AKT1_BOVIN
ID AKT1_BOVIN Reviewed; 480 AA.
AC Q01314; Q5ER96;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 188.
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; Synonyms=PKB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1718748; DOI=10.1111/j.1432-1033.1991.tb16305.x;
RA Coffer P.J., Woodgett J.R.;
RT "Molecular cloning and characterisation of a novel putative protein-serine
RT kinase related to the cAMP-dependent and protein kinase C families.";
RL Eur. J. Biochem. 201:475-481(1991).
RN [2]
RP ERRATUM OF PUBMED:1718748, AND SEQUENCE REVISION.
RX PubMed=1533586;
RA Coffer P.J., Woodgett J.R.;
RL Eur. J. Biochem. 205:1217-1218(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Khatib H.;
RT "Complete sequence of the bovine AKT1 gene.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DEPHOSPHORYLATION AT SER-473 BY PHLPP.
RX PubMed=15808505; DOI=10.1016/j.molcel.2005.03.008;
RA Gao T., Furnari F., Newton A.C.;
RT "PHLPP: a phosphatase that directly dephosphorylates Akt, promotes
RT apoptosis, and suppresses tumor growth.";
RL Mol. Cell 18:13-24(2005).
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. This is mediated through serine and/or
CC threonine phosphorylation of a range of downstream substrates. Over 100
CC substrate candidates have been reported so far, but for most of them,
CC no isoform specificity has been reported (By similarity). AKT is
CC responsible of the regulation of glucose uptake by mediating insulin-
CC induced translocation of the SLC2A4/GLUT4 glucose transporter to the
CC cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates
CC its phosphatase activity preventing dephosphorylation of the insulin
CC receptor and the attenuation of insulin signaling (By similarity).
CC Phosphorylation of TBC1D4 triggers the binding of this effector to
CC inhibitory 14-3-3 proteins, which is required for insulin-stimulated
CC glucose transport (By similarity). AKT regulates also the storage of
CC glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21'
CC and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity.
CC Phosphorylation of GSK3 isoforms by AKT is also thought to be one
CC mechanism by which cell proliferation is driven (By similarity). AKT
CC regulates also cell survival via the phosphorylation of MAP3K5
CC (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 the TORC1 signaling pathway, and leading to both
CC phosphorylation of 4E-BP1 and in activation of RPS6KB1. Also regulates
CC the TORC1 signaling pathway by catalyzing phosphorylation of CASTOR1.
CC AKT is involved in the phosphorylation of members of the FOXO factors
CC (Forkhead family of transcription factors), leading to binding of 14-3-
CC 3 proteins and cytoplasmic localization. In particular, FOXO1 is
CC phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4
CC are phosphorylated on equivalent sites. AKT has an important role in
CC the regulation of NF-kappa-B-dependent gene transcription and
CC positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response
CC element binding protein). The phosphorylation of CREB1 induces the
CC binding of accessory proteins that are necessary for the transcription
CC of pro-survival genes such as BCL2 and MCL1 (By similarity). AKT
CC phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby
CC potentially regulating ACLY activity and fatty acid synthesis (By
CC similarity). 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 (By
CC similarity). Phosphorylates PIKFYVE on 'Ser-318', which results in
CC increased PI(3)P-5 activity (By similarity). The Rho GTPase-activating
CC protein DLC1 is another substrate and its phosphorylation is implicated
CC in the regulation cell proliferation and cell growth (By similarity).
CC AKT plays a role as key modulator of the AKT-mTOR signaling pathway
CC controlling the tempo of the process of newborn neurons integration
CC during adult neurogenesis, including correct neuron positioning,
CC dendritic development and synapse formation (By similarity). Signals
CC downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the
CC effects of various growth factors such as platelet-derived growth
CC factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like
CC growth factor I (IGF-I) (By similarity). AKT mediates the antiapoptotic
CC effects of IGF-I (By similarity). Essential for the SPATA13-mediated
CC regulation of cell migration and adhesion assembly and disassembly (By
CC similarity). May be involved in the regulation of the placental
CC development (By similarity). Phosphorylates STK4/MST1 at 'Thr-120' and
CC 'Thr-387' leading to inhibition of its: kinase activity, nuclear
CC translocation, autophosphorylation and ability to phosphorylate FOXO3.
CC Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to
CC inhibition of its: cleavage, kinase activity, autophosphorylation at
CC Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates
CC SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and
CC promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259'
CC and negatively regulates its activity. Phosphorylation of BAD
CC stimulates its pro-apoptotic activity. Phosphorylates KAT6A at 'Thr-
CC 369' and this phosphorylation inhibits the interaction of KAT6A with
CC PML and negatively regulates its acetylation activity towards p53/TP53.
CC Phosphorylates palladin (PALLD), modulating cytoskeletal organization
CC and cell motility. Phosphorylates prohibitin (PHB), playing an
CC important role in cell metabolism and proliferation. Phosphorylates
CC CDKN1A, for which phosphorylation at 'Thr-145' induces its release from
CC CDK2 and cytoplasmic relocalization. These recent findings indicate
CC that the AKT1 isoform has a more specific role in cell motility and
CC proliferation. Phosphorylates CLK2 thereby controlling cell survival to
CC ionizing radiation (By similarity). Phosphorylates PCK1 at 'Ser-90',
CC reducing the binding affinity of PCK1 to oxaloacetate and changing PCK1
CC into an atypical protein kinase activity using GTP as donor (By
CC similarity). Also acts as an activator of TMEM175 potassium channel
CC activity in response to growth factors: forms the lysoK(GF) complex
CC together with TMEM175 and acts by promoting TMEM175 channel activation,
CC independently of its protein kinase activity (By similarity). Acts as a
CC negative regulator of the cGAS-STING pathway by mediating
CC phosphorylation of CGAS during mitosis, leading to its inhibition (By
CC similarity). {ECO:0000250|UniProtKB:P31749,
CC ECO:0000250|UniProtKB:P31750, ECO:0000250|UniProtKB:P47196}.
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 -!- SUBUNIT: Interacts (via the C-terminus) with CCDC88A (via its C-
CC terminus) and THEM4 (via its C-terminus). Interacts with AKTIP.
CC Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B. Interacts with
CC TRAF6. Interacts with GRB10; the interaction leads to GRB10
CC phosphorylation thus promoting YWHAE binding. Interacts with RARA; the
CC interaction phosphorylates RARA and represses its transactivation
CC activity. Interacts with MAP3K5 and TNK2. Interacts with BAD, CLK2,
CC PPP2R5B, STK3 and STK4. Interacts (via PH domain) with SIRT1. Interacts
CC with SRPK2 in a phosphorylation-dependent manner. Interacts with RAF1.
CC Interacts with PKN2 (via C-terminal domain); the interaction occurs
CC with the C-terminus cleavage products of PKN2 in apoptotic cells.
CC Interacts with TRIM13; the interaction ubiquitinates AKT1 leading to
CC its proteasomal degradation. Interacts with and phosphorylated by
CC PDPK1. Interacts with BTBD10. Interacts with KCTD20. Interacts with
CC PA2G4. Interacts with PA2G4. Interacts with KIF14; the interaction is
CC detected in the plasma membrane upon INS stimulation and promotes AKT1
CC phosphorylation. Interacts with FAM83B; activates the PI3K/AKT
CC signaling cascade. Interacts with WDFY2 (via WD repeats 1-3). Forms a
CC complex with WDFY2 and FOXO1. Interacts with FAM168A (By similarity).
CC Interacts with SYAP1 (via phosphorylated form and BSD domain); this
CC interaction is enhanced in a mTORC2-mediated manner in response to
CC epidermal growth factor (EGF) stimulation and activates AKT1 (By
CC similarity). Interacts with PKHM3 (By similarity). Interacts with
CC FKBP5/FKBP51; promoting interaction between Akt/AKT1 and PHLPP1,
CC thereby enhancing dephosphorylation and subsequent activation of
CC Akt/AKT1 (By similarity). Interacts with TMEM175; leading to formation
CC of the lysoK(GF) complex (By similarity).
CC {ECO:0000250|UniProtKB:P31749, ECO:0000250|UniProtKB:P31750,
CC ECO:0000250|UniProtKB:P47196}.
CC -!- INTERACTION:
CC Q01314; Q9R269: Ppl; Xeno; NbExp=2; IntAct=EBI-368344, EBI-368293;
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 -!- 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 (By similarity).
CC {ECO:0000250|UniProtKB:P31749}.
CC -!- PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for
CC full activity (By similarity). Activated TNK2 phosphorylates it on Tyr-
CC 176 resulting in its binding to the anionic plasma membrane
CC phospholipid PA (By similarity). This phosphorylated form localizes to
CC the cell membrane, where it is targeted by PDPK1 and PDPK2 for further
CC phosphorylations on Thr-308 and Ser-473 leading to its activation (By
CC similarity). Ser-473 phosphorylation by mTORC2 favors Thr-308
CC phosphorylation by PDPK1 (By similarity). Ser-473 phosphorylation is
CC enhanced by signaling through activated FLT3 (By similarity). Ser-473
CC is dephosphorylated by PHLPP (PubMed:15808505). Dephosphorylated at
CC Thr-308 and Ser-473 by PP2A phosphatase. The phosphorylated form of
CC PPP2R5B is required for bridging AKT1 with PP2A phosphatase. Ser-473 is
CC dephosphorylated by CPPED1, leading to termination of signaling (By
CC similarity). {ECO:0000250|UniProtKB:P31749,
CC ECO:0000269|PubMed:15808505}.
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; X61036; CAA43371.1; -; mRNA.
DR EMBL; AY781100; AAW71957.1; -; mRNA.
DR PIR; S62117; S62117.
DR RefSeq; NP_776411.1; NM_173986.2.
DR AlphaFoldDB; Q01314; -.
DR SMR; Q01314; -.
DR BioGRID; 158368; 3.
DR CORUM; Q01314; -.
DR ELM; Q01314; -.
DR IntAct; Q01314; 1.
DR STRING; 9913.ENSBTAP00000023461; -.
DR ChEMBL; CHEMBL1250377; -.
DR iPTMnet; Q01314; -.
DR PRIDE; Q01314; -.
DR GeneID; 280991; -.
DR KEGG; bta:280991; -.
DR CTD; 207; -.
DR eggNOG; KOG0690; Eukaryota.
DR InParanoid; Q01314; -.
DR OrthoDB; 614710at2759; -.
DR BRENDA; 2.7.11.1; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0099104; F:potassium channel activator activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0070848; P:response to growth factor; ISS:UniProtKB.
DR GO; GO:0060416; P:response to growth hormone; IDA:AgBase.
DR GO; GO:1990418; P:response to insulin-like growth factor stimulus; IDA:AgBase.
DR CDD; cd01241; PH_PKB; 1.
DR CDD; cd05594; STKc_PKB_alpha; 1.
DR Gene3D; 2.30.29.30; -; 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; IPR039027; RAC_alpha.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF200; PTHR24351:SF200; 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; 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;
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_0000085604"
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 450..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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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:0000250|UniProtKB:P31749"
FT MOD_RES 129
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT MOD_RES 176
FT /note="Phosphotyrosine; by TNK2"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT MOD_RES 308
FT /note="Phosphothreonine; by PDPK1"
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 MTOR; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31749"
FT MOD_RES 474
FT /note="Phosphotyrosine"
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 CONFLICT 149
FT /note="D -> E (in Ref. 1; CAA43371)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="L -> V (in Ref. 1; CAA43371)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..174
FT /note="GR -> AA (in Ref. 1; CAA43371)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="F -> S (in Ref. 1; CAA43371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 55748 MW; 152E6613C4E6ED5A CRC64;
MNDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDLEQRES PLNNFSVAQC
QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWT TAIQTVADGL KRQEEETMDF
RSGSPGENSG AEEMEVSLAK PKHRVTMNDF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI
LKKEVIVAKD EVAHTLTENR VLQNSRHPFL TALKYSFQTH DRLCFVMEYA NGGELFFHLS
RERVFSEDRA RFYGAEIVSA LDYLHSEKEV VYRDLKLENL MLDKDGHIKI TDFGLCKEGI
KDGATMKTFC GTPEYLAPEV LEDNDYGRAV DWWGLGVVMY EMMCGRLPFY NQDHEKLFEL
ILMEEIRFPR TLSPEAKSLL SGLLKKDPKQ RLGGGSEDAK EIMQHRFFAS IVWQDVYEKK
LSPPFKPQVT SETDTRYFDE EFTAQMITIT PPDQDDSMEG VDSERRPHFP QFSYSASATA
