Glycine max      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-Glm-0389
GLYMA_04G182900
2
iEKPD-Glm-1188
GLYMA_11G002600
3
iEKPD-Glm-g037
GLYMA_04G013900
I1JSQ3
100777069
4
iEKPD-Glm-0553
GLYMA_06G096300
I1K9Q4
100778348
5
iEKPD-Glm-g045
GLYMA_08G156400
I1KTP1
100778394
6
iEKPD-Glm-g014
GLYMA_04G213400
K7KLG8
100781715
7
iEKPD-Glm-g008
GLYMA_05G191200
I1K4Y6
100784942
8
iEKPD-Glm-1220
GLYMA_11G077000
I1LI15
100800422
9
iEKPD-Glm-1183
GLYMA_10G284200
K7LLZ3
100804117
10
iEKPD-Glm-1233
GLYMA_11G123500
K7LPC3
100808763
11
iEKPD-Glm-g025
GLYMA_06G152800
I1KBI7
100811499
12
iEKPD-Glm-0096
GLYMA_01G241300
I1JAW9
100816558
13
iEKPD-Glm-0065
GLYMA_01G166400
K7K483
100819389
14
iEKPD-Glm-0358
GLYMA_04G094500
I1JV67
GLYMA_04G094500
15
iEKPD-Glm-g027
GLYMA_06G013800
I1K784
GLYMA_06G013800