Arabidopsis thaliana protein interaction network
Laboratório de Biologia Integrativa e Sistêmica (LaBIS)
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AT5G65420 - ( CYCD41 (CYCLIN D41) cyclin-dependent protein kinase regulator )

24 Proteins interacs with AT5G65420
LocusMethodFSW Cellular Compartment Classification (C3)Description
AT3G48750

Experimental

pull down

Affinity Capture-MS

Reconstituted Complex

protein complementation assay

two hybrid

affinity technology

two hybrid

FSW = 0.1904

Unknown

CDC2 (CELL DIVISION CONTROL 2) CYCLIN-DEPENDENT PROTEIN KINASE/ KINASE/ PROTEIN BINDING / PROTEIN KINASE
AT4G28980

Experimental

protein complementation assay

FSW = 0.6255

Unknown

CYCLIN-DEPENDENT KINASE-ACTIVATING KINASE 1AT / CDK-ACTIVATING KINASE 1AT (CAK1)
AT1G66750

Experimental

protein complementation assay

FSW = 0.6238

Unknown

CAK4 (CDK-ACTIVATING KINASE 4) KINASE/ PROTEIN BINDING / PROTEIN SERINE/THREONINE KINASE
AT2G32710

Experimental

protein complementation assay

two hybrid

FSW = 0.5429

Unknown

KRP4 CYCLIN BINDING / CYCLIN-DEPENDENT PROTEIN KINASE INHIBITOR
AT3G24810

Experimental

protein complementation assay

FSW = 0.4571

Unknown

ICK3 CYCLIN-DEPENDENT PROTEIN KINASE INHIBITOR
AT5G48820

Experimental

protein complementation assay

FSW = 0.4808

Unknown

ICK6 (INHIBITOR/INTERACTOR WITH CYCLIN-DEPENDENT KINASE) CYCLIN BINDING / CYCLIN-DEPENDENT PROTEIN KINASE INHIBITOR
AT2G23430

Experimental

protein complementation assay

two hybrid

FSW = 0.4236

Unknown

ICK1 CYCLIN-DEPENDENT PROTEIN KINASE INHIBITOR
AT1G18040

Experimental

protein complementation assay

FSW = 0.3200

Unknown

CDKD13 (CYCLIN-DEPENDENT KINASE D13) KINASE/ PROTEIN KINASE
AT3G19150

Experimental

protein complementation assay

FSW = 0.5584

Unknown

KRP6 (KIP-RELATED PROTEIN 6) CYCLIN BINDING / CYCLIN-DEPENDENT PROTEIN KINASE INHIBITOR
AT3G50630

Experimental

protein complementation assay

FSW = 0.5022

Unknown

KRP2 (KIP-RELATED PROTEIN 2) CYCLIN-DEPENDENT PROTEIN KINASE INHIBITOR/ KINASE INHIBITOR/ PROTEIN BINDING
AT1G49620

Experimental

protein complementation assay

FSW = 0.5022

Unknown

ICK5 CYCLIN BINDING / CYCLIN-DEPENDENT PROTEIN KINASE INHIBITOR
AT1G73690

Experimental

protein complementation assay

FSW = 0.1701

Unknown

CDKD11 (CYCLIN-DEPENDENT KINASE D11) ATP BINDING / KINASE/ PROTEIN KINASE/ PROTEIN SERINE/THREONINE KINASE
AT1G76540

Experimental

interaction detection method

pull down

Reconstituted Complex

two hybrid

protein complementation assay

in vitro

FSW = 0.5193

Unknown

CDKB21 (CYCLIN-DEPENDENT KINASE B21) CYCLIN-DEPENDENT PROTEIN KINASE/ KINASE/ PROTEIN BINDING
AT5G04470

Experimental

fluorescence acceptor donor pair

FSW = 0.0645

Unknown

SIM (SIAMESE) CYCLIN-DEPENDENT PROTEIN KINASE INHIBITOR
AT3G54180

Experimental

Reconstituted Complex

protein complementation assay

two hybrid

FSW = 0.3743

Unknown

CDKB11 (CYCLIN-DEPENDENT KINASE B11) CYCLIN-DEPENDENT PROTEIN KINASE/ KINASE/ PROTEIN BINDING
AT2G38620

Experimental

protein complementation assay

two hybrid

FSW = 0.6130

Unknown

CDKB12 (CYCLIN-DEPENDENT KINASE B12) CYCLIN BINDING / KINASE/ PROTEIN SERINE/THREONINE KINASE
AT5G63610

Experimental

protein complementation assay

two hybrid

FSW = 0.1216

Unknown

CDKE1 (CYCLIN-DEPENDENT KINASE E1) ATP BINDING / KINASE/ PROTEIN KINASE/ PROTEIN SERINE/THREONINE KINASE
AT1G67580

Experimental

protein complementation assay

FSW = 0.1735

Unknown

PROTEIN KINASE FAMILY PROTEIN
AT2G27960

Experimental

protein complementation assay

FSW = 0.3484

Unknown

CKS1 (CYCLIN-DEPENDENT KINASE-SUBUNIT 1) CYCLIN-DEPENDENT PROTEIN KINASE/ PROTEIN BINDING
AT2G27970

Experimental

protein complementation assay

FSW = 0.3424

Unknown

CKS2 (CDK-SUBUNIT 2) CYCLIN-DEPENDENT PROTEIN KINASE/ CYCLIN-DEPENDENT PROTEIN KINASE REGULATOR
AT3G12280

Experimental

protein complementation assay

FSW = 0.0209

Unknown

RBR1 (RETINOBLASTOMA-RELATED 1) TRANSCRIPTION FACTOR BINDING
AT1G20930

Experimental

two hybrid

FSW = 0.4339

Unknown

CDKB22 (CYCLIN-DEPENDENT KINASE B22) CYCLIN-DEPENDENT PROTEIN KINASE/ KINASE
AT4G34160

Predicted

Shared biological function

Enriched domain pair

Co-expression

FSW = 0.6227

Unknown

CYCD31 (CYCLIN D31) CYCLIN-DEPENDENT PROTEIN KINASE REGULATOR/ PROTEIN BINDING
AT4G03270

Predicted

Enriched domain pair

Phylogenetic profile method

Co-expression

FSW = 0.8372

Unknown

CYCD61 (CYCLIN D61) CYCLIN-DEPENDENT PROTEIN KINASE

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Fasta sequences:

Proteins

DNA

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