UniProt ID | UTP25_YEAST | |
---|---|---|
UniProt AC | P40498 | |
Protein Name | U3 small nucleolar RNA-associated protein 25 | |
Gene Name | UTP25 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 721 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.. | |
Protein Sequence | MSDSSVREKNDNFRGYRKRGRQELRKIKRSSARTEGGSTETLEDVAEDIDHRSDEDEVSDVDSGDDFDIEDEEGKKEKVYDALLTILKSEHPEPKRRRREADESNKAPAEVGEDEHENTEHGPVDDQLEIENGLLGNHEDDNDDDSSGDEKDIDSEDEQDPFESHFNQVPEKFVDKLSNAFKTKSVKYKSVKGSLSDSESYIYAKPVVIGEEALVESPYRSSSIYSYFLKQRLKVQNGLLDKKTDPLTALQKKLVDPMFQYKDILYEYDSYEKDEDEYRDLYALHVLNHIYKTRDRILKNNQRLQDNPDTEHLDQGFTRPKVLIVVPTREVAYRVVDKIISKSGIDQVDKKGKFYDQFRDDSLPPKSKPKSFQHIFRGNTNDFFVVGLKFTRKAIKLYSNFYQSDIIVCSPLGIQMILENTDKKKRQDDFLSSIELMVIDQLHSIEYQNISHIFTIFDHLNKIPDQQHEADFSRIRMWYINEQAKLFRQTMVFTKYISPAANSLINGRCRNMAGRWKNHKVIGSENSSIGQSGLKIRQIFQRFDIIGNSIIEEPDYRFKFFTSVIIPGIVKSTGYEDGILIYIPDYTDFIRIRNYMKEKTTILFGDINEYSSQRQLNANRSLFQQGRLKVMLYTERLHHYRRYEIKGVKSVVFYKPPNNPEFYNEVVRFIGKNAFLGNTDLNISTVRCIYSKLDGLSLERIVGTKRAAVLSHAQKEIYEFK | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSDSSVREK ------CCCHHHHCC | 46.31 | 27717283 | |
4 | Phosphorylation | ----MSDSSVREKND ----CCCHHHHCCCC | 24.35 | 27717283 | |
5 | Phosphorylation | ---MSDSSVREKNDN ---CCCHHHHCCCCC | 30.13 | 27717283 | |
38 | Phosphorylation | SARTEGGSTETLEDV CCCCCCCCCCCHHHH | 33.65 | 27214570 | |
39 | Phosphorylation | ARTEGGSTETLEDVA CCCCCCCCCCHHHHH | 35.94 | 30377154 | |
53 | Phosphorylation | AEDIDHRSDEDEVSD HHHCCCCCCCCCCCC | 41.76 | 28889911 | |
59 | Phosphorylation | RSDEDEVSDVDSGDD CCCCCCCCCCCCCCC | 29.84 | 19795423 | |
63 | Phosphorylation | DEVSDVDSGDDFDIE CCCCCCCCCCCCCCC | 43.92 | 19795423 | |
88 | Acetylation | DALLTILKSEHPEPK HHHHHHHHCCCCCCH | 50.36 | 24489116 | |
146 | Phosphorylation | EDDNDDDSSGDEKDI CCCCCCCCCCCCCCC | 43.12 | 27738172 | |
147 | Phosphorylation | DDNDDDSSGDEKDID CCCCCCCCCCCCCCC | 58.20 | 27738172 | |
155 | Phosphorylation | GDEKDIDSEDEQDPF CCCCCCCCCCCCCHH | 47.48 | 22369663 | |
164 | Phosphorylation | DEQDPFESHFNQVPE CCCCHHHHHHHHCCH | 33.48 | 22890988 | |
176 | Acetylation | VPEKFVDKLSNAFKT CCHHHHHHHHHHHCC | 48.81 | 24489116 | |
185 | Phosphorylation | SNAFKTKSVKYKSVK HHHHCCCCCEEEEEC | 29.13 | 19823750 | |
188 | Phosphorylation | FKTKSVKYKSVKGSL HCCCCCEEEEECCCC | 13.31 | 19823750 | |
190 | Phosphorylation | TKSVKYKSVKGSLSD CCCCEEEEECCCCCC | 26.43 | 19823750 | |
194 | Phosphorylation | KYKSVKGSLSDSESY EEEEECCCCCCCCCE | 20.98 | 22369663 | |
196 | Phosphorylation | KSVKGSLSDSESYIY EEECCCCCCCCCEEE | 40.56 | 22369663 | |
198 | Phosphorylation | VKGSLSDSESYIYAK ECCCCCCCCCEEEEE | 25.68 | 22369663 | |
200 | Phosphorylation | GSLSDSESYIYAKPV CCCCCCCCEEEEECE | 22.30 | 22369663 | |
201 | Phosphorylation | SLSDSESYIYAKPVV CCCCCCCEEEEECEE | 8.23 | 22369663 | |
203 | Phosphorylation | SDSESYIYAKPVVIG CCCCCEEEEECEEEC | 10.59 | 22369663 | |
396 | Ubiquitination | KFTRKAIKLYSNFYQ HHHHHHHHHHHHHHC | 46.35 | 23749301 | |
402 | Phosphorylation | IKLYSNFYQSDIIVC HHHHHHHHCCCEEEE | 16.03 | 23749301 | |
404 | Phosphorylation | LYSNFYQSDIIVCSP HHHHHHCCCEEEEEH | 21.28 | 23749301 | |
684 | Phosphorylation | GNTDLNISTVRCIYS CCCCCCHHHHHHHHH | 21.56 | 30377154 | |
685 | Phosphorylation | NTDLNISTVRCIYSK CCCCCHHHHHHHHHC | 14.26 | 30377154 | |
692 | Ubiquitination | TVRCIYSKLDGLSLE HHHHHHHCCCCCCHH | 33.36 | 23749301 | |
692 | Acetylation | TVRCIYSKLDGLSLE HHHHHHHCCCCCCHH | 33.36 | 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 UTP25_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UTP25_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 UTP25_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-196, AND MASSSPECTROMETRY. | |
"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-196, AND MASSSPECTROMETRY. |