RIN4_ARATH - dbPTM
RIN4_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIN4_ARATH
UniProt AC Q8GYN5
Protein Name RPM1-interacting protein 4
Gene Name RIN4
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 211
Subcellular Localization Endomembrane system
Peripheral membrane protein .
Protein Description Essential regulator of plant defense, which plays a central role in resistance in case of infection by a pathogen. It is a common target for both type III avirulence proteins from P.syringae (AvrB, AvrRpm1 and AvrRpt2) and for the plant Resistance (R) proteins RPM1 and RPS2. In strains carrying the appropriate R gene for avirulence proteins of the pathogen, its association with avirulence proteins triggers a defense system including the hypersensitive response, which limits the spread of disease. In contrast, in plants lacking appropriate R genes, its association with avirulence proteins of the pathogen impairs the defense system and leads to the pathogen multiplication..
Protein Sequence MARSNVPKFGNWEAEENVPYTAYFDKARKTRAPGSKIMNPNDPEYNSDSQSQAPPHPPSSRTKPEQVDTVRRSREHMRSREESELKQFGDAGGSSNEAANKRQGRASQNNSYDNKSPLHKNSYDGTGKSRPKPTNLRADESPEKVTVVPKFGDWDENNPSSADGYTHIFNKVREERSSGANVSGSSRTPTHQSSRNPNNTSSCCCFGFGGK
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
21PhosphorylationAEENVPYTAYFDKAR
CCCCCCCEEECHHCC		14.6023111157
45PhosphorylationMNPNDPEYNSDSQSQ
CCCCCCCCCCCCCCC		25.9223776212
47PhosphorylationPNDPEYNSDSQSQAP
CCCCCCCCCCCCCCC		37.4230291188
49PhosphorylationDPEYNSDSQSQAPPH
CCCCCCCCCCCCCCC		31.3923776212
51PhosphorylationEYNSDSQSQAPPHPP
CCCCCCCCCCCCCCC		32.0623776212
59PhosphorylationQAPPHPPSSRTKPEQ
CCCCCCCCCCCCHHH		36.5823776212
60PhosphorylationAPPHPPSSRTKPEQV
CCCCCCCCCCCHHHH		50.1423776212
69PhosphorylationTKPEQVDTVRRSREH
CCHHHHHHHHHHHHH		19.6329654922
79PhosphorylationRSREHMRSREESELK
HHHHHHHHHHHHHHH		36.1527545962
83PhosphorylationHMRSREESELKQFGD
HHHHHHHHHHHHHHC		43.4019376835
94PhosphorylationQFGDAGGSSNEAANK
HHHCCCCCHHHHHHH		29.1319376835
95PhosphorylationFGDAGGSSNEAANKR
HHCCCCCHHHHHHHH		41.8019376835
107PhosphorylationNKRQGRASQNNSYDN
HHHHCCCCCCCCCCC		31.8923776212
111PhosphorylationGRASQNNSYDNKSPL
CCCCCCCCCCCCCCC		41.2223776212
112PhosphorylationRASQNNSYDNKSPLH
CCCCCCCCCCCCCCC		26.1719376835
116PhosphorylationNNSYDNKSPLHKNSY
CCCCCCCCCCCCCCC		38.6623776212
122PhosphorylationKSPLHKNSYDGTGKS
CCCCCCCCCCCCCCC		29.4230589143
123PhosphorylationSPLHKNSYDGTGKSR
CCCCCCCCCCCCCCC		27.9925561503
129PhosphorylationSYDGTGKSRPKPTNL
CCCCCCCCCCCCCCC		55.9819376835
134PhosphorylationGKSRPKPTNLRADES
CCCCCCCCCCCCCCC		53.6725368622
141PhosphorylationTNLRADESPEKVTVV
CCCCCCCCCCCEEEE		38.6230291188
146PhosphorylationDESPEKVTVVPKFGD
CCCCCCEEEECCCCC		27.1823776212
160PhosphorylationDWDENNPSSADGYTH
CCCCCCCCCCCCHHH		40.0421320696
166PhosphorylationPSSADGYTHIFNKVR
CCCCCCHHHHHHHHH		17.6430291188
177PhosphorylationNKVREERSSGANVSG
HHHHHHHHCCCCCCC		36.0825368622
178PhosphorylationKVREERSSGANVSGS
HHHHHHHCCCCCCCC		48.4225368622
183PhosphorylationRSSGANVSGSSRTPT
HHCCCCCCCCCCCCC		32.5325368622
185PhosphorylationSGANVSGSSRTPTHQ
CCCCCCCCCCCCCCC		14.7823111157
186PhosphorylationGANVSGSSRTPTHQS
CCCCCCCCCCCCCCC		43.6425368622
188PhosphorylationNVSGSSRTPTHQSSR
CCCCCCCCCCCCCCC		34.1925368622
190PhosphorylationSGSSRTPTHQSSRNP
CCCCCCCCCCCCCCC		31.7525368622
193PhosphorylationSRTPTHQSSRNPNNT
CCCCCCCCCCCCCCC		24.5425368622
194PhosphorylationRTPTHQSSRNPNNTS
CCCCCCCCCCCCCCC		29.5225368622
203S-palmitoylationNPNNTSSCCCFGFGG
CCCCCCCCCCCCCCC		2.04-
204S-palmitoylationPNNTSSCCCFGFGGK
CCCCCCCCCCCCCCC		2.02-
205S-palmitoylationNNTSSCCCFGFGGK-
CCCCCCCCCCCCCC-		4.36-
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 RIN4_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
21TPhosphorylation

21320696
160SPhosphorylation

21320696
166TPhosphorylation

21320696
203CPalmitoylation

-
204CPalmitoylation

-
205CPalmitoylation

15845764
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 RIN4_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT02_ARATHRPS2physical
12581526
NDR1_ARATHNDR1physical
17012600
RPS2_ARATHRPS2physical
17012600
RPS2_ARATHRPS2physical
19564897
PMA1_ARATHHA1physical
19564897
CSCLD_ARATHERD4physical
19564897
Y3126_ARATHAT3G61260physical
19564897
JAL5_ARATHAT1G52000physical
19564897
JAL30_ARATHPBP1physical
19564897
PMA2_ARATHHA2physical
19564897
CLAH2_ARATHAT3G08530physical
21320696
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIN4_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-107; SER-116 ANDSER-141, AND MASS SPECTROMETRY.
"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-141, 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-79 AND SER-141, AND MASSSPECTROMETRY.
"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-47 AND SER-141, AND MASSSPECTROMETRY.

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