KMT2E_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KMT2E_MOUSE
• UniProt AC: Q3UG20
• Protein Name: Inactive histone-lysine N-methyltransferase 2E {ECO:0000305}
• Gene Name: Kmt2e
• Organism: Mus musculus (Mouse).
• Sequence Length: 1868
• Subcellular Localization: Chromosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleus speckle . Absent from the nucleolus. Localizes to chromosome during interphase and to centrosomes during mitosis. Dissociation from mitotic chromosome is likely
• Protein Description: Associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription (By similarity). Chromatin interaction is mediated via the binding to tri-methylated histone H3 at 'Lys-4' (H3K4me3) (By similarity). Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation. [PubMed: 18854576]
• Protein Sequence: MSIAIPLGVDTTETSYLEMAAGSEPESVEASPVVVEKSNSFPHQLYTSSSHHSHSYIGLPYADHNYGARPPPTPPASPPPSGLISKNEVGIFTTPNFDETSSATTISTSEDGSYGTDVTRCICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERCQPRSLDKERAVLLQRRKRENMSDGDTSATESGDEVPVELYTAFQHTPTSITLTASRVPKVTDKRRKKSGEKEQNFSKCKKAFREGSRKSSRVKGSAPEIDPSSDSSNFVWETKIKAWMDRYEEANNNQYSEGVQREAQRLAQRLGSGNDSKDMNKSELSTNNSLFRPPVESHIQKNKKILKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRHEIEEGTIHLYIYSIQSIPKGTEITIAFDFDYGNCKYKVDCACLKENPECPVLKRSSESTENINSGYETRRKKGKKEKDTSKEKDIQNQNMTLDCEGTNNKIRSPETKQRKLSPLRLSVSNNQEPDFIDDMEEKTPISNEVEMESEEQIAERKRKMTREERKMEAILQAFARLEKREKRREQALERISTAKTEVKPECKESQVIADAEVVQEQVKEETAIKPAAAKVNRTKQRKSFSRSRTHIGQQRRRHRTVSMCSDIPPSSPDIEVLSQQNEIENTVLAIEPETETAVAEIIPEAEVPALNKCPTKYPKTKKHLVNEWLSEKNEKTGKPSDSLSERPLRITTDPEVLATQLNSLPGLTYSPHVYSTPKHYIRFTSPFLSEKKRRKETTENISGSCKKRWLKQALEEENSTILHRYHSPCQERSRSPTVNGENKSPLLLSDSCSLPDLTTPLKKRRLYQLLDTAYSESSTPTPSPYATPTHTDITPTDPAFATPPRIKSDDETYRNGYKPIYSPVTPVTPGTPGNTMHFENISSPESSPEIKRCTYNQEGYDRPSNMLTLGPFRNSNLTELGLQEIKTIGYTSPRSRTEVNRPCPGEKESVSDLQLGLDAVEPAALQKSMETPAHDRTEPSNQLDSTHSGRGTMYSSWVKSPDRTGVNFSVNSNLRDLTPSHQLETGGGFRVSESKCLIQQDDTRGMFLGAAVFCTSEDGLASGFGRTVNDNLIDGSCTPQNPPQKKKVSLLEYRKRQREARKSGSKPENFALISVSPHPSGSLSSSGDGCVHSSENGEQAENQASLPLPPPAAAAAATAAAAYSASSEEGSSNCPVKDANSSEKKDPEVQWTASTSVEQVRERSYQRALLLSDHRKDKDSGGESPCVSCSPSHVQSPPSSHSNHIPQVHAQSLAPSLSELMADPDAEGTEATSTSECPSPDTSQSPSKTSKPGSPGPINPAQSHGKILTKPDSHWEATATVSEADNSVHQNPEPQHRQLSSNTPALSQNHAPQAHALSANDQLPQKLPSAPTKLHCPPSPHTENPPKSSTPHTPVQHGYLSPKPPSQHLGSPFRPHHSQSPQVGTPQRETQRNFYAAAQNLQANPQQATSGALFTQTPSGQSSATYSQFNQQSLNSTAPPPPPPPPPSSYYQNQQPSANFQNYNQLKGSLSQQTVFTSGPNQALPGSTSQQSVPGHHVTPGHFLPSQNPTIHHQPAAAAVVPPPPPPPPAPGPHLIQQPSSHQQHSVAHGVGPVHAVTPGSHIHSQTAGHHLPPPPPPPGPAPHHHPPPHPTTGLQSLQAQHQHVVNSAPPPPPPPPPPPPASVLVSGHHSASGQALHHPPHQGPPLFPASAHPAVPPYPSQATHHTTLGPGPQHQPSGTGPHCPLPVAGPHLQPQGPNSIPTPTASGFCPHPHPGSVALPHGVQGPQQASPVPAQIPIHRAQVPPTFQNNYHGSGWH

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
31	Phosphorylation	EPESVEASPVVVEKS CCCCCCCCCEEEECC		25338131
230	Ubiquitination	VTDKRRKKSGEKEQN CCCHHHHCCCHHHHC		-
334	Phosphorylation	LFRPPVESHIQKNKK CCCCCHHHHHHHCHH		20531401
429	Phosphorylation	EEGTIHLYIYSIQSI CCCEEEEEEEEEECC		24719451
432	Phosphorylation	TIHLYIYSIQSIPKG EEEEEEEEEECCCCC		24719451
435	O-linked_Glycosylation	LYIYSIQSIPKGTEI EEEEEEECCCCCCEE		-
435	Phosphorylation	LYIYSIQSIPKGTEI EEEEEEECCCCCCEE		24719451
440	O-linked_Glycosylation	IQSIPKGTEITIAFD EECCCCCCEEEEEEE		-
443	Phosphorylation	IPKGTEITIAFDFDY CCCCCEEEEEEECCC		25338131
485	Phosphorylation	TENINSGYETRRKKG CCCCHHHHHHHHHCC		-
487	Phosphorylation	NINSGYETRRKKGKK CCHHHHHHHHHCCCC		-
522	Phosphorylation	GTNNKIRSPETKQRK CCCCCCCCHHHHCCC		28066266
531	Phosphorylation	ETKQRKLSPLRLSVS HHHCCCCCCCEEECC		27555448
536	Phosphorylation	KLSPLRLSVSNNQEP CCCCCEEECCCCCCC		25338131
538	Phosphorylation	SPLRLSVSNNQEPDF CCCEEECCCCCCCCC		29899451
653	Phosphorylation	NRTKQRKSFSRSRTH CHHHHCCCCCCCCCH		23737553
655	Phosphorylation	TKQRKSFSRSRTHIG HHHCCCCCCCCCHHH		23737553
656	Methylation	KQRKSFSRSRTHIGQ HHCCCCCCCCCHHHH		18967007
657	Phosphorylation	QRKSFSRSRTHIGQQ HCCCCCCCCCHHHHH		23737553
795	Phosphorylation	KHYIRFTSPFLSEKK CHHHEECCHHCCHHH		28066266
799	Phosphorylation	RFTSPFLSEKKRRKE EECCHHCCHHHCCHH		28066266
837	Phosphorylation	TILHRYHSPCQERSR CHHHHCCCCCCCCCC		23684622
843	Phosphorylation	HSPCQERSRSPTVNG CCCCCCCCCCCCCCC		27087446
845	Phosphorylation	PCQERSRSPTVNGEN CCCCCCCCCCCCCCC		21659605
847	Phosphorylation	QERSRSPTVNGENKS CCCCCCCCCCCCCCC		19060867
854	Phosphorylation	TVNGENKSPLLLSDS CCCCCCCCCEEECCC		30352176
869	Phosphorylation	CSLPDLTTPLKKRRL CCCCCCCCHHHHHHH		-
912	Phosphorylation	PTDPAFATPPRIKSD CCCCCCCCCCCCCCC		-
997	Phosphorylation	LGLQEIKTIGYTSPR HHCEEEECCCCCCCC		24759943
1000	Phosphorylation	QEIKTIGYTSPRSRT EEEECCCCCCCCCCC		24759943
1001	Phosphorylation	EIKTIGYTSPRSRTE EEECCCCCCCCCCCC		29472430
1002	Phosphorylation	IKTIGYTSPRSRTEV EECCCCCCCCCCCCC		24453211
1019	Phosphorylation	PCPGEKESVSDLQLG CCCCCCCCHHHHHHC		25293948
1021	Phosphorylation	PGEKESVSDLQLGLD CCCCCCHHHHHHCCC		25293948
1055	Phosphorylation	EPSNQLDSTHSGRGT CCCCCCCCCCCCCCC		21183079
1058	Phosphorylation	NQLDSTHSGRGTMYS CCCCCCCCCCCCEEE		21183079
1070	Phosphorylation	MYSSWVKSPDRTGVN EEEEEECCCCCCCCC		25266776
1074	Phosphorylation	WVKSPDRTGVNFSVN EECCCCCCCCCEEEC		26824392
1088	Phosphorylation	NSNLRDLTPSHQLET CCCCCCCCCCCCCCC		28066266
1090	Phosphorylation	NLRDLTPSHQLETGG CCCCCCCCCCCCCCC		28066266
1282	Phosphorylation	YQRALLLSDHRKDKD HHHHHHHHCCCCCCC		25338131
1359	Phosphorylation	TSQSPSKTSKPGSPG CCCCCCCCCCCCCCC		25619855
1360	Phosphorylation	SQSPSKTSKPGSPGP CCCCCCCCCCCCCCC		25619855
1364	Phosphorylation	SKTSKPGSPGPINPA CCCCCCCCCCCCCHH		26824392
1449	Phosphorylation	TKLHCPPSPHTENPP CCCCCCCCCCCCCCC		25266776
1452	Phosphorylation	HCPPSPHTENPPKSS CCCCCCCCCCCCCCC		26643407

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of KMT2E_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
435	S	Glycosylation	O-glycosylated at Ser-435 and Thr-440 in the SET domain by OGT which probably prevents KMT2E proteosomal-mediated degradation.	-
440	T	Glycosylation	O-glycosylated at Ser-435 and Thr-440 in the SET domain by OGT which probably prevents KMT2E proteosomal-mediated degradation.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of KMT2E_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P53_MOUSE	Trp53	physical	21423215

Drug and Disease Associations

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