Arabidopsis thaliana protein interaction network
Laboratório de Biologia Integrativa e Sistêmica (LaBIS)
Laboratório de Biologia Integrativa e Sistêmica (LaBIS)
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AT5G06410 - ( DNAJ heat shock N-terminal domain-containing protein )
15 Proteins interacs with AT5G06410Locus | Method | FSW | Cellular Compartment Classification (C3) | Description |
---|---|---|---|---|
AT4G22220 | Experimentaltwo hybridprotein complementation assay | FSW = 0.2801
| Unknown | ISU1 STRUCTURAL MOLECULE |
AT3G63490 | Predictedpull down | FSW = 0.0885
| Unknown | RIBOSOMAL PROTEIN L1 FAMILY PROTEIN |
AT3G27850 | Predictedpull down | FSW = 0.0421
| Unknown | RPL12-C (RIBOSOMAL PROTEIN L12-C) STRUCTURAL CONSTITUENT OF RIBOSOME |
AT2G28190 | PredictedSynthetic RescueSynthetic Rescueinteraction prediction | FSW = 0.0279
| Unknown | CSD2 (COPPER/ZINC SUPEROXIDE DISMUTASE 2) SUPEROXIDE DISMUTASE |
AT5G15450 | Predictedpull down | FSW = 0.0825
| Unknown | CLPB3 (CASEIN LYTIC PROTEINASE B3) ATP BINDING / ATPASE/ NUCLEOSIDE-TRIPHOSPHATASE/ NUCLEOTIDE BINDING / PROTEIN BINDING |
AT1G32990 | Predictedpull down | FSW = 0.0653
| Unknown | PRPL11 (PLASTID RIBOSOMAL PROTEIN L11) STRUCTURAL CONSTITUENT OF RIBOSOME |
ATCG00160 | Predictedpull down | FSW = 0.0722
| Unknown | CHLOROPLAST RIBOSOMAL PROTEIN S2 |
ATCG00180 | Predictedpull down | FSW = 0.0768
| Unknown | RNA POLYMERASE BETA SUBUNIT-1 |
ATCG00330 | Predictedpull down | FSW = 0.1032
| Unknown | 30S CHLOROPLAST RIBOSOMAL PROTEIN S14 |
ATCG01240 | Predictedpull down | FSW = 0.1079
| Unknown | 30S CHLOROPLAST RIBOSOMAL PROTEIN S7 |
AT5G52640 | Predictedpull down | FSW = 0.0118
| Unknown | ATHSP901 (HEAT SHOCK PROTEIN 901) ATP BINDING / UNFOLDED PROTEIN BINDING |
AT3G01020 | Predictedinterologs mapping | FSW = 0.1524
| Unknown | ISU2 (ISCU-LIKE 2) STRUCTURAL MOLECULE |
AT4G02930 | Predictedpull down | FSW = 0.0574
| Unknown | ELONGATION FACTOR TU PUTATIVE / EF-TU PUTATIVE |
AT5G53350 | Predictedpull down | FSW = 0.2268
| Unknown | CLPX ATP BINDING / ATPASE/ NUCLEOSIDE-TRIPHOSPHATASE/ NUCLEOTIDE BINDING / PROTEIN BINDING |
AT1G08830 | PredictedSynthetic RescueSynthetic Rescue | FSW = 0.0474
| Unknown | CSD1 (COPPER/ZINC SUPEROXIDE DISMUTASE 1) SUPEROXIDE DISMUTASE |
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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 commonLearn 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 = 0.0029Learn more
How to cite
If you find AtPIN interesting and want to use it in your work please cite usAtPIN: Arabidopsis thaliana Protein Interaction Network
Marcelo M Brandao, Luiza L Dantas and Marcio C Silva-Filho
BMC Bioinformatics 2009, 10:454DOI:1471-2105/10/454
Marcelo M Brandao, Luiza L Dantas and Marcio C Silva-Filho
BMC Bioinformatics 2009, 10:454DOI:1471-2105/10/454