Arabidopsis thaliana protein interaction network
Laboratório de Biologia Integrativa e Sistêmica (LaBIS)
Laboratório de Biologia Integrativa e Sistêmica (LaBIS)
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AT1G27770 - ( ACA1 (AUTO-INHIBITED CA2+-ATPASE 1) calcium channel/ calcium-transporting ATPase/ calmodulin binding )
22 Proteins interacs with AT1G27770Locus | Method | FSW | Cellular Compartment Classification (C3) | Description |
---|---|---|---|---|
AT2G41560 | PredictedEnriched domain pairPhylogenetic profile methodCo-expression | FSW = 0.6706
| Class C:plastid | ACA4 (AUTO-INHIBITED CA(2+)-ATPASE ISOFORM 4) CALCIUM-TRANSPORTING ATPASE/ CALMODULIN BINDING |
AT1G07810 | PredictedEnriched domain pairGene neighbors methodPhylogenetic profile method | FSW = 0.2250
| Class C:plasma membraneendoplasmic reticulum | ECA1 (ER-TYPE CA2+-ATPASE 1) CALCIUM-TRANSPORTING ATPASE |
AT4G37640 | PredictedEnriched domain pairPhylogenetic profile methodCo-expression | FSW = 0.5690
| Class C:plasma membraneendoplasmic reticulum | ACA2 (CALCIUM ATPASE 2) CALCIUM ION TRANSMEMBRANE TRANSPORTER/ CALCIUM-TRANSPORTING ATPASE/ CALMODULIN BINDING |
AT3G57330 | PredictedEnriched domain pairPhylogenetic profile methodCo-expression | FSW = 0.6955
| Class C:plasma membrane | ACA11 (AUTOINHIBITED CA2+-ATPASE 11) CALCIUM-TRANSPORTING ATPASE/ CALMODULIN BINDING |
AT5G57110 | PredictedEnriched domain pairPhylogenetic profile methodCo-expression | FSW = 0.5270
| Class C:plasma membrane | ACA8 (AUTOINHIBITED CA2+ -ATPASE ISOFORM 8) CALCIUM-TRANSPORTING ATPASE/ CALMODULIN BINDING / PROTEIN SELF-ASSOCIATION |
AT4G29900 | PredictedEnriched domain pairPhylogenetic profile methodCo-expression | FSW = 0.6054
| Class C:plasma membrane | ACA10 (AUTOINHIBITED CA(2+)-ATPASE 10) CALCIUM-TRANSPORTING ATPASE/ CALMODULIN BINDING |
AT3G21180 | PredictedEnriched domain pairPhylogenetic profile methodCo-expression | FSW = 0.5510
| Class C:plasma membrane | ACA9 (AUTOINHIBITED CA(2+)-ATPASE 9) CALCIUM-TRANSPORTING ATPASE/ CALMODULIN BINDING |
AT1G10130 | PredictedSynthetic LethalityEnriched domain pairGene neighbors methodPhylogenetic profile methodCo-expression | FSW = 0.1613
| Class C:endoplasmic reticulum | ECA3 (ENDOPLASMIC RETICULUM-TYPE CALCIUM-TRANSPORTING ATPASE 3) CALCIUM-TRANSPORTING ATPASE/ CALMODULIN BINDING / MANGANESE-TRANSPORTING ATPASE/ PEROXIDASE |
AT4G00900 | PredictedEnriched domain pairPhylogenetic profile methodCo-expression | FSW = 0.3894
| Class C:endoplasmic reticulum | ECA2 (ER-TYPE CA2+-ATPASE 2) CALCIUM-TRANSPORTING ATPASE |
AT1G22740 | Predictedinterologs mapping | FSW = 0.0551
| Unknown | RABG3B GTP BINDING |
AT2G25340 | PredictedAffinity Capture-Western | FSW = 0.0320
| Unknown | ATVAMP712 (VESICLE-ASSOCIATED MEMBRANE PROTEIN 712) |
AT3G63380 | PredictedEnriched domain pairPhylogenetic profile methodCo-expression | FSW = 0.7222
| Unknown | CALCIUM-TRANSPORTING ATPASE PLASMA MEMBRANE-TYPE PUTATIVE / CA(2+)-ATPASE PUTATIVE (ACA12) |
AT2G22950 | PredictedEnriched domain pairPhylogenetic profile methodCo-expression | FSW = 0.7222
| Unknown | CALCIUM-TRANSPORTING ATPASE PLASMA MEMBRANE-TYPE PUTATIVE / CA2+-ATPASE PUTATIVE (ACA7) |
AT3G22910 | PredictedEnriched domain pairPhylogenetic profile methodCo-expression | FSW = 0.5772
| Unknown | CALCIUM-TRANSPORTING ATPASE PLASMA MEMBRANE-TYPE PUTATIVE / CA(2+)-ATPASE PUTATIVE (ACA13) |
AT2G21250 | PredictedAffinity Capture-MS | FSW = 0.0127
| Unknown | MANNOSE 6-PHOSPHATE REDUCTASE (NADPH-DEPENDENT) PUTATIVE |
AT1G26530 | PredictedAffinity Capture-MS | FSW = 0.0914
| Unknown | UNKNOWN PROTEIN |
AT2G28390 | Predictedinterologs mapping | FSW = 0.1020
| Unknown | SAND FAMILY PROTEIN |
AT1G55720 | PredictedPhenotypic EnhancementPhenotypic EnhancementPhenotypic Enhancement | FSW = 0.0345
| Unknown | ATCAX6 CALCIUMCATION ANTIPORTER/ CATIONCATION ANTIPORTER |
AT3G18430 | PredictedPhenotypic Enhancement | FSW = 0.0277
| Unknown | CALCIUM-BINDING EF HAND FAMILY PROTEIN |
AT1G53710 | PredictedSynthetic Lethality | FSW = 0.0765
| Unknown | HYDROLASE/ PROTEIN SERINE/THREONINE PHOSPHATASE |
AT1G06710 | PredictedGene fusion method | FSW = 0.0645
| Unknown | PENTATRICOPEPTIDE (PPR) REPEAT-CONTAINING PROTEIN |
AT5G49770 | PredictedGene fusion method | FSW = 0.1731
| Unknown | LEUCINE-RICH REPEAT TRANSMEMBRANE PROTEIN KINASE PUTATIVE |
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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