dbPTM

NF2L2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NF2L2_HUMAN
UniProt AC	Q16236
Protein Name	Nuclear factor erythroid 2-related factor 2
Gene Name	NFE2L2
Organism	Homo sapiens (Human).
Sequence Length	605
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	MMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
28 (in isoform 2)	Ubiquitination	-	3.40	21906983
28	Ubiquitination	DILWRQDIDLGVSRE HHHHHCCCCCCCCHH	3.40	27667366
37	Ubiquitination	LGVSREVFDFSQRRK CCCCHHHHCHHHHHH	7.22	24816145
40	Phosphorylation	SREVFDFSQRRKEYE CHHHHCHHHHHHHHH	25.31	22558124
44	Ubiquitination	FDFSQRRKEYELEKQ HCHHHHHHHHHHHHH	67.83	21906983
44 (in isoform 1)	Ubiquitination	-	67.83	21906983
48 (in isoform 2)	Ubiquitination	-	11.03	21906983
48	Ubiquitination	QRRKEYELEKQKKLE HHHHHHHHHHHHHHH	11.03	27667366
53	Ubiquitination	YELEKQKKLEKERQE HHHHHHHHHHHHHHH	60.42	24816145
64	Ubiquitination	ERQEQLQKEQEKAFF HHHHHHHHHHHHHHH	70.70	27667366
64 (in isoform 1)	Ubiquitination	-	70.70	21906983
210	Phosphorylation	ENDKLVETTMVPSPE CCCEEEEEEEECCCC	16.83	30266825
211	Phosphorylation	NDKLVETTMVPSPEA CCEEEEEEEECCCCC	11.58	30266825
215	Phosphorylation	VETTMVPSPEAKLTE EEEEEECCCCCCCEE	24.78	30266825
229	Phosphorylation	EVDNYHFYSSIPSME EEECCEECCCCCHHH	6.54	27642862
243	Phosphorylation	EKEVGNCSPHFLNAF HCHHHCCCHHHHHHH	25.96	26074081
301	Phosphorylation	SISNSMPSPATLSHS CCCCCCCCCHHHHHH	20.65	-
344	Phosphorylation	AEFNDSDSGISLNTS CCCCCCCCCCCCCCC	41.81	22751928
347	Phosphorylation	NDSDSGISLNTSPSV CCCCCCCCCCCCCCC	21.06	22751928
351	Phosphorylation	SGISLNTSPSVASPE CCCCCCCCCCCCCCC	17.69	22751928
356	Phosphorylation	NTSPSVASPEHSVES CCCCCCCCCCCCCCC	28.76	22751928
374	Phosphorylation	GDTLLGLSDSEVEEL CCEEECCCHHHHHHH	36.97	-
395	Phosphorylation	VKQNGPKTPVHSSGD CCCCCCCCCCCCCCC	33.41	29449344
399	Phosphorylation	GPKTPVHSSGDMVQP CCCCCCCCCCCCCCC	35.93	29449344
400	Phosphorylation	PKTPVHSSGDMVQPL CCCCCCCCCCCCCCC	24.76	29449344
408	Phosphorylation	GDMVQPLSPSQGQST CCCCCCCCCCCCCCC	29.23	25159151
410	Phosphorylation	MVQPLSPSQGQSTHV CCCCCCCCCCCCCCC	43.50	29449344
414	Phosphorylation	LSPSQGQSTHVHDAQ CCCCCCCCCCCCCCC	27.57	29449344
415	Phosphorylation	SPSQGQSTHVHDAQC CCCCCCCCCCCCCCC	21.74	29449344
425	Phosphorylation	HDAQCENTPEKELPV CCCCCCCCCCCCCCC	15.55	29449344
432	Ubiquitination	TPEKELPVSPGHRKT CCCCCCCCCCCCCCC	19.73	29967540
433	Phosphorylation	PEKELPVSPGHRKTP CCCCCCCCCCCCCCC	24.19	30266825
437	Methylation	LPVSPGHRKTPFTKD CCCCCCCCCCCCCCC	50.92	112847407
438	Acetylation	PVSPGHRKTPFTKDK CCCCCCCCCCCCCCC	55.67	19273602
439	Ubiquitination	VSPGHRKTPFTKDKH CCCCCCCCCCCCCCC	24.48	29967540
439	Phosphorylation	VSPGHRKTPFTKDKH CCCCCCCCCCCCCCC	24.48	-
443	Acetylation	HRKTPFTKDKHSSRL CCCCCCCCCCCCHHH	66.22	19273602
445	Acetylation	KTPFTKDKHSSRLEA CCCCCCCCCCHHHHH	47.12	19273602
446	Ubiquitination	TPFTKDKHSSRLEAH CCCCCCCCCHHHHHH	40.93	29967540
447	Phosphorylation	PFTKDKHSSRLEAHL CCCCCCCCHHHHHHH	23.93	-
462	N-linked_Glycosylation	TRDELRAKALHIPFP CHHHHHHHHHCCCCC	45.08	31398338
462	Acetylation	TRDELRAKALHIPFP CHHHHHHHHHCCCCC	45.08	19273602
462	Ubiquitination	TRDELRAKALHIPFP CHHHHHHHHHCCCCC	45.08	29967540
472	Acetylation	HIPFPVEKIINLPVV CCCCCHHHHHCCCCC	49.47	19273602
472	N-linked_Glycosylation	HIPFPVEKIINLPVV CCCCCHHHHHCCCCC	49.47	31398338
487	Acetylation	DFNEMMSKEQFNEAQ CHHHHCCHHHCCHHH	37.32	14212485
487	N-linked_Glycosylation	DFNEMMSKEQFNEAQ CHHHHCCHHHCCHHH	37.32	31398338
499	N-linked_Glycosylation	EAQLALIRDIRRRGK HHHHHHHHHHHHHCC	33.87	31398338
506	Acetylation	RDIRRRGKNKVAAQN HHHHHHCCCHHHHHH	52.35	19273602
508	Acetylation	IRRRGKNKVAAQNCR HHHHCCCHHHHHHHH	36.42	19273602
516	Acetylation	VAAQNCRKRKLENIV HHHHHHHHHHHHHHH	56.96	14212473
516	Ubiquitination	VAAQNCRKRKLENIV HHHHHHHHHHHHHHH	56.96	-
518	Sumoylation	AQNCRKRKLENIVEL HHHHHHHHHHHHHHH	64.29	-
518	Sumoylation	AQNCRKRKLENIVEL HHHHHHHHHHHHHHH	64.29	-
518	Acetylation	AQNCRKRKLENIVEL HHHHHHHHHHHHHHH	64.29	19273602
518	Ubiquitination	AQNCRKRKLENIVEL HHHHHHHHHHHHHHH	64.29	29967540
524	Ubiquitination	RKLENIVELEQDLDH HHHHHHHHHHHHHHH	42.67	29967540
525	Ubiquitination	KLENIVELEQDLDHL HHHHHHHHHHHHHHH	5.05	29967540
531	Ubiquitination	ELEQDLDHLKDEKEK HHHHHHHHHHHHHHH	41.92	29967540
532	Ubiquitination	LEQDLDHLKDEKEKL HHHHHHHHHHHHHHH	8.15	29967540
533	Acetylation	EQDLDHLKDEKEKLL HHHHHHHHHHHHHHH	61.49	14212483
536	Acetylation	LDHLKDEKEKLLKEK HHHHHHHHHHHHHHH	70.99	14212459
538	Acetylation	HLKDEKEKLLKEKGE HHHHHHHHHHHHHCC	70.91	14212479
538	Ubiquitination	HLKDEKEKLLKEKGE HHHHHHHHHHHHHCC	70.91	29967540
541	Acetylation	DEKEKLLKEKGENDK HHHHHHHHHHCCCHH	68.75	14212463
543	Acetylation	KEKLLKEKGENDKSL HHHHHHHHCCCHHHH	70.68	19273602
544	Ubiquitination	EKLLKEKGENDKSLH HHHHHHHCCCHHHHH	39.78	29967540
548	Ubiquitination	KEKGENDKSLHLLKK HHHCCCHHHHHHHHH	67.51	29967540
548	Acetylation	KEKGENDKSLHLLKK HHHCCCHHHHHHHHH	67.51	19273602
549	Phosphorylation	EKGENDKSLHLLKKQ HHCCCHHHHHHHHHH	24.72	24719451
551	Ubiquitination	GENDKSLHLLKKQLS CCCHHHHHHHHHHHH	35.89	29967540
554	Acetylation	DKSLHLLKKQLSTLY HHHHHHHHHHHHHHH	44.85	19273602
554	Ubiquitination	DKSLHLLKKQLSTLY HHHHHHHHHHHHHHH	44.85	29967540
555	Acetylation	KSLHLLKKQLSTLYL HHHHHHHHHHHHHHH	57.34	19273602
558	Ubiquitination	HLLKKQLSTLYLEVF HHHHHHHHHHHHHHH	17.55	29967540
558	Phosphorylation	HLLKKQLSTLYLEVF HHHHHHHHHHHHHHH	17.55	19668370
559	Phosphorylation	LLKKQLSTLYLEVFS HHHHHHHHHHHHHHH	28.19	19668370
561	Phosphorylation	KKQLSTLYLEVFSML HHHHHHHHHHHHHHH	10.82	29759185
569	N-linked_Glycosylation	LEVFSMLRDEDGKPY HHHHHHHCCCCCCCC	36.31	31398338
574	Ubiquitination	MLRDEDGKPYSPSEY HHCCCCCCCCCCHHC	53.77	29967540
574	N-linked_Glycosylation	MLRDEDGKPYSPSEY HHCCCCCCCCCCHHC	53.77	31398338
576	Phosphorylation	RDEDGKPYSPSEYSL CCCCCCCCCCHHCCE	36.38	21690096
577	Phosphorylation	DEDGKPYSPSEYSLQ CCCCCCCCCHHCCEE	30.40	19668370
596	Acetylation	GNVFLVPKSKKPDVK CCEEEEECCCCCCCC	68.38	21196497
599	Acetylation	FLVPKSKKPDVKKN- EEEECCCCCCCCCC-	54.24	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	PKC_GROUP	-	PhosphoELM
40	S	Phosphorylation	Kinase	PKC	-	Uniprot
40	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
40	S	Phosphorylation	Kinase	PKCZ	Q05513	PSP
40	S	Phosphorylation	Kinase	PKCI	P41743	PSP
344	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
347	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
374	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
395	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
408	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
433	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
433	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
439	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
576	Y	Phosphorylation	Kinase	FYN	P06241	PSP
576	Y	Phosphorylation	Kinase	FGR	P09769	PSP
576	Y	Phosphorylation	Kinase	SRC	P12931	PSP
576	Y	Phosphorylation	Kinase	YES	P07947	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	KEAP1	Q14145	PMID:14585973
-	K	Ubiquitination	E3 ubiquitin ligase	RBX1	P62877	PMID:23274085

Functions of PTM Sites

Modified Location	Modified Residue	Modification	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.
596	K	Acetylation	21196497
Acetylation at Lys-596 and Lys-599 increases nuclear localization whereas deacetylation by SIRT1 enhances cytoplasmic presence.
599	K	Acetylation	21196497
Acetylation at Lys-596 and Lys-599 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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of NF2L2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBP_HUMAN	CREBBP	physical	11683914
KEAP1_MOUSE	Keap1	physical	9887101
KEAP1_MOUSE	Keap1	genetic	9887101
KEAP1_HUMAN	KEAP1	physical	17462537
TIF1A_HUMAN	TRIM24	physical	20211142
KEAP1_HUMAN	KEAP1	physical	15601839
CUL3_HUMAN	CUL3	physical	15367669
NCOR2_HUMAN	NCOR2	physical	15870285
CBP_HUMAN	CREBBP	physical	18241676
TYY1_HUMAN	YY1	physical	20309604
MYC_HUMAN	MYC	physical	20232342
BACH1_HUMAN	BACH1	physical	15734732
KPCD_HUMAN	PRKCD	physical	19920073
KEAP1_HUMAN	KEAP1	physical	19920073
CBP_HUMAN	CREBBP	physical	19273602
G45IP_HUMAN	GADD45GIP1	physical	20427290
KEAP1_HUMAN	KEAP1	physical	20463144
PGAM5_HUMAN	PGAM5	physical	18387606
KEAP1_HUMAN	KEAP1	physical	18387606
KEAP1_HUMAN	KEAP1	physical	20484052
KEAP1_HUMAN	KEAP1	physical	16888629
KEAP1_HUMAN	KEAP1	physical	12145307
ENC1_HUMAN	ENC1	physical	17875699
ENC1_HUMAN	ENC1	physical	18981988
KEAP1_HUMAN	KEAP1	physical	18981988
MAFG_HUMAN	MAFG	physical	22942279
MYC_HUMAN	MYC	physical	22942279
PPARG_MOUSE	Pparg	physical	10930400
SUMO1_HUMAN	SUMO1	physical	23543742
SUMO2_HUMAN	SUMO2	physical	23543742
SIAH2_HUMAN	SIAH2	physical	23645672
NFE2_HUMAN	NFE2	physical	23661758
MAFG_HUMAN	MAFG	physical	23661758
ATF4_HUMAN	ATF4	physical	23661758
ENC1_HUMAN	ENC1	physical	20511222
AHR_HUMAN	AHR	physical	20395535
RBMX_HUMAN	RBMX	physical	21988832
KEAP1_HUMAN	KEAP1	physical	23986495
BRCA1_HUMAN	BRCA1	physical	23857982
KEAP1_HUMAN	KEAP1	physical	23857982
AKT1_HUMAN	AKT1	physical	24704364
MK08_HUMAN	MAPK8	physical	24704364
MK09_HUMAN	MAPK9	physical	24704364
MP2K1_HUMAN	MAP2K1	physical	24704364
MP2K2_HUMAN	MAP2K2	physical	24704364
KEAP1_HUMAN	KEAP1	physical	24704364
KEAP1_HUMAN	KEAP1	physical	22448038
MK07_HUMAN	MAPK7	physical	23043106
HDAC1_HUMAN	HDAC1	physical	22308472
HDAC2_HUMAN	HDAC2	physical	22308472
HDAC3_HUMAN	HDAC3	physical	22308472
TNNT1_HUMAN	TNNT1	physical	25416956
WAC_HUMAN	WAC	physical	25416956
TCF20_HUMAN	TCF20	physical	24416372
UBC_HUMAN	UBC	physical	25742418
TIF1B_HUMAN	TRIM28	physical	25995248
KEAP1_HUMAN	KEAP1	physical	25628777
KEAP1_HUMAN	KEAP1	physical	26536456
JUN_HUMAN	JUN	physical	20194533
CADH1_HUMAN	CDH1	physical	22302998
KEAP1_HUMAN	KEAP1	physical	22302998
KEAP1_HUMAN	KEAP1	physical	27212020
PAQR3_HUMAN	PAQR3	physical	27212020
KEAP1_HUMAN	KEAP1	physical	22331464
KEAP1_HUMAN	KEAP1	physical	28638054
KEAP1_HUMAN	KEAP1	physical	28533375
KEAP1_HUMAN	KEAP1	physical	28939422

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 NF2L2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Acetylation-deacetylation of the transcription factor Nrf2 (nuclearfactor erythroid 2-related factor 2) regulates its transcriptionalactivity and nucleocytoplasmic localization."; Kawai Y., Garduno L., Theodore M., Yang J., Arinze I.J.; J. Biol. Chem. 286:7629-7640(2011). Cited for: ACETYLATION AT LYS-596 AND LYS-599, DEACETYLATION BY SIRT1, ANDSUBCELLULAR LOCATION.	21196497 [Abstract]

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