL
  15. tetrahydrobiopterin binding Source: BHF-UCL

GO - Biological processi

  1. arginine catabolic process Source: BHF-UCL
  2. blood coagulation Source: Reactome
  3. cellular response to growth factor stimulus Source: Ensembl
  4. exogenous drug catabolic process Source: Ensembl
  5. interaction with host Source: Reactome
  6. multicellular organismal response to stress Source: BHF-UCL
  7. myoblast fusion Source: BHF-UCL
  8. negative regulation of blood pressure Source: RefGenome
  9. negative regulation of calcium ion transport into cytosol Source: BHF-UCL
  10. negative regulation of hydrolase activity Source: Ensembl
  11. negative regulation of potassium ion transport Source: Ensembl
  12. negative regulation of serotonin uptake Source: Ensembl
  13. neurotransmitter biosynthetic process Source: BHF-UCL
  14. nitric oxide biosynthetic process Source: BHF-UCL
  15. nitric oxide mediated signal transduction Source: RefGenome
  16. peptidyl-cysteine S-nitrosylation Source: BHF-UCL
  17. phagosome maturation Source: Reactome
  18. positive regulation of guanylate cyclase activity Source: RefGenome
  19. positive regulation of histone acetylation Source: Ensembl
  20. positive regulation of sodium ion transmembrane transport Source: BHF-UCL
  21. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  22. positive regulation of vasodilation Source: BHF-UCL
  23. regulation of cardiac muscle contraction Source: BHF-UCL
  24. response to heat Source: BHF-UCL
  25. response to hypoxia Source: BHF-UCL
  26. striated muscle contraction Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:HS01647-MONOMER.
ReactomeiREACT_121256. Phagosomal maturation (early endosomal stage).
REACT_23862. Nitric oxide stimulates guanylate cyclase.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitric oxide synthase, brain (EC:1.14.13.39)
Alternative name(s):
Constitutive NOS
NC-NOS
NOS type I
Neuronal NOS
Short name:
N-NOS
Short name:
nNOS
Peptidyl-cysteine S-nitrosylase NOS1
bNOS
Gene namesi
Name:NOS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:7872. NOS1.

Subcellular locationi

Cell membranesarcolemma; Peripheral membrane protein. Cell projectiondendritic spine By similarity
Note: In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glycoprotein complex. In neurons, enriched in dendritic spines By similarity.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytoskeleton Source: BHF-UCL
  3. cytosol Source: Reactome
  4. dendritic spine Source: UniProtKB-SubCell
  5. perinuclear region of cytoplasm Source: BHF-UCL
  6. photoreceptor inner segment Source: BHF-UCL
  7. protein complex Source: BHF-UCL
  8. sarcolemma Source: BHF-UCL
  9. sarcoplasmic reticulum Source: BHF-UCL
  10. synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA252.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14341434Nitric oxide synthase, brain
PRO_0000170921Add
BLAST

Post-translational modificationi

Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and Hsp40 (in vitro) By similarity.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP29475.
PaxDbiP29475.
PRIDEiP29475.

PTM databases

PhosphoSiteiP29475.

Miscellaneous databases

PMAP-CutDBP29475.

Expressioni

Tissue specificityi

Isoform 1 is ubiquitously expressed: detected in skeletal muscle and brain, also in testis, lung and kidney, and at low levels in heart, adrenal gland and retina. Not detected in the platelets. Isoform 3 is expressed only in testis. Isoform 4 is detected in testis, skeletal muscle, lung, and kidney, at low levels in the brain, but not in the heart and adrenal gland.

Gene expression databases

ArrayExpressiP29475.
BgeeiP29475.
CleanExiHS_NOS1.
GenevestigatoriP29475.

Organism-specific databases

HPAiCAB002167.

Interactioni

Subunit structurei

Homodimer. Interacts with DLG4; the interaction possibly being prevented by the association between NOS1 and CAPON. Forms a ternary complex with CAPON and RASD1. Forms a ternary complex with CAPON and SYN1. Interacts with ZDHHC23. Interacts with NOSIP; which may impair its synaptic location By similarity. Interacts with HTR4. Interacts with VAC14 By similarity. Interacts with SLC6A4 By similarity. Interacts (via N-terminal domain) with DLG4 (via N-terminal tandem pair of PDZ domains) By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
VAC14Q08AM65EBI-7164065,EBI-2107455

Protein-protein interaction databases

BioGridi110905. 17 interactions.
IntActiP29475. 3 interactions.
MINTiMINT-122019.
STRINGi9606.ENSP00000320758.

Structurei

3D structure databases

ProteinModelPortaliP29475.
SMRiP29475. Positions 12-126, 303-721, 755-1418.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 9983PDZ
Add
BLAST
Domaini760 – 940181Flavodoxin-like
Add
BLAST
Domaini995 – 1242248FAD-binding FR-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 205205Interaction with NOSIP By similarity
Add
BLAST
Regioni163 – 24583PIN (nNOS-inhibiting protein) binding
Add
BLAST
Regioni730 – 75021Calmodulin-binding Reviewed prediction
Add
BLAST
Regioni755 – 77420Tetrahydrobiopterin-binding By similarity
Add
BLAST

Domaini

The PDZ domain in the N-terminal part of the neuronal isoform participates in protein-protein interaction, and is responsible for targeting nNos to synaptic membranes in muscles. Mediates interaction with VAC14 By similarity.

Sequence similaritiesi

Belongs to the NOS family.
Contains 1 PDZ (DHR) domain.

Phylogenomic databases

eggNOGiCOG4362.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
KOiK13240.
OMAiNQMVKVE.
OrthoDBiEOG79SDW7.
PhylomeDBiP29475.
TreeFamiTF324410.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
2.30.42.10. 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.
IPR001478. PDZ.
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.
PF00595. PDZ. 1 hit.
[Graphical view]
PIRSFiPIRSF000333. NOS. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF52218. 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.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Isoform 3 is produced by different alternative splicing events implicating either the untranslated exons TEX1 (TN-NOS) or TEX1B (TN-NOSB) leading to a N-terminally truncated protein which possesses enzymatic activity comparable to that of isoform 1. The C-terminally truncated isoform 4 is produced by insertion of the TEX2 exon between exons 3 and 4 of isoform 1, leading to a frameshift and a premature stop codon.

Isoform 1 (identifier: P29475-1) [UniParc]FASTAAdd to Basket

Also known as: N-NOS-1

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

MEDHMFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG     50
AAEQSGLIQA GDIILAVNGR PLVDLSYDSA LEVLRGIASE THVVLILRGP 100
EGFTTHLETT FTGDGTPKTI RVTQPLGPPT KAVDLSHQPP AGKEQPLAVD 150
GASGPGNGPQ HAYDDGQEAG SLPHANGLAP RPPGQDPAKK ATRVSLQGRG 200
ENNELLKEIE PVLSLLTSGS RGVKGGAPAK AEMKDMGIQV DRDLDGKSHK 250
PLPLGVENDR VFNDLWGKGN VPVVLNNPYS EKEQPPTSGK QSPTKNGSPS 300
KCPRFLKVKN WETEVVLTDT LHLKSTLETG CTEYICMGSI MHPSQHARRP 350
EDVRTKGQLF PLAKEFIDQY YSSIKRFGSK AHMERLEEVN KEIDTTSTYQ 400
LKDTELIYGA KHAWRNASRC VGRIQWSKLQ VFDARDCTTA HGMFNYICNH 450
VKYATNKGNL RSAITIFPQR TDGKHDFRVW NSQLIRYAGY KQPDGSTLGD 500
PANVQFTEIC IQQGWKPPRG RFDVLPLLLQ ANGNDPELFQ IPPELVLEVP 550
IRHPKFEWFK DLGLKWYGLP AVSNMLLEIG GLEFSACPFS GWYMGTEIGV 600
RDYCDNSRYN ILEEVAKKMN LDMRKTSSLW KDQALVEINI AVLYSFQSDK 650
VTIVDHHSAT ESFIKHMENE YRCRGGCPAD WVWIVPPMSG SITPVFHQEM 700
LNYRLTPSFE YQPDPWNTHV WKGTNGTPTK RRAIGFKKLA EAVKFSAKLM 750
GQAMAKRVKA TILYATETGK SQAYAKTLCE IFKHAFDAKV MSMEEYDIVH 800
LEHETLVLVV TSTFGNGDPP ENGEKFGCAL MEMRHPNSVQ EERKSYKVRF 850
NSVSSYSDSQ KSSGDGPDLR DNFESAGPLA NVRFSVFGLG SRAYPHFCAF 900
GHAVDTLLEE LGGERILKMR EGDELCGQEE AFRTWAKKVF KAACDVFCVG 950
DDVNIEKANN SLISNDRSWK RNKFRLTFVA EAPELTQGLS NVHKKRVSAA 1000
RLLSRQNLQS PKSSRSTIFV RLHTNGSQEL QYQPGDHLGV FPGNHEDLVN 1050
ALIERLEDAP PVNQMVKVEL LEERNTALGV ISNWTDELRL PPCTIFQAFK 1100
YYLDITTPPT PLQLQQFASL ATSEKEKQRL LVLSKGLQEY EEWKWGKNPT 1150
IVEVLEEFPS IQMPATLLLT QLSLLQPRYY SISSSPDMYP DEVHLTVAIV 1200
SYRTRDGEGP IHHGVCSSWL NRIQADELVP CFVRGAPSFH LPRNPQVPCI 1250
LVGPGTGIAP FRSFWQQRQF DIQHKGMNPC PMVLVFGCRQ SKIDHIYREE 1300
TLQAKNKGVF RELYTAYSRE PDKPKKYVQD ILQEQLAESV YRALKEQGGH 1350
IYVCGDVTMA ADVLKAIQRI MTQQGKLSAE DAGVFISRMR DDNRYHEDIF 1400
GVTLRTYEVT NRLRSESIAF IEESKKDTDE VFSS 1434
Length:1,434
Mass (Da):160,970
Last modified:October 1, 1996 - v2
Checksum:i99235793B953BF37
GO
Isoform 2 (identifier: P29475-2) [UniParc]FASTAAdd to Basket

Also known as: N-NOS-2

The sequence of this isoform differs from the canonical sequence as follows:
     509-613: Missing.

Show »
Length:1,329
Mass (Da):148,919
Checksum:iDF791B80FDB12302
GO
Isoform 3 (identifier: P29475-3) [UniParc]FASTAAdd to Basket

Also known as: TN-NOS, TN-NOSB

The sequence of this isoform differs from the canonical sequence as follows:
     1-336: Missing.

Show »
Length:1,098
Mass (Da):125,113
Checksum:iA1CD5C5012436233
GO
Isoform 4 (identifier: P29475-4) [UniParc]FASTAAdd to Basket

Also known as: TEX2-insertion

The sequence of this isoform differs from the canonical sequence as follows:
     285-407: PPTSGKQSPT...TYQLKDTELI → MRKLRITEGF...PKPTWKGWKR
     408-1434: Missing.

Show »
Length:407
Mass (Da):43,838
Checksum:i7E9420C658EFACD2
GO
Isoform 5 (identifier: P29475-5) [UniParc]FASTAAdd to Basket

Also known as: nNOSmu

The sequence of this isoform differs from the canonical sequence as follows:
     844-844: K → KYPEPLRFFPRKGPPLPNGDTEVHGLAAARDSQHR

Show »
Length:1,468
Mass (Da):164,779
Checksum:i95906AC90699A0E2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti228 – 2281P → S.1 Publication
Corresponds to variant rs9658279 [ dbSNP | Ensembl ].
VAR_018948
Natural varianti394 – 3941D → A.1 Publication
Corresponds to variant rs9658356 [ dbSNP | Ensembl ].
VAR_018949
Natural varianti725 – 7251N → D.1 Publication
Corresponds to variant rs9658403 [ dbSNP | Ensembl ].
VAR_018950
Natural varianti864 – 8641G → D.1 Publication
Corresponds to variant rs9658445 [ dbSNP | Ensembl ].
VAR_018951
Natural varianti1064 – 10641Q → R.1 Publication
Corresponds to variant rs9658482 [ dbSNP | Ensembl ].
VAR_018952

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 336336Missing in isoform 3.
VSP_003571Add
BLAST
Alternative sequencei285 – 407123PPTSG…DTELI → MRKLRITEGFGVQRGSHNHP PPQENSPPQRMAAPPSVHAS SRSRTGRLRWFSLTPSTLRA HWKRDALSTSAWAPSCILLS MQGGLKTSAQKDSSSLSPKS LLINTIHQLKDLAPKPTWKG WKR in isoform 4.
VSP_003572Add
BLAST
Alternative sequencei408 – 14341027Missing in isoform 4.
VSP_003573Add
BLAST
Alternative sequencei509 – 613105Missing in isoform 2.
VSP_003574Add
BLAST
Alternative sequencei844 – 8441K → KYPEPLRFFPRKGPPLPNGD TEVHGLAAARDSQHR in isoform 5.
VSP_044916

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311K → E in AAB49040. 1 Publication
Sequence conflicti178 – 1847LAPRPPG → WPQAPR1 Publication
Sequence conflicti178 – 1847LAPRPPG → WPQAPR1 Publication
Sequence conflicti492 – 4932QP → HR in AAA36376. 1 Publication
Sequence conflicti549 – 5491V → L in AAA36376. 1 Publication
Sequence conflicti563 – 5631G → A in AAA36376. 1 Publication
Sequence conflicti1407 – 14071Y → I in AAA36376. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U17327 mRNA. Translation: AAA62405.1.
U17326
, U17299, U17300, U17301, U17302, U17303, U17304, U17305, U17307, U17308, U17309, U17310, U17311, U17312, U17313, U17314, U17315, U17316, U17317, U17318, U17319, U17320, U17321, U17322, U17323, U17324, U17325 Genomic DNA. Translation: AAB60654.1. Sequence problems.
D16408 mRNA. Translation: BAA03895.1.
L02881 mRNA. Translation: AAA36376.1.
U31466 mRNA. Translation: AAB49040.1.
U66362 Genomic DNA. No translation available.
AY445095 Genomic DNA. Translation: AAR07069.1.
AC026364 Genomic DNA. No translation available.
AC068799 Genomic DNA. No translation available.
AC073864 Genomic DNA. No translation available.
AJ004918 mRNA. Translation: CAA06218.1.
CCDSiCCDS41842.1. [P29475-1]
CCDS55890.1. [P29475-5]
PIRiG01946.
RefSeqiNP_000611.1. NM_000620.4. [P29475-1]
NP_001191142.1. NM_001204213.1. [P29475-3]
NP_001191143.1. NM_001204214.1. [P29475-3]
NP_001191147.1. NM_001204218.1. [P29475-5]
XP_006719489.1. XM_006719426.1. [P29475-5]
XP_006719490.1. XM_006719427.1. [P29475-5]
XP_006719491.1. XM_006719428.1. [P29475-1]
UniGeneiHs.654410.
Hs.684465.
Hs.684466.
Hs.684467.
Hs.735734.

Genome annotation databases

EnsembliENST00000317775; ENSP00000320758; ENSG00000089250. [P29475-1]
ENST00000338101; ENSP00000337459; ENSG00000089250. [P29475-5]
GeneIDi4842.
KEGGihsa:4842.
UCSCiuc001twm.2. human. [P29475-1]

Polymorphism databases

DMDMi1709333.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Nitric oxide synthase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U17327 mRNA. Translation: AAA62405.1 .
U17326
, U17299 , U17300 , U17301 , U17302 , U17303 , U17304 , U17305 , U17307 , U17308 , U17309 , U17310 , U17311 , U17312 , U17313 , U17314 , U17315 , U17316 , U17317 , U17318 , U17319 , U17320 , U17321 , U17322 , U17323 , U17324 , U17325 Genomic DNA. Translation: AAB60654.1 . Sequence problems.
D16408 mRNA. Translation: BAA03895.1 .
L02881 mRNA. Translation: AAA36376.1 .
U31466 mRNA. Translation: AAB49040.1 .
U66362 Genomic DNA. No translation available.
AY445095 Genomic DNA. Translation: AAR07069.1 .
AC026364 Genomic DNA. No translation available.
AC068799 Genomic DNA. No translation available.
AC073864 Genomic DNA. No translation available.
AJ004918 mRNA. Translation: CAA06218.1 .
CCDSi CCDS41842.1. [P29475-1 ]
CCDS55890.1. [P29475-5 ]
PIRi G01946.
RefSeqi NP_000611.1. NM_000620.4. [P29475-1 ]
NP_001191142.1. NM_001204213.1. [P29475-3 ]
NP_001191143.1. NM_001204214.1. [P29475-3 ]
NP_001191147.1. NM_001204218.1. [P29475-5 ]
XP_006719489.1. XM_006719426.1. [P29475-5 ]
XP_006719490.1. XM_006719427.1. [P29475-5 ]
XP_006719491.1. XM_006719428.1. [P29475-1 ]
UniGenei Hs.654410.
Hs.684465.
Hs.684466.
Hs.684467.
Hs.735734.

3D structure databases

ProteinModelPortali P29475.
SMRi P29475. Positions 12-126, 303-721, 755-1418.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110905. 17 interactions.
IntActi P29475. 3 interactions.
MINTi MINT-122019.
STRINGi 9606.ENSP00000320758.

Chemistry

BindingDBi P29475.
ChEMBLi CHEMBL2096621.
DrugBanki DB00155. L-Citrulline.
GuidetoPHARMACOLOGYi 1251.

PTM databases

PhosphoSitei P29475.

Polymorphism databases

DMDMi 1709333.

Proteomic databases

MaxQBi P29475.
PaxDbi P29475.
PRIDEi P29475.

Protocols and materials databases

DNASUi 4842.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000317775 ; ENSP00000320758 ; ENSG00000089250 . [P29475-1 ]
ENST00000338101 ; ENSP00000337459 ; ENSG00000089250 . [P29475-5 ]
GeneIDi 4842.
KEGGi hsa:4842.
UCSCi uc001twm.2. human. [P29475-1 ]

Organism-specific databases

CTDi 4842.
GeneCardsi GC12M117636.
HGNCi HGNC:7872. NOS1.
HPAi CAB002167.
MIMi 163731. gene.
neXtProti NX_P29475.
PharmGKBi PA252.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4362.
HOGENOMi HOG000220884.
HOVERGENi HBG000159.
KOi K13240.
OMAi NQMVKVE.
OrthoDBi EOG79SDW7.
PhylomeDBi P29475.
TreeFami TF324410.

Enzyme and pathway databases

BioCyci MetaCyc:HS01647-MONOMER.
Reactomei REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_23862. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

ChiTaRSi NOS1. human.
GeneWikii NOS1.
GenomeRNAii 4842.
NextBioi 18658.
PMAP-CutDB P29475.
PROi P29475.
SOURCEi Search...

Gene expression databases

ArrayExpressi P29475.
Bgeei P29475.
CleanExi HS_NOS1.
Genevestigatori P29475.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
2.30.42.10. 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.
IPR001478. PDZ.
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.
PF00595. PDZ. 1 hit.
[Graphical view ]
PIRSFi PIRSF000333. NOS. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SMARTi SM00228. PDZ. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
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.
PS50106. PDZ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural organization of the human neuronal nitric oxide synthase gene (NOS1)."
    Hall A.V., Antoniou H., Wang Y., Cheung A.H., Arbus A.M., Olson S.L., Lu W.C., Kau C.-L., Marsden P.A.
    J. Biol. Chem. 269:33082-33090(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  2. "Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines."
    Fujisawa H., Ogura T., Kurashima Y., Yokoyama T., Yamashita J., Esumi H.
    J. Neurochem. 63:140-145(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Cerebellum.
  3. "Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle."
    Nakane M., Schmidt H.H.H.W., Pollock J.S., Foerstermann U., Murad F.
    FEBS Lett. 316:175-180(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  4. "Neuronal isoform of nitric oxide synthase is expressed at low levels in human retina."
    Park C.-S., Gianotti C., Park R., Krishna G.
    Cell. Mol. Neurobiol. 16:499-515(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  5. "A novel, testis-specific mRNA transcript encoding an NH2-terminal truncated nitric-oxide synthase."
    Wang Y., Goligorsky M.S., Lin M., Wilcox J.N., Marsden P.A.
    J. Biol. Chem. 272:11392-11401(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3 AND 4).
    Tissue: Testis.
  6. NIEHS SNPs program
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-228; ALA-394; ASP-725; ASP-864 AND ARG-1064.
  7. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Isolation and characterization of a novel, human neuronal nitric oxide synthase cDNA."
    Larsson B., Phillips S.C.
    Biochem. Biophys. Res. Commun. 251:898-902(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 835-901 (ISOFORM 5), ALTERNATIVE SPLICING.
    Tissue: Skeletal muscle.

Entry informationi

Entry nameiNOS1_HUMAN
AccessioniPrimary (citable) accession number: P29475
Secondary accession number(s): E9PH30, O75713
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 163 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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