FBRL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FBRL_MOUSE
• UniProt AC: P35550
• Protein Name: rRNA 2'-O-methyltransferase fibrillarin
• Gene Name: Fbl
• Organism: Mus musculus (Mouse).
• Sequence Length: 327
• 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 by catalyzing 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 (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity)..
• Protein Sequence: MKPGFSPRGGGFGGRGGFGDRGGRGGGRGGRGGFGGGRGGFGGGGRGRGGGGGGFRGRGGGGGRGGGFQSGGNRGRGGGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKVKN

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
8	Asymmetric dimethylarginine	MKPGFSPRGGGFGGR CCCCCCCCCCCCCCC	56.01	-
8	Methylation	MKPGFSPRGGGFGGR CCCCCCCCCCCCCCC	56.01	-
15	Asymmetric dimethylarginine	RGGGFGGRGGFGDRG CCCCCCCCCCCCCCC	42.30	-
15	Methylation	RGGGFGGRGGFGDRG CCCCCCCCCCCCCCC	42.30	-
21	Asymmetric dimethylarginine	GRGGFGDRGGRGGGR CCCCCCCCCCCCCCC	50.25	-
21	Methylation	GRGGFGDRGGRGGGR CCCCCCCCCCCCCCC	50.25	-
24	Asymmetric dimethylarginine	GFGDRGGRGGGRGGR CCCCCCCCCCCCCCC	43.33	-
24	Methylation	GFGDRGGRGGGRGGR CCCCCCCCCCCCCCC	43.33	-
28	Asymmetric dimethylarginine	RGGRGGGRGGRGGFG CCCCCCCCCCCCCCC	47.90	-
28	Methylation	RGGRGGGRGGRGGFG CCCCCCCCCCCCCCC	47.90	-
31	Methylation	RGGGRGGRGGFGGGR CCCCCCCCCCCCCCC	44.90	-
31	Asymmetric dimethylarginine	RGGGRGGRGGFGGGR CCCCCCCCCCCCCCC	44.90	-
38	Methylation	RGGFGGGRGGFGGGG CCCCCCCCCCCCCCC	45.39	-
46	Methylation	GGFGGGGRGRGGGGG CCCCCCCCCCCCCCC	34.60	-
48	Dimethylation	FGGGGRGRGGGGGGF CCCCCCCCCCCCCCC	38.94	-
64	Methylation	GRGGGGGRGGGFQSG CCCCCCCCCCCCCCC	43.81	-
88	Phosphorylation	GGKRGNQSGKNVMVE CCCCCCCCCCCEEEC	56.59	25890499
108	Ubiquitination	GVFICRGKEDALVTK CEEEECCCCCEEEEC	32.82	27667366
108	Malonylation	GVFICRGKEDALVTK CEEEECCCCCEEEEC	32.82	26320211
108	Acetylation	GVFICRGKEDALVTK CEEEECCCCCEEEEC	32.82	23806337
115	Ubiquitination	KEDALVTKNLVPGES CCCEEEECCCCCCCC	40.58	22790023
122	Phosphorylation	KNLVPGESVYGEKRV CCCCCCCCCCCCCEE	26.93	29176673
124	Phosphorylation	LVPGESVYGEKRVSI CCCCCCCCCCCEEEE	28.93	-
127	Ubiquitination	GESVYGEKRVSISEG CCCCCCCCEEEECCC	54.45	22790023
127	Acetylation	GESVYGEKRVSISEG CCCCCCCCEEEECCC	54.45	23236377
130	Phosphorylation	VYGEKRVSISEGDDK CCCCCEEEECCCCCC	25.16	27087446
132	Phosphorylation	GEKRVSISEGDDKIE CCCEEEECCCCCCEE	28.20	22942356
137	Acetylation	SISEGDDKIEYRAWN EECCCCCCEEEEECC	42.02	23806337
137	Ubiquitination	SISEGDDKIEYRAWN EECCCCCCEEEEECC	42.02	22790023
140	Phosphorylation	EGDDKIEYRAWNPFR CCCCCEEEEECCHHH	14.76	25619855
164	Ubiquitination	GVDQIHIKPGAKVLY CCCEEEECCCCEEEE	24.20	22790023
171	Phosphorylation	KPGAKVLYLGAASGT CCCCEEEEEECCCCC	13.18	19854140
176	Phosphorylation	VLYLGAASGTTVSHV EEEEECCCCCCEEEH	35.82	19854140
178	Phosphorylation	YLGAASGTTVSHVSD EEECCCCCCEEEHHH	22.87	19854140
199	Phosphorylation	LVYAVEFSHRSGRDL EEEEEEEECCCCHHH	12.41	19854140
211	Acetylation	RDLINLAKKRTNIIP HHHHHHHHHHCCEEC	46.05	23236377
212	Acetylation	DLINLAKKRTNIIPV HHHHHHHHHCCEECC	59.87	-
287	Phosphorylation	SAEAVFASEVKKMQQ CHHHHHHHHHHHHHH	31.30	28542873
298	Acetylation	KMQQENMKPQEQLTL HHHHHCCCHHHHCCC	55.95	22826441
298	Ubiquitination	KMQQENMKPQEQLTL HHHHHCCCHHHHCCC	55.95	22790023

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

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
105	Q	Acetylation	Acetylated by CREBBP/CBP, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me), without affecting rRNA methylation.	-
105	Q	Acetylation	Deacetylation by SIRT7 restores methylation of 'Gln-105' of histone H2A (H2AQ104me).	-
105	Q	Methylation	Acetylated by CREBBP/CBP, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me), without affecting rRNA methylation.	-
105	Q	Methylation	Deacetylation by SIRT7 restores methylation of 'Gln-105' of histone H2A (H2AQ104me).	-

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ABCF1_HUMAN	ABCF1	physical	26496610
DHC24_HUMAN	DHCR24	physical	26496610
FLNB_HUMAN	FLNB	physical	26496610
HELLS_HUMAN	HELLS	physical	26496610
HMGA1_HUMAN	HMGA1	physical	26496610
DNJA1_HUMAN	DNAJA1	physical	26496610
IF16_HUMAN	IFI16	physical	26496610
RLA0_HUMAN	RPLP0	physical	26496610
RS27_HUMAN	RPS27	physical	26496610
COIL_HUMAN	COIL	physical	26496610
CAF1B_HUMAN	CHAF1B	physical	26496610
BECN1_HUMAN	BECN1	physical	26496610
U3IP2_HUMAN	RRP9	physical	26496610
ANM5_HUMAN	PRMT5	physical	26496610
NOP56_HUMAN	NOP56	physical	26496610
CSN8_HUMAN	COPS8	physical	26496610
STIP1_HUMAN	STIP1	physical	26496610
SO4A1_HUMAN	SLCO4A1	physical	26496610
RT02_HUMAN	MRPS2	physical	26496610
NOP58_HUMAN	NOP58	physical	26496610
PINX1_HUMAN	PINX1	physical	26496610
MEP50_HUMAN	WDR77	physical	26496610
RIOK1_HUMAN	RIOK1	physical	26496610
LSM11_HUMAN	LSM11	physical	26496610
H3C_HUMAN	H3F3C	physical	26496610

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY.
PubMed: 19367708