| UniProt ID | FBRL_YEAST | |
|---|---|---|
| UniProt AC | P15646 | |
| Protein Name | rRNA 2'-O-methyltransferase fibrillarin | |
| Gene Name | NOP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| 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. [PubMed: 1825809 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. Involved in the biogenesis of the 18S rRNA. 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] | |
| Protein Sequence | MSFRPGSRGGSRGGSRGGFGGRGGSRGGARGGSRGGFGGRGGSRGGARGGSRGGFGGRGGSRGGARGGSRGGRGGAAGGARGGAKVVIEPHRHAGVYIARGKEDLLVTKNMAPGESVYGEKRISVEEPSKEDGVPPTKVEYRVWNPFRSKLAAGIMGGLDELFIAPGKKVLYLGAASGTSVSHVSDVVGPEGVVYAVEFSHRPGRELISMAKKRPNIIPIIEDARHPQKYRMLIGMVDCVFADVAQPDQARIIALNSHMFLKDQGGVVISIKANCIDSTVDAETVFAREVQKLREERIKPLEQLTLEPYERDHCIVVGRYMRSGLKK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 15 | Phosphorylation | RGGSRGGSRGGFGGR CCCCCCCCCCCCCCC | 30.49 | 28889911 | |
| 16 | Asymmetric dimethylarginine | GGSRGGSRGGFGGRG CCCCCCCCCCCCCCC | 53.15 | - | |
| 16 | Methylation | GGSRGGSRGGFGGRG CCCCCCCCCCCCCCC | 53.15 | 23865587 | |
| 22 | Methylation | SRGGFGGRGGSRGGA CCCCCCCCCCCCCCC | 46.83 | 23865587 | |
| 30 | Methylation | GGSRGGARGGSRGGF CCCCCCCCCCCCCCC | 53.96 | 23865587 | |
| 33 | Phosphorylation | RGGARGGSRGGFGGR CCCCCCCCCCCCCCC | 30.49 | 28889911 | |
| 34 | Methylation | GGARGGSRGGFGGRG CCCCCCCCCCCCCCC | 53.15 | 23865587 | |
| 40 | Methylation | SRGGFGGRGGSRGGA CCCCCCCCCCCCCCC | 46.83 | 23865587 | |
| 48 | Methylation | GGSRGGARGGSRGGF CCCCCCCCCCCCCCC | 53.96 | 23865587 | |
| 51 | Phosphorylation | RGGARGGSRGGFGGR CCCCCCCCCCCCCCC | 30.49 | 28889911 | |
| 52 | Methylation | GGARGGSRGGFGGRG CCCCCCCCCCCCCCC | 53.15 | 23865587 | |
| 58 | Methylation | SRGGFGGRGGSRGGA CCCCCCCCCCCCCCC | 46.83 | 23865587 | |
| 69 | Phosphorylation | RGGARGGSRGGRGGA CCCCCCCCCCCCCCC | 30.49 | 17563356 | |
| 70 | Asymmetric dimethylarginine | GGARGGSRGGRGGAA CCCCCCCCCCCCCCC | 55.66 | - | |
| 70 | Methylation | GGARGGSRGGRGGAA CCCCCCCCCCCCCCC | 55.66 | 23865587 | |
| 73 | Asymmetric dimethylarginine | RGGSRGGRGGAAGGA CCCCCCCCCCCCCCC | 43.10 | - | |
| 73 | Methylation | RGGSRGGRGGAAGGA CCCCCCCCCCCCCCC | 43.10 | 23865587 | |
| 81 | Asymmetric dimethylarginine | GGAAGGARGGAKVVI CCCCCCCCCCCEEEE | 47.56 | - | |
| 81 | Methylation | GGAAGGARGGAKVVI CCCCCCCCCCCEEEE | 47.56 | 23865587 | |
| 85 | Ubiquitination | GGARGGAKVVIEPHR CCCCCCCEEEEECCC | 40.07 | 23749301 | |
| 85 | Acetylation | GGARGGAKVVIEPHR CCCCCCCEEEEECCC | 40.07 | 23572591 | |
| 102 | Ubiquitination | GVYIARGKEDLLVTK EEEEECCCCCEEEEC | 42.37 | 22817900 | |
| 102 | Acetylation | GVYIARGKEDLLVTK EEEEECCCCCEEEEC | 42.37 | 24489116 | |
| 108 | Phosphorylation | GKEDLLVTKNMAPGE CCCCEEEECCCCCCC | 19.37 | 22369663 | |
| 109 | Acetylation | KEDLLVTKNMAPGES CCCEEEECCCCCCCC | 36.93 | 24489116 | |
| 109 | Ubiquitination | KEDLLVTKNMAPGES CCCEEEECCCCCCCC | 36.93 | 24961812 | |
| 116 | Phosphorylation | KNMAPGESVYGEKRI CCCCCCCCCCCCCEE | 26.93 | 28889911 | |
| 121 | Acetylation | GESVYGEKRISVEEP CCCCCCCCEEECCCC | 51.15 | 24489116 | |
| 121 | Ubiquitination | GESVYGEKRISVEEP CCCCCCCCEEECCCC | 51.15 | 23749301 | |
| 124 | Phosphorylation | VYGEKRISVEEPSKE CCCCCEEECCCCCCC | 27.75 | 21440633 | |
| 130 | Acetylation | ISVEEPSKEDGVPPT EECCCCCCCCCCCCC | 71.22 | 24489116 | |
| 130 | Ubiquitination | ISVEEPSKEDGVPPT EECCCCCCCCCCCCC | 71.22 | 23749301 | |
| 138 | Acetylation | EDGVPPTKVEYRVWN CCCCCCCCEEEEECC | 38.55 | 24489116 | |
| 150 | Ubiquitination | VWNPFRSKLAAGIMG ECCHHHHHHHHHHHC | 37.58 | 22106047 | |
| 168 | Ubiquitination | ELFIAPGKKVLYLGA EEEECCCCEEEEEEC | 38.35 | 22817900 | |
| 169 | Ubiquitination | LFIAPGKKVLYLGAA EEECCCCEEEEEECC | 43.30 | 22817900 | |
| 299 | Ubiquitination | KLREERIKPLEQLTL HHHHHHCCCHHHHCC | 50.17 | 23749301 | |
| 299 | Acetylation | KLREERIKPLEQLTL HHHHHHCCCHHHHCC | 50.17 | 24489116 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of FBRL_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FBRL_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of FBRL_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND MASSSPECTROMETRY. | |
