RBOHD_ARATH - dbPTM
RBOHD_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBOHD_ARATH
UniProt AC Q9FIJ0
Protein Name Respiratory burst oxidase homolog protein D
Gene Name RBOHD
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 921
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Calcium-dependent NADPH oxidase that generates superoxide. Involved in the generation of reactive oxygen species (ROS) during incompatible interactions with pathogens and in UV-B and abscisic acid ROS-dependent signaling. Might be required for ROS signal amplification during light stress..
Protein Sequence MKMRRGNSSNDHELGILRGANSDTNSDTESIASDRGAFSGPLGRPKRASKKNARFADDLPKRSNSVAGGRGDDDEYVEITLDIRDDSVAVHSVQQAAGGGGHLEDPELALLTKKTLESSLNNTTSLSFFRSTSSRIKNASRELRRVFSRRPSPAVRRFDRTSSAAIHALKGLKFIATKTAAWPAVDQRFDKLSADSNGLLLSAKFWECLGMNKESKDFADQLFRALARRNNVSGDAITKEQLRIFWEQISDESFDAKLQVFFDMVDKDEDGRVTEEEVAEIISLSASANKLSNIQKQAKEYAALIMEELDPDNAGFIMIENLEMLLLQAPNQSVRMGDSRILSQMLSQKLRPAKESNPLVRWSEKIKYFILDNWQRLWIMMLWLGICGGLFTYKFIQYKNKAAYGVMGYCVCVAKGGAETLKFNMALILLPVCRNTITWLRNKTKLGTVVPFDDSLNFHKVIASGIVVGVLLHAGAHLTCDFPRLIAADEDTYEPMEKYFGDQPTSYWWFVKGVEGWTGIVMVVLMAIAFTLATPWFRRNKLNLPNFLKKLTGFNAFWYTHHLFIIVYALLIVHGIKLYLTKIWYQKTTWMYLAVPILLYASERLLRAFRSSIKPVKMIKVAVYPGNVLSLHMTKPQGFKYKSGQFMLVNCRAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRKLRTVFSEVCKPPTAGKSGLLRADGGDGNLPFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISILKDIINNMKGPDRDSDIENNNSNNNSKGFKTRKAYFYWVTREQGSFEWFKGIMDEISELDEEGIIELHNYCTSVYEEGDARVALIAMLQSLQHAKNGVDVVSGTRVKSHFAKPNWRQVYKKIAVQHPGKRIGVFYCGMPGMIKELKNLALDFSRKTTTKFDFHKENF
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
8PhosphorylationMKMRRGNSSNDHELG
CCCCCCCCCCCCCCC		33.0830291188
9PhosphorylationKMRRGNSSNDHELGI
CCCCCCCCCCCCCCE		50.7223776212
22PhosphorylationGILRGANSDTNSDTE
CEECCCCCCCCCCHH		45.3227532006
24PhosphorylationLRGANSDTNSDTESI
ECCCCCCCCCCHHHH		36.1223776212
26PhosphorylationGANSDTNSDTESIAS
CCCCCCCCCHHHHHH		48.2630291188
28PhosphorylationNSDTNSDTESIASDR
CCCCCCCHHHHHHCC		31.3023776212
30PhosphorylationDTNSDTESIASDRGA
CCCCCHHHHHHCCCC		26.0823776212
33PhosphorylationSDTESIASDRGAFSG
CCHHHHHHCCCCCCC		26.6019376835
39PhosphorylationASDRGAFSGPLGRPK
HHCCCCCCCCCCCCC		38.6830291188
63PhosphorylationADDLPKRSNSVAGGR
HHCCCCCCCCCCCCC		39.3128011693
65PhosphorylationDLPKRSNSVAGGRGD
CCCCCCCCCCCCCCC		18.0028011693
119PhosphorylationTKKTLESSLNNTTSL
CHHHHHHHCCCCCCH		26.2417317660
152PhosphorylationRVFSRRPSPAVRRFD
HHHHCCCCHHHHHCC		24.5517317660
162PhosphorylationVRRFDRTSSAAIHAL
HHHCCCCCHHHHHHH		20.9025561503
163PhosphorylationRRFDRTSSAAIHALK
HHCCCCCHHHHHHHH		22.5523111157
343PhosphorylationMGDSRILSQMLSQKL
CCCHHHHHHHHHCCC		15.9217317660
347PhosphorylationRILSQMLSQKLRPAK
HHHHHHHHCCCCCCH		21.6717317660
464PhosphorylationNFHKVIASGIVVGVL
CHHHHHHHHHHHHHH		20.2328011693
699PhosphorylationSEVCKPPTAGKSGLL
HHHCCCCCCCCCCCE		57.4817317660
703PhosphorylationKPPTAGKSGLLRADG
CCCCCCCCCCEECCC		33.4817317660
769PhosphorylationMKGPDRDSDIENNNS
CCCCCCCCCCCCCCC		41.1930407730
776PhosphorylationSDIENNNSNNNSKGF
CCCCCCCCCCCCCCC		42.9525561503
780PhosphorylationNNNSNNNSKGFKTRK
CCCCCCCCCCCCCCE		35.9625561503
889NitrationGKRIGVFYCGMPGMI
CCEEEEEECCCHHHH		5.91-
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 RBOHD_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
39SPhosphorylation

19245862
343SPhosphorylation

17651370
347SPhosphorylation

17651370
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 RBOHD_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EFR_ARATHEFRphysical
24630626
BIK1_ARATHBIK1physical
24630626
BAK1_ARATHBAK1physical
24630626
GONS5_ARATHGONST5physical
24833385
PRA1E_ARATHPRA1.Ephysical
24833385
PIP15_ARATHPIP1;5physical
24833385
UTR2_ARATHUTR2physical
24833385
RAA1B_ARATHRABA1bphysical
24833385
UTR3_ARATHUTR3physical
24833385
WAT1_ARATHWAT1physical
24833385
DIM_ARATHDWF1physical
24833385
ERECT_ARATHERphysical
24833385
ANXD1_ARATHANNAT1physical
24833385
CNIH1_ARATHAT3G12180physical
24833385
MSBP2_ARATHMAPR3physical
24833385
WTR23_ARATHAT3G28130physical
24833385
WTR18_ARATHAT3G28050physical
24833385
NRAM2_ARATHNRAMP2physical
24833385
SPCS1_ARATHAT2G22425physical
24833385
RAA1C_ARATHRABA1cphysical
24833385
RABC1_ARATHRAB18physical
24833385
RAB1B_ARATHGB2physical
24833385
TRXH7_ARATHTH7physical
24833385
MMGT_ARATHAT5G03345physical
24833385
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBOHD_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-8 AND SER-39, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of plasma membrane proteinsreveals regulatory mechanisms of plant innate immune responses.";
Nuehse T.S., Bottrill A.R., Jones A.M.E., Peck S.C.;
Plant J. 51:931-940(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-343 AND SER-347,AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis.";
Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.;
Mol. Cell. Proteomics 6:1198-1214(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-152; SER-163 ANDSER-343, AND MASS SPECTROMETRY.

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