E2F3_HUMAN - dbPTM
E2F3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID E2F3_HUMAN
UniProt AC O00716
Protein Name Transcription factor E2F3
Gene Name E2F3
Organism Homo sapiens (Human).
Sequence Length 465
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. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters (By similarity)..
Protein Sequence MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAAAAAPGAYIQILTTNTSTTSCSSSLQSGAVAAGPLLPSAPGAEQTAGSLLYTTPHGPSSRAGLLQQPPALGRGGSGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEVPDSIESLQIHLASTQGPIEVYLCPEETETHSPMKTNNQDHNGNIPKPASKDLASTNSGHSDCSVSMGNLSPLASPANLLQQTEDQIPSNLEGPFVNLLPPLLQEDYLLSLGEEEGISDLFDAYDLEKLPLVEDFMCS
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
121MethylationQQPPALGRGGSGGGG
CCCCCCCCCCCCCCC
47.34-
124PhosphorylationPALGRGGSGGGGGPP
CCCCCCCCCCCCCCC
36.7722817900
152PhosphorylationYLSDGLKTPKGKGRA
HHCCCCCCCCCCCCC
34.9629214152
163PhosphorylationKGRAALRSPDSPKTP
CCCCCCCCCCCCCCC
33.6325159151
166PhosphorylationAALRSPDSPKTPKSP
CCCCCCCCCCCCCCC
31.5125159151
168AcetylationLRSPDSPKTPKSPSE
CCCCCCCCCCCCCCH
79.8520167786
169PhosphorylationRSPDSPKTPKSPSEK
CCCCCCCCCCCCCHH
39.0625159151
171AcetylationPDSPKTPKSPSEKTR
CCCCCCCCCCCHHHC
79.0120167786
172PhosphorylationDSPKTPKSPSEKTRY
CCCCCCCCCCHHHCC
34.5625159151
174PhosphorylationPKTPKSPSEKTRYDT
CCCCCCCCHHHCCCC
59.8326074081
176AcetylationTPKSPSEKTRYDTSL
CCCCCCHHHCCCCHH
42.5160559
179PhosphorylationSPSEKTRYDTSLGLL
CCCHHHCCCCHHHHH
28.8930576142
181PhosphorylationSEKTRYDTSLGLLTK
CHHHCCCCHHHHHHH
19.5430576142
182PhosphorylationEKTRYDTSLGLLTKK
HHHCCCCHHHHHHHH
19.9730576142
188UbiquitinationTSLGLLTKKFIQLLS
CHHHHHHHHHHHHHH
45.73-
206UbiquitinationDGVLDLNKAAEVLKV
CCCCCHHHHHHHHHH
57.16-
212UbiquitinationNKAAEVLKVQKRRIY
HHHHHHHHHHHHHHH
48.04-
235PhosphorylationIHLIKKKSKNNVQWM
HHHEECCCCCCCCEE
49.88-
267PhosphorylationSKEVTELSQEEKKLD
CHHHHHHHHHHHHHH
29.3427251275
306AcetylationVTYQDIRKISGLKDQ
EEHHHHHHHCCCCCC
41.377970925
308PhosphorylationYQDIRKISGLKDQTV
HHHHHHHCCCCCCEE
40.9024719451
349PhosphorylationTQGPIEVYLCPEETE
CCCCEEEEECCCCCC
6.98-
355PhosphorylationVYLCPEETETHSPMK
EEECCCCCCCCCCCC
44.5128348404
357PhosphorylationLCPEETETHSPMKTN
ECCCCCCCCCCCCCC
34.7628348404
359PhosphorylationPEETETHSPMKTNNQ
CCCCCCCCCCCCCCC
33.8225159151

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
124SPhosphorylationKinaseCHEK1O14757
GPS
124SPhosphorylationKinaseCHEK2O96017
GPS
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:22580460

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of E2F3_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 E2F3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TFE3_HUMANTFE3physical
12748276
WNK1_HUMANWNK1physical
12748276
IPKB_HUMANPKIBphysical
12748276
CBP_HUMANCREBBPphysical
12748276
TEAD3_HUMANTEAD3physical
12748276
MYBB_HUMANMYBL2physical
12748276
MGAP_HUMANMGAphysical
12748276
SPIB_HUMANSPIBphysical
12748276
RYBP_HUMANRYBPphysical
12411495
FHL2_HUMANFHL2physical
12411495
R144A_HUMANRNF144Aphysical
12411495
SP1_MOUSESp1physical
8657141
KMT2D_HUMANKMT2Dphysical
16951254
USF1_HUMANUSF1physical
15014447
ATAD2_HUMANATAD2physical
20855524
HELLS_HUMANHELLSphysical
22157815
CCNB1_HUMANCCNB1physical
22157815
RBL1_HUMANRBL1physical
22157815
MCM4_HUMANMCM4physical
22157815
PCNA_HUMANPCNAphysical
22157815
FZR1_HUMANFZR1physical
22580460
RB_HUMANRB1physical
17380128
SRA1_HUMANSRA1physical
20398657
TIF1B_HUMANTRIM28physical
23060449
UCHL5_HUMANUCHL5physical
26396186

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 E2F3_HUMAN

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Related Literatures of Post-Translational Modification

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