PMID- 10208883
OWN - NLM
STAT- MEDLINE
DCOM- 19990601
LR  - 20161124
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 257
IP  - 3
DP  - 1999 Apr 21
TI  - Identification of a human Akt3 (protein kinase B gamma) which contains the
      regulatory serine phosphorylation site.
PG  - 906-10
AB  - The family of protein kinases called Akt, protein kinase B (PKB), or related to A
      and C kinase (RAC) have been implicated in numerous biological processes
      including adipocyte and muscle differentiation, glycogen synthesis, glucose
      uptake, apoptosis and cellular proliferation. There are 3 known isoforms of this 
      enzyme in mammalian cells (1/alpha, 2/beta and 3/gamma). Akt1 and 2 contain a key
      regulatory serine phosphorylation site in the carboxy-terminal region of the
      protein. However, the reported sequence of the rat Akt3 protein differed
      significantly from this in that it lacked 25 amino acids in the C-terminal
      region, including this key regulatory serine phosphorylation site (Biochem.
      Biophys. Res. Commun. 216, 526-534). In the present studies we show that the
      deduced sequence of human Akt3 contains this serine and that it is phosphorylated
      in response to insulin. These results indicate that human Akt3 is regulated
      similarly to Akt1 and Akt2.
CI  - Copyright 1999 Academic Press.
FAU - Nakatani, K
AU  - Nakatani K
AD  - Department of Molecular Pharmacology, Stanford University School of Medicine,
      Stanford, California, 94305, USA.
FAU - Sakaue, H
AU  - Sakaue H
FAU - Thompson, D A
AU  - Thompson DA
FAU - Weigel, R J
AU  - Weigel RJ
FAU - Roth, R A
AU  - Roth RA
LA  - eng
SI  - GENBANK/AF135794
GR  - CA63251/CA/NCI NIH HHS/United States
GR  - CA77350/CA/NCI NIH HHS/United States
GR  - DK 34926/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Insulin)
RN  - 0 (Oncogene Proteins)
RN  - 0 (RNA, Messenger)
RN  - 17885-08-4 (Phosphoserine)
RN  - EC 2.7.11.1 (AKT3 protein, human)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Western
MH  - CHO Cells
MH  - Cloning, Molecular
MH  - Cricetinae
MH  - Expressed Sequence Tags
MH  - Gene Expression Regulation/drug effects
MH  - Humans
MH  - Insulin/pharmacology
MH  - Introns/genetics
MH  - Molecular Sequence Data
MH  - Oncogene Proteins/chemistry/genetics/*metabolism
MH  - Phosphorylation/drug effects
MH  - Phosphoserine/*metabolism
MH  - Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism
MH  - Proto-Oncogene Proteins c-akt
MH  - RNA, Messenger/analysis/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 1999/04/20 00:00
MHDA- 1999/04/20 00:01
CRDT- 1999/04/20 00:00
PHST- 1999/04/20 00:00 [pubmed]
PHST- 1999/04/20 00:01 [medline]
PHST- 1999/04/20 00:00 [entrez]
AID - S0006-291X(99)90559-4 [pii]
AID - 10.1006/bbrc.1999.0559 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Apr 21;257(3):906-10. doi:
      10.1006/bbrc.1999.0559.