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

 AKT2B_XENLA             Reviewed;         485 AA.
Q6IP76;
21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
05-DEC-2018, entry version 86.
RecName: Full=RAC-beta serine/threonine-protein kinase B;
EC=2.7.11.1;
AltName: Full=Protein kinase Akt-2-B;
AltName: Full=Protein kinase B, beta-B;
Short=PKB beta-B;
AltName: Full=RAC-PK-beta-B;
Name=akt2-b;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1] {ECO:0000312|EMBL:AAH72041.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen {ECO:0000312|EMBL:AAH72041.1};
NIH - Xenopus Gene Collection (XGC) project;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Akt2-b is one of several closely related
serine/threonine-protein kinases known as the AKT kinase, 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 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q60823};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q60823};
-!- ACTIVITY REGULATION: Two specific sites, one in the kinase domain
(Thr-313) and the other in the C-terminal regulatory region (Ser-
478), need to be phosphorylated for its full activation.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. RAC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC072041; AAH72041.1; -; mRNA.
RefSeq; NP_001085101.1; NM_001091632.1.
UniGene; Xl.62681; -.
ProteinModelPortal; Q6IP76; -.
SMR; Q6IP76; -.
GeneID; 432172; -.
KEGG; xla:432172; -.
HOVERGEN; HBG108317; -.
KO; K04456; -.
GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0065002; P:intracellular protein transmembrane transport; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
GO; GO:0031340; P:positive regulation of vesicle fusion; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IEA:InterPro.
CDD; cd01241; PH_PKB; 1.
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; IPR039026; PH_PKB.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR039027; RAC_alpha/beta.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24356:SF176; PTHR24356:SF176; 1.
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; 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.
2: Evidence at transcript level;
ATP-binding; Glycoprotein; Kinase; Nucleotide-binding; Phosphoprotein;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 485 RAC-beta serine/threonine-protein kinase
B.
/FTId=PRO_0000223509.
DOMAIN 5 109 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 156 413 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 414 485 AGC-kinase C-terminal.
NP_BIND 162 170 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 279 279 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 185 185 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 313 313 Phosphothreonine. {ECO:0000250}.
MOD_RES 478 478 Phosphoserine. {ECO:0000250}.
CARBOHYD 132 132 O-linked (GlcNAc) serine. {ECO:0000250}.
CARBOHYD 135 135 O-linked (GlcNAc) serine. {ECO:0000250}.
CARBOHYD 310 310 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 317 317 O-linked (GlcNAc) threonine.
{ECO:0000250}.
SEQUENCE 485 AA; 56024 MW; 27D584109098CC56 CRC64;
MNEVMVIKEG WLQKRGEYIK TWRPRYFLLK SDGSFIGYKE KPDSTEHSLL PPLNNFSVAE
CQLMKTERPR PNTFVIRCLQ WTTVIERTFH VDTPEEREEW IIAIQTVANG LKNQVPEDEE
EEAMEVKYGS PSDVSSAEQM DVAMSKGRPK VTMNDFDYLK LLGKGTFGKV ILVREKATGL
YYAMKILRKE VIIAKDEVAH TLTESRVLQN TKHPFLTGLK YAFQTSDRLC FVMEYANGGE
LFFHLSRERV FTEDRARFYG AEIVSALEYL HSRNVVYRDI KLENLMLDKD GHVKITDFGL
CKEGITDGAT MRTFCGTPEY LAPEVLEDND YGRAVDWWGL GVVMYEMMCG RLPFYNQDHE
RLFELILMEE TRFPRTLSPE AKSLLAGLLK KDPKQRLGGG PDDAQEVMSH GFFASINWQD
VTERKLSPPF KPQVTSEIDT RYFDDEFTAQ SITLTPPDRY DNLDALESEQ RPHFPQFSYS
SSIRE


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