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RAC-beta serine/threonine-protein kinase (EC 2.7.11.1) (Protein kinase Akt-2) (Protein kinase B beta) (PKB beta) (RAC-PK-beta)

 AKT2_RAT                Reviewed;         481 AA.
P47197;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 145.
RecName: Full=RAC-beta serine/threonine-protein kinase;
EC=2.7.11.1;
AltName: Full=Protein kinase Akt-2;
AltName: Full=Protein kinase B beta;
Short=PKB beta;
AltName: Full=RAC-PK-beta;
Name=Akt2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=7999118; DOI=10.1006/bbrc.1994.2738;
Konishi H., Shinomura T., Kuroda S.I., Ono Y., Kikkawa U.;
"Molecular cloning of rat RAC protein kinase alpha and beta and their
association with protein kinase C zeta.";
Biochem. Biophys. Res. Commun. 205:817-825(1994).
[2]
FUNCTION, AND INTERACTION WITH CLK2.
PubMed=20074525; DOI=10.1016/j.cmet.2009.11.006;
Rodgers J.T., Haas W., Gygi S.P., Puigserver P.;
"Cdc2-like kinase 2 is an insulin-regulated suppressor of hepatic
gluconeogenesis.";
Cell Metab. 11:23-34(2010).
[3]
REVIEW ON FUNCTION.
PubMed=21620960; DOI=10.1016/j.cellsig.2011.05.004;
Hers I., Vincent E.E., Tavare J.M.;
"Akt signalling in health and disease.";
Cell. Signal. 23:1515-1527(2011).
[4]
REVIEW ON FUNCTION.
PubMed=21432781; DOI=10.14670/HH-26.651;
Heron-Milhavet L., Khouya N., Fernandez A., Lamb N.J.;
"Akt1 and Akt2: differentiating the aktion.";
Histol. Histopathol. 26:651-662(2011).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-451 AND SER-461, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: AKT2 is one of 3 closely related serine/threonine-
protein kinases (AKT1, AKT2 and AKT3) called the AKT kinases, and
which regulate many processes including metabolism, proliferation,
cell survival, growth and angiogenesis. This is mediated through
serine and/or threonine phosphorylation of a range of downstream
substrates. Over 100 substrate candidates have been reported so
far, but for most of them, no isoform specificity has been
reported. AKT is responsible of the regulation of glucose uptake
by mediating insulin-induced translocation of the SLC2A4/GLUT4
glucose transporter to the cell surface. Phosphorylation of PTPN1
at 'Ser-50' negatively modulates its phosphatase activity
preventing dephosphorylation of the insulin receptor and the
attenuation of insulin signaling. Phosphorylation of TBC1D4
triggers the binding of this effector to inhibitory 14-3-3
proteins, which is required for insulin-stimulated glucose
transport. AKT regulates also the storage of glucose in the form
of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at
'Ser-9', resulting in inhibition of its kinase activity.
Phosphorylation of GSK3 isoforms by AKT is also thought to be one
mechanism by which cell proliferation is driven. AKT regulates
also cell survival via the phosphorylation of MAP3K5 (apoptosis
signal-related kinase). Phosphorylation of 'Ser-83' decreases
MAP3K5 kinase activity stimulated by oxidative stress and thereby
prevents apoptosis. AKT mediates insulin-stimulated protein
synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462',
thereby activating mTORC1 signaling and leading to both
phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is
involved in the phosphorylation of members of the FOXO factors
(Forkhead family of transcription factors), leading to binding of
14-3-3 proteins and cytoplasmic localization. In particular, FOXO1
is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and
FOXO4 are phosphorylated on equivalent sites. AKT has an important
role in the regulation of NF-kappa-B-dependent gene transcription
and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-
response element binding protein). The phosphorylation of CREB1
induces the binding of accessory proteins that are necessary for
the transcription of pro-survival genes such as BCL2 and MCL1. AKT
phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby
potentially regulating ACLY activity and fatty acid synthesis.
Activates the 3B isoform of cyclic nucleotide phosphodiesterase
(PDE3B) via phosphorylation of 'Ser-273', resulting in reduced
cyclic AMP levels and inhibition of lipolysis. Phosphorylates
PIKFYVE on 'Ser-318', which results in increased PI(3)P-5
activity. The Rho GTPase-activating protein DLC1 is another
substrate and its phosphorylation is implicated in the regulation
cell proliferation and cell growth. AKT plays a role as key
modulator of the AKT-mTOR signaling pathway controlling the tempo
of the process of newborn neurons integration during adult
neurogenesis, including correct neuron positioning, dendritic
development and synapse formation. Signals downstream of
phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of
various growth factors such as platelet-derived growth factor
(PDGF), epidermal growth factor (EGF), insulin and insulin-like
growth factor I (IGF-I). AKT mediates the antiapoptotic effects of
IGF-I. Essential for the SPATA13-mediated regulation of cell
migration and adhesion assembly and disassembly. May be involved
in the regulation of the placental development.
{ECO:0000269|PubMed:20074525}.
-!- FUNCTION: One of the few specific substrates of AKT2 identified so
far is PITX2. Phosphorylation of PITX2 impairs its association
with the CCND1 mRNA-stabilizing complex thus shortening the half-
life of CCND1. AKT2 seems also to be the principal isoform
responsible of the regulation of glucose uptake. Phosphorylates
C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is
also specifically involved in skeletal muscle differentiation, one
of its substrates in this process being ANKRD2. Phosphorylates
CLK2 on 'Thr-343'. {ECO:0000269|PubMed:20074525}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Two specific sites, one in the kinase domain
(Thr-309) and the other in the C-terminal regulatory region (Ser-
474), need to be phosphorylated for its full activation.
{ECO:0000250}.
-!- SUBUNIT: Interacts with BTBD10 (By similarity). Interacts with
KCTD20 (By similarity). Interacts (via PH domain) with MTCP1,
TCL1A AND TCL1B. Interacts with TRAF6. Interacts (when
phosphorylated) with CLIP3, the interaction promotes cell membrane
localization (By similarity). Interacts with CLK2
(PubMed:20074525). Interacts with WDFY2 (via WD repeats 1-3) (By
similarity). {ECO:0000250|UniProtKB:P31751,
ECO:0000250|UniProtKB:Q60823, ECO:0000269|PubMed:20074525}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60823}.
Nucleus {ECO:0000250|UniProtKB:Q60823}. Cell membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Early
endosome {ECO:0000250|UniProtKB:Q60823}. Note=Localizes within
both nucleus and cytoplasm of proliferative primary myoblasts and
mostly within the nucleus of differentiated primary myoblasts. By
virtue of the N-terminal PH domain, is recruited to sites of the
plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2,
cell membrane targeting is also facilitared by interaction with
CLIP3. Colocalizes with WDFY2 in early endosomes.
{ECO:0000250|UniProtKB:Q60823}.
-!- DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-
kinase alpha (PIK3CA) results in its targeting to the plasma
membrane. {ECO:0000250}.
-!- PTM: Phosphorylation on Thr-309 and Ser-474 is required for full
activity. {ECO:0000250}.
-!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT2
ubiquitination. When fully phosphorylated and translocated into
the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by
TTC3, leading to its degradation by the proteasome (By
similarity). {ECO:0000250}.
-!- PTM: O-GlcNAcylation at Thr-306 and Thr-313 inhibits activating
phosphorylation at Thr-309 via disrupting the interaction between
AKT and PDK1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. RAC subfamily. {ECO:0000305}.
-!- CAUTION: In light of strong homologies in the primary amino acid
sequence, the 3 AKT kinases were long surmised to play redundant
and overlapping roles. More recent studies has brought into
question the redundancy within AKT kinase isoforms and instead
pointed to isoform specific functions in different cellular events
and diseases. AKT1 is more specifically involved in cellular
survival pathways, by inhibiting apoptotic processes; whereas AKT2
is more specific for the insulin receptor signaling pathway.
Moreover, while AKT1 and AKT2 are often implicated in many aspects
of cellular transformation, the 2 isoforms act in a complementary
opposing manner. The role of AKT3 is less clear, though it appears
to be predominantly expressed in brain. {ECO:0000305}.
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EMBL; D30041; BAA06280.1; -; mRNA.
PIR; JC2438; JC2438.
RefSeq; NP_058789.1; NM_017093.1.
UniGene; Rn.87066; -.
ProteinModelPortal; P47197; -.
SMR; P47197; -.
IntAct; P47197; 2.
STRING; 10116.ENSRNOP00000025303; -.
iPTMnet; P47197; -.
PhosphoSitePlus; P47197; -.
PaxDb; P47197; -.
GeneID; 25233; -.
KEGG; rno:25233; -.
UCSC; RGD:2082; rat.
CTD; 208; -.
RGD; 2082; Akt2.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P47197; -.
KO; K04456; -.
PhylomeDB; P47197; -.
BRENDA; 2.7.11.1; 5301.
PRO; PR:P47197; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0032593; C:insulin-responsive compartment; IDA:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043234; C:protein complex; ISO:RGD.
GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
GO; GO:0090630; P:activation of GTPase activity; ISO:RGD.
GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
GO; GO:0071486; P:cellular response to high light intensity; ISO:RGD.
GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:RGD.
GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0065002; P:intracellular protein transmembrane transport; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
GO; GO:0010748; P:negative regulation of plasma membrane long-chain fatty acid transport; ISO:RGD.
GO; GO:0033119; P:negative regulation of RNA splicing; IMP:RGD.
GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISO:RGD.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:2000147; P:positive regulation of cell motility; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:RGD.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:0046326; P:positive regulation of glucose import; IMP:RGD.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; ISO:RGD.
GO; GO:0010907; P:positive regulation of glucose metabolic process; ISO:RGD.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:RGD.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:RGD.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
GO; GO:0009967; P:positive regulation of signal transduction; IMP:RGD.
GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0031340; P:positive regulation of vesicle fusion; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IMP:RGD.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0032868; P:response to insulin; IDA:RGD.
GO; GO:0014850; P:response to muscle activity; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0006970; P:response to osmotic stress; IEP:RGD.
GO; GO:0097473; P:retinal rod cell apoptotic process; ISO:RGD.
CDD; cd05595; STKc_PKB_beta; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR034677; Akt2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00169; PH; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
SMART; SM00233; PH; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; ATP-binding; Carbohydrate metabolism;
Cell membrane; Complete proteome; Cytoplasm; Developmental protein;
Disulfide bond; Endosome; Glucose metabolism; Glycogen biosynthesis;
Glycogen metabolism; Glycoprotein; Isopeptide bond; Kinase; Manganese;
Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Sugar transport;
Transferase; Translation regulation; Transport; Ubl conjugation.
CHAIN 1 481 RAC-beta serine/threonine-protein kinase.
/FTId=PRO_0000085610.
DOMAIN 5 108 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 152 409 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 410 481 AGC-kinase C-terminal.
NP_BIND 158 166 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 230 232 Inhibitor binding. {ECO:0000250}.
REGION 277 279 Inhibitor binding. {ECO:0000250}.
REGION 292 293 Inhibitor binding. {ECO:0000250}.
ACT_SITE 275 275 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 280 280 Manganese.
{ECO:0000250|UniProtKB:P31751}.
METAL 293 293 Manganese.
{ECO:0000250|UniProtKB:P31751}.
BINDING 181 181 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 181 181 Inhibitor. {ECO:0000250}.
BINDING 200 200 Inhibitor. {ECO:0000250}.
BINDING 232 232 Inhibitor; via amide nitrogen.
{ECO:0000250}.
BINDING 236 236 Inhibitor. {ECO:0000250}.
BINDING 279 279 Inhibitor; via carbonyl oxygen.
{ECO:0000250}.
BINDING 293 293 Inhibitor. {ECO:0000250}.
BINDING 294 294 Inhibitor; via amide nitrogen.
{ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P31751}.
MOD_RES 14 14 N6-acetyllysine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 20 20 N6-acetyllysine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:P31751}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000250|UniProtKB:P31751}.
MOD_RES 128 128 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 131 131 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 178 178 Phosphotyrosine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 309 309 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000250|UniProtKB:P31751}.
MOD_RES 449 449 Phosphothreonine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 451 451 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 461 461 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 474 474 Phosphoserine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 475 475 Phosphotyrosine.
{ECO:0000250|UniProtKB:P31749}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000250|UniProtKB:P31751}.
CARBOHYD 128 128 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 131 131 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 306 306 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 313 313 O-linked (GlcNAc) threonine.
{ECO:0000250}.
DISULFID 60 77 {ECO:0000250}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P31749}.
SEQUENCE 481 AA; 55543 MW; 3C4BE65B2F376F85 CRC64;
MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP PLNNFSVAEC
QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWI RAIQMVANSL KQRGPGEDAM
DYKCGSPSDS STSEMMEVAV SKARAKVTMN DFDYLKLLGK GTFGKVILVR EKATGRYYAM
KILRKEVIIA KDEVAHTVTE SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGDLFFH
LSRERVFTED RARFYGAEIV SALEYLHSTD VVYRDIKLEN LMLDKDGHIK ITDFGLSKEG
ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF YNQDHERLFE
LILMEEIRFP RTLGPEAKSL LAGLLKKDPK QRLGGGPSDA KEVMEHRFFL SINWQDVVQK
KLLPPFKPQV TSEVDTRYFD DEFTAQSITI TPPDRYDSLG SLELDQRTHF PQFSYSASIR
E


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EIAAB31019 Homo sapiens,Human,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,PIP5K1B,PIP5K1-beta,PIP5KIbeta,Protein STM-7,PtdIns(4)P-5-kinase 1 beta,S
EIAAB41232 Map3k7ip2,Mitogen-activated protein kinase kinase kinase 7-interacting protein 2,Rat,Rattus norvegicus,Tab2,TGF-beta-activated kinase 1 and MAP3K7-binding protein 2,TGF-beta-activated kinase 1-binding
EIAAB24864 Homo sapiens,Human,MAP kinase 11,MAP kinase p38 beta,MAPK 11,MAPK11,Mitogen-activated protein kinase 11,Mitogen-activated protein kinase p38 beta,p38-2,p38b,PRKM11,SAPK2,Stress-activated protein kinas
15-288-22776 RAC-beta serine_threonine-protein kinase - EC 2.7.11.1; RAC-PK-beta; Protein kinase Akt-2; Protein kinase B. beta; PKB beta Polyclonal 0.05 mg
15-288-22776 RAC-beta serine_threonine-protein kinase - EC 2.7.11.1; RAC-PK-beta; Protein kinase Akt-2; Protein kinase B. beta; PKB beta Polyclonal 0.1 mg
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
EIAAB11062 90 kDa diacylglycerol kinase,DAG kinase beta,DAGK2,DGKB,DGK-beta,Diacylglycerol kinase beta,Diglyceride kinase beta,Homo sapiens,Human,KIAA0718


 

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