E2FB_ARATH - dbPTM
E2FB_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID E2FB_ARATH
UniProt AC Q9FV71
Protein Name Transcription factor E2FB
Gene Name E2FB
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 469
Subcellular Localization Cytoplasm. Nucleus. Interaction with DPA induces an exclusive nuclear localization, but an interaction with DPB has no effect.
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 binding of retinoblastoma-related proteins represses transactivation. Involved in the control of cell-cycle progression from G1 to S phase and from G2 to M phase. Stimulates cell proliferation and delays differentiation. Represses cell enlargement and endoreduplication in auxin-free conditions..
Protein Sequence MSEEVPQQFPSSKRQLHPSLSSMKPPLVAPGEYHRFDAAETRGGGAVADQVVSDAIVIKSTLKRKTDLVNQIVEVNELNTGVLQTPVSGKGGKAKKTSRSAKSNKSGTLASGSNAGSPGNNFAQAGTCRYDSSLGLLTKKFINLIKQAEDGILDLNKAADTLEVQKRRIYDITNVLEGIGLIEKTLKNRIQWKGLDVSKPGETIESIANLQDEVQNLAAEEARLDDQIRESQERLTSLSEDENNKRLLFVTENDIKNLPCFQNKTLIAVKAPHGTTLEVPDPDEAGGYQRRYRIILRSTMGPIDVYLVSQFEESFEDIPQADEPSNVPDEPSNVPDVPSNLPSTSGLPENHDVSMPMKEESTERNMETQEVDDTQRVYSDIESHDFVDGIMKIVPPDLDMGVDYWFRSEVGEVSITDMWPDESGPDWNQMITFDQDHAGPSDNKILEQPQTPSSPTPEESTATRSPTGS
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
113PhosphorylationSGTLASGSNAGSPGN
CCCCCCCCCCCCCCC
22.4725561503
117PhosphorylationASGSNAGSPGNNFAQ
CCCCCCCCCCCCCCC
27.5030291188
130PhosphorylationAQAGTCRYDSSLGLL
CCCCCCCCCCHHHHH
23.4823328941
251PhosphorylationNKRLLFVTENDIKNL
CCEEEEEEHHHHCCC
23.0319880383
378PhosphorylationVDDTQRVYSDIESHD
CCCHHHHHHHHHHCC
11.6523111157
379PhosphorylationDDTQRVYSDIESHDF
CCHHHHHHHHHHCCC
29.2923111157
451PhosphorylationKILEQPQTPSSPTPE
CCCCCCCCCCCCCCC
31.6423776212
453PhosphorylationLEQPQTPSSPTPEES
CCCCCCCCCCCCCHH
52.9523776212
454PhosphorylationEQPQTPSSPTPEEST
CCCCCCCCCCCCHHC
33.7130291188
456PhosphorylationPQTPSSPTPEESTAT
CCCCCCCCCCHHCCC
45.3323776212
460PhosphorylationSSPTPEESTATRSPT
CCCCCCHHCCCCCCC
22.9823776212
461PhosphorylationSPTPEESTATRSPTG
CCCCCHHCCCCCCCC
35.0123776212
463PhosphorylationTPEESTATRSPTGS-
CCCHHCCCCCCCCC-
31.5923776212
465PhosphorylationEESTATRSPTGS---
CHHCCCCCCCCC---
23.5823776212
467PhosphorylationSTATRSPTGS-----
HCCCCCCCCC-----
51.8323776212
469PhosphorylationATRSPTGS-------
CCCCCCCC-------
39.2623776212

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 E2FB_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of E2FB_ARATH !!

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 E2FB_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPA_ARATHDPAphysical
20407024
DPB_ARATHDPBphysical
20407024
RBR1_ARATHRBR1physical
20706207
PSMD6_ARATHAT4G24820physical
20706207
GSXL1_ARATHAT1G12160physical
20706207
MDHC1_ARATHAT1G04410physical
20706207
DPA_ARATHDPAphysical
11108847
DPB_ARATHDPBphysical
11108847

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of E2FB_ARATH

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Related Literatures of Post-Translational Modification

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