KMT5B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KMT5B_HUMAN
• UniProt AC: Q4FZB7
• Protein Name: Histone-lysine N-methyltransferase KMT5B {ECO:0000305}
• Gene Name: KMT5B {ECO:0000312|HGNC:HGNC:24283}
• Organism: Homo sapiens (Human).
• Sequence Length: 885
• Subcellular Localization: Nucleus . Chromosome. Associated with pericentric heterochromatin. CBX1 and CBX5 are required for the localization to pericentric heterochromatin (By similarity)..
• Protein Description: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes, such as EID3..
• Protein Sequence: MKWLGESKIMVVNGRRNGGKLSNDHQQNQSKLQHTGKDTLKAGKNAVERRSNRCNGNSGFEGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHFSKSDSFSHNNPVRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKEHVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEENMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGAFKSRVGLPAPAPVINSKYGLRETDKRLNRLKKLGDSSKNSDSQSVSSNTDADTTQEKNNATSNRKSSVGVKKNSKSRTLTRQSMSRIPASSNSTSSKLTHINNSRVPKKLKKPAKPLLSKIKLRNHCKRLEQKNASRKLEMGNLVLKEPKVVLYKNLPIKKDKEPEGPAQAAVASGCLTRHAAREHRQNPVRGAHSQGESSPCTYITRRSVRTRTNLKEASDIKLEPNTLNGYKSSVTEPCPDSGEQLQPAPVLQEEELAHETAQKGEAKCHKSDTGMSKKKSRQGKLVKQFAKIEESTPVHDSPGKDDAVPDLMGPHSDQGEHSGTVGVPVSYTDCAPSPVGCSVVTSDSFKTKDSFRTAKSKKKRRITRYDAQLILENNSGIPKLTLRRRHDSSSKTNDQENDGMNSSKISIKLSKDHDNDNNLYVAKLNNGFNSGSGSSSTKLKIQLKRDEENRGSYTEGLHENGVCCSDPLSLLESRMEVDDYSQYEEESTDDSSSSEGDEEEDDYDDDFEDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA

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
20	Acetylation	NGRRNGGKLSNDHQQ ECCCCCCCCCCHHHH		23749302
37	Acetylation	SKLQHTGKDTLKAGK HHHHHHCHHHHHHCH		23749302
69	Phosphorylation	GQSRYVPSSGMSAKE CCCCCCCCCCCCHHH		27251275
70	Phosphorylation	QSRYVPSSGMSAKEL CCCCCCCCCCCHHHH		27251275
73	Phosphorylation	YVPSSGMSAKELCEN CCCCCCCCHHHHHCC		27251275
102	Phosphorylation	FQTHKMNTSAFPSRS CCCCCCCCCCCCCCC		20068231
103	Phosphorylation	QTHKMNTSAFPSRSS CCCCCCCCCCCCCCC		20068231
107	Phosphorylation	MNTSAFPSRSSRHFS CCCCCCCCCCCCCCC		20068231
109	Phosphorylation	TSAFPSRSSRHFSKS CCCCCCCCCCCCCCC		20068231
110	Phosphorylation	SAFPSRSSRHFSKSD CCCCCCCCCCCCCCC		20068231
116	Phosphorylation	SSRHFSKSDSFSHNN CCCCCCCCCCCCCCC		27732954
118	Phosphorylation	RHFSKSDSFSHNNPV CCCCCCCCCCCCCCC		27732954
120	Phosphorylation	FSKSDSFSHNNPVRF CCCCCCCCCCCCCCC		30177828
170	Ubiquitination	ARHYFLNKNKMQEKL HHHHHCCCHHHHHHH		-
292	Ubiquitination	GRDTACVKALRDIEP CCCHHHHHHHHCCCC		-
307	Phosphorylation	GEEISCYYGDGFFGE CCEEEEEECCCCCCC		22817900
322	Phosphorylation	NNEFCECYTCERRGT CCCEEEEEEECCCCC		22817900
329	Phosphorylation	YTCERRGTGAFKSRV EEECCCCCCCCCCCC		-
334	Phosphorylation	RGTGAFKSRVGLPAP CCCCCCCCCCCCCCC		-
348	Acetylation	PAPVINSKYGLRETD CCCCCCCCCCCHHHH		25953088
373	Phosphorylation	DSSKNSDSQSVSSNT CCCCCCCCCCCCCCC		30177828
375	Phosphorylation	SKNSDSQSVSSNTDA CCCCCCCCCCCCCCC		28985074
377	Phosphorylation	NSDSQSVSSNTDADT CCCCCCCCCCCCCCC		30177828
378	Phosphorylation	SDSQSVSSNTDADTT CCCCCCCCCCCCCCH		23312004
380	Phosphorylation	SQSVSSNTDADTTQE CCCCCCCCCCCCHHH		23312004
380 (in isoform 2)	Phosphorylation	-		29507054
384	Phosphorylation	SSNTDADTTQEKNNA CCCCCCCCHHHHHCC		23312004
397	Phosphorylation	NATSNRKSSVGVKKN CCCCCCCCCCCCCCC		-
407	Phosphorylation	GVKKNSKSRTLTRQS CCCCCCCCCCCCHHH		-
407	O-linked_Glycosylation	GVKKNSKSRTLTRQS CCCCCCCCCCCCHHH		30379171
428	Acetylation	SSNSTSSKLTHINNS CCCCCCCCCCCCCCC		25953088
435	Phosphorylation	KLTHINNSRVPKKLK CCCCCCCCCCCCCCC		28348404
451	Acetylation	PAKPLLSKIKLRNHC CCHHHHHHHHHHHHH		7428783
467	Phosphorylation	RLEQKNASRKLEMGN HHHHHCCCCHHHHCC		23532336
527	Phosphorylation	NPVRGAHSQGESSPC CCCCCCCCCCCCCCC		28450419
531	Phosphorylation	GAHSQGESSPCTYIT CCCCCCCCCCCCEEE		25849741
532	Phosphorylation	AHSQGESSPCTYITR CCCCCCCCCCCEEEC		25849741
535	Phosphorylation	QGESSPCTYITRRSV CCCCCCCCEEECCCC		27732954
536	Phosphorylation	GESSPCTYITRRSVR CCCCCCCEEECCCCC		28450419
538	Phosphorylation	SSPCTYITRRSVRTR CCCCCEEECCCCCCC		27732954
544	Phosphorylation	ITRRSVRTRTNLKEA EECCCCCCCCCCCHH		-
555	Sumoylation	LKEASDIKLEPNTLN CCHHHCCCCCCCCCC		-
555	Sumoylation	LKEASDIKLEPNTLN CCHHHCCCCCCCCCC		28112733
630	Phosphorylation	FAKIEESTPVHDSPG HHHHHHCCCCCCCCC		21815630
635	Phosphorylation	ESTPVHDSPGKDDAV HCCCCCCCCCCCCCC		25849741
726	Phosphorylation	TLRRRHDSSSKTNDQ EEEECCCCCCCCCCC		22817900
728	Phosphorylation	RRRHDSSSKTNDQEN EECCCCCCCCCCCCC		24719451
761	Ubiquitination	DNNLYVAKLNNGFNS CCCEEEEEECCCCCC		-
776	Acetylation	GSGSSSTKLKIQLKR CCCCCCCCEEEEEEC		25953088
791	Phosphorylation	DEENRGSYTEGLHEN CHHHCCCCCCCCHHC		-
792	Phosphorylation	EENRGSYTEGLHENG HHHCCCCCCCCHHCC		-

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

Oops, there are no upstream regulatory protein records of KMT5B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KMT5B_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of KMT5B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESR1_HUMAN	ESR1	physical	24101509
KMT5B_HUMAN	SUV420H1	physical	24101509

Drug and Disease Associations

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