位置:首页 > 蛋白库 > AKT1_RAT
AKT1_RAT
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   03-AUG-2022, entry version 213.
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 TORC1 signaling
CC       pathway, and leading to both phosphorylation of 4E-BP1 and in
CC       activation of RPS6KB1. Also regulates the TORC1 signaling pathway by
CC       catalyzing phosphorylation of CASTOR1. 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 (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).
CC       {ECO:0000250|UniProtKB:P31749, ECO:0000250|UniProtKB:P31750,
CC       ECO:0000269|PubMed:10400692, ECO:0000269|PubMed:12107176,
CC       ECO:0000269|PubMed:15546921, ECO:0000269|PubMed:9632753,
CC       ECO:0000303|PubMed:11882383, ECO:0000303|PubMed:21432781,
CC       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).
CC       {ECO:0000250|UniProtKB:P31749, 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}.
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; 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; 14.
DR   DIP; DIP-42185N; -.
DR   IntAct; P47196; 10.
DR   MINT; P47196; -.
DR   STRING; 10116.ENSRNOP00000038369; -.
DR   BindingDB; P47196; -.
DR   ChEMBL; CHEMBL1075215; -.
DR   GlyGen; P47196; 5 sites.
DR   iPTMnet; P47196; -.
DR   PhosphoSitePlus; P47196; -.
DR   jPOST; P47196; -.
DR   PaxDb; P47196; -.
DR   PRIDE; P47196; -.
DR   ABCD; P47196; 1 sequenced antibody.
DR   GeneID; 24185; -.
DR   KEGG; rno:24185; -.
DR   UCSC; RGD:2081; rat.
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   OMA; CIDNERR; -.
DR   OrthoDB; 614710at2759; -.
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 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; IDA:RGD.
DR   GO; GO:0005829; C:cytosol; 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: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; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA: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:0007568; P:aging; IDA:RGD.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:RGD.
DR   GO; GO:0006915; P:apoptotic process; IEP:RGD.
DR   GO; GO:0048266; P:behavioral response to pain; 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:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR   GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:RGD.
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: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:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR   GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IMP:UniProtKB.
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: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:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:RGD.
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:0032091; P:negative regulation of protein binding; ISO:RGD.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:BHF-UCL.
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:NIK/NF-kappaB signaling; 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:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISO:RGD.
DR   GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; 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:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:RGD.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
DR   GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; 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:0051000; P:positive regulation of nitric-oxide synthase activity; 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: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:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IMP: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:0043491; P:protein kinase B signaling; ISO:RGD.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
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:0032880; P:regulation of protein localization; IMP:MGI.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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:0007165; P:signal transduction; IDA: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; -; 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_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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024