ELL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ELL_MOUSE
• UniProt AC: O08856
• Protein Name: RNA polymerase II elongation factor ELL
• Gene Name: Ell
• Organism: Mus musculus (Mouse).
• Sequence Length: 602
• Subcellular Localization: Nucleus . Nucleus speckle . Nucleus, Cajal body . Colocalizes with EAF2 to nuclear speckles. Colocalizes with coilin in subnuclear cajal and histone locus bodies. Translocates in the LEC complex to cajal and histone locus bodies at snRNA genes in a I
• Protein Description: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription. ELL also plays an early role before its assembly into in the SEC complex by stabilizing RNA polymerase II recruitment/initiation and entry into the pause site. Required to stabilize the pre-initiation complex and early elongation. Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription (By similarity). Elongation factor component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. [PubMed: 22195968]
• Protein Sequence: MAALKEARSYGLSCGRVSDGSRVSVFHVKLTDSALKAFESYRAHQDSVSLRPSIRFEGSQGHISIPQPDCPEEVRAFSFYLSNIGRDSPQGSFDCIQQYVSSYGDVHLDCLGSIQDKVTVCATDDSYQKARQSMAQAEEETRSRSAIVIKAGGRYMGKKVQFRKPAPGAADAVPSRKRATPINLASAIRKSSGSGASSVVQRPFRDRVLHLLALRPYRKAELLLRLQKDGLTQADKDTLDSLLQQVASVNPKDGTCTLQDCMYKSLQKDWPGYSEGDRQLLKRMLMRKLCQPQNATTDSSPPREHGRSASPSQKRPTDFIDPLASKKPRISHFTQRAQPTLNGKLGAPNGHETLLPAPGPTPSDTLSSSHLPPRLEPPRTHDPLADVSNDLGHSTQDYKHQEATPAPAPHLGLPLLTDFPQAEQPTSSSHTHSRPKKKSKKHKDKERPPEERPPAPQPDAPTAPALPPDAPGLNGACDNEPTSSSETPDYLLKYPAISSSEQRQSYKNDFNAEYSEYRSLHARIEQITRRFTQLDAQLRQLSQGSDEYETTRGQILQEYRKIKKTNTNYSCEKRRCEYLHRKLAHIKRLIAEYDQRQLQAWP

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
2	Acetylation	------MAALKEARS ------CHHHHHHHH	22.85	-
47	Phosphorylation	SYRAHQDSVSLRPSI HHHCCCCCCCCCCEE	13.67	30387612
49	Phosphorylation	RAHQDSVSLRPSIRF HCCCCCCCCCCEEEE	23.71	22802335
129	Ubiquitination	ATDDSYQKARQSMAQ CCCHHHHHHHHHHHH	36.99	22790023
133	Phosphorylation	SYQKARQSMAQAEEE HHHHHHHHHHHHHHH	15.55	20139300
150	Acetylation	SRSAIVIKAGGRYMG HCCEEEEEECCEECC	30.04	19858443
180	Phosphorylation	VPSRKRATPINLASA CCCCCCCCCCCHHHH	28.83	27600695
296	Phosphorylation	LCQPQNATTDSSPPR HCCCCCCCCCCCCCC	38.39	25619855
297	Phosphorylation	CQPQNATTDSSPPRE CCCCCCCCCCCCCCC	31.32	20469934
299	Phosphorylation	PQNATTDSSPPREHG CCCCCCCCCCCCCCC	42.52	26824392
300	Phosphorylation	QNATTDSSPPREHGR CCCCCCCCCCCCCCC	41.56	27087446
308	Phosphorylation	PPREHGRSASPSQKR CCCCCCCCCCCCCCC	37.38	27087446
310	Phosphorylation	REHGRSASPSQKRPT CCCCCCCCCCCCCCC	26.74	27087446
312	Phosphorylation	HGRSASPSQKRPTDF CCCCCCCCCCCCCCC	45.93	24453211
317	Phosphorylation	SPSQKRPTDFIDPLA CCCCCCCCCCCHHHH	47.80	24453211
528	Phosphorylation	HARIEQITRRFTQLD HHHHHHHHHHHHHHH	18.58	24719451
542	Phosphorylation	DAQLRQLSQGSDEYE HHHHHHHHCCCCCHH	24.94	30635358

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NS1BP_MOUSE	Ivns1abp	physical	20211142

Drug and Disease Associations

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