BMRB Entry 27320

Name: Hierarchical regulation of FOXO1 by AMPK and AKT through interactions with 14-3-3 proteins
Published: 2019-07-15

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27320

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Hierarchical regulation of FOXO1 by AMPK and AKT through interactions with 14-3-3 proteins

Deposition date:

2017-11-30

Original release date:

2019-07-15

Authors:

Saline, Maria; Badertscher, Lukas; Gunnarsson, Anders; Snow, Melanie; Jacso, Tomas; Norris, Tyrrell; Snijder, Arjan

Citation:

Citation: Saline, Maria; Badertscher, Lukas; Wolter, Madita; Lau, Roxanne; Gunnarsson, Anders; Jacso, Tomas; Norris, Tyrrell; Ottmann, Christian; Snijder, Arjan. "AMPK and AKT protein kinases hierarchically phosphorylate the N-terminus of the FOXO1 transcription factor, modulating interactions with 14-3-3 proteins" J. Biol. Chem. 294, 13106-13116 (2019).
PubMed: 31308176

Assembly members:

Assembly members:
N-terminal domain of FOXO1 phosphorylated on S22, polymer, 67 residues, 7622.1 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-terminal domain of FOXO1 phosphorylated on S22: MAHNHNHNHNHNHNENLYFQ GMAEAPQVVEIDPDFEPLPR PRXCTWPLPRPEFSQSNSAT SSPAPSG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	78
15N chemical shifts	41
1H chemical shifts	39

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-terminal domain of FOXO1 phosphorylated on S22	1

Entities:

Entity 1, N-terminal domain of FOXO1 phosphorylated on S22 67 residues - 7622.1 Da.

Residues 1-21 represent a non-native affinity tag, followed by the initial 45 residues in FOXO1.

1

MET

ALA

HIS

ASN

HIS

ASN

HIS

ASN

HIS

ASN

2

HIS

ASN

HIS

ASN

GLU

ASN

LEU

TYR

PHE

GLN

3

GLY

MET

ALA

GLU

ALA

PRO

GLN

VAL

GLU

4

ILE

ASP

PRO

ASP

PHE

GLU

PRO

LEU

PRO

ARG

5

PRO

ARG

SEP

CYS

THR

TRP

PRO

LEU

PRO

ARG

6

PRO

GLU

PHE

SER

GLN

SER

ASN

SER

ALA

THR

7

SER

PRO

ALA

PRO

SER

GLY

Samples:

sample_1: FOXO1 (1-45) protein HN-tagged, [U-98% 13C; U-98% 15N], 200 uM; potassium phosphate 20 mM; sodium chloride 100 mM; TCEP 1 mM; MgCl 10 mM; ATP 5 mM; DTT 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.7; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

CCPNMR, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz