ID AKT1_RAT Reviewed; 480 AA.
AC P47196;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 222.
DE RecName: Full=RAC-alpha serine/threonine-protein kinase;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase B;
DE Short=PKB;
DE AltName: Full=Protein kinase B alpha;
DE Short=PKB alpha;
DE AltName: Full=RAC-PK-alpha;
GN Name=Akt1;
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 MUTAGENESIS OF LYS-179; THR-308 AND SER-473.
RX PubMed=9632753; DOI=10.1128/mcb.18.7.3708;
RA Kitamura T., Ogawa W., Sakaue H., Hino Y., Kuroda S., Takata M.,
RA Matsumoto M., Maeda T., Konishi H., Kikkawa U., Kasuga M.;
RT "Requirement for activation of the serine-threonine kinase Akt (protein
RT kinase B) in insulin stimulation of protein synthesis but not of glucose
RT transport.";
RL Mol. Cell. Biol. 18:3708-3717(1998).
RN [3]
RP FUNCTION, PHOSPHORYLATION AT THR-308 AND SER-473, AND MUTAGENESIS OF
RP LYS-179; THR-308 AND SER-473.
RX PubMed=10400692; DOI=10.1074/jbc.274.29.20611;
RA Takata M., Ogawa W., Kitamura T., Hino Y., Kuroda S., Kotani K., Klip A.,
RA Gingras A.-C., Sonenberg N., Kasuga M.;
RT "Requirement for Akt (protein kinase B) in insulin-induced activation of
RT glycogen synthase and phosphorylation of 4E-BP1 (PHAS-1).";
RL J. Biol. Chem. 274:20611-20618(1999).
RN [4]
RP REVIEW ON FUNCTION.
RX PubMed=11882383; DOI=10.1016/s0898-6568(01)00271-6;
RA Nicholson K.M., Anderson N.G.;
RT "The protein kinase B/Akt signalling pathway in human malignancy.";
RL Cell. Signal. 14:381-395(2002).
RN [5]
RP FUNCTION IN PHOSPHORYLATION OF ACLY.
RX PubMed=12107176; DOI=10.1074/jbc.m204681200;
RA Berwick D.C., Hers I., Heesom K.J., Moule S.K., Tavare J.M.;
RT "The identification of ATP-citrate lyase as a protein kinase B (Akt)
RT substrate in primary adipocytes.";
RL J. Biol. Chem. 277:33895-33900(2002).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF PIKFYVE.
RX PubMed=15546921; DOI=10.1242/jcs.01517;
RA Berwick D.C., Dell G.C., Welsh G.I., Heesom K.J., Hers I., Fletcher L.M.,
RA Cooke F.T., Tavare J.M.;
RT "Protein kinase B phosphorylation of PIKfyve regulates the trafficking of
RT GLUT4 vesicles.";
RL J. Cell Sci. 117:5985-5993(2004).
RN [7]
RP INTERACTION WITH PA2G4.
RX PubMed=16832058; DOI=10.1073/pnas.0602923103;
RA Liu Z., Ahn J.Y., Liu X., Ye K.;
RT "Ebp1 isoforms distinctively regulate cell survival and differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10917-10922(2006).
RN [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-129, 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: AKT1 is one of 3 closely related serine/threonine-protein
CC kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate
CC many processes including metabolism, proliferation, cell survival,
CC growth and angiogenesis (PubMed:11882383, PubMed:21620960,
CC PubMed:21432781). This is mediated through serine and/or threonine
CC phosphorylation of a range of downstream substrates (PubMed:11882383,
CC PubMed:21620960, PubMed:21432781). Over 100 substrate candidates have
CC been reported so far, but for most of them, no isoform specificity has
CC been reported (PubMed:11882383, PubMed:21620960, PubMed:21432781). AKT
CC is responsible of the regulation of glucose uptake by mediating
CC insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter
CC to the cell surface (PubMed:9632753, PubMed:10400692). Phosphorylation
CC of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity
CC preventing dephosphorylation of the insulin receptor and the
CC attenuation of insulin signaling (By similarity). 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 (By similarity). AKT regulates also the storage of glucose in the form
CC of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9',
CC resulting in inhibition of its kinase activity. Phosphorylation of GSK3
CC isoforms by AKT is also thought to be one mechanism by which cell
CC proliferation is driven (By similarity). AKT regulates also cell
CC survival via the phosphorylation of MAP3K5 (apoptosis signal-related
CC kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity
CC stimulated by oxidative stress and thereby prevents apoptosis. AKT
CC mediates insulin-stimulated protein synthesis by phosphorylating TSC2
CC at 'Ser-939' and 'Thr-1462', thereby activating the mTORC1 signaling
CC pathway, and leading to both phosphorylation of 4E-BP1 and in
CC activation of RPS6KB1. Also regulates the mTORC1 signaling pathway by
CC catalyzing phosphorylation of CASTOR1 and DEPDC5. AKT is involved in
CC the 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 (By similarity). AKT phosphorylates 'Ser-454' on ATP
CC citrate lyase (ACLY), thereby potentially regulating ACLY activity and
CC fatty acid synthesis (PubMed:12107176). Activates the 3B isoform of
CC cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of
CC 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of
CC lipolysis (By similarity). Phosphorylates PIKFYVE on 'Ser-318', which
CC results in increased PI(3)P-5 activity (PubMed:15546921). The Rho
CC GTPase-activating protein DLC1 is another substrate and its
CC phosphorylation is implicated in the regulation cell proliferation and
CC cell growth (By similarity). 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 formation
CC (By similarity). Signals downstream of phosphatidylinositol 3-kinase
CC (PI(3)K) to mediate the effects of various growth factors such as
CC platelet-derived growth factor (PDGF), epidermal growth factor (EGF),
CC insulin and insulin-like growth factor I (IGF-I) (By similarity). AKT
CC mediates the antiapoptotic effects of IGF-I (By similarity). Essential
CC for the SPATA13-mediated regulation of cell migration and adhesion
CC assembly and disassembly (By similarity). May be involved in the
CC regulation of the placental development (By similarity). Phosphorylates
CC STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its:
CC kinase activity, nuclear translocation, autophosphorylation and ability
CC to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-
CC 384' leading to inhibition of its: cleavage, kinase activity,
CC autophosphorylation at Thr-180, binding to RASSF1 and nuclear
CC translocation. Phosphorylates SRPK2 and enhances its kinase activity
CC towards SRSF2 and ACIN1 and promotes its nuclear translocation.
CC Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity.
CC Phosphorylation of BAD stimulates its pro-apoptotic activity.
CC Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the
CC interaction of KAT6A with PML and negatively regulates its acetylation
CC activity towards p53/TP53. Phosphorylates palladin (PALLD), modulating
CC cytoskeletal organization and cell motility. Phosphorylates prohibitin
CC (PHB), playing an important role in cell metabolism and proliferation.
CC Phosphorylates CDKN1A, for which phosphorylation at 'Thr-145' induces
CC its release from CDK2 and cytoplasmic relocalization. These recent
CC findings indicate that the AKT1 isoform has a more specific role in
CC cell motility and proliferation. Phosphorylates CLK2 thereby
CC controlling cell survival to ionizing radiation (By similarity).
CC Phosphorylates PCK1 at 'Ser-90', reducing the binding affinity of PCK1
CC to oxaloacetate and changing PCK1 into an atypical protein kinase
CC activity using GTP as donor (By similarity). Also acts as an activator
CC of TMEM175 potassium channel activity in response to growth factors:
CC forms the lysoK(GF) complex together with TMEM175 and acts by promoting
CC TMEM175 channel activation, independently of its protein kinase
CC activity (By similarity). Acts as a negative regulator of the cGAS-
CC STING pathway by mediating phosphorylation of CGAS during mitosis,
CC leading to its inhibition (By similarity). Acts as an inhibitor of tRNA
CC methylation by mediating phosphorylation of the N-terminus of METTL1,
CC thereby inhibiting METTL1 methyltransferase activity (By similarity).
CC In response to LPAR1 receptor pathway activation, phosphorylates
CC Rabin8/RAB3IP which alters its activity and phosphorylates WDR44 which
CC induces WDR44 binding to Rab11, thereby switching Rab11 vesicular
CC function from preciliary trafficking to endocytic recycling (By
CC similarity). {ECO:0000250|UniProtKB:P31749,
CC ECO:0000250|UniProtKB:P31750, ECO:0000269|PubMed:10400692,
CC ECO:0000269|PubMed:12107176, ECO:0000269|PubMed:15546921,
CC ECO:0000269|PubMed:9632753, ECO:0000303|PubMed:11882383,
CC ECO:0000303|PubMed:21432781, ECO:0000303|PubMed:21620960}.
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: Three specific sites, one in the kinase domain
CC (Thr-308) and the two other ones in the C-terminal regulatory region
CC (Ser-473 and Tyr-474), need to be phosphorylated for its full
CC activation.
CC -!- SUBUNIT: Interacts (via the C-terminus) with CCDC88A (via its C-
CC terminus). Interacts with GRB10; the interaction leads to GRB10
CC phosphorylation thus promoting YWHAE-binding. Interacts with AGAP2
CC (isoform 2/PIKE-A); the interaction occurs in the presence of guanine
CC nucleotides. Interacts with AKTIP. Interacts (via PH domain) with
CC MTCP1, TCL1A and TCL1B. Interacts with CDKN1B; the interaction
CC phosphorylates CDKN1B promoting 14-3-3 binding and cell-cycle
CC progression. Interacts with MAP3K5 and TRAF6. Interacts with BAD,
CC PPP2R5B, STK3 and STK4. Interacts (via PH domain) with SIRT1. Interacts
CC with SRPK2 in a phosphorylation-dependent manner. Interacts with TNK2
CC and CLK2. Interacts with RAF1. Interacts (via the C-terminus) with
CC THEM4 (via its C-terminus). Interacts with TRIM13; the interaction
CC ubiquitinates AKT1 leading to its proteasomal degradation. Interacts
CC with and phosphorylated by PDPK1 (By similarity). Interacts with BTBD10
CC (By similarity). Interacts with KCTD20 (By similarity). Interacts with
CC PA2G4 (PubMed:16832058). Interacts with KIF14; the interaction is
CC detected in the plasma membrane upon INS stimulation and promotes AKT1
CC phosphorylation (By similarity). Interacts with FAM83B; activates the
CC PI3K/AKT signaling cascade (By similarity). Interacts with WDFY2 (via
CC WD repeats 1-3) (By similarity). Forms a complex with WDFY2 and FOXO1
CC (By similarity). Interacts with FAM168A (By similarity). Interacts with
CC SYAP1 (via phosphorylated form and BSD domain); this interaction is
CC enhanced in a mTORC2-mediated manner in response to epidermal growth
CC factor (EGF) stimulation and activates AKT1 (By similarity). Interacts
CC with PKHM3 (By similarity). Interacts with FKBP5/FKBP51; promoting
CC interaction between Akt/AKT1 and PHLPP1, thereby enhancing
CC dephosphorylation and subsequent activation of Akt/AKT1 (By
CC similarity). Interacts with TMEM175; leading to formation of the
CC lysoK(GF) complex (By similarity). {ECO:0000250|UniProtKB:P31749,
CC ECO:0000250|UniProtKB:P31750, ECO:0000269|PubMed:16832058}.
CC -!- INTERACTION:
CC P47196; P04797: Gapdh; NbExp=3; IntAct=EBI-7204362, EBI-349219;
CC P47196; Q63369: Nfkb1; NbExp=9; IntAct=EBI-7204362, EBI-8498561;
CC P47196; O70436: Smad2; NbExp=2; IntAct=EBI-7204362, EBI-7948047;
CC P47196; P84025: Smad3; NbExp=4; IntAct=EBI-7204362, EBI-7201857;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31750}. Nucleus
CC {ECO:0000250|UniProtKB:P31750}. Cell membrane
CC {ECO:0000250|UniProtKB:P31750}. Note=Nucleus after activation by
CC integrin-linked protein kinase 1 (ILK1). Nuclear translocation is
CC enhanced by interaction with TCL1A (By similarity). Phosphorylation on
CC Tyr-176 by TNK2 results in its localization to the cell membrane where
CC it is targeted for further phosphorylations on Thr-308 and Ser-473
CC leading to its activation and the activated form translocates to the
CC nucleus. Colocalizes with WDFY2 in intracellular vesicles (By
CC similarity). {ECO:0000250|UniProtKB:P31749}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Low levels found in liver with
CC slightly higher levels present in thymus and testis.
CC -!- DOMAIN: Binding of the PH domain to phosphatidylinositol 3,4,5-
CC trisphosphate (PI(3,4,5)P3) following phosphatidylinositol 3-kinase
CC alpha (PIK3CA) activity results in its targeting to the plasma
CC membrane. The PH domain mediates interaction with TNK2 and Tyr-176 is
CC also essential for this interaction (By similarity).
CC {ECO:0000250|UniProtKB:P31749}.
CC -!- DOMAIN: The AGC-kinase C-terminal mediates interaction with THEM4.
CC {ECO:0000250|UniProtKB:P31749}.
CC -!- PTM: O-GlcNAcylation at Thr-305 and Thr-312 inhibits activating
CC phosphorylation at Thr-308 via disrupting the interaction between AKT1
CC and PDPK1. O-GlcNAcylation at Ser-473 also probably interferes with
CC phosphorylation at this site. {ECO:0000250|UniProtKB:P31749}.
CC -!- PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for
CC full activity (PubMed:10400692). Activated TNK2 phosphorylates it on
CC Tyr-176 resulting in its binding to the anionic plasma membrane
CC phospholipid PA. This phosphorylated form localizes to the cell
CC membrane, where it is targeted by PDPK1 and PDPK2 for further
CC phosphorylations on Thr-308 and Ser-473 leading to its activation. Ser-
CC 473 phosphorylation by mTORC2 favors Thr-308 phosphorylation by PDPK1.
CC Phosphorylated at Thr-308 and Ser-473 by IKBKE and TBK1 (By
CC similarity). Ser-473 phosphorylation is enhanced by signaling through
CC activated FLT3 (By similarity). Ser-473 is dephosphorylated by PHLPP
CC (By similarity). Dephosphorylated at Thr-308 and Ser-473 by PP2A
CC phosphatase. The phosphorylated form of PPP2R5B is required for
CC bridging AKT1 with PP2A phosphatase. Ser-473 is dephosphorylated by
CC CPPED1, leading to termination of signaling (By similarity). AIM2 acts
CC as an inhibitor of AKT1 by inhibiting phosphorylation Ser-473: AIM2
CC acts both by inhibiting the activity of PRKDC/DNA-PK kinase and
CC promoting dephosphorylation by PP2A phosphatase (By similarity).
CC {ECO:0000250|UniProtKB:P31749, ECO:0000250|UniProtKB:P31750,
CC ECO:0000269|PubMed:10400692}.
CC -!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
CC polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT1 ubiquitination
CC is critical for phosphorylation and activation. When ubiquitinated, it
CC translocates to the plasma membrane, where it becomes phosphorylated.
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. Ubiquitinated via 'Lys-48'-linked
CC polyubiquitination by ZNRF1, leading to its degradation by the
CC proteasome. Also ubiquitinated by TRIM13 leading to its proteasomal
CC degradation. Phosphorylated, undergoes 'Lys-48'-linked
CC polyubiquitination preferentially at Lys-284 catalyzed by MUL1, leading
CC to its proteasomal degradation (By similarity).
CC {ECO:0000250|UniProtKB:P31749, ECO:0000250|UniProtKB:P31750}.
CC -!- PTM: Acetylated on Lys-14 and Lys-20 by the histone acetyltransferases
CC EP300 and KAT2B. Acetylation results in reduced phosphorylation and
CC inhibition of activity. Deacetylated at Lys-14 and Lys-20 by SIRT1.
CC SIRT1-mediated deacetylation relieves the inhibition (By similarity).
CC {ECO:0000250|UniProtKB:P31749}.
CC -!- PTM: Cleavage by caspase-3/CASP3 (By similarity). Cleaved at the
CC caspase-3 consensus site Asp-462 during apoptosis, resulting in down-
CC regulation of the AKT signaling pathway and decreased cell survival (By
CC similarity). {ECO:0000250|UniProtKB:P31749,
CC ECO:0000250|UniProtKB:P31750}.
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; D30040; BAA06279.1; -; mRNA.
DR PIR; JC2437; JC2437.
DR RefSeq; NP_150233.1; NM_033230.2.
DR RefSeq; XP_006240693.1; XM_006240631.2.
DR AlphaFoldDB; P47196; -.
DR SMR; P47196; -.
DR BioGRID; 246375; 15.
DR DIP; DIP-42185N; -.
DR IntAct; P47196; 10.
DR MINT; P47196; -.
DR STRING; 10116.ENSRNOP00000038369; -.
DR BindingDB; P47196; -.
DR ChEMBL; CHEMBL1075215; -.
DR GlyCosmos; P47196; 5 sites, No reported glycans.
DR GlyGen; P47196; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P47196; -.
DR PhosphoSitePlus; P47196; -.
DR jPOST; P47196; -.
DR PaxDb; 10116-ENSRNOP00000038369; -.
DR ABCD; P47196; 1 sequenced antibody.
DR Ensembl; ENSRNOT00055050101; ENSRNOP00055041243; ENSRNOG00055028853.
DR Ensembl; ENSRNOT00060046687; ENSRNOP00060038823; ENSRNOG00060026743.
DR Ensembl; ENSRNOT00065048586; ENSRNOP00065039837; ENSRNOG00065028102.
DR GeneID; 24185; -.
DR KEGG; rno:24185; -.
DR UCSC; RGD:2081; rat.
DR AGR; RGD:2081; -.
DR CTD; 207; -.
DR RGD; 2081; Akt1.
DR VEuPathDB; HostDB:ENSRNOG00000028629; -.
DR eggNOG; KOG0690; Eukaryota.
DR HOGENOM; CLU_000288_11_0_1; -.
DR InParanoid; P47196; -.
DR OrthoDB; 3028764at2759; -.
DR PhylomeDB; P47196; -.
DR TreeFam; TF102004; -.
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-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-RNO-165159; MTOR signalling.
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-203615; eNOS activation.
DR Reactome; R-RNO-211163; AKT-mediated inactivation of FOXO1A.
DR Reactome; R-RNO-354192; Integrin signaling.
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-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-RNO-450604; KSRP (KHSRP) binds and destabilizes mRNA.
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-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
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-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
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-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-RNO-9604323; Negative regulation of NOTCH4 signaling.
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:P47196; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000028629; Expressed in heart and 19 other cell types or tissues.
DR Genevisible; P47196; RN.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISO:RGD.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:RGD.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:RGD.
DR GO; GO:0099104; F:potassium channel activator activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; ISO:RGD.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:BHF-UCL.
DR GO; GO:0120283; F:protein serine/threonine kinase binding; IPI:BHF-UCL.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IPI:BHF-UCL.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:RGD.
DR GO; GO:0006924; P:activation-induced cell death of T cells; ISO:RGD.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:RGD.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; ISO:RGD.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0030030; P:cell projection organization; IDA:MGI.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:RGD.
DR GO; GO:0036294; P:cellular response to decreased oxygen levels; ISO:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:RGD.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; ISO:RGD.
DR GO; GO:1901653; P:cellular response to peptide; ISO:RGD.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:RGD.
DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0072655; P:establishment of protein localization to mitochondrion; ISO:RGD.
DR GO; GO:0097194; P:execution phase of apoptosis; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0007281; P:germ cell development; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:UniProtKB.
DR GO; GO:0060709; P:glycogen cell differentiation involved in embryonic placenta development; ISO:RGD.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; ISO:RGD.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD.
DR GO; GO:0072656; P:maintenance of protein location in mitochondrion; ISO:RGD.
DR GO; GO:0022605; P:mammalian oogenesis stage; ISO:RGD.
DR GO; GO:0001893; P:maternal placenta development; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR GO; GO:0110099; P:negative regulation of calcium import into the mitochondrion; IMP:RGD.
DR GO; GO:0045792; P:negative regulation of cell size; IDA:MGI.
DR GO; GO:0160049; P:negative regulation of cGAS/STING signaling pathway; ISO:RGD.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IDA:RGD.
DR GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0010748; P:negative regulation of long-chain fatty acid import across plasma membrane; ISO:RGD.
DR GO; GO:2000402; P:negative regulation of lymphocyte migration; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0150033; P:negative regulation of protein localization to lysosome; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0045861; P:negative regulation of proteolysis; ISO:RGD.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0032929; P:negative regulation of superoxide anion generation; IMP:RGD.
DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISO:RGD.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:RGD.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:RGD.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO: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:1903721; P:positive regulation of I-kappaB phosphorylation; ISO:RGD.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:RGD.
DR GO; GO:0046622; P:positive regulation of organ growth; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:RGD.
DR GO; GO:1905552; P:positive regulation of protein localization to endoplasmic reticulum; ISO:RGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IMP:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:MGI.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0030163; P:protein catabolic process; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR GO; GO:1903715; P:regulation of aerobic respiration; IMP:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:RGD.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; ISO:RGD.
DR GO; GO:0031641; P:regulation of myelination; ISO:RGD.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0110002; P:regulation of tRNA methylation; ISO:RGD.
DR GO; GO:0034405; P:response to fluid shear stress; ISO:RGD.
DR GO; GO:0032094; P:response to food; ISO:RGD.
DR GO; GO:0070848; P:response to growth factor; ISO:RGD.
DR GO; GO:0060416; P:response to growth hormone; ISS:AgBase.
DR GO; GO:0009408; P:response to heat; ISO:RGD.
DR GO; GO:0009725; P:response to hormone; ISO:RGD.
DR GO; GO:1990418; P:response to insulin-like growth factor stimulus; ISS:AgBase.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISS:ParkinsonsUK-UCL.
DR GO; GO:0070141; P:response to UV-A; ISO:RGD.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; ISO:RGD.
DR GO; GO:0021510; P:spinal cord development; IDA:RGD.
DR GO; GO:0051146; P:striated muscle cell differentiation; ISO:RGD.
DR GO; GO:0006412; P:translation; IMP:UniProtKB.
DR CDD; cd01241; PH_PKB; 1.
DR CDD; cd05594; STKc_PKB_alpha; 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; IPR034676; Akt1.
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:SF200; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 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.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; ATP-binding; Carbohydrate metabolism;
KW Cell membrane; Cytoplasm; Developmental protein; Disulfide bond;
KW Glucose metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycoprotein; Isopeptide bond; Kinase; Membrane; Neurogenesis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Sugar transport; Transferase;
KW Translation regulation; Transport; Ubl conjugation.
FT CHAIN 1..480
FT /note="RAC-alpha serine/threonine-protein kinase"
FT /id="PRO_0000085607"
FT DOMAIN 5..108
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 150..408
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 409..480
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 451..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 14..19
FT /ligand="1D-myo-inositol 1,3,4,5-tetrakisphosphate"
FT /ligand_id="ChEBI:CHEBI:57895"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT BINDING 23..25
FT /ligand="1D-myo-inositol 1,3,4,5-tetrakisphosphate"
FT /ligand_id="ChEBI:CHEBI:57895"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT BINDING 53
FT /ligand="1D-myo-inositol 1,3,4,5-tetrakisphosphate"
FT /ligand_id="ChEBI:CHEBI:57895"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT BINDING 86
FT /ligand="1D-myo-inositol 1,3,4,5-tetrakisphosphate"
FT /ligand_id="ChEBI:CHEBI:57895"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT BINDING 156..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT SITE 462
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:P31750"
FT MOD_RES 14
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT MOD_RES 20
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 126
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT MOD_RES 129
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 176
FT /note="Phosphotyrosine; by TNK2"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT MOD_RES 308
FT /note="Phosphothreonine; by IKKE, PDPK1 and TBK1"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT MOD_RES 450
FT /note="Phosphothreonine; by MTOR"
FT /evidence="ECO:0000250|UniProtKB:P31750"
FT MOD_RES 473
FT /note="Phosphoserine; by IKKE, MTOR and TBK1; alternate"
FT /evidence="ECO:0000305|PubMed:10400692"
FT MOD_RES 474
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT CARBOHYD 126
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT CARBOHYD 129
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT CARBOHYD 305
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT CARBOHYD 312
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT CARBOHYD 473
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31750"
FT DISULFID 60..77
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT DISULFID 296..310
FT /evidence="ECO:0000250|UniProtKB:P31751"
FT CROSSLNK 284
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT MUTAGEN 179
FT /note="K->D: Lacks kinase activity. Inhibits insulin-
FT induced activation of glycogen synthase when expressed."
FT /evidence="ECO:0000269|PubMed:10400692,
FT ECO:0000269|PubMed:9632753"
FT MUTAGEN 308
FT /note="T->A: Inhibits insulin-induced activation of
FT endogenous Akt1, insulin-stimulated protein synthesis,
FT insulin-induced activation of glycogen synthase and
FT insulin-induced phosphorylation of 4E-BP1 in a dominant
FT negative manner when overexpressed; when associated with A-
FT 473."
FT /evidence="ECO:0000269|PubMed:10400692,
FT ECO:0000269|PubMed:9632753"
FT MUTAGEN 473
FT /note="S->A: Inhibits insulin-induced activation of
FT endogenous Akt1, insulin-stimulated protein synthesis,
FT insulin-induced activation of glycogen synthase and
FT insulin-induced phosphorylation of 4E-BP1 in a dominant
FT negative manner when overexpressed; when associated with A-
FT 308."
FT /evidence="ECO:0000269|PubMed:10400692,
FT ECO:0000269|PubMed:9632753"
SQ SEQUENCE 480 AA; 55735 MW; 5DCAAE7134366D04 CRC64;
MNDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDVEQRES PLNNFSVAQC
QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWT TAIQTVADGL KRQEEETMDF
RSGSPSDNSG AEEMEVALAK PKHRVTMNEF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI
LKKEVIVAKD EVAHTLTENR VLQNSRHPFL TALKYSFQTH DRLCFVMEYA NGGELFFHLS
RERVFSEDRA RFYGAEIVSA LDYLHSEKNV VYRDLKLENL MLDKDGHIKI TDFGLCKEGI
KDGATMKTFC GTPEYLAPEV LEDNDYGRAV DWWGLGVVMY EMMCGRLPFY NQDHEKLFEL
ILMEEIRFPR TLGPEAKSLL SGLLKKDPTQ RLGGGSEDAK EIMQHRFFAN IVWQDVYEKK
LSPPFKPQVT SETDTRYFDE EFTAQMITIT PPDQDDSMEC VDSERRPHFP QFSYSASGTA
//
