UniProt ID | PRP28_YEAST | |
---|---|---|
UniProt AC | P23394 | |
Protein Name | Pre-mRNA-splicing ATP-dependent RNA helicase PRP28 | |
Gene Name | PRP28 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 588 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating the first covalent step of splicing.. | |
Protein Sequence | MARPIDVSQLIAGINKKKGLDENTSGKISKPRFLNKQERSKQERLKENEESLTPTQSDSAKVEIKKVNSRDDSFFNETNDKKRNPSKQNGSKFHFSWNESEDTLSGYDPIVSTRAIDLLWKGKTPKNAAESSYMGKHWTEKSLHEMNERDWRILKEDYAIVTKGGTVENPLRNWEELNIIPRDLLRVIIQELRFPSPTPIQRITIPNVCNMKQYRDFLGVASTGSGKTLAFVIPILIKMSRSPPRPPSLKIIDGPKALILAPTRELVQQIQKETQKVTKIWSKESNYDCKVISIVGGHSLEEISFSLSEGCDILVATPGRLIDSLENHLLVMKQVETLVLDEADKMIDLGFEDQVTNILTKVDINADSAVNRQTLMFTATMTPVIEKIAAGYMQKPVYATIGVETGSEPLIQQVVEYADNDEDKFKKLKPIVAKYDPPIIIFINYKQTADWLAEKFQKETNMKVTILHGSKSQEQREHSLQLFRTNKVQIMIATNVAARGLDIPNVSLVVNFQISKKMDDYIHRIGRTGRAANEGTAVSFVSAAEDESLIRELYKYVRKHDPLNSNIFSEAVKNKYNVGKQLSNEIIY | |
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 |
---|---|---|---|---|---|
36 | Acetylation | SKPRFLNKQERSKQE CCCHHCCHHHHHHHH | 56.54 | 25381059 | |
51 | Phosphorylation | RLKENEESLTPTQSD HHHHCHHCCCCCCCC | 31.22 | 28889911 | |
53 | Phosphorylation | KENEESLTPTQSDSA HHCHHCCCCCCCCCC | 33.30 | 25752575 | |
55 | Phosphorylation | NEESLTPTQSDSAKV CHHCCCCCCCCCCEE | 35.15 | 24961812 | |
57 | Phosphorylation | ESLTPTQSDSAKVEI HCCCCCCCCCCEEEE | 35.69 | 24961812 | |
59 | Phosphorylation | LTPTQSDSAKVEIKK CCCCCCCCCEEEEEE | 34.92 | 24961812 | |
69 | Phosphorylation | VEIKKVNSRDDSFFN EEEEECCCCCCCHHC | 39.82 | 19823750 | |
73 | Phosphorylation | KVNSRDDSFFNETND ECCCCCCCHHCCCCC | 35.71 | 19823750 | |
92 | Acetylation | PSKQNGSKFHFSWNE CCCCCCCCCEEECCC | 44.23 | 25381059 | |
374 | Phosphorylation | DSAVNRQTLMFTATM CCCCCHHHHEEEEEC | 19.56 | 27017623 | |
378 | Phosphorylation | NRQTLMFTATMTPVI CHHHHEEEEECHHHH | 13.78 | 27017623 | |
382 | Phosphorylation | LMFTATMTPVIEKIA HEEEEECHHHHHHHH | 15.28 | 27017623 | |
400 | Phosphorylation | MQKPVYATIGVETGS CCCCEEEEEECCCCC | 10.69 | 21551504 | |
417 | Phosphorylation | LIQQVVEYADNDEDK HHHHHHHHCCCCHHH | 13.98 | 21551504 |
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 PRP28_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRP28_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 PRP28_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-69, AND MASSSPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND MASSSPECTROMETRY. |