E2F1_HUMAN - dbPTM
E2F1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID E2F1_HUMAN
UniProt AC Q01094
Protein Name Transcription factor E2F1
Gene Name E2F1
Organism Homo sapiens (Human).
Sequence Length 437
Subcellular Localization Nucleus .
Protein Description Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters. [PubMed: 20176812 Positively regulates transcription of RRP1B]
Protein Sequence MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF
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
31PhosphorylationALRLLDSSQIVIISA
HHHHCCCCCEEEEEE
24.4811459832
96PhosphorylationKRRLDLETDHQYLAE
CCCCCCCCCHHHHHH
46.18-
109MethylationAESSGPARGRGRHPG
HHCCCCCCCCCCCCC
38.17-
111MethylationSSGPARGRGRHPGKG
CCCCCCCCCCCCCCC
33.16-
113MethylationGPARGRGRHPGKGVK
CCCCCCCCCCCCCCC
31.31-
117AcetylationGRGRHPGKGVKSPGE
CCCCCCCCCCCCCCC
66.0510675335
117NeddylationGRGRHPGKGVKSPGE
CCCCCCCCCCCCCCC
66.05-
120AcetylationRHPGKGVKSPGEKSR
CCCCCCCCCCCCCHH
60.6510675335
120NeddylationRHPGKGVKSPGEKSR
CCCCCCCCCCCCCHH
60.65-
121PhosphorylationHPGKGVKSPGEKSRY
CCCCCCCCCCCCHHC
35.4124719451
125AcetylationGVKSPGEKSRYETSL
CCCCCCCCHHCHHHC
46.2610675335
125NeddylationGVKSPGEKSRYETSL
CCCCCCCCHHCHHHC
46.26-
131PhosphorylationEKSRYETSLNLTTKR
CCHHCHHHCCHHHHH
11.8822210691
135PhosphorylationYETSLNLTTKRFLEL
CHHHCCHHHHHHHHH
29.2422210691
136PhosphorylationETSLNLTTKRFLELL
HHHCCHHHHHHHHHH
24.32-
161UbiquitinationNWAAEVLKVQKRRIY
HHHHHHHHHHHHHHH
48.04-
164UbiquitinationAEVLKVQKRRIYDIT
HHHHHHHHHHHHHHH
46.78-
185NeddylationQLIAKKSKNHIQWLG
HHHHHHCCCCEEECC
62.52-
185MethylationQLIAKKSKNHIQWLG
HHHHHHCCCCEEECC
62.5220603083
302PhosphorylationVFLCPEETVGGISPG
EEECCHHCCCCCCCC
23.8423663014
307PhosphorylationEETVGGISPGKTPSQ
HHCCCCCCCCCCCCC
30.7623663014
311PhosphorylationGGISPGKTPSQEVTS
CCCCCCCCCCCCCCC
33.8023663014
313PhosphorylationISPGKTPSQEVTSEE
CCCCCCCCCCCCCHH
44.1823663014
317PhosphorylationKTPSQEVTSEEENRA
CCCCCCCCCHHHHCC
29.6623663014
318PhosphorylationTPSQEVTSEEENRAT
CCCCCCCCHHHHCCC
48.4623663014
325PhosphorylationSEEENRATDSATIVS
CHHHHCCCCCCEEEC
27.5228176443
327PhosphorylationEENRATDSATIVSPP
HHHCCCCCCEEECCC
23.9828176443
329PhosphorylationNRATDSATIVSPPPS
HCCCCCCEEECCCCC
26.3428176443
332PhosphorylationTDSATIVSPPPSSPP
CCCCEEECCCCCCCC
28.0420616879
336PhosphorylationTIVSPPPSSPPSSLT
EEECCCCCCCCHHCC
62.3430108239
337PhosphorylationIVSPPPSSPPSSLTT
EECCCCCCCCHHCCC
46.7520616879
340PhosphorylationPPPSSPPSSLTTDPS
CCCCCCCHHCCCCCC
41.1730108239
341PhosphorylationPPSSPPSSLTTDPSQ
CCCCCCHHCCCCCCH
35.1930108239
343PhosphorylationSSPPSSLTTDPSQSL
CCCCHHCCCCCCHHH
30.9728176443
344PhosphorylationSPPSSLTTDPSQSLL
CCCHHCCCCCCHHHH
51.7328176443
347PhosphorylationSSLTTDPSQSLLSLE
HHCCCCCCHHHHCCC
34.9028176443
349PhosphorylationLTTDPSQSLLSLEQE
CCCCCCHHHHCCCHH
35.3028176443
352PhosphorylationDPSQSLLSLEQEPLL
CCCHHHHCCCHHHHH
34.8428176443
364PhosphorylationPLLSRMGSLRAPVDE
HHHHHHCCCCCCCCH
12.8222496350
375PhosphorylationPVDEDRLSPLVAADS
CCCHHHCHHHHHHHH
19.6530266825
382PhosphorylationSPLVAADSLLEHVRE
HHHHHHHHHHHHHHH
30.0830266825
403PhosphorylationPEEFISLSPPHEALD
CHHHHCCCCCHHHHH
29.6020616879
433PhosphorylationDCDFGDLTPLDF---
CCCCCCCCCCCC---
26.9210428966

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
31SPhosphorylationKinaseATMQ13315
PSP
31SPhosphorylationKinaseATRQ13535
PSP
332SPhosphorylationKinaseCDK1P06493
PSP
332SPhosphorylationKinaseTBK1Q9UHD2
PSP
337SPhosphorylationKinaseCDK1P06493
PSP
337SPhosphorylationKinaseMAP3K7O43318
GPS
364SPhosphorylationKinaseCHK2O96017
PSP
375SPhosphorylationKinaseCDK8P49336
PSP
403SPhosphorylationKinaseCDK7P50613
PSP
403SPhosphorylationKinaseGSK3BP49841
PSP
403SPhosphorylationKinaseP38BQ15759
PSP
403SPhosphorylationKinaseMAPK11Q9WUI1
GPS
433TPhosphorylationKinaseCDK7P50613
PSP
433TPhosphorylationKinaseGSK3BP49841
PSP
433TPhosphorylationKinaseP38BQ15759
PSP
433TPhosphorylationKinaseMAPK11Q9WUI1
GPS
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:10559858
-KUbiquitinationE3 ubiquitin ligaseEP300Q09472
PMID:15917652
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:22580462

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
364SPhosphorylation

12717439

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 E2F1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOA6_HUMANNCOA6physical
14638867
TOPB1_HUMANTOPBP1physical
12697828
NECD_HUMANNDNphysical
14593116
NSE3_HUMANNDNL2physical
14593116
PHB_HUMANPHBphysical
14500729
IPKB_HUMANPKIBphysical
12748276
CBP_HUMANCREBBPphysical
12748276
TEAD3_HUMANTEAD3physical
12748276
MYBB_HUMANMYBL2physical
12748276
SPIB_HUMANSPIBphysical
12748276
MGAP_HUMANMGAphysical
12748276
TRRAP_HUMANTRRAPphysical
9708738
PHB_HUMANPHBphysical
12065415
HDAC1_HUMANHDAC1physical
10734134
RBBP4_HUMANRBBP4physical
10734134
TP53B_HUMANTP53BP1physical
8896460
MDM4_HUMANMDM4physical
12532331
SP1_HUMANSP1physical
8657142
R144A_HUMANRNF144Aphysical
12411495
FHL2_HUMANFHL2physical
12411495
CDK2_HUMANCDK2physical
7969176
CCNA2_HUMANCCNA2physical
7969176
SP1_HUMANSP1physical
10547281
SP2_HUMANSP2physical
10547281
SP4_HUMANSP4physical
10547281
SP3_HUMANSP3physical
10547281
RB_HUMANRB1physical
8230483
RBL1_HUMANRBL1physical
8230483
NFKB1_HUMANNFKB1physical
9368006
NFKB1_MOUSENfkb1physical
9368006
PHB_HUMANPHBphysical
10523633
ARI3A_HUMANARID3Aphysical
9780002
TFDP1_HUMANTFDP1physical
9780002
CCNA1_HUMANCCNA1physical
10022926
TFDP1_HUMANTFDP1physical
7739537
TFDP2_HUMANTFDP2physical
7739537
TFDP1_HUMANTFDP1physical
8405995
SP1_HUMANSP1physical
8657141
SP1_MOUSESp1physical
8657141
SKP2_HUMANSKP2physical
10559858
CUL1_HUMANCUL1physical
10559858
CDK7_HUMANCDK7physical
10428966
TF2H1_HUMANGTF2H1physical
10428966
PURA_HUMANPURAphysical
10597240
NECD_HUMANNDNphysical
9422723
GSK3B_HUMANGSK3Bphysical
18367454
CCNA1_HUMANCCNA1physical
16774918
MDM2_HUMANMDM2physical
16170383
SKP2_HUMANSKP2physical
16170383
BRD2_HUMANBRD2physical
17111193
TBP_HUMANTBPphysical
17111193
1433T_HUMANYWHAQphysical
15494392
RB_HUMANRB1physical
16766265
MCPH1_HUMANMCPH1physical
18660752
RB_HUMANRB1physical
11839806
CDN1A_HUMANCDKN1Aphysical
15964998
TRRAP_HUMANTRRAPphysical
11418595
KAT2A_HUMANKAT2Aphysical
11418595
RB_HUMANRB1physical
15485920
PHB_HUMANPHBphysical
15141164
KAT5_HUMANKAT5physical
15121871
ASH2L_HUMANASH2Lphysical
17612494
TOPB1_HUMANTOPBP1physical
20413589
NRIP1_HUMANNRIP1physical
20410059
ATAD2_HUMANATAD2physical
20855524
KC1A_HUMANCSNK1A1physical
19759023
RB_HUMANRB1physical
22078878
IGF1_HUMANIGF1physical
14681231
FZR1_HUMANFZR1physical
22580462
APC5_HUMANANAPC5physical
22580462
ANDR_HUMANARphysical
22508987
TIF1B_HUMANTRIM28physical
22496453
RB_HUMANRB1physical
9553123
ESR1_HUMANESR1physical
22216287
RB_HUMANRB1physical
19477924
DDB1_HUMANDDB1physical
9418871
DDB2_HUMANDDB2physical
9418871
XIAP_HUMANXIAPphysical
21653699
BIRC2_HUMANBIRC2physical
21653699
BIRC3_HUMANBIRC3physical
21653699
RB_HUMANRB1physical
8346196
RB_HUMANRB1physical
17380128
CEBPD_HUMANCEBPDphysical
15674331
RB_HUMANRB1physical
9632788
TBP_HUMANTBPphysical
8255752
RB_HUMANRB1physical
10393912
RB_HUMANRB1physical
19249677
ANM2_HUMANPRMT2physical
16616919
NCOA3_HUMANNCOA3physical
15169882
RB_HUMANRB1physical
9315635
CEBPE_HUMANCEBPEphysical
12947005
RB_HUMANRB1physical
12947005
RB_HUMANRB1physical
18391203
PARP1_HUMANPARP1physical
14627987
TBP_HUMANTBPphysical
9400991
TF2H1_HUMANGTF2H1physical
9400991
TFB1_YEASTTFB1physical
9400991
ERCC3_HUMANERCC3physical
9400991
TBP_YEASTSPT15physical
9400991
RB_HUMANRB1physical
9400991
UHRF2_HUMANUHRF2physical
23833190
NCOR2_HUMANNCOR2physical
20195357
STAT1_HUMANSTAT1physical
20195357
STML1_HUMANSTOML1physical
20195357
RARA_HUMANRARAphysical
24608861
VHL_HUMANVHLphysical
24112038
SIR1_HUMANSIRT1physical
24112038
LTOR5_HUMANLAMTOR5physical
23352642
RB_HUMANRB1physical
19058874
KAT2B_HUMANKAT2Bphysical
15123636
CBP_HUMANCREBBPphysical
8932363
TFDP1_HUMANTFDP1physical
25368385
TFDP1_HUMANTFDP1physical
9501179
TFDP2_HUMANTFDP2physical
9501179
RBL1_HUMANRBL1physical
9501179
RB_HUMANRB1physical
9501179
BIN1_HUMANBIN1physical
25257171
RB_HUMANRB1physical
25257171
PSDE_HUMANPSMD14physical
26510456
RN126_HUMANRNF126physical
26234677
UCHL5_HUMANUCHL5physical
26396186
HDAC1_HUMANHDAC1physical
26468294
UBE3A_HUMANUBE3Aphysical
28074012
RB_HUMANRB1physical
28074012
RB_HUMANRB1physical
10891495

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 E2F1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Regulation of E2F1 activity by acetylation.";
Martinez-Balbas M.A., Bauer U.M., Nielsen S.J., Brehm A.,Kouzarides T.;
EMBO J. 19:662-671(2000).
Cited for: ACETYLATION AT LYS-117; LYS-120 AND LYS-125, DNA-BINDING, INTERACTIONWITH KAT2B, FUNCTION, AND MUTAGENESIS OF LYS-117; LYS-120 AND LYS-125.
Phosphorylation
ReferencePubMed
"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-375, AND MASSSPECTROMETRY.
"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-375, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASSSPECTROMETRY.

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