NFE2_MOUSE - dbPTM
NFE2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NFE2_MOUSE
UniProt AC Q07279
Protein Name Transcription factor NF-E2 45 kDa subunit
Gene Name Nfe2
Organism Mus musculus (Mouse).
Sequence Length 373
Subcellular Localization Nucleus, PML body. Cytoplasm. The sumoylated form locates to the nuclear bodies PML oncogenic domains (PODs). Translocated to the cytoplasm through interaction with ITCH (By similarity)..
Protein Description Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron..
Protein Sequence MPPCPPQQNRNRLSQLPVGELGEMELTWQEIMSITELQGLNVPSETSFEPQAPTPYPGPLPPPTYCPCSIHPDAGFSLPPPSYELPASTPHVPELPYSYGNVAIPVSKPLTLSGLLNEPLPDHLALLDIGLPVGQPKPQEDPESDSGLSLNYSDAESLELEGMEAGRRRSEYVDMYPVEYPYSLMPNSLAHPNYTLPPTETPLALESSSGPVRAKPAVRGEAGSRDERRALAMKIPFPTDKIVNLPVDDFNELLAQYPLTESQLALVRDIRRRGKNKVAAQNCRKRKLETIVQLERELERLSSERERLLRARGEADRTLEVMRQQLAELYHDIFQHLRDESGNSYSPEEYVLQQAADGAIFLVPRGTKMEATD
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
157PhosphorylationLNYSDAESLELEGME
CCCCHHHHHHHCCHH
28.9419966288
170PhosphorylationMEAGRRRSEYVDMYP
HHHHCCCHHCCCCEE
31.3119966288

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
157SPhosphorylationKinaseMAPK8Q91Y86
Uniprot
170SPhosphorylationKinasePRKACAP05132
GPS
170SPhosphorylationKinasePKA-FAMILY-GPS
170SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NFE2_MOUSE !!

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 NFE2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ORC2_MOUSEOrc2physical
20211142
MBB1A_MOUSEMybbp1aphysical
20211142
KAT2B_MOUSEKat2bphysical
20211142
PER1_MOUSEPer1physical
20211142
REQU_MOUSEDpf2physical
20211142
KDM5C_MOUSEKdm5cphysical
20211142
KDM5D_MOUSEKdm5dphysical
20211142
SNAI1_MOUSESnai1physical
20211142
SPT4A_MOUSESupt4aphysical
20211142
TIAR_MOUSETial1physical
20211142
TS101_MOUSETsg101physical
20211142
UBIP1_MOUSEUbp1physical
20211142
ZSCA2_MOUSEZscan2physical
20211142
ASH2L_MOUSEAsh2lphysical
20211142
TF2H2_MOUSEGtf2h2physical
20211142
ZN292_MOUSEZfp292physical
20211142
PDLI4_MOUSEPdlim4physical
20211142
PLRG1_MOUSEPlrg1physical
20211142
TRIP4_MOUSETrip4physical
20211142
ANR49_MOUSEAnkrd49physical
20211142
RNF14_MOUSERnf14physical
20211142
SMCE1_MOUSESmarce1physical
20211142
SIR2_MOUSESirt2physical
20211142
ASB1_MOUSEAsb1physical
20211142
ZDHC6_MOUSEZdhhc6physical
20211142
T2EB_MOUSEGtf2e2physical
20211142
RPB4_MOUSEPolr2dphysical
20211142
ASB12_MOUSEAsb12physical
20211142
ERCC8_MOUSEErcc8physical
20211142
MMS19_MOUSEMms19physical
20211142
T2EA_MOUSEGtf2e1physical
20211142
PBX4_MOUSEPbx4physical
20211142
SIR1_MOUSESirt1physical
20211142
CSDC2_MOUSECsdc2physical
20211142
CHD4_MOUSEChd4physical
20211142
MED21_MOUSEMed21physical
20211142
TLE6_MOUSETle6physical
20211142
ASH1L_MOUSEAsh1lphysical
20211142
KDM4B_MOUSEKdm4bphysical
20211142
CSDE1_MOUSECsde1physical
20211142
RPB2_MOUSEPolr2bphysical
20211142
ZN592_MOUSEZfp592physical
20211142
CARTF_MOUSECarfphysical
20211142
HIF1N_MOUSEHif1anphysical
20211142
GCFC2_MOUSEGcfc2physical
20211142
MK08_MOUSEMapk8physical
19966288
ASH2L_MOUSEAsh2lphysical
17707229
RBBP5_MOUSERbbp5physical
17707229
WDR5_MOUSEWdr5physical
17707229
MEN1_MOUSEMen1physical
17707229
MAFK_MOUSEMafkphysical
17707229
WWP1_HUMANWWP1physical
9753456

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NFE2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"JNK-mediated turnover and stabilization of the transcription factorp45/NF-E2 during differentiation of murine erythroleukemia cells.";
Lee T.L., Shyu Y.C., Hsu P.H., Chang C.W., Wen S.C., Hsiao W.Y.,Tsai M.D., Shen C.K.;
Proc. Natl. Acad. Sci. U.S.A. 107:52-57(2010).
Cited for: PHOSPHORYLATION AT SER-157, INTERACTION WITH MAPK8, UBIQUITINATION,MASS SPECTROMETRY, AND MUTAGENESIS OF SER-157.
"Regulation of the erythroid transcription factor NF-E2 by cyclicadenosine monophosphate-dependent protein kinase.";
Casteel D., Suhasini M., Gudi T., Naima R., Pilz R.B.;
Blood 91:3193-3201(1998).
Cited for: PHOSPHORYLATION AT SER-170, FUNCTION, AND MUTAGENESIS OF SER-170.

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