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AKT kinase-transforming protein (EC 2.7.11.1)

 AKT_MLVAT               Reviewed;         501 AA.
P31748;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
20-JUN-2018, entry version 103.
RecName: Full=AKT kinase-transforming protein;
EC=2.7.11.1;
Name=V-AKT;
AKT8 murine leukemia virus.
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Gammaretrovirus; Murine leukemia virus.
NCBI_TaxID=11790;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1833819; DOI=10.1126/science.1833819;
Bellacosa A., Testa J.R., Staal S.P., Tsichlis P.N.;
"A retroviral oncogene, akt, encoding a serine-threonine kinase
containing an SH2-like region.";
Science 254:274-277(1991).
[2]
INTERACTION WITH THEM4.
PubMed=11598301; DOI=10.1126/science.1062030;
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M.,
Hemmings B.A.;
"Carboxyl-terminal modulator protein (CTMP), a negative regulator of
PKB/Akt and v-Akt at the plasma membrane.";
Science 294:374-380(2001).
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with mouse THEM4.
{ECO:0000269|PubMed:11598301}.
-!- DOMAIN: The AGC-kinase C-terminal mediates interaction with THEM4.
-!- PTM: Autophosphorylated on threonine and serine residues.
-!- MISCELLANEOUS: This protein is synthesized as a Gag-Akt
polyprotein.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. RAC subfamily. {ECO:0000305}.
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EMBL; M80675; AAA42545.1; -; Genomic_DNA.
ProteinModelPortal; P31748; -.
SMR; P31748; -.
ChEMBL; CHEMBL3627590; -.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0060416; P:response to growth hormone; ISS:AgBase.
GO; GO:1990418; P:response to insulin-like growth factor stimulus; ISS:AgBase.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd05594; STKc_PKB_alpha; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR034676; Akt1.
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; 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;
ATP-binding; Host-virus interaction; Kinase; Nucleotide-binding;
Oncogene; Phosphoprotein; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 501 AKT kinase-transforming protein.
/FTId=PRO_0000085614.
DOMAIN 26 129 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 171 429 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 430 501 AGC-kinase C-terminal.
NP_BIND 177 185 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 295 295 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 200 200 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 347 347 Phosphotyrosine. {ECO:0000250}.
SEQUENCE 501 AA; 57870 MW; 5AEFDE58CD42F773 CRC64;
AREETLIIIP GLPLSLGATD TMNDVAIVKE GWLHKRGEYI KTWRPRYFLL KNDGTFIGYK
ERPQDVDQRE SPLNNFSVAQ CQLMKTERPR PNTFIIRCLQ WTTVIERTFH VETPEEREEW
ATAIQTVADG LKRQEEETMD FRSGSPSDNS GAEEMEVSLA KPKHRVTMNE FEYLKLLGKG
TFGKVILVKE KATGRYYAMK ILKKEVIVAK DEVAHTLTEN RVLQNSRHPF LTALKYSFQT
HDRLCFVMEY ANGGELFFHL SRERVFSEDR ARFYGAEIVS ALDYLHSEKN VVYRDLKLEN
LMLDKDGHIK ITDFGLCKEG IKDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM
YEMMCGRLPF YNQDHEKLFE LILMEEIRFP RTLGPEAKSL LSGLLKKDPT QRLGGGSEDA
KEIMQHRFFA NIVWQDVYEK KLSPPFKPQV TSETDTRYFD EEFTAQMITI TPPDQDDSME
CVDSERRPHF PQFSYSASGT A


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