Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Phototropin-1  

UniProtKB / Swiss-Prot ID :  PHOT1_ARATH

Gene Name (Synonyms) : 
PHOT1, JK224, NPH1, RPT1 At3g45780T6D9_110  

Species :  Arabidopsis thaliana (Mouse-ear cress). 

Subcellular Localization :  Cell membrane; Peripheral membrane protein. Cytoplasm. 

Protein Function :  Protein kinase that acts as a blue-light photoreceptor in a signal-transduction pathway for photo-induced movements. Required for blue-light mediated mRNA destabilization. Mediates calcium spiking of extracellular origin in response to low rate of blue light. Mediates also rapid membrane depolarization and growth inhibition in response to blue light. Necessary for root phototropism. Involved in hypocotyl phototropism under low rate but not under high rate blue light. Contributes to the chloroplast accumulation but seems to be not required for chloroplast translocation. Regulates stomata opening and photomorphogenesis response of leaf tissue. Confers sensitivity to drought. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening. 

Protein Sequence MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPDNPVFRPEPPAWQNLSDPRGTSPQPRPQQEPAPS...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCEEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant -
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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
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
58Phosphoserine.PRGTSPQPR
CCCCCCCCC
25.10UniProtKB
Link-
170Phosphoserine.SGEMSDGDV
HHCCCCCCC
33.85UniProtKB
Link-
185Phosphoserine.IPRVSEDLK
CCCCHHHHH
27.03UniProtKB
Link
234S-4a-FMN cysteine.VGRNCRFLQ
HHCCCCCCC
2.91UniProtKB
Link
350Phosphoserine.PRALSESTN
HHHHHHHHC
28.63UniProtKB
Link-
376Phosphoserine.ARRMSENVV
HHHHHHHHH
24.98UniProtKB
Link-
410Phosphoserine.SRKSSLSFM
CCCCCCCEE
30.94UniProtKB
Link-
450Phosphoserine.ERPESVDDK
HCCCCCCCH
33.26UniProtKB
Link-
512S-4a-FMN cysteine.LGRNCRFLQ
HHHCCCEEE
2.91UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"In vivo phosphorylation site mapping and functional characterizationof Arabidopsis phototropin 1.";
Sullivan S., Thomson C.E., Lamont D.J., Jones M.A., Christie J.M.;
Mol. Plant 1:178-194(2008).
Cited for: FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT SER-58; SER-185;SER-350 AND SER-410, FMN BINDING, AUTOPHOSPHORYLATION, AND SUBCELLULARLOCATION.
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-170; SER-350;SER-376; SER-410 AND SER-450, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures