UniProt ID | REF2_YEAST | |
---|---|---|
UniProt AC | P42073 | |
Protein Name | RNA end formation protein 2 | |
Gene Name | REF2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 533 | |
Subcellular Localization | Nucleus . | |
Protein Description | RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Negative regulator of poly(A) synthesis. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. REF2 is required for 3'-end formation of snoRNAs.. | |
Protein Sequence | MSAPVPQLVNISHALQASTIQQIRLDMVDFNKDCKLSSIQLARIDKYIDSLQAALNQFTKDNLHIERKEKNVTEADIQLYSGLKSMYLDYLNQLIKLKHEKQHHSTPPIANDVSLDFFVNQLPKFSPEERKNYIDNLILNKNSHNRLSKMDGLVDAVINLCVLDTSVAENVRSYMKLLDTLGFQKGSNSTGTKANLKKKLASSKAKIKDSEKEKEKEKDKSKVKMKTKLKPSPLLNNDDKNSSPSPTASTSSMKKLKSGLFNKNEAKSTESLPTSSKKKLSFSKYLNKDDADMTKLGTKRSIDVDFKVNPEASTVASNIISSSTSGSSTTTVATPASSEEPLKKKTKISVQDSNVQSILRNGKPKKARISSIKFLDDSQLIKVYGDDLPNQGLQVSPTQLKKILKPFKEGEPKEIILFEDMSIKLKPLDLMFLKNTNSDDYMDISETKGGPIHCETRTPLIYRKNFNHFNPDLNKRPPREPIEFDLNGNTNSTPTIAKAFGKNSLLLRKDRGGLPYKHVPIVKRNKYPPRPVH | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
46 | Acetylation | IQLARIDKYIDSLQA HHHHHHHHHHHHHHH | 41.56 | 24489116 | |
105 | Phosphorylation | KHEKQHHSTPPIAND HHHHCCCCCCCCCCC | 40.25 | 22369663 | |
106 | Phosphorylation | HEKQHHSTPPIANDV HHHCCCCCCCCCCCC | 28.82 | 22369663 | |
114 | Phosphorylation | PPIANDVSLDFFVNQ CCCCCCCCHHHHHHC | 25.69 | 21440633 | |
174 | Phosphorylation | VAENVRSYMKLLDTL HHHHHHHHHHHHHHH | 6.41 | 28889911 | |
193 | Acetylation | GSNSTGTKANLKKKL CCCCCCCHHHHHHHH | 36.30 | 25381059 | |
232 | Phosphorylation | MKTKLKPSPLLNNDD CCCCCCCCCCCCCCC | 26.96 | 21440633 | |
242 | Phosphorylation | LNNDDKNSSPSPTAS CCCCCCCCCCCCCCC | 49.74 | 22369663 | |
243 | Phosphorylation | NNDDKNSSPSPTAST CCCCCCCCCCCCCCH | 38.50 | 22369663 | |
245 | Phosphorylation | DDKNSSPSPTASTSS CCCCCCCCCCCCHHH | 36.51 | 22369663 | |
247 | Phosphorylation | KNSSPSPTASTSSMK CCCCCCCCCCHHHHH | 37.26 | 22369663 | |
249 | Phosphorylation | SSPSPTASTSSMKKL CCCCCCCCHHHHHHH | 31.16 | 22369663 | |
250 | Phosphorylation | SPSPTASTSSMKKLK CCCCCCCHHHHHHHH | 23.51 | 22369663 | |
251 | Phosphorylation | PSPTASTSSMKKLKS CCCCCCHHHHHHHHH | 26.41 | 22369663 | |
252 | Phosphorylation | SPTASTSSMKKLKSG CCCCCHHHHHHHHHC | 34.41 | 22369663 | |
254 | Acetylation | TASTSSMKKLKSGLF CCCHHHHHHHHHCCC | 57.83 | 25381059 | |
258 | Phosphorylation | SSMKKLKSGLFNKNE HHHHHHHHCCCCCCC | 51.68 | 21440633 | |
268 | Phosphorylation | FNKNEAKSTESLPTS CCCCCCCCCCCCCCC | 44.44 | 28889911 | |
271 | Phosphorylation | NEAKSTESLPTSSKK CCCCCCCCCCCCCCC | 39.47 | 30377154 | |
281 | Phosphorylation | TSSKKKLSFSKYLNK CCCCCHHCHHHHCCC | 36.03 | 21440633 | |
283 | Phosphorylation | SKKKLSFSKYLNKDD CCCHHCHHHHCCCCC | 19.60 | 21440633 | |
284 | Acetylation | KKKLSFSKYLNKDDA CCHHCHHHHCCCCCC | 52.31 | 24489116 | |
288 | Acetylation | SFSKYLNKDDADMTK CHHHHCCCCCCCCHH | 55.16 | 22865919 | |
294 | Phosphorylation | NKDDADMTKLGTKRS CCCCCCCHHCCCCCE | 24.54 | 21440633 | |
295 | Acetylation | KDDADMTKLGTKRSI CCCCCCHHCCCCCEE | 37.98 | 25381059 | |
346 | Phosphorylation | EEPLKKKTKISVQDS CCCCCCCCCEECCCH | 42.35 | 30377154 | |
378 | Phosphorylation | SIKFLDDSQLIKVYG EEEECCHHHHEEHHC | 26.93 | 27214570 | |
396 | Phosphorylation | PNQGLQVSPTQLKKI CCCCCCCCHHHHHHH | 14.85 | 22369663 | |
398 | Phosphorylation | QGLQVSPTQLKKILK CCCCCCHHHHHHHHH | 38.74 | 22369663 | |
502 | Acetylation | TIAKAFGKNSLLLRK HHHHHHCCCCEEEEE | 36.59 | 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 REF2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of REF2_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 REF2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND MASSSPECTROMETRY. |