AKT2_RAT
ID AKT2_RAT Reviewed; 481 AA.
AC P47197;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=7999118; DOI=10.1006/bbrc.1994.2738;
RA Konishi H., Shinomura T., Kuroda S.I., Ono Y., Kikkawa U.;
RT "Molecular cloning of rat RAC protein kinase alpha and beta and their
RT association with protein kinase C zeta.";
RL Biochem. Biophys. Res. Commun. 205:817-825(1994).
RN [2]
RP FUNCTION, AND INTERACTION WITH CLK2.
RX PubMed=20074525; DOI=10.1016/j.cmet.2009.11.006;
RA Rodgers J.T., Haas W., Gygi S.P., Puigserver P.;
RT "Cdc2-like kinase 2 is an insulin-regulated suppressor of hepatic
RT gluconeogenesis.";
RL Cell Metab. 11:23-34(2010).
RN [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-451 AND SER-461, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
CC {ECO:0000269|PubMed:20074525}.
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 {ECO:0000269|PubMed:20074525}.
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 with BTBD10 (By similarity). Interacts with KCTD20
CC (By similarity). Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B.
CC Interacts with TRAF6. Interacts (when phosphorylated) with CLIP3, the
CC interaction promotes cell membrane localization (By similarity).
CC Interacts with CLK2 (PubMed:20074525). Interacts with WDFY2 (via WD
CC repeats 1-3) (By similarity). {ECO:0000250|UniProtKB:P31751,
CC ECO:0000250|UniProtKB:Q60823, ECO:0000269|PubMed:20074525}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60823}. Nucleus
CC {ECO:0000250|UniProtKB:Q60823}. Cell membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Early endosome
CC {ECO:0000250|UniProtKB:Q60823}. 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. {ECO:0000250|UniProtKB:Q60823}.
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}.
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DR EMBL; D30041; BAA06280.1; -; mRNA.
DR PIR; JC2438; JC2438.
DR RefSeq; NP_058789.1; NM_017093.1.
DR AlphaFoldDB; P47197; -.
DR BMRB; P47197; -.
DR SMR; P47197; -.
DR IntAct; P47197; 1.
DR STRING; 10116.ENSRNOP00000025303; -.
DR GlyGen; P47197; 4 sites.
DR iPTMnet; P47197; -.
DR PhosphoSitePlus; P47197; -.
DR jPOST; P47197; -.
DR PaxDb; P47197; -.
DR PRIDE; P47197; -.
DR GeneID; 25233; -.
DR KEGG; rno:25233; -.
DR UCSC; RGD:2082; rat.
DR CTD; 208; -.
DR RGD; 2082; Akt2.
DR eggNOG; KOG0690; Eukaryota.
DR InParanoid; P47197; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; P47197; -.
DR BRENDA; 2.7.11.1; 5301.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-RNO-165158; Activation of AKT2.
DR Reactome; R-RNO-165181; Inhibition of TSC complex formation by PKB.
DR Reactome; R-RNO-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-RNO-198693; AKT phosphorylates targets in the nucleus.
DR Reactome; R-RNO-199418; Negative regulation of the PI3K/AKT network.
DR Reactome; R-RNO-211163; AKT-mediated inactivation of FOXO1A.
DR Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-RNO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-RNO-389513; CTLA4 inhibitory signaling.
DR Reactome; R-RNO-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-RNO-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-RNO-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR Reactome; R-RNO-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-RNO-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-RNO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-RNO-9607240; FLT3 Signaling.
DR Reactome; R-RNO-9614399; Regulation of localization of FOXO transcription factors.
DR Reactome; R-RNO-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR PRO; PR:P47197; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032593; C:insulin-responsive compartment; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:RGD.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0071486; P:cellular response to high light intensity; ISO:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:RGD.
DR GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
DR GO; GO:0010748; P:negative regulation of long-chain fatty acid import across plasma membrane; ISO:RGD.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IMP:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:2000147; P:positive regulation of cell motility; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:RGD.
DR GO; GO:0010907; P:positive regulation of glucose metabolic process; ISO:RGD.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:RGD.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:RGD.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0009967; P:positive regulation of signal transduction; IMP:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; ISS:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:RGD.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IDA:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0006970; P:response to osmotic stress; IEP:RGD.
DR GO; GO:0097473; P:retinal rod cell apoptotic process; ISO:RGD.
DR CDD; cd01241; PH_PKB; 1.
DR CDD; cd05595; STKc_PKB_beta; 1.
DR Gene3D; 2.30.29.30; -; 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 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; SSF56112; SSF56112; 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.
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_0000085610"
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:0000250|UniProtKB:P31751"
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:22673903"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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"
SQ SEQUENCE 481 AA; 55543 MW; 3C4BE65B2F376F85 CRC64;
MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP PLNNFSVAEC
QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWI RAIQMVANSL KQRGPGEDAM
DYKCGSPSDS STSEMMEVAV SKARAKVTMN DFDYLKLLGK GTFGKVILVR EKATGRYYAM
KILRKEVIIA KDEVAHTVTE SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGDLFFH
LSRERVFTED RARFYGAEIV SALEYLHSTD VVYRDIKLEN LMLDKDGHIK ITDFGLSKEG
ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF YNQDHERLFE
LILMEEIRFP RTLGPEAKSL LAGLLKKDPK QRLGGGPSDA KEVMEHRFFL SINWQDVVQK
KLLPPFKPQV TSEVDTRYFD DEFTAQSITI TPPDRYDSLG SLELDQRTHF PQFSYSASIR
E
