UniProt ID | PRP22_YEAST | |
---|---|---|
UniProt AC | P24384 | |
Protein Name | Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22 | |
Gene Name | PRP22 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1145 | |
Subcellular Localization | Nucleus. | |
Protein Description | Acts late in the splicing of pre-mRNA. Mediates the release of the spliced mRNA from spliceosomes.. | |
Protein Sequence | MSDISKLIGAIVGSDDPVIIEFVLNIINKSGNLQEFIRNIQKLDAGISYEDSIKMYNAFLGKQEEEKVRNKVKSSPLSQKINQVLKDDVNLDDPVVTEFVLSILNKSKSITEFQEQLNLMQSGLDNETIFKIYQIASPPVMKEEVSVLPSTKIPAKIEAKIEEEVQKIESLDPSPVLHKVYEGKVRNITTFGCFVQIFGTRMKNCDGLVHISEMSDQRTLDPHDVVRQGQHIFVEVIKIQNNGKISLSMKNIDQHSGEIRKRNTESVEDRGRSNDAHTSRNMKNKIKRRALTSPERWEIRQLIASGAASIDDYPELKDEIPINTSYLTAKRDDGSIVNGNTEKVDSKLEEQQRDETDEIDVELNTDDGPKFLKDQQVKGAKKYEMPKITKVPRGFMNRSAINGSNAIRDHREEKLRKKREIEQQIRKQQSFDDPTKNKKDSRNEIQMLKNQLIVTEWEKNRMNESISYGKRTSLPISAQRQTLPVYAMRSELIQAVRDNQFLVIVGETGSGKTTQITQYLDEEGFSNYGMIGCTQPRRVAAVSVAKRVAEEVGCKVGHDVGYTIRFEDVTGPDTRIKYMTDGMLQREALLDPEMSKYSVIMLDEAHERTVATDVLFALLKKAAIKRPELKVIVTSATLNSAKFSEYFLNCPIINIPGKTFPVEVLYSQTPQMDYIEAALDCVIDIHINEGPGDILVFLTGQEEIDSCCEILYDRVKTLGDSIGELLILPVYSALPSEIQSKIFEPTPKGSRKVVFATNIAETSITIDGIYYVVDPGFAKINIYNARAGIEQLIVSPISQAQANQRKGRAGRTGPGKCYRLYTESAFYNEMLENTVPEIQRQNLSHTILMLKAMGINDLLKFDFMDPPPKNLMLNALTELYHLQSLDDEGKLTNLGKEMSLFPMDPTLSRSLLSSVDNQCSDEIVTIISMLSVQNVFYRPKDRQLEADSKKAKFHHPYGDHLTLLNVYTRWQQANYSEQYCKTNFLHFRHLKRARDVKSQISMIFKKIGLKLISCHSDPDLIRKTFVSGFFMNAAKRDSQVGYKTINGGTEVGIHPSSSLYGKEYEYVMYHSIVLTSREYMSQVTSIEPQWLLEVAPHFYKAGDAESQSRKKAKIIPLHNKFAKDQNSWRLSSIRQSRERALGIKR | |
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 |
---|---|---|---|---|---|
74 | Phosphorylation | KVRNKVKSSPLSQKI HHHHHHHCCHHHHHH | 39.93 | 30377154 | |
75 | Phosphorylation | VRNKVKSSPLSQKIN HHHHHHCCHHHHHHH | 24.92 | 23749301 | |
246 | Phosphorylation | IQNNGKISLSMKNID EECCCEEEEEEECCC | 20.20 | 29136822 | |
248 | Phosphorylation | NNGKISLSMKNIDQH CCCEEEEEEECCCCC | 22.41 | 29136822 | |
256 | Phosphorylation | MKNIDQHSGEIRKRN EECCCCCCCCHHHCC | 32.27 | 29136822 | |
292 | Phosphorylation | KIKRRALTSPERWEI HHHHHHCCCHHHHHH | 41.05 | 22369663 | |
293 | Phosphorylation | IKRRALTSPERWEIR HHHHHCCCHHHHHHH | 26.13 | 22369663 | |
305 | Phosphorylation | EIRQLIASGAASIDD HHHHHHHHCCCCCCC | 23.21 | 24961812 | |
430 | Phosphorylation | QQIRKQQSFDDPTKN HHHHHHCCCCCCCCC | 28.31 | 30377154 | |
473 | Phosphorylation | ISYGKRTSLPISAQR CCCCCCCCCCCCCCC | 35.86 | 23749301 | |
482 | Phosphorylation | PISAQRQTLPVYAMR CCCCCCCCCCCHHHH | 34.91 | 22890988 | |
486 | Phosphorylation | QRQTLPVYAMRSELI CCCCCCCHHHHHHHH | 7.85 | 22890988 | |
490 | Phosphorylation | LPVYAMRSELIQAVR CCCHHHHHHHHHHHH | 24.54 | 22890988 | |
562 | Phosphorylation | KVGHDVGYTIRFEDV CCCCCCCCEEEEEEC | 9.99 | 19823750 | |
563 | Phosphorylation | VGHDVGYTIRFEDVT CCCCCCCEEEEEECC | 10.35 | 19823750 | |
570 | Phosphorylation | TIRFEDVTGPDTRIK EEEEEECCCCCCEEE | 56.15 | 19823750 | |
574 | Phosphorylation | EDVTGPDTRIKYMTD EECCCCCCEEEEECC | 37.11 | 19823750 | |
577 | Acetylation | TGPDTRIKYMTDGML CCCCCEEEEECCCHH | 26.19 | 25381059 | |
578 | Phosphorylation | GPDTRIKYMTDGMLQ CCCCEEEEECCCHHC | 11.68 | 19823750 | |
580 | Phosphorylation | DTRIKYMTDGMLQRE CCEEEEECCCHHCHH | 26.72 | 19823750 | |
1024 | Phosphorylation | DPDLIRKTFVSGFFM CHHHHHHHHHHCCCC | 21.30 | 28132839 | |
1120 | Acetylation | KIIPLHNKFAKDQNS EEECCCHHHCCCCCC | 35.63 | 25381059 | |
1132 | Phosphorylation | QNSWRLSSIRQSRER CCCHHHHHHHHHHHH | 26.78 | 28889911 |
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 PRP22_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRP22_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 PRP22_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
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-293, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND MASSSPECTROMETRY. |