dbPTM

EZH2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EZH2_MOUSE
UniProt AC	Q61188
Protein Name	Histone-lysine N-methyltransferase EZH2 {ECO:0000305}
Gene Name	Ezh2 {ECO:0000312\|MGI:MGI:107940}
Organism	Mus musculus (Mouse).
Sequence Length	746
Subcellular Localization	Nucleus. Chromosome. Localizes to the inactive X chromosome in trophoblast stem cells.
Protein Description	Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2. Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXA7, HOXB6 and HOXC8. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-ARNTL/BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription..
Protein Sequence	MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKTMFSSNRQKILERTETLNQEWKQRRIQPVHIMTSVSSLRGTRECSVTSDLDFPAQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPDEREEKQKDLEDNRDDKETCPPRKFPADKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTISVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPVPTEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Phosphorylation	CWRKRVKSEYMRLRQ CCHHHHHHHHHHHHH	30.97	-
55	Phosphorylation	KILERTETLNQEWKQ HHHHHHHHHCHHHHH	30.32	29514104
75	O-linked_Glycosylation	VHIMTSVSSLRGTRE EEEEEEHHHCCCCCE	24.34	-
76	Phosphorylation	HIMTSVSSLRGTREC EEEEEHHHCCCCCEE	21.67	-
228	Phosphorylation	DKIFEAISSMFPDKG HHHHHHHHHHCCCCC	23.85	29895711
302	Phosphorylation	FLHPFHATPNTYKRK CCCCCCCCCCCCCCC	14.43	26745281
305	Phosphorylation	PFHATPNTYKRKNTE CCCCCCCCCCCCCCC	31.46	26745281
306	Phosphorylation	FHATPNTYKRKNTET CCCCCCCCCCCCCCC	18.55	26745281
309	Acetylation	TPNTYKRKNTETALD CCCCCCCCCCCCHHC	65.16	2415355
339	Phosphorylation	KEFAAALTAERIKTP HHHHHHHHHHHCCCC	23.03	21123648
345	Phosphorylation	LTAERIKTPPKRPGG HHHHHCCCCCCCCCC	42.31	25159016
362	Phosphorylation	RGRLPNNSSRPSTPT CCCCCCCCCCCCCCE	34.07	21082442
363	Phosphorylation	GRLPNNSSRPSTPTI CCCCCCCCCCCCCEE	50.78	21082442
366	Phosphorylation	PNNSSRPSTPTISVL CCCCCCCCCCEEEEE	46.00	27087446
367	Phosphorylation	NNSSRPSTPTISVLE CCCCCCCCCEEEEEE	27.43	27087446
369	Phosphorylation	SSRPSTPTISVLESK CCCCCCCEEEEEEEC	26.44	21149613
371	Phosphorylation	RPSTPTISVLESKDT CCCCCEEEEEEECCC	24.11	25266776
375	Phosphorylation	PTISVLESKDTDSDR CEEEEEEECCCCCCC	31.50	26160508
378	Phosphorylation	SVLESKDTDSDREAG EEEEECCCCCCCCCC	40.93	27087446
380	Phosphorylation	LESKDTDSDREAGTE EEECCCCCCCCCCCC	40.43	28418008
386	Phosphorylation	DSDREAGTETGGENN CCCCCCCCCCCCCCC	37.10	29550500
388	Phosphorylation	DREAGTETGGENNDK CCCCCCCCCCCCCCH	50.77	23375375
404	Phosphorylation	EEEKKDETSSSSEAN HHHHHCCCCCHHHHH	44.00	23375375
405	Phosphorylation	EEKKDETSSSSEANS HHHHCCCCCHHHHHH	26.61	23375375
406	Phosphorylation	EKKDETSSSSEANSR HHHCCCCCHHHHHHH	45.35	23375375
407	Phosphorylation	KKDETSSSSEANSRC HHCCCCCHHHHHHHC	31.78	23375375
408	Phosphorylation	KDETSSSSEANSRCQ HCCCCCHHHHHHHCC	42.55	29550500
412	Phosphorylation	SSSSEANSRCQTPIK CCHHHHHHHCCCCCC	41.29	26643407
416	Phosphorylation	EANSRCQTPIKMKPN HHHHHCCCCCCCCCC	30.52	24453211
474	Phosphorylation	YEFRVKESSIIAPVP EEEEECCCCEEECCC	22.56	25619855
482	Phosphorylation	SIIAPVPTEDVDTPP CEEECCCCCCCCCCC	45.08	26824392
487	Phosphorylation	VPTEDVDTPPRKKKR CCCCCCCCCCCCHHH	34.73	26824392
568	Phosphorylation	RCKAQCNTKQCPCYL EEECCCCCCCCCEEE	30.07	-

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
21	S	Phosphorylation	Kinase	AKT1	P31750	Uniprot
345	T	Phosphorylation	Kinase	CDK1	P06493	PSP
345	T	Phosphorylation	Kinase	CDK1	P11440	Uniprot
345	T	Phosphorylation	Kinase	CDK2	P97377	Uniprot
416	T	Phosphorylation	Kinase	CDK2	P24941	PSP
487	T	Phosphorylation	Kinase	CDK1	P06493	PSP
696	Y	Phosphorylation	Kinase	SRC	P05480	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
75	S	Glycosylation	-
Glycosylated: O-GlcNAcylation at Ser-75 by OGT increases stability of EZH2 and facilitates the formation of H3K27me3 by the PRC2/EED-EZH2 complex.
345	T	Phosphorylation	-
Phosphorylation at Thr-345 by CDK1 and CDK2 promotes maintenance of H3K27me3 levels at EZH2-target loci, thus leading to epigenetic gene silencing (By similarity).

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 EZH2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SUZ12_MOUSE	Suz12	physical	20123894
RBBP4_MOUSE	Rbbp4	physical	20123894
MTF2_MOUSE	Mtf2	physical	20123894
JARD2_MOUSE	Jarid2	physical	20123894
AEBP2_MOUSE	Aebp2	physical	20123894
PHF1_MOUSE	Phf1	physical	20123894
JARD2_MOUSE	Jarid2	physical	20064375
EED_MOUSE	Eed	physical	20064375
CITE4_MOUSE	Cited4	physical	20211142
EED_MOUSE	Eed	physical	20064376
SUZ12_MOUSE	Suz12	physical	20064376
RBBP4_MOUSE	Rbbp4	physical	20064376
AEBP2_MOUSE	Aebp2	physical	20064376
JARD2_MOUSE	Jarid2	physical	20064376
MTF2_MOUSE	Mtf2	physical	20064376
STK38_MOUSE	Stk38	physical	20064376
RBBP7_MOUSE	Rbbp7	physical	20064376
SETX_MOUSE	Setx	physical	20064376
TRI35_MOUSE	Trim35	physical	20064376
CLOCK_MOUSE	Clock	physical	16717091
BMAL1_MOUSE	Arntl	physical	16717091
CRY1_MOUSE	Cry1	physical	16717091
RBL2_MOUSE	Rbl2	physical	15077161
H31T_HUMAN	HIST3H3	physical	22619169
MYOD1_MOUSE	Myod1	physical	22333916
RPB1_MOUSE	Polr2a	physical	22305566
TLE1_MOUSE	Tle1	physical	22439931
HDAC1_MOUSE	Hdac1	physical	22439931
EED_MOUSE	Eed	physical	22094255
DNMT1_MOUSE	Dnmt1	physical	22094255
SUZ12_MOUSE	Suz12	physical	24040135
SUZ12_MOUSE	Suz12	physical	23624935
EED_MOUSE	Eed	physical	23624935
BRCA1_MOUSE	Brca1	physical	23624935
EED_MOUSE	Eed	physical	24457600
MDM2_MOUSE	Mdm2	physical	26748827
PJA1_MOUSE	Pja1	physical	28067271
RBBP4_MOUSE	Rbbp4	physical	25680957
SUZ12_MOUSE	Suz12	physical	25680957
EZH2_MOUSE	Ezh2	physical	25680957
ODB2_MOUSE	Dbt	physical	25680957
EPOP_MOUSE	E130012A19Rik	physical	25680957
EZH1_MOUSE	Ezh1	physical	25680957
EED_MOUSE	Eed	physical	25680957
MTF2_MOUSE	Mtf2	physical	25680957
RBBP7_MOUSE	Rbbp7	physical	25680957
JARD2_MOUSE	Jarid2	physical	25680957
AEBP2_MOUSE	Aebp2	physical	25680957
DDX27_MOUSE	Ddx27	physical	25680957
NOC3L_MOUSE	Noc3l	physical	25680957
WIZ_MOUSE	Wiz	physical	25680957
ODBB_MOUSE	Bckdhb	physical	25680957
EHMT1_MOUSE	Ehmt1	physical	25680957
EHMT2_MOUSE	Ehmt2	physical	25680957
Z518A_MOUSE	Zfp518a	physical	25680957
LCOR_MOUSE	Lcor	physical	25680957
VANG1_MOUSE	Vangl1	physical	25680957
CBX5_MOUSE	Cbx5	physical	25680957
H10_MOUSE	H1f0	physical	25680957
H1T_MOUSE	Hist1h1t	physical	25680957
MY18A_MOUSE	Myo18a	physical	25680957
HMMR_MOUSE	Hmmr	physical	25680957
ARVC_MOUSE	Arvcf	physical	25680957

Drug and Disease Associations

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

Regulatory Network of EZH2_MOUSE

Related Literatures of Post-Translational Modification

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