Arabidopsis thaliana protein interaction network
Laboratório de Biologia Integrativa e Sistêmica (LaBIS)
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AT3G13170 - ( ATSPO11-1 ATP binding / DNA binding / DNA topoisomerase (ATP-hydrolyzing)/ catalytic )

15 Proteins interacs with AT3G13170
LocusMethodFSW Cellular Compartment Classification (C3)Description
AT5G60440

Experimental

FSW = 0.0329

Unknown

AGL62 (AGAMOUS-LIKE 62) DNA BINDING / TRANSCRIPTION FACTOR
AT4G14180Experimental

two hybrid

FSW = 0.0381

Unknown

ATPRD1 (ARABIDOPSIS THALIANA PUTATIVE RECOMBINATION INITIATION DEFECT 1) PROTEIN BINDING / PROTEIN HOMODIMERIZATION
AT3G48750

Predicted

biochemical

Phenotypic Enhancement

interaction prediction

FSW = 0.0209

Unknown

CDC2 (CELL DIVISION CONTROL 2) CYCLIN-DEPENDENT PROTEIN KINASE/ KINASE/ PROTEIN BINDING / PROTEIN KINASE
AT5G52640

Predicted

synthetic growth defect

FSW = 0.0045

Unknown

ATHSP901 (HEAT SHOCK PROTEIN 901) ATP BINDING / UNFOLDED PROTEIN BINDING
AT5G64630

Predicted

Phenotypic Suppression

FSW = 0.0485

Unknown

FAS2 (FASCIATA 2) NUCLEOTIDE BINDING / PROTEIN BINDING
AT5G44200

Predicted

Phenotypic Enhancement

Phenotypic Suppression

FSW = 0.0653

Unknown

CBP20 (CAP-BINDING PROTEIN 20) RNA BINDING / RNA CAP BINDING
AT5G35530

Predicted

two hybrid

FSW = 0.0395

Unknown

40S RIBOSOMAL PROTEIN S3 (RPS3C)
AT2G31970

Predicted

Phenotypic Enhancement

Phenotypic Suppression

FSW = 0.0439

Unknown

RAD50 ATP BINDING / NUCLEASE/ ZINC ION BINDING
AT5G57450

Predicted

Phenotypic Suppression

Phenotypic Suppression

FSW = 0.0416

Unknown

XRCC3 ATP BINDING / DAMAGED DNA BINDING / PROTEIN BINDING / SINGLE-STRANDED DNA BINDING
AT1G47500

Predicted

two hybrid

FSW = 0.0653

Unknown

ATRBP47C (RNA-BINDING PROTEIN 47C) RNA BINDING
AT4G01985

Predicted

two hybrid

FSW = 0.0426

Unknown

UNKNOWN PROTEIN
AT1G10930

Predicted

Phenotypic Suppression

FSW = 0.0421

Unknown

RECQ4A ATP BINDING / ATP-DEPENDENT HELICASE/ HELICASE/ NUCLEIC ACID BINDING
AT4G29170

Predicted

Phenotypic Suppression

FSW = 0.1053

Unknown

ATMND1
AT4G30870

Predicted

Synthetic Rescue

FSW = 0.0567

Unknown

MUS81 (MMS AND UV SENSITIVE 81) ENDONUCLEASE/ NUCLEIC ACID BINDING
AT5G02820

Predicted

Phylogenetic profile method

FSW = 0.4158

Unknown

RHL2 (ROOT HAIRLESS 2) ATP BINDING / DNA BINDING / DNA TOPOISOMERASE (ATP-HYDROLYZING)/ IDENTICAL PROTEIN BINDING / PROTEIN BINDING

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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