FOXM1_HUMAN - dbPTM
FOXM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXM1_HUMAN
UniProt AC Q08050
Protein Name Forkhead box protein M1
Gene Name FOXM1
Organism Homo sapiens (Human).
Sequence Length 763
Subcellular Localization Nucleus.
Protein Description Transcriptional factor regulating the expression of cell cycle genes essential for DNA replication and mitosis. Plays a role in the control of cell proliferation. Plays also a role in DNA breaks repair participating in the DNA damage checkpoint response..
Protein Sequence MKTSPRRPLILKRRRLPLPVQNAPSETSEEEPKRSPAQQESNQAEASKEVAESNSCKFPAGIKIINHPTMPNTQVVAIPNNANIHSIITALTAKGKESGSSGPNKFILISCGGAPTQPPGLRPQTQTSYDAKRTEVTLETLGPKPAARDVNLPRPPGALCEQKRETCADGEAAGCTINNSLSNIQWLRKMSSDGLGSRSIKQEMEEKENCHLEQRQVKVEEPSRPSASWQNSVSERPPYSYMAMIQFAINSTERKRMTLKDIYTWIEDHFPYFKHIAKPGWKNSIRHNLSLHDMFVRETSANGKVSFWTIHPSANRYLTLDQVFKPLDPGSPQLPEHLESQQKRPNPELRRNMTIKTELPLGARRKMKPLLPRVSSYLVPIQFPVNQSLVLQPSVKVPLPLAASLMSSELARHSKRVRIAPKVLLAEEGIAPLSSAGPGKEEKLLFGEGFSPLLPVQTIKEEEIQPGEEMPHLARPIKVESPPLEEWPSPAPSFKEESSHSWEDSSQSPTPRPKKSYSGLRSPTRCVSEMLVIQHRERRERSRSRRKQHLLPPCVDEPELLFSEGPSTSRWAAELPFPADSSDPASQLSYSQEVGGPFKTPIKETLPISSTPSKSVLPRTPESWRLTPPAKVGGLDFSPVQTSQGASDPLPDPLGLMDLSTTPLQSAPPLESPQRLLSSEPLDLISVPFGNSSPSDIDVPKPGSPEPQVSGLAANRSLTEGLVLDTMNDSLSKILLDISFPGLDEDPLGPDNINWSQFIPELQ
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
3Phosphorylation-----MKTSPRRPLI
-----CCCCCCCCCC
42.5428102081
4Phosphorylation----MKTSPRRPLIL
----CCCCCCCCCCC
15.7622094256
25PhosphorylationLPVQNAPSETSEEEP
CCCCCCCCCCCCCCC
51.6128634298
27PhosphorylationVQNAPSETSEEEPKR
CCCCCCCCCCCCCCC
45.8628634298
28PhosphorylationQNAPSETSEEEPKRS
CCCCCCCCCCCCCCC
38.6728634298
35PhosphorylationSEEEPKRSPAQQESN
CCCCCCCCHHHHHHH
30.6222094256
41PhosphorylationRSPAQQESNQAEASK
CCHHHHHHHHHHHHH
29.8825850435
57UbiquitinationVAESNSCKFPAGIKI
HHHHCCCCCCCCCEE
54.96-
63AcetylationCKFPAGIKIINHPTM
CCCCCCCEEECCCCC
36.29115613807
140PhosphorylationRTEVTLETLGPKPAA
CCEEEEECCCCCCCC
39.8822210691
163SumoylationPGALCEQKRETCADG
CCCCCHHCCCCCCCC
29.8828112733
189UbiquitinationSNIQWLRKMSSDGLG
HHHHHHHHHCCCCCC
40.75-
191PhosphorylationIQWLRKMSSDGLGSR
HHHHHHHCCCCCCCH
28.4530576142
192PhosphorylationQWLRKMSSDGLGSRS
HHHHHHCCCCCCCHH
32.0027251275
197PhosphorylationMSSDGLGSRSIKQEM
HCCCCCCCHHHHHHH
28.0927251275
201SumoylationGLGSRSIKQEMEEKE
CCCCHHHHHHHHHHH
41.26-
201SumoylationGLGSRSIKQEMEEKE
CCCCHHHHHHHHHHH
41.2628112733
218SumoylationHLEQRQVKVEEPSRP
CCEECCCCCCCCCCC
35.27-
218SumoylationHLEQRQVKVEEPSRP
CCEECCCCCCCCCCC
35.27-
251PhosphorylationMIQFAINSTERKRMT
HHHHHHCCCHHCCCC
26.07-
252PhosphorylationIQFAINSTERKRMTL
HHHHHCCCHHCCCCH
35.01-
278"N6,N6-dimethyllysine"PYFKHIAKPGWKNSI
CHHHHCCCCCHHHHH
43.38-
278MethylationPYFKHIAKPGWKNSI
CHHHHCCCCCHHHHH
43.3823644510
278UbiquitinationPYFKHIAKPGWKNSI
CHHHHCCCCCHHHHH
43.38-
282"N6,N6-dimethyllysine"HIAKPGWKNSIRHNL
HCCCCCHHHHHHHCC
46.89-
282MethylationHIAKPGWKNSIRHNL
HCCCCCHHHHHHHCC
46.8923644510
284PhosphorylationAKPGWKNSIRHNLSL
CCCCHHHHHHHCCCH
19.7828188228
306PhosphorylationTSANGKVSFWTIHPS
ECCCCCEEEEEECCC
20.6726074081
309PhosphorylationNGKVSFWTIHPSANR
CCCEEEEEECCCCCC
13.8526074081
313PhosphorylationSFWTIHPSANRYLTL
EEEEECCCCCCEEEH
24.8226074081
317PhosphorylationIHPSANRYLTLDQVF
ECCCCCCEEEHHHCC
12.1226074081
319PhosphorylationPSANRYLTLDQVFKP
CCCCCEEEHHHCCCC
21.2526074081
325SumoylationLTLDQVFKPLDPGSP
EEHHHCCCCCCCCCC
45.9028112733
331PhosphorylationFKPLDPGSPQLPEHL
CCCCCCCCCCCHHHH
18.1722094256
340PhosphorylationQLPEHLESQQKRPNP
CCHHHHHHHHCCCCH
44.2529523821
354PhosphorylationPELRRNMTIKTELPL
HHHHHCCEECCCCCC
23.9124719451
356SumoylationLRRNMTIKTELPLGA
HHHCCEECCCCCCCC
27.12-
356SumoylationLRRNMTIKTELPLGA
HHHCCEECCCCCCCC
27.1228112733
357PhosphorylationRRNMTIKTELPLGAR
HHCCEECCCCCCCCH
38.6124719451
376PhosphorylationPLLPRVSSYLVPIQF
CCCCCHHEEEEEEEC
21.4517101782
422SumoylationKRVRIAPKVLLAEEG
CCCEECCHHHHHCCC
36.17-
422AcetylationKRVRIAPKVLLAEEG
CCCEECCHHHHHCCC
36.17115613803
422SumoylationKRVRIAPKVLLAEEG
CCCEECCHHHHHCCC
36.1728112733
422UbiquitinationKRVRIAPKVLLAEEG
CCCEECCHHHHHCCC
36.17-
434PhosphorylationEEGIAPLSSAGPGKE
CCCCCCHHHCCCCCH
19.6528555341
435PhosphorylationEGIAPLSSAGPGKEE
CCCCCHHHCCCCCHH
44.9528555341
440SumoylationLSSAGPGKEEKLLFG
HHHCCCCCHHEEECC
66.87-
440AcetylationLSSAGPGKEEKLLFG
HHHCCCCCHHEEECC
66.87115613805
440SumoylationLSSAGPGKEEKLLFG
HHHCCCCCHHEEECC
66.8728112733
440UbiquitinationLSSAGPGKEEKLLFG
HHHCCCCCHHEEECC
66.87-
443UbiquitinationAGPGKEEKLLFGEGF
CCCCCHHEEECCCCC
52.13-
451PhosphorylationLLFGEGFSPLLPVQT
EECCCCCCCCCCCEE
26.0422094256
460SumoylationLLPVQTIKEEEIQPG
CCCCEECCHHHCCCC
63.56-
460SumoylationLLPVQTIKEEEIQPG
CCCCEECCHHHCCCC
63.56-
478SumoylationPHLARPIKVESPPLE
CCCCCCCCCCCCCHH
42.50-
478SumoylationPHLARPIKVESPPLE
CCCCCCCCCCCCCHH
42.50-
481PhosphorylationARPIKVESPPLEEWP
CCCCCCCCCCHHHCC
34.5030266825
489PhosphorylationPPLEEWPSPAPSFKE
CCHHHCCCCCCCCCC
34.4622094256
495SumoylationPSPAPSFKEESSHSW
CCCCCCCCCCCCCCC
65.98-
495SumoylationPSPAPSFKEESSHSW
CCCCCCCCCCCCCCC
65.98-
501PhosphorylationFKEESSHSWEDSSQS
CCCCCCCCCCCCCCC
33.8220363803
505PhosphorylationSSHSWEDSSQSPTPR
CCCCCCCCCCCCCCC
20.8225627689
506PhosphorylationSHSWEDSSQSPTPRP
CCCCCCCCCCCCCCC
47.1825627689
508PhosphorylationSWEDSSQSPTPRPKK
CCCCCCCCCCCCCCC
32.4620363803
510PhosphorylationEDSSQSPTPRPKKSY
CCCCCCCCCCCCCCC
36.8622094256
516PhosphorylationPTPRPKKSYSGLRSP
CCCCCCCCCCCCCCC
30.5629396449
517PhosphorylationTPRPKKSYSGLRSPT
CCCCCCCCCCCCCCC
18.6821712546
518PhosphorylationPRPKKSYSGLRSPTR
CCCCCCCCCCCCCCC
38.1429396449
522PhosphorylationKSYSGLRSPTRCVSE
CCCCCCCCCCCHHHH
35.3522094256
524PhosphorylationYSGLRSPTRCVSEML
CCCCCCCCCHHHHHH
37.6429396449
581PhosphorylationELPFPADSSDPASQL
CCCCCCCCCCCHHHC
38.4522199227
582PhosphorylationLPFPADSSDPASQLS
CCCCCCCCCCHHHCC
48.4322199227
586PhosphorylationADSSDPASQLSYSQE
CCCCCCHHHCCCCCC
36.7222199227
589PhosphorylationSDPASQLSYSQEVGG
CCCHHHCCCCCCCCC
18.3322199227
590PhosphorylationDPASQLSYSQEVGGP
CCHHHCCCCCCCCCC
23.9822199227
591PhosphorylationPASQLSYSQEVGGPF
CHHHCCCCCCCCCCC
19.2522199227
596 (in isoform 2)Phosphorylation-29.6415024056
600PhosphorylationEVGGPFKTPIKETLP
CCCCCCCCCCCCCCC
30.5322094256
603SumoylationGPFKTPIKETLPISS
CCCCCCCCCCCCCCC
45.94-
603AcetylationGPFKTPIKETLPISS
CCCCCCCCCCCCCCC
45.94115613799
603SumoylationGPFKTPIKETLPISS
CCCCCCCCCCCCCCC
45.94-
605PhosphorylationFKTPIKETLPISSTP
CCCCCCCCCCCCCCC
32.6022199227
609PhosphorylationIKETLPISSTPSKSV
CCCCCCCCCCCCCCC
26.6430266825
610PhosphorylationKETLPISSTPSKSVL
CCCCCCCCCCCCCCC
45.0930266825
611PhosphorylationETLPISSTPSKSVLP
CCCCCCCCCCCCCCC
25.4530266825
613PhosphorylationLPISSTPSKSVLPRT
CCCCCCCCCCCCCCC
37.3430266825
614AcetylationPISSTPSKSVLPRTP
CCCCCCCCCCCCCCC
45.87115613801
615PhosphorylationISSTPSKSVLPRTPE
CCCCCCCCCCCCCCC
32.9726074081
620PhosphorylationSKSVLPRTPESWRLT
CCCCCCCCCCCCCCC
29.4822094256
623PhosphorylationVLPRTPESWRLTPPA
CCCCCCCCCCCCCCC
20.7825159151
627PhosphorylationTPESWRLTPPAKVGG
CCCCCCCCCCCEECC
20.7422094256
638PhosphorylationKVGGLDFSPVQTSQG
EECCCCCCCCCCCCC
24.6722094256
660PhosphorylationPLGLMDLSTTPLQSA
CCCCCCCCCCCCCCC
26.4329523821
661PhosphorylationLGLMDLSTTPLQSAP
CCCCCCCCCCCCCCC
39.4729523821
662PhosphorylationGLMDLSTTPLQSAPP
CCCCCCCCCCCCCCC
20.7329523821
666PhosphorylationLSTTPLQSAPPLESP
CCCCCCCCCCCCCCC
50.8829523821
672PhosphorylationQSAPPLESPQRLLSS
CCCCCCCCCCHHHCC
33.7322094256
678PhosphorylationESPQRLLSSEPLDLI
CCCCHHHCCCCCCEE
36.9330177828
679PhosphorylationSPQRLLSSEPLDLIS
CCCHHHCCCCCCEEE
43.1130177828
686PhosphorylationSEPLDLISVPFGNSS
CCCCCEEECCCCCCC
30.9129802988
692PhosphorylationISVPFGNSSPSDIDV
EECCCCCCCHHHCCC
43.9629116813
693PhosphorylationSVPFGNSSPSDIDVP
ECCCCCCCHHHCCCC
32.2129116813
695PhosphorylationPFGNSSPSDIDVPKP
CCCCCCHHHCCCCCC
49.5028387310
704PhosphorylationIDVPKPGSPEPQVSG
CCCCCCCCCCCCCCC
34.3222094256
710PhosphorylationGSPEPQVSGLAANRS
CCCCCCCCCCCCCCC
23.8922199227
717PhosphorylationSGLAANRSLTEGLVL
CCCCCCCCCCCCCCH
39.1825159151
719PhosphorylationLAANRSLTEGLVLDT
CCCCCCCCCCCCHHH
29.2926055452
726PhosphorylationTEGLVLDTMNDSLSK
CCCCCHHHCCHHHHH
17.4526055452
730PhosphorylationVLDTMNDSLSKILLD
CHHHCCHHHHHHHHH
29.5425159151
732PhosphorylationDTMNDSLSKILLDIS
HHCCHHHHHHHHHCC
22.9222199227
739PhosphorylationSKILLDISFPGLDED
HHHHHHCCCCCCCCC
25.6728112733

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
4SPhosphorylationKinaseCDK4P11802
PSP
35SPhosphorylationKinaseCDK4P11802
PSP
361SPhosphorylationKinaseCHEK2O96017
GPS
376SPhosphorylationKinaseCHEK2O96017
Uniprot
451SPhosphorylationKinaseCDK6Q00534
PSP
451SPhosphorylationKinaseCDK4P11802
PSP
474SPhosphorylationKinaseGSK3BP49841
PSP
489SPhosphorylationKinaseCDK6Q00534
PSP
489SPhosphorylationKinaseCDK4P11802
PSP
508SPhosphorylationKinaseCDK6Q00534
PSP
508SPhosphorylationKinaseCDK4P11802
PSP
510TPhosphorylationKinaseCDK6Q00534
PSP
510TPhosphorylationKinaseCDK4P11802
PSP
522SPhosphorylationKinaseCDK4P11802
PSP
522SPhosphorylationKinaseCDK6Q00534
PSP
596TPhosphorylationKinaseCDK2P24941
PSP
596TPhosphorylationKinaseCDK1P06493
PSP
600TPhosphorylationKinaseCDK6Q00534
PSP
600TPhosphorylationKinaseCDK4P11802
PSP
600TPhosphorylationKinaseCDK1P06493
PSP
611TPhosphorylationKinaseCDK6Q00534
PSP
611TPhosphorylationKinaseCDK4P11802
PSP
611TPhosphorylationKinaseCDK1P06493
Uniprot
620TPhosphorylationKinaseCDK4P11802
PSP
620TPhosphorylationKinaseCDK1P06493
PSP
620TPhosphorylationKinaseCDK6Q00534
PSP
627TPhosphorylationKinaseCDK6Q00534
PSP
627TPhosphorylationKinaseCDK4P11802
PSP
693SPhosphorylationKinaseCDK1P06493
Uniprot
704SPhosphorylationKinaseCDK6Q00534
PSP
704SPhosphorylationKinaseCDK4P11802
PSP
730SPhosphorylationKinasePLK1P53350
Uniprot
739SPhosphorylationKinasePLK1P53350
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:18573889

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOXM1_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 FOXM1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBTB3_HUMANZBTB3physical
20211142
THIL_HUMANACAT1physical
22939629
OS9_HUMANOS9physical
21988832
SP1_HUMANSP1physical
23635401
SUMO1_HUMANSUMO1physical
24362530
FZR1_HUMANFZR1physical
24362530
FZR1_HUMANFZR1physical
18758239
LIN9_HUMANLIN9physical
25609649
MYBB_HUMANMYBL2physical
25609649
LIN54_HUMANLIN54physical
25609649
KIF22_HUMANKIF22physical
25609649
LIN37_HUMANLIN37physical
25609649
LRWD1_HUMANLRWD1physical
25609649
ORC2_HUMANORC2physical
25609649
SMCA5_HUMANSMARCA5physical
25609649
ZC11A_HUMANZC3H11Aphysical
25609649
SYDC_HUMANDARSphysical
25609649
PRC1_HUMANPRC1physical
25609649
HERC5_HUMANHERC5physical
25609649
SYIC_HUMANIARSphysical
25609649
BMS1_HUMANBMS1physical
25609649
TRM1L_HUMANTRMT1Lphysical
25609649
DDX52_HUMANDDX52physical
25609649
DEP1A_HUMANDEPDC1physical
25609649
DNJC9_HUMANDNAJC9physical
25609649
ECT2_HUMANECT2physical
25609649
TF3C4_HUMANGTF3C4physical
25609649
SYLC_HUMANLARSphysical
25609649
SYPM_HUMANPARS2physical
25609649
PESC_HUMANPES1physical
25609649
PRP8_HUMANPRPF8physical
25609649
SYQ_HUMANQARSphysical
25609649
RBMX_HUMANRBMXphysical
25609649
SNUT1_HUMANSART1physical
25609649
SMC2_HUMANSMC2physical
25609649
U520_HUMANSNRNP200physical
25609649
OTUB1_HUMANOTUB1physical
26148240
OTUB1_HUMANOTUB1physical
27167337
GSK3A_HUMANGSK3Aphysical
26912724
GSK3B_HUMANGSK3Bphysical
26912724
AXIN1_HUMANAXIN1physical
26912724
FBXW7_HUMANFBXW7physical
26912724
UBP5_HUMANUSP5physical
26912724
RN168_HUMANRNF168physical
27526106
RNF8_HUMANRNF8physical
27526106
UBP5_HUMANUSP5physical
28807830

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 FOXM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-331; THR-620 ANDTHR-627, AND MASS SPECTROMETRY.
"Plk1-dependent phosphorylation of FoxM1 regulates a transcriptionalprogramme required for mitotic progression.";
Fu Z., Malureanu L., Huang J., Wang W., Li H., van Deursen J.M.,Tindall D.J., Chen J.;
Nat. Cell Biol. 10:1076-1082(2008).
Cited for: FUNCTION, PHOSPHORYLATION AT THR-611; SER-693; SER-730 AND SER-739,AND MUTAGENESIS OF THR-611; SER-693; SER-730 AND SER-739.
"Chk2 mediates stabilization of the FoxM1 transcription factor tostimulate expression of DNA repair genes.";
Tan Y., Raychaudhuri P., Costa R.H.;
Mol. Cell. Biol. 27:1007-1016(2007).
Cited for: FUNCTION IN DNA REPAIR, AND PHOSPHORYLATION AT SER-376 BY CHEK2.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704, AND MASSSPECTROMETRY.

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