PHOT1_ARATH - dbPTM
PHOT1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHOT1_ARATH
UniProt AC O48963
Protein Name Phototropin-1
Gene Name PHOT1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 996
Subcellular Localization Cell membrane
Peripheral membrane protein. Cytoplasm.
Protein Description Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Phosphorylates BLUS1, a kinase involved in stomatal opening. Required for blue light mediated mRNA destabilization. Mediates calcium spiking of extracellular origin in response to a low rate of blue light. Also mediates rapid membrane depolarization and growth inhibition in response to blue light. Necessary for root phototropism. Involved in hypocotyl phototropism under a low rate but not under a high rate of blue light. Contributes to the chloroplast accumulation but seems not to be 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 MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPDNPVFRPEPPAWQNLSDPRGTSPQPRPQQEPAPSNPVRSDQEIAVTTSWMALKDPSPETISKKTITAEKPQKSAVAAEQRAAEWGLVLKTDTKTGKPQGVGVRNSGGTENDPNGKKTTSQRNSQNSCRSSGEMSDGDVPGGRSGIPRVSEDLKDALSTFQQTFVVSDATKPDYPIMYASAGFFNMTGYTSKEVVGRNCRFLQGSGTDADELAKIRETLAAGNNYCGRILNYKKDGTSFWNLLTIAPIKDESGKVLKFIGMQVEVSKHTEGAKEKALRPNGLPESLIRYDARQKDMATNSVTELVEAVKRPRALSESTNLHPFMTKSESDELPKKPARRMSENVVPSGRRNSGGGRRNSMQRINEIPEKKSRKSSLSFMGIKKKSESLDESIDDGFIEYGEEDDEISDRDERPESVDDKVRQKEMRKGIDLATTLERIEKNFVITDPRLPDNPIIFASDSFLELTEYSREEILGRNCRFLQGPETDLTTVKKIRNAIDNQTEVTVQLINYTKSGKKFWNIFHLQPMRDQKGEVQYFIGVQLDGSKHVEPVRNVIEETAVKEGEDLVKKTAVNIDEAVRELPDANMTPEDLWANHSKVVHCKPHRKDSPPWIAIQKVLESGEPIGLKHFKPVKPLGSGDTGSVHLVELVGTDQLFAMKAMDKAVMLNRNKVHRARAEREILDLLDHPFLPALYASFQTKTHICLITDYYPGGELFMLLDRQPRKVLKEDAVRFYAAQVVVALEYLHCQGIIYRDLKPENVLIQGNGDISLSDFDLSCLTSCKPQLLIPSIDEKKKKKQQKSQQTPIFMAEPMRASNSFVGTEEYIAPEIISGAGHTSAVDWWALGILMYEMLYGYTPFRGKTRQKTFTNVLQKDLKFPASIPASLQVKQLIFRLLQRDPKKRLGCFEGANEVKQHSFFKGINWALIRCTNPPELETPIFSGEAENGEKVVDPELEDLQTNVF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
12PhosphorylationEKPSTKPSSRTLPRD
CCCCCCCCCCCCCCC		33.7325561503
15PhosphorylationSTKPSSRTLPRDTRG
CCCCCCCCCCCCCCC		42.9625561503
23PhosphorylationLPRDTRGSLEVFNPS
CCCCCCCCEEEECCC		20.33-
57PhosphorylationNLSDPRGTSPQPRPQ
CCCCCCCCCCCCCCC		38.2123776212
58PhosphorylationLSDPRGTSPQPRPQQ
CCCCCCCCCCCCCCC		25.1027532006
70PhosphorylationPQQEPAPSNPVRSDQ
CCCCCCCCCCCCCCC		56.7423776212
92PhosphorylationWMALKDPSPETISKK
EEECCCCCHHHCCCC		45.5625561503
97PhosphorylationDPSPETISKKTITAE
CCCHHHCCCCEEECC		35.2025561503
109PhosphorylationTAEKPQKSAVAAEQR
ECCCCCCHHHHHHHH		23.8025561503
130PhosphorylationVLKTDTKTGKPQGVG
EEEEECCCCCCCCEE		53.1623776212
141PhosphorylationQGVGVRNSGGTENDP
CCEEEECCCCCCCCC		28.2123776212
144PhosphorylationGVRNSGGTENDPNGK
EEECCCCCCCCCCCC		34.8323776212
159PhosphorylationKTTSQRNSQNSCRSS
CCCCHHCCCCCHHCC		32.6919376835
162PhosphorylationSQRNSQNSCRSSGEM
CHHCCCCCHHCCCCC		11.8519376835
165PhosphorylationNSQNSCRSSGEMSDG
CCCCCHHCCCCCCCC		47.2023776212
166PhosphorylationSQNSCRSSGEMSDGD
CCCCHHCCCCCCCCC		21.3023776212
170PhosphorylationCRSSGEMSDGDVPGG
HHCCCCCCCCCCCCC		33.8523776212
179PhosphorylationGDVPGGRSGIPRVSE
CCCCCCCCCCCCCCH		44.3319880383
185PhosphorylationRSGIPRVSEDLKDAL
CCCCCCCCHHHHHHH		27.0330291188
234OtherKEVVGRNCRFLQGSG
HHHCCCCCEECCCCC		2.91-
234OtherKEVVGRNCRFLQGSG
HHHCCCCCEECCCCC		2.91-
240PhosphorylationNCRFLQGSGTDADEL
CCEECCCCCCCHHHH		26.0917586839
242PhosphorylationRFLQGSGTDADELAK
EECCCCCCCHHHHHH		29.7017586839
350PhosphorylationVKRPRALSESTNLHP
HHCCCHHCCCCCCCC		28.6330291188
352PhosphorylationRPRALSESTNLHPFM
CCCHHCCCCCCCCCC		21.1523776212
353PhosphorylationPRALSESTNLHPFMT
CCHHCCCCCCCCCCC		37.4323776212
360PhosphorylationTNLHPFMTKSESDEL
CCCCCCCCCCCCCCC		31.6219376835
362PhosphorylationLHPFMTKSESDELPK
CCCCCCCCCCCCCCC		32.9223172892
364PhosphorylationPFMTKSESDELPKKP
CCCCCCCCCCCCCCC		43.4023172892
376PhosphorylationKKPARRMSENVVPSG
CCCCCCCCCCCCCCC		24.9830291188
394PhosphorylationSGGGRRNSMQRINEI
CCCCCCCCHHHHHCC		17.9327545962
406PhosphorylationNEIPEKKSRKSSLSF
HCCCHHHCCCCCCCC		56.8819880383
409PhosphorylationPEKKSRKSSLSFMGI
CHHHCCCCCCCCCCC		35.0923776212
410PhosphorylationEKKSRKSSLSFMGIK
HHHCCCCCCCCCCCC		30.9423776212
412PhosphorylationKSRKSSLSFMGIKKK
HCCCCCCCCCCCCCC		18.3530291188
420PhosphorylationFMGIKKKSESLDESI
CCCCCCCCCCCCCCC		41.1023776212
422PhosphorylationGIKKKSESLDESIDD
CCCCCCCCCCCCCCC		48.4923776212
426PhosphorylationKSESLDESIDDGFIE
CCCCCCCCCCCCHHH		30.8623776212
434PhosphorylationIDDGFIEYGEEDDEI
CCCCHHHCCCCCCCC		25.6423776212
442PhosphorylationGEEDDEISDRDERPE
CCCCCCCCCCCCCCC		25.2523776212
450PhosphorylationDRDERPESVDDKVRQ
CCCCCCCCCCHHHHH		33.2623776212
512OtherEEILGRNCRFLQGPE
HHHHCCCCCCCCCCC		2.91-
512OtherEEILGRNCRFLQGPE
HHHHCCCCCCCCCCC		2.91-
851PhosphorylationEPMRASNSFVGTEEY
CCCCCCCCCCCCCHH		20.8629654922
918PhosphorylationFPASIPASLQVKQLI
CCCCCCHHHHHHHHH		17.6128011693
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PHOT1_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHOT1_ARATH !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PHOT1_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHOT1_ARATHPHOT1physical
18585389
RPT3_ARATHNPH3physical
10542152
PKS2_ARATHPKS2physical
20071603
PKS1_ARATHPKS1physical
20071603
RPT3_ARATHNPH3physical
20071603
UBQ10_ARATHUBQ10physical
21990941
RPT2_ARATHRPT2physical
19524572
Y1044_ARATHAT1G30440physical
19524572
14336_ARATHGRF6physical
19524572
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHOT1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.

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