UniProt ID | UTP15_YEAST | |
---|---|---|
UniProt AC | Q04305 | |
Protein Name | U3 small nucleolar RNA-associated protein 15 | |
Gene Name | UTP15 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 513 | |
Subcellular Localization | Nucleus, nucleolus . Associated with ribosomal chromatin, even in the absence of transcription. | |
Protein Description | Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I together with a subset of U3 proteins required for transcription (t-UTPs).. | |
Protein Sequence | MSTARPRIITSKAPLLPQQTTPEQRYWRQYTSAQLVKEHNSVTHISFNPQHPHDFAVTSSTRVQIFSSRTRQVIKTFSRFKDVVYSASFRSDGKLLCAGDATGLVSVYDSYNPRTILLSINASTHPTHVTKFHTQDNKILATASDDRVTRLWDISNAYEPQLELTGATDYVRTLSFIPAAPHLVATGSYDGLIRLYDTRSSGSTPIYSLNHDQPVENVIAVSPTQIVSCGGNNFKVWDLTSNKKLYERGNFNKAVTCLDYVENFDSPMQSALIASSLDGHVKVFDPLDNFQVKFGWKFSGPVLSCAVSPSTAQGNRHLVAGLSSGLLAIRTKKKEKRSSDKENAPASFNKNAKSNNFQRMMRGSEYQGDQEHIIHNDKVRSQRRMRAFERNINQFKWSEALDNAFVPGMAKELTLTVLQELRKRGKVRVALYGRDESTLEPLLNWCLKGIEDVRSASIVADWVAVVLELYGNTLESSPVLQELMIDLKTKVRHEIHKSKEAQRIEGMLQLLTS | |
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 |
---|---|---|---|---|---|
20 | Phosphorylation | APLLPQQTTPEQRYW CCCCCCCCCHHHHHH | 38.79 | 27017623 | |
21 | Phosphorylation | PLLPQQTTPEQRYWR CCCCCCCCHHHHHHH | 22.08 | 27017623 | |
81 | Ubiquitination | IKTFSRFKDVVYSAS HHHHHHHCCEEEEEE | 48.80 | 23749301 | |
91 | Phosphorylation | VYSASFRSDGKLLCA EEEEEECCCCCEEEC | 49.02 | 19779198 | |
108 | Phosphorylation | ATGLVSVYDSYNPRT CCCEEEEECCCCCCE | 7.52 | 19779198 | |
138 | Acetylation | KFHTQDNKILATASD EEECCCCEEEEECCC | 47.59 | 24489116 | |
222 | Phosphorylation | VENVIAVSPTQIVSC CCCEEEECCCEEEEE | 17.13 | 28889911 | |
297 | Acetylation | FQVKFGWKFSGPVLS EEEEEECEECCCEEE | 29.99 | 24489116 | |
339 | Phosphorylation | KKKEKRSSDKENAPA CCCCCCCCCCCCCCC | 57.65 | 30377154 | |
347 | Phosphorylation | DKENAPASFNKNAKS CCCCCCCCCCCCHHC | 28.44 | 30377154 | |
353 | Acetylation | ASFNKNAKSNNFQRM CCCCCCHHCCCHHHH | 64.21 | 25381059 | |
414 | Phosphorylation | PGMAKELTLTVLQEL CCHHHHHHHHHHHHH | 22.83 | 30377154 | |
416 | Phosphorylation | MAKELTLTVLQELRK HHHHHHHHHHHHHHH | 17.59 | 30377154 | |
497 | Acetylation | KVRHEIHKSKEAQRI HHHHHHHHHHHHHHH | 69.73 | 25381059 |
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 UTP15_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UTP15_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 UTP15_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-222, AND MASSSPECTROMETRY. |