FOXO4_HUMAN - dbPTM
FOXO4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXO4_HUMAN
UniProt AC P98177
Protein Name Forkhead box protein O4
Gene Name FOXO4
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization Cytoplasm. Nucleus. When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation. Monoubiquitination increases nuclear localization. When deubiquitinated, translocated from nucleus to cytoplasm.
Protein Description Transcription factor involved in the regulation of the insulin signaling pathway. Binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. Down-regulates expression of HIF1A and suppresses hypoxia-induced transcriptional activation of HIF1A-modulated genes. Also involved in negative regulation of the cell cycle. Involved in increased proteasome activity in embryonic stem cells (ESCs) by activating expression of PSMD11 in ESCs, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity..
Protein Sequence MDPGNENSATEAAAIIDLDPDFEPQSRPRSCTWPLPRPEIANQPSEPPEVEPDLGEKVHTEGRSEPILLPSRLPEPAGGPQPGILGAVTGPRKGGSRRNAWGNQSYAELISQAIESAPEKRLTLAQIYEWMVRTVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIKVHNEATGKSSWWMLNPEGGKSGKAPRRRAASMDSSSKLLRGRSKAPKKKPSVLPAPPEGATPTSPVGHFAKWSGSPCSRNREEADMWTTFRPRSSSNASSVSTRLSPLRPESEVLAEEIPASVSSYAGGVPPTLNEGLELLDGLNLTSSHSLLSRSGLSGFSLQHPGVTGPLHTYSSSLFSPAEGPLSAGEGCFSSSQALEALLTSDTPPPPADVLMTQVDPILSQAPTLLLLGGLPSSSKLATGVGLCPKPLEAPGPSSLVPTLSMIAPPPVMASAPIPKALGTPVLTPPTEAASQDRMPQDLDLDMYMENLECDMDNIISDLMDEGEGLDFNFEPDP
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
8PhosphorylationMDPGNENSATEAAAI
CCCCCCCCHHHHHHH		30.3222210691
26PhosphorylationDPDFEPQSRPRSCTW
CCCCCCCCCCCCCCC		55.7726074081
30PhosphorylationEPQSRPRSCTWPLPR
CCCCCCCCCCCCCCC		20.6928450419
32PhosphorylationQSRPRSCTWPLPRPE
CCCCCCCCCCCCCHH		31.2219664994
45PhosphorylationPEIANQPSEPPEVEP
HHHCCCCCCCCCCCC		53.6328450419
64PhosphorylationKVHTEGRSEPILLPS
CCCCCCCCCCEECCC		59.5927499020
71PhosphorylationSEPILLPSRLPEPAG
CCCEECCCCCCCCCC		46.5525278378
111PhosphorylationQSYAELISQAIESAP
HHHHHHHHHHHHHCH		26.6118187866
144PhosphorylationYFKDKGDSNSSAGWK
CCCCCCCCCCCHHHH		47.4821406692
146PhosphorylationKDKGDSNSSAGWKNS
CCCCCCCCCHHHHHH		26.0521406692
147PhosphorylationDKGDSNSSAGWKNSI
CCCCCCCCHHHHHHH		34.7421406692
151UbiquitinationSNSSAGWKNSIRHNL
CCCCHHHHHHHHHHH		39.64-
153PhosphorylationSSAGWKNSIRHNLSL
CCHHHHHHHHHHHHH		19.7819221179
159PhosphorylationNSIRHNLSLHSKFIK
HHHHHHHHHCCCEEE		29.3822817900
163AcetylationHNLSLHSKFIKVHNE
HHHHHCCCEEEEECC		40.1225953088
172PhosphorylationIKVHNEATGKSSWWM
EEEECCCCCCCCEEE		38.6832142685
174AcetylationVHNEATGKSSWWMLN
EECCCCCCCCEEEEC		36.6425953088
186AcetylationMLNPEGGKSGKAPRR
EECCCCCCCCCCCHH		67.8812964026
189AcetylationPEGGKSGKAPRRRAA
CCCCCCCCCCHHHHC		63.4112964026
197PhosphorylationAPRRRAASMDSSSKL
CCHHHHCCCCCCHHH		23.3428176443
200PhosphorylationRRAASMDSSSKLLRG
HHHCCCCCCHHHHCC		28.06-
201PhosphorylationRAASMDSSSKLLRGR
HHCCCCCCHHHHCCC		27.5123532336
202PhosphorylationAASMDSSSKLLRGRS
HCCCCCCHHHHCCCC		31.1322210691
203AcetylationASMDSSSKLLRGRSK
CCCCCCHHHHCCCCC		54.1925953088
217PhosphorylationKAPKKKPSVLPAPPE
CCCCCCCCCCCCCCC		45.2023312004
227PhosphorylationPAPPEGATPTSPVGH
CCCCCCCCCCCCCCC		37.6528122231
229PhosphorylationPPEGATPTSPVGHFA
CCCCCCCCCCCCCHH		41.1125850435
230PhosphorylationPEGATPTSPVGHFAK
CCCCCCCCCCCCHHC		20.8428348404
239PhosphorylationVGHFAKWSGSPCSRN
CCCHHCCCCCCCCCC		28.7827251275
241PhosphorylationHFAKWSGSPCSRNRE
CHHCCCCCCCCCCHH		19.7427251275
244PhosphorylationKWSGSPCSRNREEAD
CCCCCCCCCCHHHHH		35.6527251275
254PhosphorylationREEADMWTTFRPRSS
HHHHHHHHEECCCCC		14.9322210691
255PhosphorylationEEADMWTTFRPRSSS
HHHHHHHEECCCCCC		11.3522210691
260PhosphorylationWTTFRPRSSSNASSV
HHEECCCCCCCCCCC		40.5823403867
261PhosphorylationTTFRPRSSSNASSVS
HEECCCCCCCCCCCC		28.9724719451
262PhosphorylationTFRPRSSSNASSVST
EECCCCCCCCCCCCC		37.3510217147
265PhosphorylationPRSSSNASSVSTRLS
CCCCCCCCCCCCCCC		35.21-
268PhosphorylationSSNASSVSTRLSPLR
CCCCCCCCCCCCCCC		15.12-
272PhosphorylationSSVSTRLSPLRPESE
CCCCCCCCCCCCHHH		20.7124719451
278PhosphorylationLSPLRPESEVLAEEI
CCCCCCHHHHHHHHC		35.37-
288PhosphorylationLAEEIPASVSSYAGG
HHHHCCCCHHHHCCC		19.71-
292PhosphorylationIPASVSSYAGGVPPT
CCCCHHHHCCCCCCC		11.19-
314PhosphorylationLDGLNLTSSHSLLSR
HHCCCCCCCCCHHHC		29.2629759185
315PhosphorylationDGLNLTSSHSLLSRS
HCCCCCCCCCHHHCC		16.3229759185
317PhosphorylationLNLTSSHSLLSRSGL
CCCCCCCCHHHCCCC		32.7124719451
320PhosphorylationTSSHSLLSRSGLSGF
CCCCCHHHCCCCCCC		29.6924719451
407AcetylationGGLPSSSKLATGVGL
CCCCCCCCCCCCCCC		44.0512964026
451PhosphorylationPIPKALGTPVLTPPT
CCCHHHCCCCCCCCC		15.8620959475
455PhosphorylationALGTPVLTPPTEAAS
HHCCCCCCCCCHHHC		27.7020959475
458PhosphorylationTPVLTPPTEAASQDR
CCCCCCCCHHHCCCC		39.1921406692
462PhosphorylationTPPTEAASQDRMPQD
CCCCHHHCCCCCCCC		39.3921406692
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
32TPhosphorylationKinaseAKT1P31749
Uniprot
32TPhosphorylationKinaseAKT-FAMILY-GPS
197SPhosphorylationKinaseAKT1P31749
Uniprot
197SPhosphorylationKinasePKB_GROUP-PhosphoELM
197SPhosphorylationKinaseAKT-FAMILY-GPS
227TPhosphorylationKinaseMAPK8P45983
GPS
230SPhosphorylationKinaseMAPK8P45983
GPS
262SPhosphorylationKinasePKB_GROUP-PhosphoELM
262SPhosphorylationKinaseAKT-FAMILY-GPS
262SPhosphorylationKinaseAKT1P31749
Uniprot
265SPhosphorylationKinaseCSNK1A1P48729
GPS
268SPhosphorylationKinaseCSNK1A1P48729
GPS
451TPhosphorylationKinaseMAPK9P45984
GPS
451TPhosphorylationKinaseMAPK8P45983
GPS
451TPhosphorylationKinaseAKT-FAMILY-GPS
451TPhosphorylationKinasePKB_GROUP-PhosphoELM
455TPhosphorylationKinaseMAPK9P45984
GPS
455TPhosphorylationKinaseMAPK8P45983
GPS
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:18665269
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOXO4_HUMAN !!
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 FOXO4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMAD4_HUMANSMAD4physical
15084259
XPO1_HUMANXPO1physical
11313479
PIN1_HUMANPIN1physical
18794148
MDM2_HUMANMDM2physical
18665269
UBP7_HUMANUSP7physical
16964248
CTNB1_HUMANCTNNB1physical
15905404
CBP_HUMANCREBBPphysical
15126506
SIR1_HUMANSIRT1physical
15126506
NLK_HUMANNLKphysical
20874444
CBP_HUMANCREBBPphysical
20874444
UBP7_HUMANUSP7physical
20874444
MDM2_HUMANMDM2physical
21525355
ATX3_HUMANATXN3physical
21536589
AKT1_HUMANAKT1physical
15688030
REL_HUMANRELphysical
25416956
FEN1_HUMANFEN1physical
25609649
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 FOXO4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND MASSSPECTROMETRY.
"Regulation of intracellular localization and transcriptional activityof FOXO4 by protein kinase B through phosphorylation at the motifsites conserved among the FOXO family.";
Matsuzaki H., Ichino A., Hayashi T., Yamamoto T., Kikkawa U.;
J. Biochem. 138:485-491(2005).
Cited for: PHOSPHORYLATION AT THR-32; SER-197 AND SER-262, AND MUTAGENESIS OFTHR-32; SER-197 AND SER-262.
"Regulation of nuclear translocation of forkhead transcription factorAFX by protein kinase B.";
Takaishi H., Konishi H., Matsuzaki H., Ono Y., Shirai Y., Saito N.,Kitamura T., Ogawa W., Kasuga M., Kikkawa U., Nishizuka Y.;
Proc. Natl. Acad. Sci. U.S.A. 96:11836-11841(1999).
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-197 AND SER-262, ANDMUTAGENESIS OF THR-32; SER-197 AND SER-262.
"Direct control of the forkhead transcription factor AFX by proteinkinase B.";
Kops G.J.P.L., de Ruiter N.D., De Vries-Smits A.M.M., Powell D.R.,Bos J.L., Burgering B.M.T.;
Nature 398:630-634(1999).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-262, AND MUTAGENESIS OFSER-197 AND SER-262.

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