FOXO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FOXO1_HUMAN
• UniProt AC: Q12778
• Protein Name: Forkhead box protein O1
• Gene Name: FOXO1
• Organism: Homo sapiens (Human).
• Sequence Length: 655
• Subcellular Localization: Cytoplasm . Nucleus . Shuttles between the cytoplasm and nucleus. Largely nuclear in unstimulated cells. In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus (By similarity). Insulin-induced phosphorylation at Ser-256 by PKB/AKT1 leads, via
• Protein Description: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner. Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity)..
• Protein Sequence: MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGSAAANPDAAAGLPSASAAAVSADFMSNLSLLEESEDFPQAPGSVAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQPPPPGPLSQHPPVPPAAAGPLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRSRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGEGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPIQTLQDNKSSYGGMSQYNCAPGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVMMGPNSVMSTYGSQASHNKMMNPSSHTHPGHAQQTSAVNGRPLPHTVSTMPHTSGMNRLTQVKTPVQVPLPHPMQMSALGGYSSVSSCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Phosphorylation	EPLPRPRSCTWPLPR CCCCCCCCCCCCCCC	20.69	26074081
24	Phosphorylation	LPRPRSCTWPLPRPE CCCCCCCCCCCCCCC	31.22	19664994
153	Phosphorylation	AGQPRKSSSSRRNAW CCCCCCCCCHHCCCC	35.05	-
164	Phosphorylation	RNAWGNLSYADLITK CCCCCCCCHHHHHHH	23.44	17929957
182	Phosphorylation	SSAEKRLTLSQIYEW HHHHHHCCHHHHHHH	28.53	-
203	Phosphorylation	YFKDKGDSNSSAGWK CCCCCCCCCCCHHHH	47.48	21406692
205	Phosphorylation	KDKGDSNSSAGWKNS CCCCCCCCCHHHHHH	26.05	21406692
206	Phosphorylation	DKGDSNSSAGWKNSI CCCCCCCCHHHHHHH	34.74	21406692
210	Ubiquitination	SNSSAGWKNSIRHNL CCCCHHHHHHHHHHH	39.64	-
212	Phosphorylation	SSAGWKNSIRHNLSL CCHHHHHHHHHHHEE	19.78	19221179
218	Phosphorylation	NSIRHNLSLHSKFIR HHHHHHHEEECEEEE	29.38	27251275
222	Acetylation	HNLSLHSKFIRVQNE HHHEEECEEEEEEEC	33.78	31250005
231	Phosphorylation	IRVQNEGTGKSSWWM EEEEECCCCCCCEEE	34.95	23403867
234	Phosphorylation	QNEGTGKSSWWMLNP EECCCCCCCEEEECC	32.32	22817900
235	Phosphorylation	NEGTGKSSWWMLNPE ECCCCCCCEEEECCC	28.39	22817900
245	Acetylation	MLNPEGGKSGKSPRR EECCCCCCCCCCHHH	67.88	19666589
248	Acetylation	PEGGKSGKSPRRRAA CCCCCCCCCHHHHHH	65.46	19666589
249	Phosphorylation	EGGKSGKSPRRRAAS CCCCCCCCHHHHHHH	27.45	18356527
251	Methylation	GKSGKSPRRRAASMD CCCCCCHHHHHHHCC	48.05	-
253	Methylation	SGKSPRRRAASMDNN CCCCHHHHHHHCCCC	35.47	-
256	Phosphorylation	SPRRRAASMDNNSKF CHHHHHHHCCCCHHH	26.19	23401153
261	Phosphorylation	AASMDNNSKFAKSRS HHHCCCCHHHHHHHH	35.09	23401153
262	Acetylation	ASMDNNSKFAKSRSR HHCCCCHHHHHHHHH	52.01	20543840
265	Acetylation	DNNSKFAKSRSRAAK CCCHHHHHHHHHHHH	49.92	20543840
274	Acetylation	RSRAAKKKASLQSGQ HHHHHHHHHHHHCCC	42.36	20543840
276	Phosphorylation	RAAKKKASLQSGQEG HHHHHHHHHHCCCCC	35.50	23403867
279	Phosphorylation	KKKASLQSGQEGAGD HHHHHHHCCCCCCCC	47.97	26657352
287	Phosphorylation	GQEGAGDSPGSQFSK CCCCCCCCCCCCCCC	30.18	19664994
290	Phosphorylation	GAGDSPGSQFSKWPA CCCCCCCCCCCCCCC	31.28	29255136
293	Phosphorylation	DSPGSQFSKWPASPG CCCCCCCCCCCCCCC	26.61	23403867
294	Acetylation	SPGSQFSKWPASPGS CCCCCCCCCCCCCCC	59.49	31249999
298	Phosphorylation	QFSKWPASPGSHSND CCCCCCCCCCCCCCC	26.22	25159151
301	Phosphorylation	KWPASPGSHSNDDFD CCCCCCCCCCCCCCC	27.42	23403867
303	Phosphorylation	PASPGSHSNDDFDNW CCCCCCCCCCCCCCC	43.59	20363803
311	Phosphorylation	NDDFDNWSTFRPRTS CCCCCCCCCCCCCCC	24.75	27251275
312	Phosphorylation	DDFDNWSTFRPRTSS CCCCCCCCCCCCCCC	18.45	27251275
317	O-linked_Glycosylation	WSTFRPRTSSNASTI CCCCCCCCCCCCCCC	38.91	21540332
317	Phosphorylation	WSTFRPRTSSNASTI CCCCCCCCCCCCCCC	38.91	23403867
318	O-linked_Glycosylation	STFRPRTSSNASTIS CCCCCCCCCCCCCCC	23.91	21805451
318	Phosphorylation	STFRPRTSSNASTIS CCCCCCCCCCCCCCC	23.91	30108239
319	Phosphorylation	TFRPRTSSNASTISG CCCCCCCCCCCCCCC	35.48	15668399
322	Phosphorylation	PRTSSNASTISGRLS CCCCCCCCCCCCCCC	30.44	23927012
323	Phosphorylation	RTSSNASTISGRLSP CCCCCCCCCCCCCCC	19.42	30108239
325	Phosphorylation	SSNASTISGRLSPIM CCCCCCCCCCCCCCC	20.25	23927012
329	Phosphorylation	STISGRLSPIMTEQD CCCCCCCCCCCCCCC	15.83	29255136
333	Phosphorylation	GRLSPIMTEQDDLGE CCCCCCCCCCCCCCC	31.08	29255136
345	Phosphorylation	LGEGDVHSMVYPPSA CCCCCCCCCCCCHHH	15.14	23927012
348	Phosphorylation	GDVHSMVYPPSAAKM CCCCCCCCCHHHHHH	10.77	23927012
351	Phosphorylation	HSMVYPPSAAKMAST CCCCCCHHHHHHHHH	36.03	23927012
383	Phosphorylation	DNLNLLSSPTSLTVS HHHHHCCCCCEEEEE	31.97	22817900
394	Phosphorylation	LTVSTQSSPGTMMQQ EEEECCCCCCCCCCC	19.96	22817900
402	Phosphorylation	PGTMMQQTPCYSFAP CCCCCCCCCCCCCCC	9.83	22817900
416	Phosphorylation	PPNTSLNSPSPNYQK CCCCCCCCCCCCCCC	31.86	22817900
418	Phosphorylation	NTSLNSPSPNYQKYT CCCCCCCCCCCCCCC	26.12	22817900
424	Phosphorylation	PSPNYQKYTYGQSSM CCCCCCCCCCCCCCC	6.94	27080861
425	Phosphorylation	SPNYQKYTYGQSSMS CCCCCCCCCCCCCCC	28.36	27080861
426	Phosphorylation	PNYQKYTYGQSSMSP CCCCCCCCCCCCCCC	15.30	27080861
429	Phosphorylation	QKYTYGQSSMSPLPQ CCCCCCCCCCCCCCC	24.52	25159151
430	Phosphorylation	KYTYGQSSMSPLPQM CCCCCCCCCCCCCCC	18.52	25159151
432	Phosphorylation	TYGQSSMSPLPQMPI CCCCCCCCCCCCCCC	25.82	18669648
467	Phosphorylation	GLLKELLTSDSPPHN HHHHHHHHCCCCCCC	43.01	23401153
468	Phosphorylation	LLKELLTSDSPPHND HHHHHHHCCCCCCCC	35.74	23401153
470	Phosphorylation	KELLTSDSPPHNDIM HHHHHCCCCCCCCCC	39.85	23401153
478	Phosphorylation	PPHNDIMTPVDPGVA CCCCCCCCCCCCCCC	22.09	23927012
489	Phosphorylation	PGVAQPNSRVLGQNV CCCCCCCCCCCCCCC	30.37	23403867
505	Phosphorylation	MGPNSVMSTYGSQAS CCCCCHHHHCCCHHC	19.13	17525332
509	Phosphorylation	SVMSTYGSQASHNKM CHHHHCCCHHCCCCC	16.50	17525332
550	O-linked_Glycosylation	VSTMPHTSGMNRLTQ EECCCCCCCCCCCCC	32.77	21540332
597	Acetylation	MGLLHQEKLPSDLDG CCCCCCCCCCCCCCC	60.16	11791325
647	O-linked_Glycosylation	SFPHSVKTTTHSWVS CCCCCCCCCCCCCCC	34.47	21540332
648	Phosphorylation	FPHSVKTTTHSWVSG CCCCCCCCCCCCCCC	19.45	-
648	O-linked_Glycosylation	FPHSVKTTTHSWVSG CCCCCCCCCCCCCCC	19.45	21540332
649	Phosphorylation	PHSVKTTTHSWVSG- CCCCCCCCCCCCCC-	21.10	-
649	O-linked_Glycosylation	PHSVKTTTHSWVSG- CCCCCCCCCCCCCC-	21.10	21540332
651	Phosphorylation	SVKTTTHSWVSG--- CCCCCCCCCCCC---	27.38	-
651	O-linked_Glycosylation	SVKTTTHSWVSG--- CCCCCCCCCCCC---	27.38	21540332
654	Phosphorylation	TTTHSWVSG------ CCCCCCCCC------	32.31	-
654	O-linked_Glycosylation	TTTHSWVSG------ CCCCCCCCC------	32.31	21540332

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
22	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
24	T	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
24	T	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
24	T	Phosphorylation	Kinase	SGK-FAMILY	-	GPS
24	T	Phosphorylation	Kinase	SGK1	O00141	Uniprot
24	T	Phosphorylation	Kinase	SGK_GROUP	-	PhosphoELM
24	T	Phosphorylation	Kinase	AKT1	P31749	Uniprot
24	T	Phosphorylation	Kinase	AKT2	P31751	Uniprot
153	S	Phosphorylation	Kinase	PKACA	P17612	PSP
212	S	Phosphorylation	Kinase	STK4	Q13043	GPS
212	S	Phosphorylation	Kinase	MST1	P26927	Uniprot
218	S	Phosphorylation	Kinase	MST1	P26927	Uniprot
234	S	Phosphorylation	Kinase	MST1	P26927	Uniprot
235	S	Phosphorylation	Kinase	MST1	P26927	Uniprot
249	S	Phosphorylation	Kinase	CDK1	P11440	PSP
249	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
249	S	Phosphorylation	Kinase	CDK4	P11802	PSP
249	S	Phosphorylation	Kinase	CDK2	P97377	PSP
249	S	Phosphorylation	Kinase	CDK2	P24941	PSP
249	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
256	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
256	S	Phosphorylation	Kinase	SGK-FAMILY	-	GPS
256	S	Phosphorylation	Kinase	SGK_GROUP	-	PhosphoELM
256	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
256	S	Phosphorylation	Kinase	SGK1	O00141	Uniprot
256	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
276	S	Phosphorylation	Kinase	PKACA	P17612	PSP
298	S	Phosphorylation	Kinase	CDK2	P97377	PSP
298	S	Phosphorylation	Kinase	CDK2	P24941	PSP
319	S	Phosphorylation	Kinase	SGK-FAMILY	-	GPS
319	S	Phosphorylation	Kinase	SGK_GROUP	-	PhosphoELM
319	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
319	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
319	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
322	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
322	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
322	S	Phosphorylation	Kinase	SGK1	O00141	Uniprot
322	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
322	S	Phosphorylation	Kinase	CK1	-	Uniprot
322	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
325	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
325	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
325	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
325	S	Phosphorylation	Kinase	CK1	-	Uniprot
325	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
329	S	Phosphorylation	Kinase	NLK	Q9UBE8	PSP
329	S	Phosphorylation	Kinase	DYRK1A	P85051	PSP
329	S	Phosphorylation	Kinase	DYR1A	Q13627	PhosphoELM
649	T	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:19321440
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO32	Q969P5	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:15668399
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:19483080
-	K	Ubiquitination	E3 ubiquitin ligase	DET1	Q7L5Y6	PMID:18815134
-	K	Ubiquitination	E3 ubiquitin ligase	DET1#COP1	Q7L5Y6#Q8NHY2	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:24859451

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
24	T	Phosphorylation	Phosphorylation on Thr-24 is required for binding 14-3-3 proteins.	10358075
24	T	Phosphorylation	Phosphorylation of Ser-256 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-319, permitting phosphorylation of Ser-322 and Ser-325, probably by CDK1, leading to nuclear exclusion and loss of function.	10358075
24	T	Phosphorylation	In response to growth factors, phosphorylation on Thr-24, Ser-256 and Ser-322 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity.	10358075
24	T	Phosphorylation	Dephosphorylated on Thr-24 and Ser-256 by PP2A in beta-cells under oxidative stress leading to nuclear retention (By similarity).	10358075
24	T	Oxidation	Dephosphorylated on Thr-24 and Ser-256 by PP2A in beta-cells under oxidative stress leading to nuclear retention (By similarity).	10358075
212	S	Oxidation	Phosphorylation by STK4/MST1 on Ser-212, upon oxidative stress, inhibits binding to 14-3-3 proteins and nuclear export.	19221179
212	S	Phosphorylation	Phosphorylation by STK4/MST1 on Ser-212, upon oxidative stress, inhibits binding to 14-3-3 proteins and nuclear export.	19221179
249	S	Phosphorylation	Phosphorylation of Ser-249 by CDK1 disrupts binding of 14-3-3 proteins leading to nuclear accumulation and has no effect on DNA-binding nor transcriptional activity.	18356527
256	S	Phosphorylation	Methylation inhibits AKT1-mediated phosphorylation at Ser-256 and is increased by oxidative stress.	10358075
256	S	Phosphorylation	Phosphorylation of Ser-256 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-319, permitting phosphorylation of Ser-322 and Ser-325, probably by CDK1, leading to nuclear exclusion and loss of function.	10358075
256	S	Phosphorylation	PPIA/CYPA promotes its dephosphorylation on Ser-256.	10358075
256	S	Phosphorylation	It increases the phosphorylation at Ser-256.	10358075
256	S	Phosphorylation	In response to growth factors, phosphorylation on Thr-24, Ser-256 and Ser-322 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity.	10358075
256	S	Phosphorylation	Dephosphorylated on Thr-24 and Ser-256 by PP2A in beta-cells under oxidative stress leading to nuclear retention (By similarity).	10358075
256	S	Oxidation	Methylation inhibits AKT1-mediated phosphorylation at Ser-256 and is increased by oxidative stress.	10358075
256	S	Oxidation	Dephosphorylated on Thr-24 and Ser-256 by PP2A in beta-cells under oxidative stress leading to nuclear retention (By similarity).	10358075
256	S	Methylation	Methylation inhibits AKT1-mediated phosphorylation at Ser-256 and is increased by oxidative stress.	10358075
262	K	Acetylation	Acetylation at Lys-262, Lys-265 and Lys-274 are necessary for autophagic cell death induction.	20543840
265	K	Acetylation	Acetylation at Lys-262, Lys-265 and Lys-274 are necessary for autophagic cell death induction.	20543840
274	K	Acetylation	Acetylation at Lys-262, Lys-265 and Lys-274 are necessary for autophagic cell death induction.	20543840
319	S	Phosphorylation	Phosphorylation of Ser-256 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-319, permitting phosphorylation of Ser-322 and Ser-325, probably by CDK1, leading to nuclear exclusion and loss of function.	10358075
322	S	Phosphorylation	In response to growth factors, phosphorylation on Thr-24, Ser-256 and Ser-322 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity.	11980723
322	S	Phosphorylation	Phosphorylation of Ser-256 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-319, permitting phosphorylation of Ser-322 and Ser-325, probably by CDK1, leading to nuclear exclusion and loss of function.	11980723
325	S	Phosphorylation	Phosphorylation of Ser-256 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-319, permitting phosphorylation of Ser-322 and Ser-325, probably by CDK1, leading to nuclear exclusion and loss of function.	11980723
329	S	Phosphorylation	Phosphorylation of Ser-329 is independent of IGF1 and leads to reduced function.	11311120

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of FOXO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD4_HUMAN	SMAD4	physical	15084259
CBP_HUMAN	CREBBP	physical	10973497
1433G_HUMAN	YWHAG	physical	11237865
1433Z_HUMAN	YWHAZ	physical	11237865
TSC2_HUMAN	TSC2	physical	17077083
CEBPB_HUMAN	CEBPB	physical	11893744
HNF4A_HUMAN	HNF4A	physical	12519792
PARP1_HUMAN	PARP1	physical	19281796
HXA11_HUMAN	HOXA11	physical	19727442
SKP2_HUMAN	SKP2	physical	15668399
PML_HUMAN	PML	physical	16154098
SIR1_HUMAN	SIRT1	physical	16154098
CBP_HUMAN	CREBBP	physical	16154098
CBP_HUMAN	CREBBP	physical	15220471
SIR2_HUMAN	SIRT2	physical	15220471
SIR2_HUMAN	SIRT2	physical	20543840
ATG7_HUMAN	ATG7	physical	20543840
MDM2_HUMAN	MDM2	physical	19321440
ESR1_HUMAN	ESR1	physical	11353774
RARA_HUMAN	RARA	physical	11353774
SIR1_HUMAN	SIRT1	physical	22013015
FHL2_HUMAN	FHL2	physical	15692560
SIR1_HUMAN	SIRT1	physical	15692560
EP300_HUMAN	EP300	physical	15890677
1433T_HUMAN	YWHAQ	physical	24419059
CBP_HUMAN	CREBBP	physical	24419059
EP300_HUMAN	EP300	physical	24419059
ATG7_HUMAN	ATG7	physical	23640897
FOXO1_HUMAN	FOXO1	physical	25609649
FOXO4_HUMAN	FOXO4	physical	25609649
RECQ1_HUMAN	RECQL	physical	25609649
CUX1_HUMAN	CUX1	physical	25609649
CASP_HUMAN	CUX1	physical	25609649
EP300_HUMAN	EP300	physical	25609649
DLX5_HUMAN	DLX5	physical	25609649
HXD13_HUMAN	HOXD13	physical	25609649
SATB1_HUMAN	SATB1	physical	25609649
SATB2_HUMAN	SATB2	physical	25609649
SMCA4_HUMAN	SMARCA4	physical	25609649
CBP_HUMAN	CREBBP	physical	25609649
SETD7_HUMAN	SETD7	physical	25609649
MO4L2_HUMAN	MORF4L2	physical	25609649
SNX17_HUMAN	SNX17	physical	25609649
RB_HUMAN	RB1	physical	25609649
DNJC9_HUMAN	DNAJC9	physical	25609649
KAPCA_HUMAN	PRKACA	physical	21177856
CRY1_HUMAN	CRY1	physical	27412556
MDM2_HUMAN	MDM2	physical	27412556

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 268220: Rhabdomyosarcoma 2 (RMS2)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Hippo/Mst1 stimulates transcription of the proapoptotic mediator NOXAin a FoxO1-dependent manner.";
Valis K., Prochazka L., Boura E., Chladova J., Obsil T., Rohlena J.,Truksa J., Dong L.F., Ralph S.J., Neuzil J.;
Cancer Res. 71:946-954(2011).
Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-212.
PubMed: 21245099

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND MASSSPECTROMETRY.
PubMed: 19413330

"Activation of FOXO1 by Cdk1 in cycling cells and postmitoticneurons.";
Yuan Z., Becker E.B.E., Merlo P., Yamada T., DiBacco S., Konishi Y.,Schaefer E.M., Bonni A.;
Science 319:1665-1668(2008).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-249 BY CDK1, INTERACTION WITH CDK1AND 14-3-3 PROTEINS, AND MUTAGENESIS OF SER-249.
PubMed: 18356527

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND MASSSPECTROMETRY.
PubMed: 18669648

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-509, ANDMASS SPECTROMETRY.
PubMed: 17525332

"Two novel phosphorylation sites on FKHR that are critical for itsnuclear exclusion.";
Rena G., Woods Y.L., Prescott A.R., Peggie M., Unterman T.G.,Williams M.R., Cohen P.;
EMBO J. 21:2263-2271(2002).
Cited for: PHOSPHORYLATION AT THR-24; SER-256; SER-319; SER-322; SER-325 ANDSER-329.
PubMed: 11980723

"The kinase DYRK1A phosphorylates the transcription factor FKHR atSer329 in vitro, a novel in vivo phosphorylation site.";
Woods Y.L., Rena G., Morrice N., Barthel A., Becker W., Guo S.,Unterman T.G., Cohen P.;
Biochem. J. 355:597-607(2001).
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-329, AND MUTAGENESIS OFSER-329.
PubMed: 11311120

"Phosphorylation of the transcription factor forkhead family memberFKHR by protein kinase B.";
Rena G., Guo S., Cichy S.C., Unterman T.G., Cohen P.;
J. Biol. Chem. 274:17179-17183(1999).
Cited for: PHOSPHORYLATION AT THR-24; SER-256 AND SER-319.
PubMed: 10358075