E4F1_HUMAN - dbPTM
E4F1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID E4F1_HUMAN
UniProt AC Q66K89
Protein Name Transcription factor E4F1
Gene Name E4F1
Organism Homo sapiens (Human).
Sequence Length 784
Subcellular Localization Nucleus, nucleoplasm. Cytoplasm. A small fraction is detected in the cytoplasm. Excluded from the nucleolus where it is targeted upon CDKN2A overexpression. Localizes to the mitotic spindle during embryogenesis..
Protein Description May function as a transcriptional repressor. May also function as a ubiquitin ligase mediating ubiquitination of chromatin-associated TP53. Functions in cell survival and proliferation through control of the cell cycle. Functions in the p53 and pRB tumor suppressor pathways and regulates the cyclin CCNA2 transcription.; Identified as a cellular target of the adenoviral oncoprotein E1A, it is required for both transcriptional activation and repression of viral genes..
Protein Sequence MEGAMAVRVTAAHTAEAQAEAGREAGEGAVAAVAAALAPSGFLGLPAPFSEEDEDDVHRCGRCQAEFTALEDFVQHKIQKACQRAPPEALPATPATTALLGQEVVPAAPGPEEPITVAHIVVEAASLAADISHASDLVGGGHIKEVIVAAEAELGDGEMAEAPGSPRQQGLGLAGEGEQAQVKLLVNKDGRYVCALCHKTFKTGSILKAHMVTHSSRKDHECKLCGASFRTKGSLIRHHRRHTDERPYKCSKCGKSFRESGALTRHLKSLTPCTEKIRFSVSKDVVVSKEDARAGSGAGAAGLGTATSSVTGEPIETSPVIHLVTDAKGTVIHEVHVQMQELSLGMKALAPEPPVSQELPCSSEGSRENLLHQAMQNSGIVLERAAGEEGALEPAPAAGSSPQPLAVAAPQLPVLEVQPLETQVASEASAVPRTHPCPQCSETFPTAATLEAHKRGHTGPRPFACAQCGKAFPKAYLLKKHQEVHVRERRFRCGDCGKLYKTIAHVRGHRRVHSDERPYPCPKCGKRYKTKNAQQVHFRTHLEEKPHVCQFCSRGFREKGSLVRHVRHHTGEKPFKCYKCGRGFAEHGTLNRHLRTKGGCLLEVEELLVSEDSPAAATTVLTEDPHTVLVEFSSVVADTQEYIIEATADDAETSEATEIIEGTQTEVDSHIMKVVQQIVHQASAGHQIIVQNVTMDEETALGPEAAAADTITIATPESLTEQVAMTLASAISEGTVLAARAGTSGTEQATVTMVSSEDIEILEHAGELVIASPEGQLEVQTVIV
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
50PhosphorylationLGLPAPFSEEDEDDV
CCCCCCCCCCCCCCC		38.7325159151
165PhosphorylationEMAEAPGSPRQQGLG
CCCCCCCCCCCCCCC		18.8220860994
188UbiquitinationQVKLLVNKDGRYVCA
EEEEEECCCCCEEEE		54.82-
202SumoylationALCHKTFKTGSILKA
EEECCEECCCCHHHE		58.15-
202SumoylationALCHKTFKTGSILKA
EEECCEECCCCHHHE		58.15-
205PhosphorylationHKTFKTGSILKAHMV
CCEECCCCHHHEEEE		29.9424719451
213PhosphorylationILKAHMVTHSSRKDH
HHHEEEECCCCCCCC		14.4127732954
215PhosphorylationKAHMVTHSSRKDHEC
HEEEECCCCCCCCCC		23.6020068231
216PhosphorylationAHMVTHSSRKDHECK
EEEECCCCCCCCCCC		35.4327732954
223SumoylationSRKDHECKLCGASFR
CCCCCCCCCCCCEEC		43.77-
223SumoylationSRKDHECKLCGASFR
CCCCCCCCCCCCEEC		43.77-
243PhosphorylationIRHHRRHTDERPYKC
HHHCCCCCCCCCCCC		37.4324719451
251PhosphorylationDERPYKCSKCGKSFR
CCCCCCCCCCCCCHH		27.16-
256PhosphorylationKCSKCGKSFRESGAL
CCCCCCCCHHHCCHH		18.1524719451
260PhosphorylationCGKSFRESGALTRHL
CCCCHHHCCHHHHHH		25.7225159151
268UbiquitinationGALTRHLKSLTPCTE
CHHHHHHHHCCCCCC		36.9829967540
269PhosphorylationALTRHLKSLTPCTEK
HHHHHHHHCCCCCCE		43.7827251275
289UbiquitinationSKDVVVSKEDARAGS
CCCEEEEHHHHCCCC		48.26-
289SumoylationSKDVVVSKEDARAGS
CCCEEEEHHHHCCCC		48.26-
289SumoylationSKDVVVSKEDARAGS
CCCEEEEHHHHCCCC		48.26-
296PhosphorylationKEDARAGSGAGAAGL
HHHHCCCCCCCCCCC		25.2028122231
307PhosphorylationAAGLGTATSSVTGEP
CCCCCCCCCCCCCCC		22.7528122231
308PhosphorylationAGLGTATSSVTGEPI
CCCCCCCCCCCCCCC		21.9828122231
309PhosphorylationGLGTATSSVTGEPIE
CCCCCCCCCCCCCCC		21.2428122231
311PhosphorylationGTATSSVTGEPIETS
CCCCCCCCCCCCCCC		37.4628122231
317PhosphorylationVTGEPIETSPVIHLV
CCCCCCCCCCEEEEE		38.7618669648
318PhosphorylationTGEPIETSPVIHLVT
CCCCCCCCCEEEEEE		12.3629496963
325PhosphorylationSPVIHLVTDAKGTVI
CCEEEEEECCCCCEE		36.2821712546
396UbiquitinationEGALEPAPAAGSSPQ
CCCCCCCCCCCCCCC		33.1029967540
400PhosphorylationEPAPAAGSSPQPLAV
CCCCCCCCCCCCCEE		33.8326074081
401PhosphorylationPAPAAGSSPQPLAVA
CCCCCCCCCCCCEEE		27.0029496963
458PhosphorylationEAHKRGHTGPRPFAC
HHHHCCCCCCCCCEE		52.2725159151
501UbiquitinationGDCGKLYKTIAHVRG
CCHHHHHHHHHHHCC		43.84-
514PhosphorylationRGHRRVHSDERPYPC
CCCCCCCCCCCCCCC		38.0127732954
519PhosphorylationVHSDERPYPCPKCGK
CCCCCCCCCCCCCCC		24.5627732954
545UbiquitinationFRTHLEEKPHVCQFC
EEHHHCCCCCHHHHC		30.92-
545SumoylationFRTHLEEKPHVCQFC
EEHHHCCCCCHHHHC		30.92-
545SumoylationFRTHLEEKPHVCQFC
EEHHHCCCCCHHHHC		30.92-
559SumoylationCSRGFREKGSLVRHV
CCCCHHHCCCHHHHH		49.93-
559SumoylationCSRGFREKGSLVRHV
CCCCHHHCCCHHHHH		49.93-
570PhosphorylationVRHVRHHTGEKPFKC
HHHHCCCCCCCCCCE		40.69-
573UbiquitinationVRHHTGEKPFKCYKC
HCCCCCCCCCCEEEC		58.0429967540
589PhosphorylationRGFAEHGTLNRHLRT
CCCHHHCCHHHHHHC		23.83-
613PhosphorylationELLVSEDSPAAATTV
EEEECCCCCCCEEEE		16.6424275569
627PhosphorylationVLTEDPHTVLVEFSS
EECCCCCEEEEEEEE		22.4122468782
653PhosphorylationATADDAETSEATEII
EECCCCCCCCCCHHH		33.3229759185
654PhosphorylationTADDAETSEATEIIE
ECCCCCCCCCCHHHC		19.4229759185
657PhosphorylationDAETSEATEIIEGTQ
CCCCCCCCHHHCCCH		24.5429759185
772PhosphorylationAGELVIASPEGQLEV
CCEEEEECCCCCEEE		16.6226074081
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

Oops, there are no upstream regulatory protein records of E4F1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of E4F1_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 E4F1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EHMT2_HUMANEHMT2physical
16189514
CDN2A_HUMANCDKN2Aphysical
12446718
ARF_HUMANCDKN2Aphysical
12446718
RB_HUMANRB1physical
10869426
P53_HUMANTP53physical
10644996
HDAC1_HUMANHDAC1physical
12730668
HDAC1_HUMANHDAC1physical
21666599
T7L1A_DANREtcf7l1aphysical
21666599
KR107_HUMANKRTAP10-7physical
25416956
RASF1_HUMANRASSF1physical
14729613
FHL2_HUMANFHL2physical
16652157
P53_HUMANTP53physical
16652157
HIC2_HUMANHIC2physical
28514442
ABT1_HUMANABT1physical
28514442
LIN41_HUMANTRIM71physical
28514442
H11_HUMANHIST1H1Aphysical
28514442
UBE2O_HUMANUBE2Ophysical
28514442
RL36L_HUMANRPL36ALphysical
28514442
RL26L_HUMANRPL26L1physical
28514442
RL26_HUMANRPL26physical
28514442
RT35_HUMANMRPS35physical
28514442
ZNF70_HUMANZNF70physical
28514442
ZN579_HUMANZNF579physical
28514442
PTCD3_HUMANPTCD3physical
28514442
RT09_HUMANMRPS9physical
28514442
RT07_HUMANMRPS7physical
28514442
RS27A_HUMANRPS27Aphysical
28514442
RT05_HUMANMRPS5physical
28514442
RT23_HUMANMRPS23physical
28514442
ZSC25_HUMANZSCAN25physical
28514442
ZN574_HUMANZNF574physical
28514442
YBOX3_HUMANYBX3physical
28514442
RT29_HUMANDAP3physical
28514442
LTBP4_HUMANLTBP4physical
28514442
GZF1_HUMANGZF1physical
28514442
YBOX1_HUMANYBX1physical
28514442
ZBT11_HUMANZBTB11physical
28514442
SURF6_HUMANSURF6physical
28514442
STAU2_HUMANSTAU2physical
28514442
ZC3H8_HUMANZC3H8physical
28514442
RT33_HUMANMRPS33physical
28514442
ZN771_HUMANZNF771physical
28514442
RPF1_HUMANRPF1physical
28514442
ZBT24_HUMANZBTB24physical
28514442
ZN638_HUMANZNF638physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
RT11_HUMANMRPS11physical
28514442
ZCHC9_HUMANZCCHC9physical
28514442
RENT1_HUMANUPF1physical
28514442
RS8_HUMANRPS8physical
28514442
RT02_HUMANMRPS2physical
28514442
RL19_HUMANRPL19physical
28514442
RS3A_HUMANRPS3Aphysical
28514442
RT31_HUMANMRPS31physical
28514442
RT18C_HUMANMRPS18Cphysical
28514442
ZN770_HUMANZNF770physical
28514442
RT24_HUMANMRPS24physical
28514442
NSA2_HUMANNSA2physical
28514442
RS24_HUMANRPS24physical
28514442
C1QBP_HUMANC1QBPphysical
28514442
SF3B1_HUMANSF3B1physical
28514442
RS16_HUMANRPS16physical
28514442
DDX21_HUMANDDX21physical
28514442
DKC1_HUMANDKC1physical
28514442
RT22_HUMANMRPS22physical
28514442
LARP7_HUMANLARP7physical
28514442
MOV10_HUMANMOV10physical
28514442
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 E4F1_HUMAN

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Related Literatures of Post-Translational Modification
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-50, AND MASSSPECTROMETRY.

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