E2F8_HUMAN - dbPTM
E2F8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID E2F8_HUMAN
UniProt AC A0AVK6
Protein Name Transcription factor E2F8
Gene Name E2F8
Organism Homo sapiens (Human).
Sequence Length 867
Subcellular Localization Nucleus .
Protein Description Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1: component of a feedback loop in S phase by repressing the expression of E2F1, thereby preventing p53/TP53-dependent apoptosis. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene..
Protein Sequence MENEKENLFCEPHKRGLMKTPLKESTTANIVLAEIQPDFGPLTTPTKPKEGSQGEPWTPTANLKMLISAVSPEIRNRDQKRGLFDNRSGLPEAKDCIHEHLSGDEFEKSQPSRKEKSLGLLCHKFLARYPNYPNPAVNNDICLDEVAEELNVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLNKTLGTLKSIGEENKYAEQIMMIKKKEYEQEFDFIKSYSIEDHIIKSNTGPNGHPDMCFVELPGVEFRAASVNSRKDKSLRVMSQKFVMLFLVSTPQIVSLEVAAKILIGEDHVEDLDKSKFKTKIRRLYDIANVLSSLDLIKKVHVTEERGRKPAFKWTGPEISPNTSGSSPVIHFTPSDLEVRRSSKENCAKNLFSTRGKPNFTRHPSLIKLVKSIESDRRKINSAPSSPIKTNKAESSQNSAPFPSKMAQLAAICKMQLEEQSSESRQKVKVQLARSGPCKPVAPLDPPVNAEMELTAPSLIQPLGMVPLIPSPLSSAVPLILPQAPSGPSYAIYLQPTQAHQSVTPPQGLSPTVCTTHSSKATGSKDSTDATTEKAANDTSKASASTRPGSLLPAPERQGAKSRTREPAGERGSKRASMLEDSGSKKKFKEDLKGLENVSATLFPSGYLIPLTQCSSLGAESILSGKENSSALSPNHRIYSSPIAGVIPVTSSELTAVNFPSFHVTPLKLMVSPTSVAAVPVGNSPALASSHPVPIQNPSSAIVNFTLQHLGLISPNVQLSASPGSGIVPVSPRIESVNVAPENAGTQQGRATNYDSPVPGQSQPNGQSVAVTGAQQPVPVTPKGSQLVAESFFRTPGGPTKPTSSSCMDFEGANKTSLGTLFVPQRKLEVSTEDVH
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
20PhosphorylationHKRGLMKTPLKESTT
CCCCCCCCCCCCCCC		21.6423898821
25PhosphorylationMKTPLKESTTANIVL
CCCCCCCCCCCCEEE		29.4828102081
26PhosphorylationKTPLKESTTANIVLA
CCCCCCCCCCCEEEE		30.9028102081
27PhosphorylationTPLKESTTANIVLAE
CCCCCCCCCCEEEEE		27.3028102081
43PhosphorylationQPDFGPLTTPTKPKE
CCCCCCCCCCCCCCC		33.5926657352
44PhosphorylationPDFGPLTTPTKPKEG
CCCCCCCCCCCCCCC		36.3225850435
46PhosphorylationFGPLTTPTKPKEGSQ
CCCCCCCCCCCCCCC		58.8625850435
52PhosphorylationPTKPKEGSQGEPWTP
CCCCCCCCCCCCCCC		35.7823401153
58PhosphorylationGSQGEPWTPTANLKM
CCCCCCCCCCHHHHH		22.8327273156
60PhosphorylationQGEPWTPTANLKMLI
CCCCCCCCHHHHHHH		22.3225262027
68PhosphorylationANLKMLISAVSPEIR
HHHHHHHHHCCHHHH		20.7527987026
71PhosphorylationKMLISAVSPEIRNRD
HHHHHHCCHHHHCHH		19.2829255136
102PhosphorylationDCIHEHLSGDEFEKS
HHHHHHHCCCHHHHC		46.2123401153
124UbiquitinationSLGLLCHKFLARYPN
HHHHHHHHHHHHCCC		40.87-
188UbiquitinationHGRHNLNKTLGTLKS
CCCCCHHHHHHHHHH		48.5729967540
194UbiquitinationNKTLGTLKSIGEENK
HHHHHHHHHHCCCCH		39.6129967540
202PhosphorylationSIGEENKYAEQIMMI
HHCCCCHHHHHHHHH		27.27-
211AcetylationEQIMMIKKKEYEQEF
HHHHHHCHHHHHHHC		39.657494089
211UbiquitinationEQIMMIKKKEYEQEF
HHHHHHCHHHHHHHC		39.6529967540
212UbiquitinationQIMMIKKKEYEQEFD
HHHHHCHHHHHHHCC		61.6029967540
222UbiquitinationEQEFDFIKSYSIEDH
HHHCCHHHCCCHHHC		43.2529967540
224PhosphorylationEFDFIKSYSIEDHII
HCCHHHCCCHHHCEE		14.5223312004
225PhosphorylationFDFIKSYSIEDHIIK
CCHHHCCCHHHCEEC		26.9627067055
265PhosphorylationVNSRKDKSLRVMSQK
CCCCCCHHHHHHCCE		31.3829083192
270PhosphorylationDKSLRVMSQKFVMLF
CHHHHHHCCEEHHHH		27.6229083192
280PhosphorylationFVMLFLVSTPQIVSL
EHHHHHCCCCCEEEH		36.20-
305UbiquitinationDHVEDLDKSKFKTKI
CCHHHCCHHHHHHHH		63.9429967540
316PhosphorylationKTKIRRLYDIANVLS
HHHHHHHHHHHHHHH		11.9521406692
323PhosphorylationYDIANVLSSLDLIKK
HHHHHHHHHHHHHHH		25.2729396449
324PhosphorylationDIANVLSSLDLIKKV
HHHHHHHHHHHHHHH		23.0329396449
330UbiquitinationSSLDLIKKVHVTEER
HHHHHHHHHCCCCCC		30.49-
346PhosphorylationRKPAFKWTGPEISPN
CCCCCCCCCCCCCCC		43.3728450419
351PhosphorylationKWTGPEISPNTSGSS
CCCCCCCCCCCCCCC		15.5028450419
354PhosphorylationGPEISPNTSGSSPVI
CCCCCCCCCCCCCEE		37.5423401153
355PhosphorylationPEISPNTSGSSPVIH
CCCCCCCCCCCCEEE		43.2319276368
357PhosphorylationISPNTSGSSPVIHFT
CCCCCCCCCCEEECC		31.1019276368
358PhosphorylationSPNTSGSSPVIHFTP
CCCCCCCCCEEECCH		27.0619276368
364PhosphorylationSSPVIHFTPSDLEVR
CCCEEECCHHHHHHH		14.0226074081
366PhosphorylationPVIHFTPSDLEVRRS
CEEECCHHHHHHHHH		52.3427732954
388UbiquitinationNLFSTRGKPNFTRHP
HCHHCCCCCCCCCCH		33.2329967540
392PhosphorylationTRGKPNFTRHPSLIK
CCCCCCCCCCHHHHH		34.4123882029
396PhosphorylationPNFTRHPSLIKLVKS
CCCCCCHHHHHHHHH		36.2823312004
403PhosphorylationSLIKLVKSIESDRRK
HHHHHHHHHHHHHHH		24.90-
406PhosphorylationKLVKSIESDRRKINS
HHHHHHHHHHHHHHC		34.45-
413PhosphorylationSDRRKINSAPSSPIK
HHHHHHHCCCCCCCC		45.0623401153
416PhosphorylationRKINSAPSSPIKTNK
HHHHCCCCCCCCCCC		48.7622617229
417PhosphorylationKINSAPSSPIKTNKA
HHHCCCCCCCCCCCC		29.5923401153
421PhosphorylationAPSSPIKTNKAESSQ
CCCCCCCCCCCCCCC		42.5430001349
436UbiquitinationNSAPFPSKMAQLAAI
CCCCCCHHHHHHHHH		38.1929967540
455PhosphorylationLEEQSSESRQKVKVQ
HHHCCHHHHHHHHHH		41.7923532336
608PhosphorylationERGSKRASMLEDSGS
HHHHHHHHHHCCCCC		28.1226437602
613PhosphorylationRASMLEDSGSKKKFK
HHHHHCCCCCCHHHH		35.2726437602
660PhosphorylationILSGKENSSALSPNH
HHCCCCCCCCCCCCC		20.3426074081
661PhosphorylationLSGKENSSALSPNHR
HCCCCCCCCCCCCCC		44.8225849741
664PhosphorylationKENSSALSPNHRIYS
CCCCCCCCCCCCCCC		24.3128985074
670PhosphorylationLSPNHRIYSSPIAGV
CCCCCCCCCCCCCEE		11.7626074081
671PhosphorylationSPNHRIYSSPIAGVI
CCCCCCCCCCCCEEE		27.5426074081
672PhosphorylationPNHRIYSSPIAGVIP
CCCCCCCCCCCEEEE		11.8926074081
751PhosphorylationISPNVQLSASPGSGI
CCCCEEEECCCCCCE		15.0326074081
753PhosphorylationPNVQLSASPGSGIVP
CCEEEECCCCCCEEE		26.8126074081
756PhosphorylationQLSASPGSGIVPVSP
EEECCCCCCEEECCC		28.8226074081
762PhosphorylationGSGIVPVSPRIESVN
CCCEEECCCCEEEEE		11.4626074081
767PhosphorylationPVSPRIESVNVAPEN
ECCCCEEEEEECCCC		19.3426074081
777PhosphorylationVAPENAGTQQGRATN
ECCCCCCCCCCCCCC		18.46-
803PhosphorylationNGQSVAVTGAQQPVP
CCCEEEEECCCCCCC		19.6425850435
812PhosphorylationAQQPVPVTPKGSQLV
CCCCCCCCCCCCCEE		17.1425850435
822PhosphorylationGSQLVAESFFRTPGG
CCCEEEEECCCCCCC		21.6824719451
834PhosphorylationPGGPTKPTSSSCMDF
CCCCCCCCCCCCCCC		42.6822210691
862PhosphorylationPQRKLEVSTEDVH--
CCCCEEECCCCCC--		19.39-
863PhosphorylationQRKLEVSTEDVH---
CCCEEECCCCCC---		41.18-
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 E2F8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of E2F8_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 E2F8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TTC33_HUMANTTC33physical
26186194
TTC33_HUMANTTC33physical
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 E2F8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND MASSSPECTROMETRY.

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