FOXO3_HUMAN - dbPTM
FOXO3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXO3_HUMAN
UniProt AC O43524
Protein Name Forkhead box protein O3 {ECO:0000305}
Gene Name FOXO3 {ECO:0000312|HGNC:HGNC:3821}
Organism Homo sapiens (Human).
Sequence Length 673
Subcellular Localization Cytoplasm, cytosol . Nucleus . Mitochondrion matrix . Mitochondrion outer membrane
Peripheral membrane protein
Cytoplasmic side . Retention in the cytoplasm contributes to its inactivation (PubMed:10102273, PubMed:15084260, PubMed:16751106). Tran
Protein Description Transcriptional activator which triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress. [PubMed: 10102273]
Protein Sequence MAEAPASPAPLSPLEVELDPEFEPQSRPRSCTWPLQRPELQASPAKPSGETAADSMIPEEEDDEDDEDGGGRAGSAMAIGGGGGSGTLGSGLLLEDSARVLAPGGQDPGSGPATAAGGLSGGTQALLQPQQPLPPPQPGAAGGSGQPRKCSSRRNAWGNLSYADLITRAIESSPDKRLTLSQIYEWMVRCVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFMRVQNEGTGKSSWWIINPDGGKSGKAPRRRAVSMDNSNKYTKSRGRAAKKKAALQTAPESADDSPSQLSKWPGSPTSRSSDELDAWTDFRSRTNSNASTVSGRLSPIMASTELDEVQDDDAPLSPMLYSSSASLSPSVSKPCTVELPRLTDMAGTMNLNDGLTENLMDDLLDNITLPPSQPSPTGGLMQRSSSFPYTTKGSGLGSPTSSFNSTVFGPSSLNSLRQSPMQTIQENKPATFSSMSHYGNQTLQDLLTSDSLSHSDVMMTQSDPLMSQASTAVSAQNSRRNVMLRNDPMMSFAAQPNQGSLVNQNLLHHQHQTQGALGGSRALSNSVSNMGLSESSSLGSAKHQQQSPVSQSMQTLSDSLSGSSLYSTSANLPVMGHEKFPSDLDLDMFNGSLECDMESIIRSELMDADGLDFNFDSLISTQNVVGLNVGNFTGAKQASSQSWVPG
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 Orthologous
Protein Cluster
7Phosphorylation-MAEAPASPAPLSPL
-CCCCCCCCCCCCCC
22.1228355574
12PhosphorylationPASPAPLSPLEVELD
CCCCCCCCCCEEECC
26.7828355574
26PhosphorylationDPEFEPQSRPRSCTW
CCCCCCCCCCCCCCC
55.7726552605
30PhosphorylationEPQSRPRSCTWPLQR
CCCCCCCCCCCCCCC
20.6925159151
32PhosphorylationQSRPRSCTWPLQRPE
CCCCCCCCCCCCCHH
31.2217200115
43PhosphorylationQRPELQASPAKPSGE
CCHHHCCCCCCCCCC
16.6625159151
46MethylationELQASPAKPSGETAA
HHCCCCCCCCCCCCH
43.0022820736
48PhosphorylationQASPAKPSGETAADS
CCCCCCCCCCCCHHH
48.8623927012
51PhosphorylationPAKPSGETAADSMIP
CCCCCCCCCHHHCCC
30.5830140170
55PhosphorylationSGETAADSMIPEEED
CCCCCHHHCCCCCCC
17.5530140170
75PhosphorylationDGGGRAGSAMAIGGG
CCCCCCCCEEEECCC
17.5625850435
85PhosphorylationAIGGGGGSGTLGSGL
EECCCCCCCCCCCCC
31.7025850435
87PhosphorylationGGGGGSGTLGSGLLL
CCCCCCCCCCCCCEE
29.6427251275
90PhosphorylationGGSGTLGSGLLLEDS
CCCCCCCCCCEECCC
29.4027050516
149MethylationGGSGQPRKCSSRRNA
CCCCCCCCCCCCCCC
45.1922820736
161PhosphorylationRNAWGNLSYADLITR
CCCCCCCCHHHHHHH
23.44-
162PhosphorylationNAWGNLSYADLITRA
CCCCCCCHHHHHHHH
13.8027642862
179PhosphorylationSSPDKRLTLSQIYEW
CCCCCCEEHHHHHHH
28.5322137581
181PhosphorylationPDKRLTLSQIYEWMV
CCCCEEHHHHHHHHH
14.8630622161
184PhosphorylationRLTLSQIYEWMVRCV
CEEHHHHHHHHHHHH
8.90-
200PhosphorylationYFKDKGDSNSSAGWK
HCCCCCCCCCCHHHH
47.4821406692
202PhosphorylationKDKGDSNSSAGWKNS
CCCCCCCCCHHHHHH
26.0521406692
203PhosphorylationDKGDSNSSAGWKNSI
CCCCCCCCHHHHHHH
34.7421406692
207UbiquitinationSNSSAGWKNSIRHNL
CCCCHHHHHHHHHHH
39.64-
209PhosphorylationSSAGWKNSIRHNLSL
CCHHHHHHHHHHHHH
19.7820110348
215PhosphorylationNSIRHNLSLHSRFMR
HHHHHHHHHHHEEEE
29.3822817900
228PhosphorylationMRVQNEGTGKSSWWI
EEEEECCCCCCCEEE
34.9523403867
230MethylationVQNEGTGKSSWWIIN
EEECCCCCCCEEEEC
40.9522820736
231PhosphorylationQNEGTGKSSWWIINP
EECCCCCCCEEEECC
32.3222817900
232PhosphorylationNEGTGKSSWWIINPD
ECCCCCCCEEEECCC
29.8922817900
242AcetylationIINPDGGKSGKAPRR
EECCCCCCCCCCCCC
62.6625953088
242UbiquitinationIINPDGGKSGKAPRR
EECCCCCCCCCCCCC
62.66PubMed
243PhosphorylationINPDGGKSGKAPRRR
ECCCCCCCCCCCCCC
49.1226434776
245AcetylationPDGGKSGKAPRRRAV
CCCCCCCCCCCCCEE
63.41101542399
253PhosphorylationAPRRRAVSMDNSNKY
CCCCCEECCCCCCCH
21.3127273156
257PhosphorylationRAVSMDNSNKYTKSR
CEECCCCCCCHHHHH
30.3620068231
259AcetylationVSMDNSNKYTKSRGR
ECCCCCCCHHHHHHH
54.8614976264
259UbiquitinationVSMDNSNKYTKSRGR
ECCCCCCCHHHHHHH
54.86PubMed
260PhosphorylationSMDNSNKYTKSRGRA
CCCCCCCHHHHHHHH
24.5323927012
262MethylationDNSNKYTKSRGRAAK
CCCCCHHHHHHHHHH
34.7622820736
271AcetylationRGRAAKKKAALQTAP
HHHHHHHHHHHHCCC
37.8822820736
271MethylationRGRAAKKKAALQTAP
HHHHHHHHHHHHCCC
37.8822820736
276PhosphorylationKKKAALQTAPESADD
HHHHHHHCCCCCCCC
45.0630266825
280PhosphorylationALQTAPESADDSPSQ
HHHCCCCCCCCCHHH
35.6230266825
284O-linked_GlycosylationAPESADDSPSQLSKW
CCCCCCCCHHHHHCC
27.3130379171
284PhosphorylationAPESADDSPSQLSKW
CCCCCCCCHHHHHCC
27.3123927012
286O-linked_GlycosylationESADDSPSQLSKWPG
CCCCCCHHHHHCCCC
47.9430379171
286PhosphorylationESADDSPSQLSKWPG
CCCCCCHHHHHCCCC
47.9430266825
289PhosphorylationDDSPSQLSKWPGSPT
CCCHHHHHCCCCCCC
25.6630266825
290AcetylationDSPSQLSKWPGSPTS
CCHHHHHCCCCCCCC
67.0314976264
290MethylationDSPSQLSKWPGSPTS
CCHHHHHCCCCCCCC
67.0322820736
290UbiquitinationDSPSQLSKWPGSPTS
CCHHHHHCCCCCCCC
67.03PubMed
294PhosphorylationQLSKWPGSPTSRSSD
HHHCCCCCCCCCCHH
22.4118204439
296PhosphorylationSKWPGSPTSRSSDEL
HCCCCCCCCCCHHHH
38.1723927012
297PhosphorylationKWPGSPTSRSSDELD
CCCCCCCCCCHHHHH
33.2823927012
299PhosphorylationPGSPTSRSSDELDAW
CCCCCCCCHHHHHHH
41.7430266825
300PhosphorylationGSPTSRSSDELDAWT
CCCCCCCHHHHHHHH
33.7130266825
307PhosphorylationSDELDAWTDFRSRTN
HHHHHHHHCHHHHCC
27.2923927012
311PhosphorylationDAWTDFRSRTNSNAS
HHHHCHHHHCCCCCC
43.3723927012
313PhosphorylationWTDFRSRTNSNASTV
HHCHHHHCCCCCCCC
44.2227794612
315PhosphorylationDFRSRTNSNASTVSG
CHHHHCCCCCCCCCC
32.9127732954
318PhosphorylationSRTNSNASTVSGRLS
HHCCCCCCCCCCCCC
33.3221602804
319PhosphorylationRTNSNASTVSGRLSP
HCCCCCCCCCCCCCC
19.1127794612
321PhosphorylationNSNASTVSGRLSPIM
CCCCCCCCCCCCCCC
20.4821602804
325PhosphorylationSTVSGRLSPIMASTE
CCCCCCCCCCCCCCC
15.8328348404
330PhosphorylationRLSPIMASTELDEVQ
CCCCCCCCCCCCCCC
12.6828348404
331PhosphorylationLSPIMASTELDEVQD
CCCCCCCCCCCCCCC
30.9128348404
344PhosphorylationQDDDAPLSPMLYSSS
CCCCCCCCHHHCCCC
13.7518204439
348PhosphorylationAPLSPMLYSSSASLS
CCCCHHHCCCCCCCC
10.5626074081
349PhosphorylationPLSPMLYSSSASLSP
CCCHHHCCCCCCCCC
17.5426074081
350PhosphorylationLSPMLYSSSASLSPS
CCHHHCCCCCCCCCC
19.1626074081
351PhosphorylationSPMLYSSSASLSPSV
CHHHCCCCCCCCCCC
18.8826074081
353PhosphorylationMLYSSSASLSPSVSK
HHCCCCCCCCCCCCC
31.1826074081
355PhosphorylationYSSSASLSPSVSKPC
CCCCCCCCCCCCCCC
16.7826074081
357PhosphorylationSSASLSPSVSKPCTV
CCCCCCCCCCCCCEE
35.3326074081
359PhosphorylationASLSPSVSKPCTVEL
CCCCCCCCCCCEEEC
34.9126074081
363PhosphorylationPSVSKPCTVELPRLT
CCCCCCCEEECCCCC
26.0726074081
370PhosphorylationTVELPRLTDMAGTMN
EEECCCCCCCCCCCC
25.6326074081
395PhosphorylationDDLLDNITLPPSQPS
HHHHHHCCCCCCCCC
39.19-
399PhosphorylationDNITLPPSQPSPTGG
HHCCCCCCCCCCCCC
53.4322137581
402PhosphorylationTLPPSQPSPTGGLMQ
CCCCCCCCCCCCCCC
27.7028348404
411O-linked_GlycosylationTGGLMQRSSSFPYTT
CCCCCCCCCCCCCCC
17.2830379171
411PhosphorylationTGGLMQRSSSFPYTT
CCCCCCCCCCCCCCC
17.2827732954
412PhosphorylationGGLMQRSSSFPYTTK
CCCCCCCCCCCCCCC
37.8827732954
413PhosphorylationGLMQRSSSFPYTTKG
CCCCCCCCCCCCCCC
31.3325159151
416PhosphorylationQRSSSFPYTTKGSGL
CCCCCCCCCCCCCCC
25.6528985074
418O-linked_GlycosylationSSSFPYTTKGSGLGS
CCCCCCCCCCCCCCC
27.8030379171
419MethylationSSFPYTTKGSGLGSP
CCCCCCCCCCCCCCC
43.1922820736
421PhosphorylationFPYTTKGSGLGSPTS
CCCCCCCCCCCCCCC
32.1922617229
425PhosphorylationTKGSGLGSPTSSFNS
CCCCCCCCCCCCCCC
30.0118204439
427PhosphorylationGSGLGSPTSSFNSTV
CCCCCCCCCCCCCCC
38.4122617229
428PhosphorylationSGLGSPTSSFNSTVF
CCCCCCCCCCCCCCC
35.9928102081
429PhosphorylationGLGSPTSSFNSTVFG
CCCCCCCCCCCCCCC
30.8125106551
432PhosphorylationSPTSSFNSTVFGPSS
CCCCCCCCCCCCHHH
24.7628450419
433PhosphorylationPTSSFNSTVFGPSSL
CCCCCCCCCCCHHHH
22.4328464451
438PhosphorylationNSTVFGPSSLNSLRQ
CCCCCCHHHHHHHHC
48.0828450419
439PhosphorylationSTVFGPSSLNSLRQS
CCCCCHHHHHHHHCC
34.4028450419
442PhosphorylationFGPSSLNSLRQSPMQ
CCHHHHHHHHCCCCC
30.1725106551
446PhosphorylationSLNSLRQSPMQTIQE
HHHHHHCCCCCHHHH
18.8625690035
450PhosphorylationLRQSPMQTIQENKPA
HHCCCCCHHHHCCCC
20.5525690035
475O-linked_GlycosylationQTLQDLLTSDSLSHS
CHHHHHHHCCCCCHH
37.4730379171
476O-linked_GlycosylationTLQDLLTSDSLSHSD
HHHHHHHCCCCCHHH
25.7730379171
482O-linked_GlycosylationTSDSLSHSDVMMTQS
HCCCCCHHHEEECCC
28.6430379171
551O-linked_GlycosylationLGGSRALSNSVSNMG
CCHHHHHHHHHHCCC
26.5230379171
551PhosphorylationLGGSRALSNSVSNMG
CCHHHHHHHHHHCCC
26.5228857561
553PhosphorylationGSRALSNSVSNMGLS
HHHHHHHHHHCCCCC
24.4428857561
555PhosphorylationRALSNSVSNMGLSES
HHHHHHHHCCCCCCC
22.4119060867
564PhosphorylationMGLSESSSLGSAKHQ
CCCCCCCCHHCCCHH
46.1328555341
569AcetylationSSSLGSAKHQQQSPV
CCCHHCCCHHHCCCC
43.5814976264
569UbiquitinationSSSLGSAKHQQQSPV
CCCHHCCCHHHCCCC
43.58PubMed
574PhosphorylationSAKHQQQSPVSQSMQ
CCCHHHCCCCCHHHH
23.9627251275
588PhosphorylationQTLSDSLSGSSLYST
HHHHHHHCCCCCCCC
40.3522137581
626PhosphorylationSLECDMESIIRSELM
CEECCHHHHHHHHHC
19.3722137581
644PhosphorylationGLDFNFDSLISTQNV
CCCCCHHHHEECCCE
24.3814702039
666O-linked_GlycosylationFTGAKQASSQSWVPG
CCCCCCCCCCCCCCC
26.8130379171
666PhosphorylationFTGAKQASSQSWVPG
CCCCCCCCCCCCCCC
26.8127251275
667PhosphorylationTGAKQASSQSWVPG-
CCCCCCCCCCCCCC-
31.1127251275
669PhosphorylationAKQASSQSWVPG---
CCCCCCCCCCCC---
31.8027251275

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
7SPhosphorylationKinaseMAPK14Q16539
GPS
12SPhosphorylationKinaseMAPK14Q16539
GPS
12SPhosphorylationKinaseMAPK3P27361
GPS
12SPhosphorylationKinaseMAPK1P28482
GPS
30SPhosphorylationKinaseAMPKQ9Y478
Uniprot
30SPhosphorylationKinasePRKAA1Q13131
GPS
32TPhosphorylationKinaseSGK_GROUP-PhosphoELM
32TPhosphorylationKinasePKB_GROUP-PhosphoELM
32TPhosphorylationKinaseSGK-FAMILY-GPS
32TPhosphorylationKinaseAKT-FAMILY-GPS
32TPhosphorylationKinasePIM1P11309
PSP
32TPhosphorylationKinaseAKT1P47196
PSP
32TPhosphorylationKinaseAKT1P31749
Uniprot
179TPhosphorylationKinaseAMPKQ9Y478
Uniprot
179TPhosphorylationKinaseAMPK-FAMILY-GPS
179TPhosphorylationKinasePRKAA2P54646
GPS
179TPhosphorylationKinasePRKAA1Q13131
GPS
209SPhosphorylationKinaseSTK4Q13043
GPS
209SPhosphorylationKinaseMST1P26927
Uniprot
215SPhosphorylationKinaseSTK4Q13043
GPS
215SPhosphorylationKinaseMAPKAPK5Q8IW41
Uniprot
231SPhosphorylationKinaseSTK4Q13043
GPS
232SPhosphorylationKinaseSTK4Q13043
GPS
243SPhosphorylationKinaseSTK4Q13043
GPS
253SPhosphorylationKinaseSGK_GROUP-PhosphoELM
253SPhosphorylationKinaseAKT1P47196
PSP
253SPhosphorylationKinaseAKT1P31749
Uniprot
253SPhosphorylationKinasePKB_GROUP-PhosphoELM
253SPhosphorylationKinaseSGK-FAMILY-GPS
253SPhosphorylationKinaseMAPKAPK5Q8IW41
Uniprot
253SPhosphorylationKinaseAKT1P31750
PSP
253SPhosphorylationKinaseAKT-FAMILY-GPS
253SPhosphorylationKinasePIM1P11309
PSP
294SPhosphorylationKinaseMAPK3P27361
GPS
294SPhosphorylationKinaseMAPK14Q16539
GPS
294SPhosphorylationKinaseMAPK1P28482
GPS
299SPhosphorylationKinaseCAMK2AQ9UQM7
Uniprot
315SPhosphorylationKinaseSGK_GROUP-PhosphoELM
315SPhosphorylationKinaseSGK1O00141
Uniprot
315SPhosphorylationKinaseSGK-FAMILY-GPS
344SPhosphorylationKinaseMAPK1P28482
GPS
344SPhosphorylationKinaseMAPK3P27361
GPS
344SPhosphorylationKinaseMAPK14Q16539
GPS
399SPhosphorylationKinasePRKAA1Q13131
GPS
399SPhosphorylationKinaseAMPKQ9Y478
Uniprot
399SPhosphorylationKinaseAMPK-FAMILY-GPS
399SPhosphorylationKinasePRKAA2P54646
GPS
413SPhosphorylationKinaseAMPK-FAMILY-GPS
413SPhosphorylationKinaseAMPKQ9Y478
Uniprot
413SPhosphorylationKinasePRKAA2P54646
GPS
413SPhosphorylationKinasePRKAA1Q13131
GPS
425SPhosphorylationKinaseMAPK14Q16539
GPS
425SPhosphorylationKinaseMAPK1P28482
GPS
425SPhosphorylationKinaseMAPK3P27361
GPS
551SPhosphorylationKinaseMAPKAPK5Q8IW41
Uniprot
555SPhosphorylationKinaseMAPKAPK5Q8IW41
Uniprot
555SPhosphorylationKinasePRKAA2P54646
GPS
555SPhosphorylationKinaseAMPK-FAMILY-GPS
555SPhosphorylationKinasePRKAA1Q13131
GPS
555SPhosphorylationKinaseAMPKQ9Y478
Uniprot
574SPhosphorylationKinaseMAPK8P45983
GPS
588SPhosphorylationKinasePRKAA1Q13131
GPS
588SPhosphorylationKinasePRKAA2P54646
GPS
588SPhosphorylationKinaseAMPKQ9Y478
Uniprot
588SPhosphorylationKinaseAMPK-FAMILY-GPS
626SPhosphorylationKinasePRKAA2P54646
GPS
626SPhosphorylationKinasePRKAA1Q13131
GPS
626SPhosphorylationKinaseAMPK-FAMILY-GPS
626SPhosphorylationKinaseAMPKQ9Y478
Uniprot
644SPhosphorylationKinaseIKBKBO14920
GPS
644SPhosphorylationKinaseCHUKO15111
GPS
644SPhosphorylationKinaseIKBKEQ14164
GPS
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:20625400
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:21841822
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:19321440

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
12SPhosphorylation

29445193
30SPhosphorylation

29445193
32TPhosphorylation

10102273
209SOxidation

16751106
209SPhosphorylation

16751106
253SPhosphorylation

10102273
271KMethylation

22820736
299SPhosphorylation

23805378
315SPhosphorylation

10102273
644SPhosphorylation

15084260
644Subiquitylation

15084260

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of FOXO3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMAD4_HUMANSMAD4physical
15084259
UBP7_HUMANUSP7physical
16964248
1433E_HUMANYWHAEphysical
20562859
1433F_HUMANYWHAHphysical
20562859
1433B_HUMANYWHABphysical
20562859
PGK1_HUMANPGK1physical
20562859
FKBP4_HUMANFKBP4physical
20562859
CTNB1_HUMANCTNNB1physical
15905404
H2AX_HUMANH2AFXphysical
18344987
BRCA1_HUMANBRCA1physical
18344987
RAD17_HUMANRAD17physical
18344987
ATM_HUMANATMphysical
18344987
SIR1_HUMANSIRT1physical
15126506
CBP_HUMANCREBBPphysical
15126506
FACD2_HUMANFANCD2physical
20040763
EP300_HUMANEP300physical
19592618
VDR_HUMANVDRphysical
20733005
SIR1_HUMANSIRT1physical
20733005
MDM2_HUMANMDM2physical
19321440
SKP2_HUMANSKP2physical
21841822
SMAD3_HUMANSMAD3physical
21532621
SMAD4_HUMANSMAD4physical
21532621
CBP_HUMANCREBBPphysical
22474372
FBW1A_HUMANBTRCphysical
20625400
MK01_HUMANMAPK1physical
18204439
MDM2_HUMANMDM2physical
18204439
CDT1_HUMANCDT1physical
22451935
SKP2_HUMANSKP2physical
22310285
IKKA_HUMANCHUKphysical
15084260
IKKB_HUMANIKBKBphysical
15084260
1433B_HUMANYWHABphysical
19940129
SIR1_HUMANSIRT1physical
14976264
EP300_MOUSEEp300physical
11896584
PP2AB_HUMANPPP2CBphysical
26280018
PLK1_HUMANPLK1physical
26280018
PTPA_HUMANPPP2R4physical
26280018
2AAA_HUMANPPP2R1Aphysical
26280018
2AAB_HUMANPPP2R1Bphysical
26280018
UBP7_HUMANUSP7physical
26280018
1433E_HUMANYWHAEphysical
26280018
ATGA1_HUMANATG101physical
23640897
TRRAP_HUMANTRRAPphysical
25609649
CBP_HUMANCREBBPphysical
25609649
EP300_HUMANEP300physical
25609649
RBL1_HUMANRBL1physical
25609649
CDC27_HUMANCDC27physical
25609649
FOXK1_HUMANFOXK1physical
25609649
RB_HUMANRB1physical
25609649
PNKP_HUMANPNKPphysical
25609649
ARHG2_HUMANARHGEF2physical
25609649
TAF5L_HUMANTAF5Lphysical
25609649
TERT_HUMANTERTphysical
26370108
CBY1_HUMANCBY1physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FOXO3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The MK5/PRAK kinase and Myc form a negative feedback loop that isdisrupted during colorectal tumorigenesis.";
Kress T.R., Cannell I.G., Brenkman A.B., Samans B., Gaestel M.,Roepman P., Burgering B.M., Bushell M., Rosenwald A., Eilers M.;
Mol. Cell 41:445-457(2011).
Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND PHOSPHORYLATION ATSER-215; SER-253; SER-551 AND SER-555.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-12 AND SER-280,AND MASS SPECTROMETRY.
"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-280; SER-284 ANDSER-286, AND MASS SPECTROMETRY.
"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-280 AND SER-284, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND THR-427, ANDMASS SPECTROMETRY.
"The energy sensor AMP-activated protein kinase directly regulates themammalian FOXO3 transcription factor.";
Greer E.L., Oskoui P.R., Banko M.R., Maniar J.M., Gygi M.P.,Gygi S.P., Brunet A.;
J. Biol. Chem. 282:30107-30119(2007).
Cited for: PHOSPHORYLATION AT THR-179; SER-399; SER-413; SER-555; SER-588 ANDSER-626, MUTAGENESIS OF THR-179; SER-399; SER-413; SER-555; SER-588AND SER-626, AND SUBCELLULAR LOCATION.
"A conserved MST-FOXO signaling pathway mediates oxidative-stressresponses and extends life span.";
Lehtinen M.K., Yuan Z., Boag P.R., Yang Y., Villen J., Becker E.B.E.,DiBacco S., de la Iglesia N., Gygi S.P., Blackwell T.K., Bonni A.;
Cell 125:987-1001(2006).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-209, INTERACTION WITH STK4/MST1 ANDYWHAB, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-209.
"Protein kinase SGK mediates survival signals by phosphorylating theforkhead transcription factor FKHRL1 (FOXO3a).";
Brunet A., Park J., Tran H., Hu L.S., Hemmings B.A., Greenberg M.E.;
Mol. Cell. Biol. 21:952-965(2001).
Cited for: PHOSPHORYLATION AT SER-315.
"Akt promotes cell survival by phosphorylating and inhibiting aForkhead transcription factor.";
Brunet A., Bonni A., Zigmond M.J., Lin M.Z., Juo P., Hu L.S.,Anderson M.J., Arden K.C., Blenis J., Greenberg M.E.;
Cell 96:857-868(1999).
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-32; SER-253 ANDSER-315, AND MUTAGENESIS OF THR-32; SER-253 AND SER-315.

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