FBRL_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FBRL_DROME
• UniProt AC: Q9W1V3
• Protein Name: rRNA 2'-O-methyltransferase fibrillarin
• Gene Name: Fib {ECO:0000312|EMBL:AAF46950.1}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 344
• Subcellular Localization: Nucleus, nucleolus. Fibrillar region of the nucleolus..
• Protein Description: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity)..
• Protein Sequence: MGKPGFSPRGGGGGGGGGGGGFRGRGGGGGGGGGGFGGGRGRGGGGDRGGRGGFGGGRGGGGRGGGGGGGRGAFGGRGGGGGRGGGGRGGGGRGGGGRGGGAGGFKGGKTVTIEPHRHEGVFIARGKEDALVTRNFVPGSEVYGEKRISVETNGEKIEYRVWNPFRSKLAAAVLGGVEQIHMPPGSKVLYLGAASGTTVSHVSDVVGPEGLVYAVEFSHRSGRDLINVAKKRTNIIPIIEDARHPHKYRMLVGMVDTIFADVAQPDQGRIVALNAQHFLKNGGHFVISIKASCIDSTAQPEAVFAAEVKKMQADKLKPQEQLTLEPYERDHAVVVGVYRPPPKQ

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
9	Methylation	GKPGFSPRGGGGGGG CCCCCCCCCCCCCCC	56.01	-
9	Asymmetric dimethylarginine	GKPGFSPRGGGGGGG CCCCCCCCCCCCCCC	56.01	-
23	Asymmetric dimethylarginine	GGGGGGFRGRGGGGG CCCCCCCCCCCCCCC	36.85	-
23	Methylation	GGGGGGFRGRGGGGG CCCCCCCCCCCCCCC	36.85	-
25	Methylation	GGGGFRGRGGGGGGG CCCCCCCCCCCCCCC	36.01	-
25	Asymmetric dimethylarginine	GGGGFRGRGGGGGGG CCCCCCCCCCCCCCC	36.01	-
40	Methylation	GGGFGGGRGRGGGGD CCCCCCCCCCCCCCC	34.60	-
40	Asymmetric dimethylarginine	GGGFGGGRGRGGGGD CCCCCCCCCCCCCCC	34.60	-
42	Asymmetric dimethylarginine	GFGGGRGRGGGGDRG CCCCCCCCCCCCCCC	38.94	-
42	Methylation	GFGGGRGRGGGGDRG CCCCCCCCCCCCCCC	38.94	-
48	Asymmetric dimethylarginine	GRGGGGDRGGRGGFG CCCCCCCCCCCCCCC	53.38	-
48	Methylation	GRGGGGDRGGRGGFG CCCCCCCCCCCCCCC	53.38	-
51	Asymmetric dimethylarginine	GGGDRGGRGGFGGGR CCCCCCCCCCCCCCC	44.90	-
51	Methylation	GGGDRGGRGGFGGGR CCCCCCCCCCCCCCC	44.90	-
58	Methylation	RGGFGGGRGGGGRGG CCCCCCCCCCCCCCC	43.81	-
58	Asymmetric dimethylarginine	RGGFGGGRGGGGRGG CCCCCCCCCCCCCCC	43.81	-
63	Methylation	GGRGGGGRGGGGGGG CCCCCCCCCCCCCCC	43.81	-
63	Asymmetric dimethylarginine	GGRGGGGRGGGGGGG CCCCCCCCCCCCCCC	43.81	-
71	Asymmetric dimethylarginine	GGGGGGGRGAFGGRG CCCCCCCCCCCCCCC	36.22	-
71	Methylation	GGGGGGGRGAFGGRG CCCCCCCCCCCCCCC	36.22	-
77	Asymmetric dimethylarginine	GRGAFGGRGGGGGRG CCCCCCCCCCCCCCC	40.75	-
77	Methylation	GRGAFGGRGGGGGRG CCCCCCCCCCCCCCC	40.75	-
83	Asymmetric dimethylarginine	GRGGGGGRGGGGRGG CCCCCCCCCCCCCCC	43.81	-
83	Methylation	GRGGGGGRGGGGRGG CCCCCCCCCCCCCCC	43.81	-
88	Asymmetric dimethylarginine	GGRGGGGRGGGGRGG CCCCCCCCCCCCCCC	43.81	-
88	Methylation	GGRGGGGRGGGGRGG CCCCCCCCCCCCCCC	43.81	-
93	Asymmetric dimethylarginine	GGRGGGGRGGGGRGG CCCCCCCCCCCCCCC	43.81	-
93	Methylation	GGRGGGGRGGGGRGG CCCCCCCCCCCCCCC	43.81	-
98	Asymmetric dimethylarginine	GGRGGGGRGGGAGGF CCCCCCCCCCCCCCC	43.81	-
98	Methylation	GGRGGGGRGGGAGGF CCCCCCCCCCCCCCC	43.81	-
109	Acetylation	AGGFKGGKTVTIEPH CCCCCCCCEEEEECC	48.79	21791702
146	Acetylation	GSEVYGEKRISVETN CCEEECCCEEEEEEC	51.15	21791702
149	Phosphorylation	VYGEKRISVETNGEK EECCCEEEEEECCCE	20.24	19429919

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRK_DROME	grk	physical	23213441

Drug and Disease Associations

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