Triticum aestivum      Atypical/PIKK


※ PIKK family introduction

    Phosphatidylinositol-3 kinase-related kinases (PIKKs) belong to atypical protein kinase group, which share little similarity of kinase catalytic domain. PIKKs family contains six members which are involved in responding to various stresses, including DNA damage, blocks in DNA replication, availability of nutrients and errors in mRNA splicing. The protein kinase domain of PIKKS, located in C-terminus, is always flanked by two conserved domain, known as FAT and FATC domain, which may interact and participate in kinase regulation (1). ATM, one of family member, is involved in responding to a specific type of DNA damage, such as DNA double strand breaks, and controls the cell-cycle progression by phosphorylates multiple substrates including p53 and Chk2. In addition, ATM also locates in cytoplasmic especially in neuronal or neuron-like cells (2). Ataxia telangiectasia and Rad3-related protein (ATR) acts as a DNA damage sensor. Activated by DNA lesions including base adducts, crosslinks, DSBs, and compounds that directly promote replication stress such as hydroxyurea and aphidicolin and phosphorylates multiple substrates to control the DNA replication and mitosis (3). mTOR is a serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. mTOR is regulated by dynamic changes in cellular localization (3). Transformation/transcription domain-associated protein (TRRAP) is also structurally related to the PIKK family. TRRAP proteins (Tra1 in budding yeast) are common components of many histone acetyltransferase (HAT) complexes, and mediate a variety of cellular processes by recruiting HAT complexes to chromatin (4).

Reference
1. Lempiainen, H. and Halazonetis, T.D. (2009) Emerging common themes in regulation of PIKKs and PI3Ks. EMBO J, 28, 3067-3073. PMID: 19779456
2. Yang, D.Q., Halaby, M.J., Li, Y., Hibma, J.C. and Burn, P. (2011) Cytoplasmic ATM protein kinase: an emerging therapeutic target for diabetes, cancer and neuronal degeneration. Drug Discov Today, 16, 332-338. PMID: 21315178
3. Lovejoy, C.A. and Cortez, D. (2009) Common mechanisms of PIKK regulation. DNA Repair (Amst), 8, 1004-1008. PMID: 19464237
4. Kanoh, J. and Yanagida, M. (2007) Tel2: a common partner of PIK-related kinases and a link between DNA checkpoint and nutritional response? Genes Cells, 12, 1301-1304. PMID: 18076567


There are 15 genes.  Reviewed (0 or Unreviewed (15

No.StatusiEKPD IDEnsemble Gene IDUniProt AccessionGene Name
1
iEKPD-Tra-0118
TRIAE_CS42_1AL_TGACv1_004231_AA0052880
2
iEKPD-Tra-0119
TRIAE_CS42_1AL_TGACv1_004390_AA0053390
A0A1D5S070
3
iEKPD-Tra-0453
TRIAE_CS42_1DL_TGACv1_062190_AA0210370
A0A1D5SV88
4
iEKPD-Tra-0821
TRIAE_CS42_2AS_TGACv1_115152_AA0371240
A0A1D5TRR7
5
iEKPD-Tra-1433
TRIAE_CS42_2DS_TGACv1_179693_AA0608660
A0A1D5V374
6
iEKPD-Tra-2328
TRIAE_CS42_4AL_TGACv1_290462_AA0985650
A0A1D5X6Q8
7
iEKPD-Tra-2896
TRIAE_CS42_5AS_TGACv1_393898_AA1277040
A0A1D5YV45
8
iEKPD-Tra-3133
TRIAE_CS42_5BS_TGACv1_423579_AA1379900
A0A1D6S478
9
iEKPD-Tra-3395
TRIAE_CS42_5DS_TGACv1_457148_AA1483110
A0A1D6A2C2
10
iEKPD-Tra-4257
TRIAE_CS42_7BL_TGACv1_578421_AA1894450
A0A1D6C8S8
11
iEKPD-Tra-4762
TRIAE_CS42_U_TGACv1_643113_AA2127430
A0A1D6DHU9
12
iEKPD-Tra-g011
TRIAE_CS42_1BL_TGACv1_030873_AA0102800
A0A1D5S999
13
iEKPD-Tra-g043
TRIAE_CS42_4AL_TGACv1_290029_AA0980640
A0A1D5X5K6
14
iEKPD-Tra-g036
TRIAE_CS42_4DS_TGACv1_361238_AA1164160
A0A1D5Y628
15
iEKPD-Tra-g001
TRIAE_CS42_4DS_TGACv1_361292_AA1165110
A0A1D5Y6A5