Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Nitric oxide synthase, brain  

UniProtKB / Swiss-Prot ID :  NOS1_RAT

Gene Name (Synonyms) : 
Nos1, Bnos  

Species :  Rattus norvegicus (Rat). 

Subcellular Localization :  Cell membrane, sarcolemma; Peripheral membrane protein (By similarity). Cell projection, dendritic spine (By similarity). Note=In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glyco 

Protein Function :  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. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Inhibitory transmitter for non- adrenergic and non-cholinergic nerves in the colorectum. 

Protein Sequence MEENTFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNDR...
Predicted Secondary Structure CCCCCCCCCCCCCCEEEEEEEECCCCCEEEEEEECCCCCCEEEEEECCCCHHHHCCCCCCCCEEEEECCE...
Protein Variant -
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
24N6-acetyllysineLFKRKVGGL
EEECCCCCE
45.91Phosphositeplus
Link
33N6-acetyllysineGFLVKERVS
EEEEEECCC
41.78Phosphositeplus
Link
38N6-acetyllysineERVSKPPVI
ECCCCCCEE
50.95Phosphositeplus
Link
131N6-acetyllysineGPPTKAVDL
CCCCCCCCC
52.79Phosphositeplus
Link
229N6-acetyllysineKAEMKDTGI
CCCCEECCC
43.58Phosphositeplus
Link-
245N6-acetyllysineGKSHKAPPL
CCCCCCCCC
70.45Phosphositeplus
Link-
374Phosphoserine (PKA_group)KRFGSKAHM
HCCCCHHHH
24.77PhosphoELM
Link-
741PhosphoserineAVKFSAKLM
HHHHHHHHH
20.83Phosphositeplus
Link-
754N6-acetyllysineAKRVKATIL
CCCCEEEEE
43.79Phosphositeplus
Link-
847PhosphoserineVRFNSVSSY
CCCCCHHHH
22.21Phosphositeplus
Link-
847Phosphoserine (RSK_group)VRFNSVSSY
CCCCCHHHH
22.21PhosphoELM
Link-
856N6-acetyllysineSDSRKSSGD
HHHHHHCCC
53.58Phosphositeplus
Link-
989N6-acetyllysineSNVHKKRVS
CCCCCCCCC
37.68Phosphositeplus
Link-
1296PhosphothreonineYREETLQAK
HHHHHHHHH
21.29Phosphositeplus
Link-
1300N6-acetyllysineTLQAKNKGV
HHHHHCCCC
46.35Phosphositeplus
Link-
1321N6-acetyllysineDRPKKYVQD
CCCCEEEEH
54.02Phosphositeplus
Link-
1371N6-acetyllysineTQQGKLSEE
HHHCCCCHH
44.49Phosphositeplus
Link-
1412PhosphoserineLRSESIAFI
HHHHHHHHH
22.06Phosphositeplus
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Drug Reference
- top -
Related Literatures of Post-Translational Modification
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures