E2F6_HUMAN - dbPTM
E2F6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID E2F6_HUMAN
UniProt AC O75461
Protein Name Transcription factor E2F6
Gene Name E2F6
Organism Homo sapiens (Human).
Sequence Length 281
Subcellular Localization Nucleus.
Protein Description Inhibitor of E2F-dependent transcription. Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3'. Has a preference for the 5'-TTTCCCGC-3' E2F recognition site. E2F6 lacks the transcriptional activation and pocket protein binding domains. Appears to regulate a subset of E2F-dependent genes whose products are required for entry into the cell cycle but not for normal cell cycle progression. May silence expression via the recruitment of a chromatin remodeling complex containing histone H3-K9 methyltransferase activity. Overexpression delays the exit of cells from the S-phase..
Protein Sequence MSQQRPARKLPSLLLDPTEETVRRRCRDPINVEGLLPSKIRINLEDNVQYVSMRKALKVKRPRFDVSLVYLTRKFMDLVRSAPGGILDLNKVATKLGVRKRRVYDITNVLDGIDLVEKKSKNHIRWIGSDLSNFGAVPQQKKLQEELSDLSAMEDALDELIKDCAQQLFELTDDKENERLAYVTYQDIHSIQAFHEQIVIAVKAPAETRLDVPAPREDSITVHIRSTNGPIDVYLCEVEQGQTSNKRSEGVGTSSSESTHPEGPEEEENPQQSEELLEVSN
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
9SumoylationSQQRPARKLPSLLLD
CCCCCCCCCCHHHCC
67.8528112733
9UbiquitinationSQQRPARKLPSLLLD
CCCCCCCCCCHHHCC
67.85-
12PhosphorylationRPARKLPSLLLDPTE
CCCCCCCHHHCCCCH
41.93-
21PhosphorylationLLDPTEETVRRRCRD
HCCCCHHHHHHHCCC
17.0624719451
38PhosphorylationNVEGLLPSKIRINLE
CCCCCCCCCEEEECC
40.4624719451
43 (in isoform 2)Ubiquitination-27.77-
50PhosphorylationNLEDNVQYVSMRKAL
ECCCCEEEEEHHHHH
7.1028796482
52PhosphorylationEDNVQYVSMRKALKV
CCCEEEEEHHHHHCC
14.1328796482
66 (in isoform 2)Ubiquitination-4.36-
74AcetylationSLVYLTRKFMDLVRS
EEHHHHHHHHHHHHH
39.547303075
86 (in isoform 2)Ubiquitination-3.1621906983
91AcetylationGGILDLNKVATKLGV
CCCCCHHHHHHHHCC
40.317298809
95UbiquitinationDLNKVATKLGVRKRR
CHHHHHHHHCCCCCC
33.24-
95AcetylationDLNKVATKLGVRKRR
CHHHHHHHHCCCCCC
33.247298819
100AcetylationATKLGVRKRRVYDIT
HHHHCCCCCCEEEHH
41.997298829
109UbiquitinationRVYDITNVLDGIDLV
CEEEHHHHCCCCCCH
3.74-
109 (in isoform 2)Ubiquitination-3.7421906983
110UbiquitinationVYDITNVLDGIDLVE
EEEHHHHCCCCCCHH
5.61-
118UbiquitinationDGIDLVEKKSKNHIR
CCCCCHHHHCCCCEE
55.6721906983
118 (in isoform 1)Ubiquitination-55.6721906983
119UbiquitinationGIDLVEKKSKNHIRW
CCCCHHHHCCCCEEE
53.83-
141UbiquitinationFGAVPQQKKLQEELS
CCCCCCHHHHHHHHH
50.642190698
141 (in isoform 1)Ubiquitination-50.6421906983
142UbiquitinationGAVPQQKKLQEELSD
CCCCCHHHHHHHHHH
51.57-
175UbiquitinationLFELTDDKENERLAY
HHHHCCCCCCCEEEE
66.31-
221PhosphorylationAPREDSITVHIRSTN
CCCCCEEEEEEEECC
15.2422985185
226PhosphorylationSITVHIRSTNGPIDV
EEEEEEEECCCCEEE
26.14-
243PhosphorylationCEVEQGQTSNKRSEG
EEECCCCCCCCCCCC
40.88-
280PhosphorylationSEELLEVSN------
HHHHHHHCC------
27.7028509920

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
12SPhosphorylationKinaseCHEK1O14757
GPS
52SPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of E2F6_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 E2F6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RYBP_HUMANRYBPphysical
11171983
TFDP1_HUMANTFDP1physical
16189514
TFDP2_HUMANTFDP2physical
16189514
RING1_HUMANRING1physical
11171983
RYBP_HUMANRYBPphysical
12411495
EZH1_HUMANEZH1physical
16565076
EZH2_HUMANEZH2physical
16565076
KMT2A_HUMANKMT2Aphysical
16951254
KMT2D_HUMANKMT2Dphysical
16951254
EPC1_MOUSEEpc1physical
15536069
TFDP1_MOUSETfdp1physical
15536069
EPC1_HUMANEPC1physical
15536069
EED_HUMANEEDphysical
15536069
EZH2_HUMANEZH2physical
15536069
LMBL2_HUMANL3MBTL2physical
21596310
A4_HUMANAPPphysical
21832049
TFDP1_HUMANTFDP1physical
25416956
TFDP2_HUMANTFDP2physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
MGAP_HUMANMGAphysical
26186194
TFDP1_HUMANTFDP1physical
26186194
RYBP_HUMANRYBPphysical
26186194
COMD6_HUMANCOMMD6physical
26186194
COMD4_HUMANCOMMD4physical
26186194
TFDP2_HUMANTFDP2physical
26186194
WDR5_HUMANWDR5physical
26186194
RING2_HUMANRNF2physical
26186194
LMBL2_HUMANL3MBTL2physical
26186194
PCGF6_HUMANPCGF6physical
26186194
TFDP1_HUMANTFDP1physical
9501179
TFDP2_HUMANTFDP2physical
9501179
TFDP2_HUMANTFDP2physical
21516116
PCGF6_HUMANPCGF6physical
28514442
LMBL2_HUMANL3MBTL2physical
28514442
TFDP2_HUMANTFDP2physical
28514442
RYBP_HUMANRYBPphysical
28514442
HDAC1_HUMANHDAC1physical
28514442
COMD4_HUMANCOMMD4physical
28514442
WDR5_HUMANWDR5physical
28514442
TFDP1_HUMANTFDP1physical
28514442
MGAP_HUMANMGAphysical
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 E2F6_HUMAN

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Related Literatures of Post-Translational Modification

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