EHMT2_MOUSE - dbPTM
EHMT2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EHMT2_MOUSE
UniProt AC Q9Z148
Protein Name Histone-lysine N-methyltransferase EHMT2
Gene Name Ehmt2
Organism Mus musculus (Mouse).
Sequence Length 1263
Subcellular Localization Nucleus. Chromosome . Almost excluded form nucleoli. Associates with euchromatic regions. Does not associate with heterochromatin. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2 (By similarity). Interacts with CDYL. Interacts with REST
Protein Description Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself..
Protein Sequence MRGLPRGRGLMRARGRGRAAPTGGRGRGRGGAHRGRGRPRSLLSLPRAQASWAPQLPAGLTGPPVPCLPSQGEAPAEMGALLLEKEPRGAAERVHSSLGDTPQSEETLPKANPDSLEPAGPSSPASVTVTVGDEGADTPVGAASLIGDEPESLEGDGGRIVLGHATKSFPSSPSKGGACPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAATAGPEPSPATTAAQEGQPKVHRARKTMSKPSNGQPPIPEKRPPEVQHFRMSDDMHLGKVTSDVAKRRKLNSGSLSEDLGSAGGSGDIILEKGEPRPLEEWETVVGDDFSLYYDAYSVDERVDSDSKSEVEALAEQLSEEEEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRRKREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGFEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELLGCNAAILKRETMRPSSRVALMVLCEAHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDASEAQEVTIPRGDGGTPPIGTAAPALPPLAHDAPGRADTSQPSARMRGHGEPRRPPCDPLADTIDSSGPSLTLPNGGCLSAVGLPPGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQLGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIDVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNAQCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQLNRKLRLGVGNRAVRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRSCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLPDLSSLPPINT
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
40Asymmetric dimethylarginineHRGRGRPRSLLSLPR
CCCCCCCCCHHCCCH		38.28-
40MethylationHRGRGRPRSLLSLPR
CCCCCCCCCHHCCCH		38.2824129315
41PhosphorylationRGRGRPRSLLSLPRA
CCCCCCCCHHCCCHH		36.0221743459
44PhosphorylationGRPRSLLSLPRAQAS
CCCCCHHCCCHHHHC		41.4421743459
96PhosphorylationGAAERVHSSLGDTPQ
CHHHHHHHHCCCCCC		25.1326824392
97PhosphorylationAAERVHSSLGDTPQS
HHHHHHHHCCCCCCC		22.8428066266
101PhosphorylationVHSSLGDTPQSEETL
HHHHCCCCCCCCCCC		22.7926643407
104PhosphorylationSLGDTPQSEETLPKA
HCCCCCCCCCCCCCC		38.3126643407
107PhosphorylationDTPQSEETLPKANPD
CCCCCCCCCCCCCCC		44.2928066266
115PhosphorylationLPKANPDSLEPAGPS
CCCCCCCCCCCCCCC		35.5723649490
122PhosphorylationSLEPAGPSSPASVTV
CCCCCCCCCCCEEEE		48.3022006019
123PhosphorylationLEPAGPSSPASVTVT
CCCCCCCCCCEEEEE		27.8427087446
126PhosphorylationAGPSSPASVTVTVGD
CCCCCCCEEEEEECC		23.0021659605
128PhosphorylationPSSPASVTVTVGDEG
CCCCCEEEEEECCCC		14.1525293948
130PhosphorylationSPASVTVTVGDEGAD
CCCEEEEEECCCCCC		14.9225293948
138PhosphorylationVGDEGADTPVGAASL
ECCCCCCCCCCEEHH		21.2425293948
144PhosphorylationDTPVGAASLIGDEPE
CCCCCEEHHHCCCCC		21.7124453211
167"N6,N6-dimethyllysine"IVLGHATKSFPSSPS
EEEEEEECCCCCCCC		51.38-
167MethylationIVLGHATKSFPSSPS
EEEEEEECCCCCCCC		51.38-
171PhosphorylationHATKSFPSSPSKGGA
EEECCCCCCCCCCCC		53.5230635358
172PhosphorylationATKSFPSSPSKGGAC
EECCCCCCCCCCCCC		33.1726745281
174PhosphorylationKSFPSSPSKGGACPS
CCCCCCCCCCCCCCC		45.9730635358
186PhosphorylationCPSRAKMSMTGAGKS
CCCCCCCCCCCCCCC		16.7025159016
188PhosphorylationSRAKMSMTGAGKSPP
CCCCCCCCCCCCCCH		19.3025159016
193PhosphorylationSMTGAGKSPPSVQSL
CCCCCCCCCHHHHHH		40.9226824392
196PhosphorylationGAGKSPPSVQSLAMR
CCCCCCHHHHHHHHH		35.8521659605
199PhosphorylationKSPPSVQSLAMRLLS
CCCHHHHHHHHHHHC		18.8826643407
221PhosphorylationATAGPEPSPATTAAQ
CCCCCCCCCCCHHHH		26.0429514104
239"N6,N6,N6-trimethyllysine"PKVHRARKTMSKPSN
CCCCCCCCCCCCCCC		47.82-
239MethylationPKVHRARKTMSKPSN
CCCCCCCCCCCCCCC		47.82-
285PhosphorylationAKRRKLNSGSLSEDL
HHHCCCCCCCCCCCH		39.9527087446
287PhosphorylationRRKLNSGSLSEDLGS
HCCCCCCCCCCCHHC		28.6627087446
289PhosphorylationKLNSGSLSEDLGSAG
CCCCCCCCCCHHCCC		30.6622942356
294PhosphorylationSLSEDLGSAGGSGDI
CCCCCHHCCCCCCCE		30.9119060867
298PhosphorylationDLGSAGGSGDIILEK
CHHCCCCCCCEEEEC		32.1621183079
374 (in isoform 2)Phosphorylation-70.7129514104
375 (in isoform 2)Phosphorylation-74.2227566939
378 (in isoform 2)Phosphorylation-58.2929514104
403PhosphorylationKKKWRKDSPWVKPSR
HHHHHCCCCCCCCCH		24.5628066266
452PhosphorylationLELPSEGTLSPNHAG
CCCCCCCCCCCCCCC		21.7322668510
454PhosphorylationLPSEGTLSPNHAGVS
CCCCCCCCCCCCCCC		24.4029514104
461PhosphorylationSPNHAGVSNDTSSLE
CCCCCCCCCCCCCCC		28.2422006019
464PhosphorylationHAGVSNDTSSLETER
CCCCCCCCCCCCCCC		25.1924759943
465PhosphorylationAGVSNDTSSLETERG
CCCCCCCCCCCCCCC		35.4721743459
466PhosphorylationGVSNDTSSLETERGF
CCCCCCCCCCCCCCC		32.1121743459
469PhosphorylationNDTSSLETERGFEEL
CCCCCCCCCCCCCCC		35.9521743459
608PhosphorylationIPRGDGGTPPIGTAA
ECCCCCCCCCCCCCC		31.2725521595
613PhosphorylationGGTPPIGTAAPALPP
CCCCCCCCCCCCCCC		21.9925619855
635PhosphorylationRADTSQPSARMRGHG
CCCCCCCCHHHCCCC		22.37-
798PhosphorylationVQLGGCVYSKEEDGS
HHCCCCEEECCCCCC		20.36-
939PhosphorylationLRNKEGDTAWDLTPE
HCCCCCCCCCCCCCC		40.27-
1044PhosphorylationNCLCGQLSIRCWYDK
CCEECCEEEEEEECC		10.4922942356
1100UbiquitinationLQLYRTAKMGWGVRA
HHHHHHHCCCCCEEE		37.0122790023
1161PhosphorylationARYYGNISRFINHLC
CEEECCHHHHHHHHC		25.74-
1199PhosphorylationFSSRDIRTGEELGFD
EECCCCCCCCCCCCC		49.64-
1257PhosphorylationELLPDLSSLPPINT-
HHCCCHHHCCCCCC-		52.79-
1263PhosphorylationSSLPPINT-------
HHCCCCCC-------		40.48-
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
287SPhosphorylationKinaseMTORQ9JLN9
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
239KMethylation

-
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 EHMT2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H33_MOUSEH3f3aphysical
15939934
DNM3A_MOUSEDnmt3aphysical
18953337
DNM3B_MOUSEDnmt3bphysical
18953337
WIZ_MOUSEWizphysical
25680957
EHMT2_MOUSEEhmt2physical
25680957
EHMT1_MOUSEEhmt1physical
25680957
CWC15_MOUSECwc15physical
25680957
RBBP4_MOUSERbbp4physical
25680957
CBX5_MOUSECbx5physical
25680957
SUZ12_MOUSESuz12physical
25680957
Z518A_MOUSEZfp518aphysical
25680957
GLRX5_MOUSEGlrx5physical
25680957
CBX1_MOUSECbx1physical
25680957
UHRF1_MOUSEUhrf1physical
25680957
EED_MOUSEEedphysical
25680957
MTF2_MOUSEMtf2physical
25680957
EZH2_MOUSEEzh2physical
25680957
RTF2_MOUSERtfdc1physical
25680957
LN28A_MOUSELin28aphysical
25680957
CDYL_MOUSECdylphysical
25680957
EZH1_MOUSEEzh1physical
25680957
MK67I_MOUSENifkphysical
25680957
CSK21_MOUSECsnk2a1physical
25680957
POGZ_MOUSEPogzphysical
25680957
MBD3_MOUSEMbd3physical
25680957
CDYL2_MOUSECdyl2physical
25680957
MTA1_MOUSEMta1physical
25680957
CHAP1_MOUSEChamp1physical
25680957
LCOR_MOUSELcorphysical
25680957
MPP8_MOUSEMphosph8physical
25680957
MIER2_MOUSEMier2physical
25680957
MBTD1_MOUSEMbtd1physical
25680957
SUMF1_MOUSESumf1physical
25680957
DNMT1_MOUSEDnmt1physical
25680957
MCAF1_MOUSEAtf7ipphysical
25680957
I2BPL_MOUSEIrf2bplphysical
25680957
HIRP3_MOUSEHirip3physical
25680957
PALLD_MOUSEPalldphysical
25680957
DENR_MOUSEDenrphysical
25680957
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EHMT2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-608, AND MASSSPECTROMETRY.

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