AB36G_ARATH - dbPTM
AB36G_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AB36G_ARATH
UniProt AC Q9XIE2
Protein Name ABC transporter G family member 36
Gene Name ABCG36
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1469
Subcellular Localization Cell membrane
Multi-pass membrane protein . Incoporated into pathogen-induced papillae and haustorial encasement structures.
Protein Description Key factor that controls the extent of cell death in the defense response. Necessary for both callose deposition and glucosinolate activation in response to pathogens. Required for limiting invasion by nonadapted powdery mildews. Confers resistance to cadmium (Cd) and lead (Pb), probably as an efflux pump of Cd2+ or Cd conjugates, and possibly, of chemicals that mediate pathogen resistance..
Protein Sequence MDYNPNLPPLGGGGVSMRRSISRSVSRASRNIEDIFSSGSRRTQSVNDDEEALKWAAIEKLPTYSRLRTTLMNAVVEDDVYGNQLMSKEVDVTKLDGEDRQKFIDMVFKVAEQDNERILTKLRNRIDRVGIKLPTVEVRYEHLTIKADCYTGNRSLPTLLNVVRNMGESALGMIGIQFAKKAQLTILKDISGVIKPGRMTLLLGPPSSGKTTLLLALAGKLDKSLQVSGDITYNGYQLDEFVPRKTSAYISQNDLHVGIMTVKETLDFSARCQGVGTRYDLLNELARREKDAGIFPEADVDLFMKASAAQGVKNSLVTDYTLKILGLDICKDTIVGDDMMRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTFQIVKCLQQIVHLNEATVLMSLLQPAPETFDLFDDIILVSEGQIVYQGPRDNILEFFESFGFKCPERKGTADFLQEVTSKKDQEQYWVNPNRPYHYIPVSEFASRYKSFHVGTKMSNELAVPFDKSRGHKAALVFDKYSVSKRELLKSCWDKEWLLMQRNAFFYVFKTVQIVIIAAITSTLFLRTEMNTRNEGDANLYIGALLFGMIINMFNGFAEMAMMVSRLPVFYKQRDLLFYPSWTFSLPTFLLGIPSSILESTAWMVVTYYSIGFAPDASRFFKQFLLVFLIQQMAASLFRLIASVCRTMMIANTGGALTLLLVFLLGGFLLPKGKIPDWWGWAYWVSPLTYAFNGLVVNEMFAPRWMNKMASSNSTIKLGTMVLNTWDVYHQKNWYWISVGALLCFTALFNILFTLALTYLNPLGKKAGLLPEEENEDADQGKDPMRRSLSTADGNRRGEVAMGRMSRDSAAEASGGAGNKKGMVLPFTPLAMSFDDVKYFVDMPGEMRDQGVTETRLQLLKGVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDVRISGFPKVQETFARISGYCEQTDIHSPQVTVRESLIFSAFLRLPKEVGKDEKMMFVDQVMELVELDSLRDSIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRAVRNTVDTGRTVVCTIHQPSIDIFEAFDELMLMKRGGQVIYAGPLGQNSHKVVEYFESFPGVSKIPEKYNPATWMLEASSLAAELKLSVDFAELYNQSALHQRNKALVKELSVPPAGASDLYFATQFSQNTWGQFKSCLWKQWWTYWRSPDYNLVRFIFTLATSLLIGTVFWQIGGNRSNAGDLTMVIGALYAAIIFVGINNCSTVQPMVAVERTVFYRERAAGMYSAMPYAISQVTCELPYVLIQTVYYSLIVYAMVGFEWKAEKFFWFVFVSYFSFLYWTYYGMMTVSLTPNQQVASIFASAFYGIFNLFSGFFIPRPKIPKWWIWYYWICPVAWTVYGLIVSQYGDVETRIQVLGGAPDLTVKQYIEDHYGFQSDFMGPVAAVLIAFTVFFAFIFAFCIRTLNFQTR
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
1Acetylation-------MDYNPNLP
-------CCCCCCCC		49.8622223895
16PhosphorylationPLGGGGVSMRRSISR
CCCCCCHHHHHHHHH		15.1730589143
29PhosphorylationSRSVSRASRNIEDIF
HHHHHHHHCCHHHHH		25.4229797451
37PhosphorylationRNIEDIFSSGSRRTQ
CCHHHHHHCCCCCCC		33.8427532006
38PhosphorylationNIEDIFSSGSRRTQS
CHHHHHHCCCCCCCC		30.0027532006
40PhosphorylationEDIFSSGSRRTQSVN
HHHHHCCCCCCCCCC		22.1230291188
43PhosphorylationFSSGSRRTQSVNDDE
HHCCCCCCCCCCCHH		24.8815308754
45PhosphorylationSGSRRTQSVNDDEEA
CCCCCCCCCCCHHHH		23.4419880383
63PhosphorylationAAIEKLPTYSRLRTT
HHHHCCCCHHHHHHH		44.5617317660
69PhosphorylationPTYSRLRTTLMNAVV
CCHHHHHHHHHHHHH		28.9519376835
70PhosphorylationTYSRLRTTLMNAVVE
CHHHHHHHHHHHHHC		19.9919376835
81PhosphorylationAVVEDDVYGNQLMSK
HHHCCCCCCCCCCCC		19.8419376835
87PhosphorylationVYGNQLMSKEVDVTK
CCCCCCCCCCCCEEE		33.9719376835
224PhosphorylationLAGKLDKSLQVSGDI
HHCCCCCCEEEECCE		24.5728011693
277PhosphorylationARCQGVGTRYDLLNE
HHCCCCCCHHHHHHH		24.5325368622
279PhosphorylationCQGVGTRYDLLNELA
CCCCCCHHHHHHHHH		15.6925368622
494PhosphorylationFHVGTKMSNELAVPF
CCCCCCCCCCEECCC		28.8015308754
671PhosphorylationLIQQMAASLFRLIAS
HHHHHHHHHHHHHHH		20.6429797451
823PhosphorylationGKDPMRRSLSTADGN
CCCCCHHHCCCCCCC		19.1223776212
825PhosphorylationDPMRRSLSTADGNRR
CCCHHHCCCCCCCCC		23.8519880383
826PhosphorylationPMRRSLSTADGNRRG
CCHHHCCCCCCCCCC		33.7823776212
841PhosphorylationEVAMGRMSRDSAAEA
CEECCCCCHHHHHHH		31.4115308754
844PhosphorylationMGRMSRDSAAEASGG
CCCCCHHHHHHHCCC		28.4115308754
849PhosphorylationRDSAAEASGGAGNKK
HHHHHHHCCCCCCCC		29.3025561503
960PhosphorylationISGYCEQTDIHSPQV
HHCCCCCCCCCCCCC		18.0319880383
1020PhosphorylationLPGVTGLSTEQRKRL
CCCCCCCCHHHHHHH		31.1019880383
1092SulfoxidationAFDELMLMKRGGQVI
HHHHHHCHHCCCEEE		1.4123289948
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 AB36G_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
40SPhosphorylation

28910579
45SPhosphorylation

14506206
841SPhosphorylation

28910579
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 AB36G_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AFR_ARATHAFRphysical
26315018
PUB23_ARATHPUB23physical
26315018
WNK4_ARATHWNK4physical
26315018
GRH1_ARATHGRH1physical
26315018
FBW3_ARATHFBX2physical
26315018
EBF1_ARATHEBF1physical
26315018
GID2_ARATHSLY1physical
26315018
SKI20_ARATHAT3G59940physical
26315018
FBK30_ARATHAT1G80440physical
26315018
MPK7_ARATHMPK7physical
26315018
MPK10_ARATHMPK10physical
26315018
MPK16_ARATHMPK16physical
26315018
MSRB3_ARATHMSRB3physical
26315018
PLCD4_ARATHPLC4physical
26315018
CML12_ARATHTCH3physical
26315018
KIC_ARATHAT2G46600physical
26315018
CALM2_ARATHCAM3physical
26315018
CALM3_ARATHCAM3physical
26315018
CALM5_ARATHCAM3physical
26315018
CALM7_ARATHCAM7physical
26315018
CML8_ARATHCAM8physical
26315018
CML9_ARATHCAM9physical
26315018
CML37_ARATHCML37physical
26315018
CML38_ARATHCML38physical
26315018
CNBL4_ARATHSOS3physical
26315018
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AB36G_ARATH

loading...

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-40 AND SER-825, 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-40; SER-45 AND SER-825,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-40 AND SER-45, AND MASSSPECTROMETRY.
"Temporal analysis of sucrose-induced phosphorylation changes inplasma membrane proteins of Arabidopsis.";
Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,Schulze W.X.;
Mol. Cell. Proteomics 6:1711-1726(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-825, ANDMASS SPECTROMETRY.
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database.";
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
Plant Cell 16:2394-2405(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-40; THR-43;SER-45; SER-494; SER-841 AND SER-844, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory