ID AKT2_MOUSE Reviewed; 481 AA. AC Q60823; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 205. DE RecName: Full=RAC-beta serine/threonine-protein kinase; DE EC=2.7.11.1; DE AltName: Full=Protein kinase Akt-2; DE AltName: Full=Protein kinase B beta; DE Short=PKB beta; DE AltName: Full=RAC-PK-beta; GN Name=Akt2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus; RX PubMed=7566964; RA Altomare D.A., Guo K., Cheng J.Q., Sonoda G., Walsh K., Testa J.R.; RT "Cloning, chromosomal localization and expression analysis of the mouse RT Akt2 oncogene."; RL Oncogene 11:1055-1060(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Retina, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP INTERACTION WITH WDFY2. RX PubMed=16792529; DOI=10.1042/bj20060511; RA Fritzius T., Burkard G., Haas E., Heinrich J., Schweneker M., Bosse M., RA Zimmermann S., Frey A.D., Caelers A., Bachmann A.S., Moelling K.; RT "A WD-FYVE protein binds to the kinases Akt and PKCzeta/lambda."; RL Biochem. J. 399:9-20(2006). RN [4] RP INTERACTION WITH BTBD10. RX PubMed=18160256; DOI=10.1016/j.cellsig.2007.11.004; RA Nawa M., Kanekura K., Hashimoto Y., Aiso S., Matsuoka M.; RT "A novel Akt/PKB-interacting protein promotes cell adhesion and inhibits RT familial amyotrophic lateral sclerosis-linked mutant SOD1-induced neuronal RT death via inhibition of PP2A-mediated dephosphorylation of Akt/PKB."; RL Cell. Signal. 20:493-505(2008). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND THR-451, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP FUNCTION IN PHOSPHORYLATION OF PTIX2. RX PubMed=20019746; DOI=10.1038/cdd.2009.194; RA Gherzi R., Trabucchi M., Ponassi M., Gallouzi I.E., Rosenfeld M.G., RA Briata P.; RT "Akt2-mediated phosphorylation of Pitx2 controls Ccnd1 mRNA decay during RT muscle cell differentiation."; RL Cell Death Differ. 17:975-983(2010). RN [7] RP INTERACTION WITH WDFY2, AND SUBCELLULAR LOCATION. RX PubMed=20189988; DOI=10.1074/jbc.m110.110536; RA Walz H.A., Shi X., Chouinard M., Bue C.A., Navaroli D.M., Hayakawa A., RA Zhou Q.L., Nadler J., Leonard D.M., Corvera S.; RT "Isoform-specific regulation of Akt signaling by the endosomal protein RT WDFY2."; RL J. Biol. Chem. 285:14101-14108(2010). RN [8] RP FUNCTION IN PHOSPHORYLATION OF C2CD5. RX PubMed=21907143; DOI=10.1016/j.cmet.2011.06.015; RA Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., RA Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., RA Kruger M., Jiang Z.Y.; RT "C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into RT the plasma membrane."; RL Cell Metab. 14:378-389(2011). RN [9] RP REVIEW ON FUNCTION. RX PubMed=21620960; DOI=10.1016/j.cellsig.2011.05.004; RA Hers I., Vincent E.E., Tavare J.M.; RT "Akt signalling in health and disease."; RL Cell. Signal. 23:1515-1527(2011). RN [10] RP REVIEW ON FUNCTION. RX PubMed=21432781; DOI=10.14670/hh-26.651; RA Heron-Milhavet L., Khouya N., Fernandez A., Lamb N.J.; RT "Akt1 and Akt2: differentiating the aktion."; RL Histol. Histopathol. 26:651-662(2011). RN [11] RP INTERACTION WITH KCTD20. RX PubMed=24156551; DOI=10.1186/1471-2091-14-27; RA Nawa M., Matsuoka M.; RT "KCTD20, a relative of BTBD10, is a positive regulator of Akt."; RL BMC Biochem. 14:27-27(2013). CC -!- FUNCTION: AKT2 is one of 3 closely related serine/threonine-protein CC kinases (AKT1, AKT2 and AKT3) called the AKT kinases, and which CC regulate many processes including metabolism, proliferation, cell CC survival, growth and angiogenesis. This is mediated through serine CC and/or threonine phosphorylation of a range of downstream substrates. CC Over 100 substrate candidates have been reported so far, but for most CC of them, no isoform specificity has been reported. AKT is responsible CC of the regulation of glucose uptake by mediating insulin-induced CC translocation of the SLC2A4/GLUT4 glucose transporter to the cell CC surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its CC phosphatase activity preventing dephosphorylation of the insulin CC receptor and the attenuation of insulin signaling. Phosphorylation of CC TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 CC proteins, which is required for insulin-stimulated glucose transport. CC AKT regulates also the storage of glucose in the form of glycogen by CC phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in CC inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by CC AKT is also thought to be one mechanism by which cell proliferation is CC driven. AKT regulates also cell survival via the phosphorylation of CC MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' CC decreases MAP3K5 kinase activity stimulated by oxidative stress and CC thereby prevents apoptosis. AKT mediates insulin-stimulated protein CC synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby CC activating mTORC1 signaling and leading to both phosphorylation of 4E- CC BP1 and in activation of RPS6KB1. AKT is involved in the CC phosphorylation of members of the FOXO factors (Forkhead family of CC transcription factors), leading to binding of 14-3-3 proteins and CC cytoplasmic localization. In particular, FOXO1 is phosphorylated at CC 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated CC on equivalent sites. AKT has an important role in the regulation of NF- CC kappa-B-dependent gene transcription and positively regulates the CC activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). CC The phosphorylation of CREB1 induces the binding of accessory proteins CC that are necessary for the transcription of pro-survival genes such as CC BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase CC (ACLY), thereby potentially regulating ACLY activity and fatty acid CC synthesis. Activates the 3B isoform of cyclic nucleotide CC phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting CC in reduced cyclic AMP levels and inhibition of lipolysis. CC Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P- CC 5 activity. The Rho GTPase-activating protein DLC1 is another substrate CC and its phosphorylation is implicated in the regulation cell CC proliferation and cell growth. AKT plays a role as key modulator of the CC AKT-mTOR signaling pathway controlling the tempo of the process of CC newborn neurons integration during adult neurogenesis, including CC correct neuron positioning, dendritic development and synapse CC formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) CC to mediate the effects of various growth factors such as platelet- CC derived growth factor (PDGF), epidermal growth factor (EGF), insulin CC and insulin-like growth factor I (IGF-I). AKT mediates the CC antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated CC regulation of cell migration and adhesion assembly and disassembly. May CC be involved in the regulation of the placental development. Involved in CC the inhibition of ciliogenesis associated with RAB8-dependent cilia CC growth (By similarity). {ECO:0000250|UniProtKB:P31751}. CC -!- FUNCTION: One of the few specific substrates of AKT2 identified so far CC is PITX2. Phosphorylation of PITX2 impairs its association with the CC CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. CC AKT2 seems also to be the principal isoform responsible of the CC regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during CC insulin-stimulated adipocytes. AKT2 is also specifically involved in CC skeletal muscle differentiation, one of its substrates in this process CC being ANKRD2. Phosphorylates CLK2 on 'Thr-343'. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; CC -!- ACTIVITY REGULATION: Two specific sites, one in the kinase domain (Thr- CC 309) and the other in the C-terminal regulatory region (Ser-474), need CC to be phosphorylated for its full activation. {ECO:0000250}. CC -!- SUBUNIT: Interacts (via PH domain) with MTCP1, TCL1A and TCL1B. CC Interacts with CLK2, PBH2 and TRAF6. Interacts (when phosphorylated) CC with CLIP3, the interaction promotes cell membrane localization (By CC similarity). Interacts with BTBD10 (PubMed:18160256). Interacts with CC KCTD20 (PubMed:24156551). Interacts with WDFY2 (via WD repeats 1-3) CC (PubMed:16792529, PubMed:20189988). {ECO:0000250|UniProtKB:P31751, CC ECO:0000269|PubMed:16792529, ECO:0000269|PubMed:18160256, CC ECO:0000269|PubMed:20189988, ECO:0000269|PubMed:24156551}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20189988}. Nucleus CC {ECO:0000269|PubMed:20189988}. Cell membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. Early endosome CC {ECO:0000269|PubMed:20189988}. Note=Localizes within both nucleus and CC cytoplasm of proliferative primary myoblasts and mostly within the CC nucleus of differentiated primary myoblasts. By virtue of the N- CC terminal PH domain, is recruited to sites of the plasma membrane CC containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting CC is also facilitared by interaction with CLIP3. Colocalizes with WDFY2 CC in early endosomes (PubMed:20189988). {ECO:0000250, CC ECO:0000269|PubMed:20189988}. CC -!- DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-kinase CC alpha (PIK3CA) results in its targeting to the plasma membrane. CC {ECO:0000250}. CC -!- PTM: Phosphorylation on Thr-309 and Ser-474 is required for full CC activity. {ECO:0000250}. CC -!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked CC polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT2 ubiquitination. CC When fully phosphorylated and translocated into the nucleus, undergoes CC 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its CC degradation by the proteasome (By similarity). {ECO:0000250}. CC -!- PTM: O-GlcNAcylation at Thr-306 and Thr-313 inhibits activating CC phosphorylation at Thr-309 via disrupting the interaction between AKT CC and PDK1. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. RAC subfamily. {ECO:0000305}. CC -!- CAUTION: In light of strong homologies in the primary amino acid CC sequence, the 3 AKT kinases were long surmised to play redundant and CC overlapping roles. More recent studies has brought into question the CC redundancy within AKT kinase isoforms and instead pointed to isoform CC specific functions in different cellular events and diseases. AKT1 is CC more specifically involved in cellular survival pathways, by inhibiting CC apoptotic processes; whereas AKT2 is more specific for the insulin CC receptor signaling pathway. Moreover, while AKT1 and AKT2 are often CC implicated in many aspects of cellular transformation, the 2 isoforms CC act in a complementary opposing manner. The role of AKT3 is less clear, CC though it appears to be predominantly expressed in brain. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U22445; AAA83557.1; -; mRNA. DR EMBL; BC026151; AAH26151.1; -; mRNA. DR EMBL; BC040377; AAH40377.1; -; mRNA. DR CCDS; CCDS21027.1; -. DR RefSeq; NP_001103678.1; NM_001110208.2. DR RefSeq; NP_001318037.1; NM_001331108.1. DR RefSeq; NP_001318038.1; NM_001331109.1. DR RefSeq; NP_031460.1; NM_007434.4. DR RefSeq; XP_006539540.1; XM_006539477.1. DR RefSeq; XP_006539543.1; XM_006539480.1. DR RefSeq; XP_006539544.1; XM_006539481.3. DR AlphaFoldDB; Q60823; -. DR BMRB; Q60823; -. DR SMR; Q60823; -. DR BioGRID; 198057; 17. DR IntAct; Q60823; 25. DR STRING; 10090.ENSMUSP00000103981; -. DR ChEMBL; CHEMBL5382; -. DR GlyCosmos; Q60823; 4 sites, No reported glycans. DR GlyGen; Q60823; 5 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q60823; -. DR PhosphoSitePlus; Q60823; -. DR EPD; Q60823; -. DR jPOST; Q60823; -. DR MaxQB; Q60823; -. DR PaxDb; 10090-ENSMUSP00000103981; -. DR ProteomicsDB; 296016; -. DR Pumba; Q60823; -. DR Antibodypedia; 3775; 1866 antibodies from 50 providers. DR DNASU; 11652; -. DR Ensembl; ENSMUST00000051356.12; ENSMUSP00000052103.6; ENSMUSG00000004056.16. DR Ensembl; ENSMUST00000108343.8; ENSMUSP00000103980.2; ENSMUSG00000004056.16. DR Ensembl; ENSMUST00000108344.9; ENSMUSP00000103981.3; ENSMUSG00000004056.16. DR Ensembl; ENSMUST00000167435.8; ENSMUSP00000132141.2; ENSMUSG00000004056.16. DR GeneID; 11652; -. DR KEGG; mmu:11652; -. DR UCSC; uc009fwr.2; mouse. DR AGR; MGI:104874; -. DR CTD; 208; -. DR MGI; MGI:104874; Akt2. DR VEuPathDB; HostDB:ENSMUSG00000004056; -. DR eggNOG; KOG0690; Eukaryota. DR GeneTree; ENSGT00940000157189; -. DR HOGENOM; CLU_000288_11_0_1; -. DR InParanoid; Q60823; -. DR OMA; DRCECLG; -. DR OrthoDB; 3028764at2759; -. DR PhylomeDB; Q60823; -. DR TreeFam; TF102004; -. DR BRENDA; 2.7.11.1; 3474. DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling. DR Reactome; R-MMU-1358803; Downregulation of ERBB2:ERBB3 signaling. DR Reactome; R-MMU-165158; Activation of AKT2. DR Reactome; R-MMU-165181; Inhibition of TSC complex formation by PKB. DR Reactome; R-MMU-198323; AKT phosphorylates targets in the cytosol. DR Reactome; R-MMU-198693; AKT phosphorylates targets in the nucleus. DR Reactome; R-MMU-199418; Negative regulation of the PI3K/AKT network. DR Reactome; R-MMU-211163; AKT-mediated inactivation of FOXO1A. DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex. DR Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling. DR Reactome; R-MMU-389513; CTLA4 inhibitory signaling. DR Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma. DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation. DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation. DR Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors. DR Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition. DR Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry. DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs. DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity. DR Reactome; R-MMU-9607240; FLT3 Signaling. DR Reactome; R-MMU-9614399; Regulation of localization of FOXO transcription factors. DR Reactome; R-MMU-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling. DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway. DR BioGRID-ORCS; 11652; 4 hits in 84 CRISPR screens. DR ChiTaRS; Akt2; mouse. DR PRO; PR:Q60823; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q60823; Protein. DR Bgee; ENSMUSG00000004056; Expressed in hindlimb stylopod muscle and 228 other cell types or tissues. DR ExpressionAtlas; Q60823; baseline and differential. DR GO; GO:0005938; C:cell cortex; IMP:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell. DR GO; GO:0032593; C:insulin-responsive compartment; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0032587; C:ruffle membrane; IMP:UniProtKB. DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI. DR GO; GO:0031982; C:vesicle; ISO:MGI. DR GO; GO:0005524; F:ATP binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0140677; F:molecular function activator activity; ISO:MGI. DR GO; GO:0004672; F:protein kinase activity; IDA:MGI. DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI. DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR GO; GO:0071486; P:cellular response to high light intensity; IMP:MGI. DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI. DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI. DR GO; GO:0006006; P:glucose metabolic process; IMP:MGI. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0010748; P:negative regulation of long-chain fatty acid import across plasma membrane; ISO:MGI. DR GO; GO:0033119; P:negative regulation of RNA splicing; ISO:MGI. DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:MGI. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI. DR GO; GO:2000147; P:positive regulation of cell motility; ISO:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:0046326; P:positive regulation of glucose import; IGI:MGI. DR GO; GO:0010907; P:positive regulation of glucose metabolic process; ISO:MGI. DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:MGI. DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:MGI. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI. DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI. DR GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:MGI. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI. DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB. DR GO; GO:0009967; P:positive regulation of signal transduction; ISO:MGI. DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0072659; P:protein localization to plasma membrane; IGI:MGI. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0032868; P:response to insulin; ISO:MGI. DR GO; GO:0097473; P:retinal rod cell apoptotic process; IMP:MGI. DR CDD; cd01241; PH_PKB; 1. DR CDD; cd05595; STKc_PKB_beta; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR034677; Akt2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR039026; PH_PKB. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24351:SF192; PROTEIN KINASE C; 1. DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q60823; MM. PE 1: Evidence at protein level; KW Acetylation; Apoptosis; ATP-binding; Carbohydrate metabolism; KW Cell membrane; Cytoplasm; Developmental protein; Disulfide bond; Endosome; KW Glucose metabolism; Glycogen biosynthesis; Glycogen metabolism; KW Glycoprotein; Kinase; Manganese; Membrane; Metal-binding; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Sugar transport; Transferase; KW Translation regulation; Transport; Ubl conjugation. FT CHAIN 1..481 FT /note="RAC-beta serine/threonine-protein kinase" FT /id="PRO_0000085609" FT DOMAIN 5..108 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 152..409 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 410..481 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT ACT_SITE 275 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 158..166 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 181 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 280 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:P31751" FT BINDING 293 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:P31751" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P31751" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31751" FT MOD_RES 126 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 309 FT /note="Phosphothreonine; by PDPK1" FT /evidence="ECO:0000250|UniProtKB:P31751" FT MOD_RES 447 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31751" FT MOD_RES 451 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 474 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31751" FT MOD_RES 478 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31751" FT CARBOHYD 128 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CARBOHYD 131 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CARBOHYD 306 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT CARBOHYD 313 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT DISULFID 60..77 FT /evidence="ECO:0000250" FT DISULFID 297..311 FT /evidence="ECO:0000250|UniProtKB:P31751" SQ SEQUENCE 481 AA; 55742 MW; 4AB4A9C4FB9CFA7D CRC64; MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP PLNNFSVAEC QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM RAIQMVANSL KQRGPGEDAM DYKCGSPSDS STSEMMEVAV NKARAKVTMN DFDYLKLLGK GTFGKVILVR EKATGRYYAM KILRKEVIIA KDEVAHTVTE SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH LSRERVFTED RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF YNQDHERLFE LILMEEIRFP RTLGPEAKSL LAGLLKKDPK QRLGGGPSDA KEVMEHRFFL SINWQDVVQK KLLPPFKPQV TSEVDTRYFD DEFTAQSITI TPPDRYDSLD PLELDQRTHF PQFSYSASIR E //