Interaction Details


Details of experiments between NC_000001.11 and Q6IN84
Note that the results of all experiments are listed, regardless of the modification states of the fragments.



Experiment series 1

Protein A

Protein: 4945_HAP
Fragment: 203681644-203681669
Construct: Biotin-TCAGCCCTCCGTTTTGTCACCTACAC

Protein B

Protein: MRM1
Fragment: 1-353
Construct: endogenous protein (K562)
Average holdup BI: 0.79
Immobilized partner concentration (10-6M): 5
P value: 3.14
Experiment method: nHU_K562
Details of affinity fitting: hyperbolic binding equation
Number of measurements: 3
Measured pKd: 5.87
Experimental Details

-log10(P Two-sided unpaired T-test (3 vs 6))


Experiment series 2

Protein A

Protein: 51_HAP
Fragment: 203681832-203681862
Construct: Biotin-GAATTGAGAGGTATCTTACCGCTCCCACTCC

Protein B

Protein: MRM1
Fragment: 1-353
Construct: endogenous protein (K562)
Average holdup BI: 0.72
Immobilized partner concentration (10-6M): 5
P value: 2.26
Experiment method: nHU_K562
Details of affinity fitting: hyperbolic binding equation
Number of measurements: 3
Measured pKd: 5.72
Experimental Details

-log10(P Two-sided unpaired T-test (3 vs 6))


Experiment series 3

Protein A

Protein: 4945_WT
Fragment: 203681644-203681669
Modification: rs10751449/rs10736845
Construct: Biotin-TCAGCCCTCCGTATCGTCACCTACAC

Protein B

Protein: MRM1
Fragment: 1-353
Construct: endogenous protein (K562)
Average holdup BI: 0.78
Immobilized partner concentration (10-6M): 5
P value: 3.05
Experiment method: nHU_K562
Details of affinity fitting: hyperbolic binding equation
Number of measurements: 3
Measured pKd: 5.84
Experimental Details

-log10(P Two-sided unpaired T-test (3 vs 6))


Experiment series 4

Protein A

Protein: 51_WT
Fragment: 203681832-203681862
Modification: rs10751451
Construct: Biotin-GAATTGAGAGGTATCTTATCGCTCCCACTCC

Protein B

Protein: MRM1
Fragment: 1-353
Construct: endogenous protein (K562)
Average holdup BI: 0.79
Immobilized partner concentration (10-6M): 5
P value: 3.11
Experiment method: nHU_K562
Details of affinity fitting: hyperbolic binding equation
Number of measurements: 3
Measured pKd: 5.87
Experimental Details

-log10(P Two-sided unpaired T-test (3 vs 6))