NFE2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NFE2_HUMAN
• UniProt AC: Q16621
• Protein Name: Transcription factor NF-E2 45 kDa subunit
• Gene Name: NFE2
• Organism: Homo sapiens (Human).
• 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.
• 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: MSPCPPQQSRNRVIQLSTSELGEMELTWQEIMSITELQGLNAPSEPSFEPQAPAPYLGPPPPTTYCPCSIHPDSGFPLPPPPYELPASTSHVPDPPYSYGNMAIPVSKPLSLSGLLSEPLQDPLALLDIGLPAGPPKPQEDPESDSGLSLNYSDAESLELEGTEAGRRRSEYVEMYPVEYPYSLMPNSLAHSNYTLPAAETPLALEPSSGPVRAKPTARGEAGSRDERRALAMKIPFPTDKIVNLPVDDFNELLARYPLTESQLALVRDIRRRGKNKVAAQNCRKRKLETIVQLERELERLTNERERLLRARGEADRTLEVMRQQLTELYRDIFQHLRDESGNSYSPEEYALQQAADGTIFLVPRGTKMEATD

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
2	Phosphorylation	------MSPCPPQQS ------CCCCCHHHH	34.90	23186163
107	Phosphorylation	GNMAIPVSKPLSLSG CCCCEECCCCCCCCC	24.17	24719451
108	Ubiquitination	NMAIPVSKPLSLSGL CCCEECCCCCCCCCC	50.65	19966288
137	Ubiquitination	GLPAGPPKPQEDPES CCCCCCCCCCCCCCC	63.57	19966288
157	Phosphorylation	LNYSDAESLELEGTE CCCCHHHHCEECCCH	28.94	19966288
170	Phosphorylation	TEAGRRRSEYVEMYP CHHHHCHHCCEEEEE	31.31	-
176	Phosphorylation	RSEYVEMYPVEYPYS HHCCEEEEECCCCCC	7.22	-
180	Phosphorylation	VEMYPVEYPYSLMPN EEEEECCCCCCCCCC	14.01	-
182	Phosphorylation	MYPVEYPYSLMPNSL EEECCCCCCCCCCCC	17.34	-
194	Phosphorylation	NSLAHSNYTLPAAET CCCCCCCCCCCCCCC	16.81	-
215	Ubiquitination	SSGPVRAKPTARGEA CCCCCCCCCCCCCCC	32.13	19966288
234	Ubiquitination	ERRALAMKIPFPTDK HHHHHHHCCCCCCHH	41.44	19966288
241	Ubiquitination	KIPFPTDKIVNLPVD CCCCCCHHCCCCCHH	51.54	1996628
346	Phosphorylation	DESGNSYSPEEYALQ CCCCCCCCHHHHHHH	26.17	19966288
368	Sumoylation	FLVPRGTKMEATD-- EEEECCCCCEECC--	37.25	-
368	Ubiquitination	FLVPRGTKMEATD-- EEEECCCCCEECC--	37.25	-
368	Sumoylation	FLVPRGTKMEATD-- EEEECCCCCEECC--	37.25	16287851

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
157	S	Phosphorylation	Kinase	JNK1	P45983	PSP
170	S	Phosphorylation	Kinase	PKA	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:18718448

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NFE2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NFE2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBP_HUMAN	CREBBP	physical	11154691
NFE2_HUMAN	NFE2	physical	11154691
ITCH_HUMAN	ITCH	physical	18718448
SSX5_HUMAN	SSX5	physical	20211142
SCND1_HUMAN	SCAND1	physical	20211142
YAP1_HUMAN	YAP1	physical	9305852
NEDD4_MOUSE	Nedd4	physical	9305852
YAP1_MOUSE	Yap1	physical	9305852
NEDD4_HUMAN	NEDD4	physical	9305852
NF2L3_HUMAN	NFE2L3	physical	23661758
NFE2_HUMAN	NFE2	physical	23661758
ATF4_HUMAN	ATF4	physical	23661758
THIO_HUMAN	TXN	physical	21988832
FBW1A_HUMAN	BTRC	physical	25416956

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.