NF2L2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NF2L2_MOUSE
• UniProt AC: Q60795
• Protein Name: Nuclear factor erythroid 2-related factor 2
• Gene Name: Nfe2l2
• Organism: Mus musculus (Mouse).
• Sequence Length: 597
• Subcellular Localization: Cytoplasm, cytosol . Nucleus . Cytosolic under unstressed conditions, translocates into the nucleus upon induction by electrophilic agents.
• Protein Description: Transcription activator that binds to antioxidant response (ARE) elements in the promoter regions of target genes. Important for the coordinated up-regulation of genes in response to oxidative stress. May be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region..
• Protein Sequence: MMDLELPPPGLQSQQDMDLIDILWRQDIDLGVSREVFDFSQRQKDYELEKQKKLEKERQEQLQKEQEKAFFAQFQLDEETGEFLPIQPAQHIQTDTSGSASYSQVAHIPKQDALYFEDCMQLLAETFPFVDDHESLALDIPSHAESSVFTAPHQAQSLNSSLEAAMTDLSSIEQDMEQVWQELFSIPELQCLNTENKQLADTTAVPSPEATLTEMDSNYHFYSSISSLEKEVGNCGPHFLHGFEDSFSSILSTDDASQLTSLDSNPTLNTDFGDEFYSAFIAEPSDGGSMPSSAAISQSLSELLDGTIEGCDLSLCKAFNPKHAEGTMEFNDSDSGISLNTSPSRASPEHSVESSIYGDPPPGFSDSEMEELDSAPGSVKQNGPKAQPAHSPGDTVQPLSPAQGHSAPMRESQCENTTKKEVPVSPGHQKAPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVDDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLGHLKDEREKLLREKGENDRNLHLLKRRLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDTKKN

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
40	Phosphorylation	SREVFDFSQRQKDYE CHHHHCHHHHHHHHH	26.71	19920073
207	Phosphorylation	ADTTAVPSPEATLTE CCCCCCCCCCCCCEE	28.86	-
335	Phosphorylation	MEFNDSDSGISLNTS EEECCCCCCEECCCC	41.81	22751928
338	Phosphorylation	NDSDSGISLNTSPSR CCCCCCEECCCCCCC	21.06	22751928
342	Phosphorylation	SGISLNTSPSRASPE CCEECCCCCCCCCCC	21.58	22751928
347	Phosphorylation	NTSPSRASPEHSVES CCCCCCCCCCCCCCC	29.70	22751928
351	Phosphorylation	SRASPEHSVESSIYG CCCCCCCCCCCHHCC	26.39	21245377
355	Phosphorylation	PEHSVESSIYGDPPP CCCCCCCHHCCCCCC	13.31	21245377
365	Phosphorylation	GDPPPGFSDSEMEEL CCCCCCCCHHHHHHH	46.25	-
391	Phosphorylation	PKAQPAHSPGDTVQP CCCCCCCCCCCCCCC	32.46	28576409
395	Phosphorylation	PAHSPGDTVQPLSPA CCCCCCCCCCCCCCC	27.27	26643407
400	Phosphorylation	GDTVQPLSPAQGHSA CCCCCCCCCCCCCCC	25.52	26643407
406	Phosphorylation	LSPAQGHSAPMRESQ CCCCCCCCCCCCHHH	40.67	28066266
425	Phosphorylation	TKKEVPVSPGHQKAP CCCCCCCCCCCCCCC	21.06	23384938
454	N-linked_Glycosylation	TRDELRAKALHIPFP CHHHHHHHHHCCCCC	45.08	-
464	N-linked_Glycosylation	HIPFPVEKIINLPVD CCCCCHHHHHCCCHH	49.47	-
479	N-linked_Glycosylation	DFNEMMSKEQFNEAQ HHHHHHCHHHCCHHH	37.32	-
491	N-linked_Glycosylation	EAQLALIRDIRRRGK HHHHHHHHHHHHHCC	33.87	-
550	Phosphorylation	HLLKRRLSTLYLEVF HHHHHHHHHHHHHHH	17.98	-
561	N-linked_Glycosylation	LEVFSMLRDEDGKPY HHHHHHHCCCCCCCC	36.31	-
566	N-linked_Glycosylation	MLRDEDGKPYSPSEY HHCCCCCCCCCCHHC	53.77	-
568	Phosphorylation	RDEDGKPYSPSEYSL CCCCCCCCCCHHCCE	36.38	19920073
588	Acetylation	GNVFLVPKSKKPDTK CCEEEEECCCCCCCC	68.38	21196497
591	Acetylation	FLVPKSKKPDTKKN- EEEECCCCCCCCCC-	56.04	21196497

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
40	S	Phosphorylation	Kinase	PRKCA	P20444	GPS
40	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
40	S	Phosphorylation	Kinase	PKC	-	Uniprot
335	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
335	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
338	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
338	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
342	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
347	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
351	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
355	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
550	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
568	Y	Phosphorylation	Kinase	FYN	P39688	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Keap1	Q9Z2X8	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
40	S	Oxidation	Phosphorylation of Ser-40 by PKC in response to oxidative stress dissociates NFE2L2 from its cytoplasmic inhibitor KEAP1, promoting its translocation into the nucleus.	-
40	S	Phosphorylation	Phosphorylation of Ser-40 by PKC in response to oxidative stress dissociates NFE2L2 from its cytoplasmic inhibitor KEAP1, promoting its translocation into the nucleus.	-
588	K	Acetylation	Acetylation at Lys-588 and Lys-591 increases nuclear localization whereas deacetylation by SIRT1 enhances cytoplasmic presence.	-
591	K	Acetylation	Acetylation at Lys-588 and Lys-591 increases nuclear localization whereas deacetylation by SIRT1 enhances cytoplasmic presence.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NF2L2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATF4_RAT	Atf4	physical	11274184
KEAP1_MOUSE	Keap1	physical	18358244
JUND_MOUSE	Jund	physical	18358244
FOS_MOUSE	Fos	physical	18358244
MAFK_MOUSE	Mafk	physical	18358244
NRF1_MOUSE	Nrf1	physical	18358244
CERS2_MOUSE	Cers2	physical	20211142
FBW1A_MOUSE	Btrc	physical	21245377
KEAP1_MOUSE	Keap1	physical	19279002
CDN1A_MOUSE	Cdkn1a	physical	19560419
KEAP1_MOUSE	Keap1	physical	19560419
KEAP1_MOUSE	Keap1	physical	15143058
KEAP1_MOUSE	Keap1	physical	17903176
KEAP1_MOUSE	Keap1	physical	16581765
TIF1B_HUMAN	TRIM28	physical	21382013
SMC4_HUMAN	SMC4	physical	21382013
CLH1_HUMAN	CLTC	physical	21382013
SMRC2_HUMAN	SMARCC2	physical	21382013
RAD50_HUMAN	RAD50	physical	21382013
TRI33_HUMAN	TRIM33	physical	21382013
FBW1A_MOUSE	Btrc	physical	22964642
ATG7_MOUSE	Atg7	genetic	20173742
KEAP1_MOUSE	Keap1	physical	12145307
MK07_MOUSE	Mapk7	physical	23043106

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.