PKMYT1

protein kinase, membrane associated tyrosine/threonine 1
Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase (PKMYT1) is a member of the serine/threonine protein kinase family. This kinase preferentially phosphorylates and inactivates cyclin-dependent kinase 1 (CDK1), and thus negatively regulates cell cycle G2/M transition. This kinase is associated with the membrane throughout the cell cycle. Its activity is highly regulated during the cell cycle. Protein kinases AKT1/PKB and PLK (Polo-like kinase) have been shown to phosphorylate and regulate the activity of this kinase. Alternatively spliced transcript variants encoding distinct isoforms have been reported.


TCGA Data Summary

These figures show a summary of data collected by the cancer genome atlas for PKMYT1. The mutations heatmaps shows the fraction samples with each type of genetic mutation, while the copy number variation shows the percentage of samples where a deletion or amplication was dectected. Finally, the mRNA expression tab shows the amount of mRNA detected on a log-2 scale for each cancer type. The X-axis cancer type abbreviations are described here. This summary of the cancer genome atlas (TCGA) was collated from firebrowse developed by the Broad Institute. The code used to produce these figures is available through github.


PDB Kinase Domains

Kinase Domain Structure:

  • Title: Structure of human Membrane-associated Tyrosine- and Threonine-specific cdc2-inhibitory kinase MYT1 (PKMYT1)
  • Resolution: 1.7

Associated Compounds:

  • DIMETHYL SULFOXIDE
  • 1,2-ETHANEDIOL

View This Structure on RCSB PDB

Kinase Domain Structure:

  • Title: CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH PHA-848125
  • Resolution: 1.7

Associated Compounds:

  • N,1,4,4-TETRAMETHYL-8-{[4-(4-METHYLPIPERAZIN-1-YL)PHENYL]AMINO}-4,5-DIHYDRO-1H-PYRAZOLO[4,3-H]QUINAZOLINE-3-CARBOXAMIDE
  • DI(HYDROXYETHYL)ETHER

View This Structure on RCSB PDB

Kinase Domain Structure:

  • Title: CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH MK1775
  • Resolution: 2.13

Associated Compounds:

  • 1-[6-(2-hydroxypropan-2-yl)pyridin-2-yl]-6-{[4-(4-methylpiperazin-1-yl)phenyl]amino}-2-(prop-2-en-1-yl)-1,2-dihydro-3H-pyrazolo[3,4-d]pyrimidin-3-one
  • DI(HYDROXYETHYL)ETHER

View This Structure on RCSB PDB

Kinase Domain Structure:

  • Title: CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN (de-phosphorylated) IN COMPLEX WITH SARACATINIB
  • Resolution: 1.8

Associated Compounds:

  • 1,2-ETHANEDIOL
  • N-(5-CHLORO-1,3-BENZODIOXOL-4-YL)-7-[2-(4-METHYLPIPERAZIN-1-YL)ETHOXY]-5-(TETRAHYDRO-2H-PYRAN-4-YLOXY)QUINAZOLIN-4-AMINE
  • DI(HYDROXYETHYL)ETHER

View This Structure on RCSB PDB

Kinase Domain Structure:

  • Title: CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN (UNTREATED) IN COMPLEX WITH SARACATINIB
  • Resolution: 2.7

Associated Compounds:

  • 1,2-ETHANEDIOL
  • N-(5-CHLORO-1,3-BENZODIOXOL-4-YL)-7-[2-(4-METHYLPIPERAZIN-1-YL)ETHOXY]-5-(TETRAHYDRO-2H-PYRAN-4-YLOXY)QUINAZOLIN-4-AMINE

View This Structure on RCSB PDB

Kinase Domain Structure:

  • Title: CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH BOSUTINIB
  • Resolution: 1.56

Associated Compounds:

  • 4-[(2,4-dichloro-5-methoxyphenyl)amino]-6-methoxy-7-[3-(4-methylpiperazin-1-yl)propoxy]quinoline-3-carbonitrile
  • DIMETHYL SULFOXIDE
  • 1,2-ETHANEDIOL
  • DI(HYDROXYETHYL)ETHER

View This Structure on RCSB PDB

Kinase Domain Structure:

  • Title: CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH Bosutinib isomer
  • Resolution: 1.5

Associated Compounds:

  • 1,2-ETHANEDIOL
  • DI(HYDROXYETHYL)ETHER
  • 4-[(3,5-DICHLORO-4-METHOXYPHENYL)AMINO]-6-METHOXY-7-[3-(4-METHYLPIPERAZIN-1-YL)PROPOXY]QUINOLINE-3-CARBONITRILE

View This Structure on RCSB PDB

Kinase Domain Structure:

  • Title: CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH Dasatinib
  • Resolution: 1.92

Associated Compounds:

  • N-(2-CHLORO-6-METHYLPHENYL)-2-({6-[4-(2-HYDROXYETHYL)PIPERAZIN-1-YL]-2-METHYLPYRIMIDIN-4-YL}AMINO)-1,3-THIAZOLE-5-CARBOXAMIDE
  • CHLORIDE ION
  • 1,2-ETHANEDIOL
  • PHOSPHOTHREONINE

View This Structure on RCSB PDB

Kinase Domain Structure:

  • Title: CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH Pelitinib
  • Resolution: 2.25

Associated Compounds:

  • (2E)-N-{4-[(3-chloro-4-fluorophenyl)amino]-3-cyano-7-ethoxyquinolin-6-yl}-4-(dimethylamino)but-2-enamide
  • 1,2-ETHANEDIOL
  • SULFATE ION

View This Structure on RCSB PDB

Interaction Networks

INDRA (Integrated Network and Dynamical Reasoning Assembler) is an automated model assembly system drawing from natural language processing systems and structured databases. It collects mechanistic and causal assertions, represents them in a standardized form (INDRA Statements), and assembles them into various modeling formalisms including causal graphs and dynamical models. More information on this work can be found on Github. In this particular figure, several interaction-types are depicted; physical complexes (blue), phosphorylation (black), and general up- or downregulation (green and red, respectively). Biomacromolecules are represented as squares, small molecule as circles, and biological processes and diamonds. The thickness of each line reflects a confidence score, with thicker lines higher in confidence.

Affinity Purification - Mass Spectrometry


PRM Peptides


The calibration reverse curve plot with linear robust regression analysis is shown [1]. The observed concentrations of the stable isotopically labeled peptide surrogate was obtained for each peptide using LC-MS in parallel reaction mode with a constant quantity of natural isotope abundance peptide as the internal standard (25 fmol/µL) [2]. The analyte matrix was a tryptic digest of pooled patient derived xenografts (1 µg/µL) that was prepared according to CPTAC-SOP. Each of the three most intense peptide fragment ions is depicted as a different symbol. The measurements from replicate LC-MS analyses are depicted as the same symbol [3] The LOD was determined using a non-parametric method with eight LC-MS analyses without added analyte [4]. The LOQ was generated from the LOD [5]. The plots are dimensioned such that the theoretical line is at a 45° angle to facilitate assessment of peptide recovery and performance. The LOD, LOQ, and regression parameters are summarize in the Table.

  1. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2855883/
  2. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3494192/
  3. https://proteomics.cancer.gov/sites/default/files/assay-characterization-guidance-document.pdf
  4. http://clinchem.aaccjnls.org/content/50/4/732
  5. “Algorithms, Routines and S Functions for Robust Statistics” (CRC Press, Boca Raton, Florida, USA, 1993)

View Peptide Parameters



The robust linear regression analysis of peak area ratios from admixtures of the indicated concentration of the synthetic natural abundance peptide and a constant quantity of the stable isotope labeled peptide (25 fmol) is shown [1]. The sample matrix was a tryptic digest of bovine serum albumin (100 ng/µL). The three most intense fragment ion ions from three LC-MS analyses were used to generate the robust linear regression line equation (nine independent measurements at each concentration). The mean of the nine measurements and standard deviations are shown. Only measurements with concentrations greater than the LOD that was determined in the tumor matrix was used for the standard curve (see legend for the calibration curve for this peptide).

  1. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2855883/

View Peptide Transistions



The calibration reverse curve plot with linear robust regression analysis is shown [1]. The observed concentrations of the stable isotopically labeled peptide surrogate was obtained for each peptide using LC-MS in parallel reaction mode with a constant quantity of natural isotope abundance peptide as the internal standard (25 fmol/µL) [2]. The analyte matrix was a tryptic digest of pooled patient derived xenografts (1 µg/µL) that was prepared according to CPTAC-SOP. Each of the three most intense peptide fragment ions is depicted as a different symbol. The measurements from replicate LC-MS analyses are depicted as the same symbol [3] The LOD was determined using a non-parametric method with eight LC-MS analyses without added analyte [4]. The LOQ was generated from the LOD [5]. The plots are dimensioned such that the theoretical line is at a 45° angle to facilitate assessment of peptide recovery and performance. The LOD, LOQ, and regression parameters are summarize in the Table.

  1. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2855883/
  2. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3494192/
  3. https://proteomics.cancer.gov/sites/default/files/assay-characterization-guidance-document.pdf
  4. http://clinchem.aaccjnls.org/content/50/4/732
  5. “Algorithms, Routines and S Functions for Robust Statistics” (CRC Press, Boca Raton, Florida, USA, 1993)

View Peptide Parameters



The robust linear regression analysis of peak area ratios from admixtures of the indicated concentration of the synthetic natural abundance peptide and a constant quantity of the stable isotope labeled peptide (25 fmol) is shown [1]. The sample matrix was a tryptic digest of bovine serum albumin (100 ng/µL). The three most intense fragment ion ions from three LC-MS analyses were used to generate the robust linear regression line equation (nine independent measurements at each concentration). The mean of the nine measurements and standard deviations are shown. Only measurements with concentrations greater than the LOD that was determined in the tumor matrix was used for the standard curve (see legend for the calibration curve for this peptide).

  1. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2855883/

View Peptide Transistions



The calibration reverse curve plot with linear robust regression analysis is shown [1]. The observed concentrations of the stable isotopically labeled peptide surrogate was obtained for each peptide using LC-MS in parallel reaction mode with a constant quantity of natural isotope abundance peptide as the internal standard (25 fmol/µL) [2]. The analyte matrix was a tryptic digest of pooled patient derived xenografts (1 µg/µL) that was prepared according to CPTAC-SOP. Each of the three most intense peptide fragment ions is depicted as a different symbol. The measurements from replicate LC-MS analyses are depicted as the same symbol [3] The LOD was determined using a non-parametric method with eight LC-MS analyses without added analyte [4]. The LOQ was generated from the LOD [5]. The plots are dimensioned such that the theoretical line is at a 45° angle to facilitate assessment of peptide recovery and performance. The LOD, LOQ, and regression parameters are summarize in the Table.

  1. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2855883/
  2. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3494192/
  3. https://proteomics.cancer.gov/sites/default/files/assay-characterization-guidance-document.pdf
  4. http://clinchem.aaccjnls.org/content/50/4/732
  5. “Algorithms, Routines and S Functions for Robust Statistics” (CRC Press, Boca Raton, Florida, USA, 1993)

View Peptide Parameters



The robust linear regression analysis of peak area ratios from admixtures of the indicated concentration of the synthetic natural abundance peptide and a constant quantity of the stable isotope labeled peptide (25 fmol) is shown [1]. The sample matrix was a tryptic digest of bovine serum albumin (100 ng/µL). The three most intense fragment ion ions from three LC-MS analyses were used to generate the robust linear regression line equation (nine independent measurements at each concentration). The mean of the nine measurements and standard deviations are shown. Only measurements with concentrations greater than the LOD that was determined in the tumor matrix was used for the standard curve (see legend for the calibration curve for this peptide).

  1. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2855883/

View Peptide Transistions


Available Assays, Cell Lines and Animal Models
Horizon KO HAP1 Cell Lines
IMPC Mouse KO
NanoBRET Assay
PKMYT1-NanoLuc® is available from Promega under catalog number: NV1871.