Arabidopsis thaliana protein interaction network
Laboratório de Biologia Integrativa e Sistêmica (LaBIS)
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AT4G26090 - ( RPS2 (RESISTANT TO P SYRINGAE 2) protein binding )

12 Proteins interacs with AT4G26090
LocusMethodFSW Cellular Compartment Classification (C3)Description
AT1G72150

Experimental

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Affinity Capture-MS

affinity technology

FSW = 0.2667

Class D:

cytosol (p = 0.67)

PATL1 (PATELLIN 1) TRANSPORTER
AT1G69840

Experimental

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Affinity Capture-MS

affinity technology

FSW = 0.2045

Class D:

cytosol (p = 0.67)

BAND 7 FAMILY PROTEIN
AT3G14210

Experimental

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Affinity Capture-MS

affinity technology

FSW = 0.1524

Unknown

ESM1 (EPITHIOSPECIFIER MODIFIER 1) CARBOXYLESTERASE/ HYDROLASE ACTING ON ESTER BONDS
AT3G01290

Experimental

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Affinity Capture-MS

affinity technology

FSW = 0.2813

Class D:

cytosol (p = 0.67)

BAND 7 FAMILY PROTEIN
AT5G58140

Experimental

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Affinity Capture-MS

affinity technology

FSW = 0.0711

Class D:

nucleus (p = 0.78)

PHOT2 (PHOTOTROPIN 2) FMN BINDING / BLUE LIGHT PHOTORECEPTOR/ KINASE/ PROTEIN SERINE/THREONINE KINASE
AT3G25070

Experimental

coimmunoprecipitation

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Affinity Capture-MS

Affinity Capture-Western

affinity technology

FSW = 0.1333

Class D:

nucleus (p = 0.78)

RIN4 (RPM1 INTERACTING PROTEIN 4) PROTEIN BINDING
AT4G30120

Experimental

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Affinity Capture-MS

affinity technology

FSW = 0.2133

Class D:

cytosol (p = 0.67)

HMA3 (HEAVY METAL ATPASE 3) ATPASE COUPLED TO TRANSMEMBRANE MOVEMENT OF IONS PHOSPHORYLATIVE MECHANISM
AT2G45960

Experimental

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Affinity Capture-MS

affinity technology

FSW = 0.0194

Unknown

PIP1B (NAMED PLASMA MEMBRANE INTRINSIC PROTEIN 1B) WATER CHANNEL
AT3G45780

Experimental

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Affinity Capture-MS

affinity technology

FSW = 0.0201

Class D:

nucleus (p = 0.78)

cytosol (p = 0.67)

PHOT1 (PHOTOTROPIN 1) FMN BINDING / BLUE LIGHT PHOTORECEPTOR/ KINASE/ PROTEIN BINDING / PROTEIN SERINE/THREONINE KINASE
AT4G08850

Experimental

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Affinity Capture-MS

affinity technology

FSW = 0.1185

Class D:

cytosol (p = 0.67)

KINASE
AT4G25230

Experimental

two hybrid

FSW = 0.0972

Unknown

RIN2 (RPM1 INTERACTING PROTEIN 2) PROTEIN BINDING / UBIQUITIN-PROTEIN LIGASE/ ZINC ION BINDING
AT5G51450

Experimental

two hybrid

FSW = 0.0933

Unknown

RIN3 (RPM1 INTERACTING PROTEIN 3) PROTEIN BINDING / UBIQUITIN-PROTEIN LIGASE/ ZINC ION BINDING

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Fasta sequences:

Proteins

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Quick help

Experimental: This means that the indicated PPI was experimentally demonstrated using Arabidopsis thaliana proteins as model of study. The experiment indicated links to the publication of which this interaction was annotated from
Predicted: The indicated PPI was proposed based on ortholgs studies. The experiment indicated links to the publication of the orthologous PPI was annotated from

FSW

FSW is the Functional Similarity Weight. It represents the proportion of interaction partners that two proteins have in common

Learn more - FSWeight top ranked cut offs

C3

Class A: The PPI is a direct evidence (experimental), the subcellular location was experimentally demonstrated and both, target and source, were indicated as expressed in same cellular compartment
Class B: The PPI is a direct evidence (experimental), the subcellular location was experimentally demonstrated but both, target and source, were indicated as expressed in different cellular compartment
Class C: Same as Class A but the PPI is predicted
Class D: Same as Class A but subcellular location was predicted. P(exp|pred) indicates the probability of this particular predicted location be experimentally demonstrated given all data available on AtPINDB
Unknown: There is no available data to calculate the C3 or the data does not fit onto any class previously described

PEP

PEP is the posterior probability of this particular PPI be experimentally demonstrated once it was predicted. For this release p = 0.0030. If they share same cell compartment p = 0.0029

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How to cite

If you find AtPIN interesting and want to use it in your work please cite us

AtPIN: Arabidopsis thaliana Protein Interaction Network
Marcelo M Brandao, Luiza L Dantas and Marcio C Silva-Filho
BMC Bioinformatics 2009, 10:454

DOI:1471-2105/10/454