UniProt ID | MAK5_YEAST | |
---|---|---|
UniProt AC | P38112 | |
Protein Name | ATP-dependent RNA helicase MAK5 | |
Gene Name | MAK5 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 773 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. Required for the maintenance of dsRNA killer plasmid.. | |
Protein Sequence | MGKKRAPQKGKTVTKPQEIIVDESKLNWKPVDIPDTLDDFGGFYGLEEIDGVDVKVVDGKVTFVTKKDSKVLKDSNKEKVGDDQESVENESGSDSESELLEFKNLDDIKEGELSAASYSSSDEDEQGNIESSKLTDPSEDVDEDVDEDVLKENVFNKDINIDDISPVNLPEWTNLAPLSMTILQSLQNLNFLRPTEIQKKSIPVIMQGVDVMGKASTGSGKTLAYGIPIVEKLISNFSQKNKKPISLIFTPTRELAHQVTDHLKKICEPVLAKSQYSILSLTGGLSIQKQQRLLKYDNSGQIVIATPGRFLELLEKDNTLIKRFSKVNTLILDEADRLLQDGHFDEFEKIIKHLLVERRKNRENSEGSSKIWQTLIFSATFSIDLFDKLSSSRQVKDRRFKNNEDELNAVIQHLMSKIHFNSKPVIIDTNPESKVSSQIKESLIECPPLERDLYCYYFLTMFPGTTLIFCNAIDSVKKLTVYLNNLGIPAFQIHSSMTQKNRLKSLERFKQQSAKQKTINHSNPDSVQLSTVLIASDVAARGLDIPGVQHVIHYHLPRSTDIYIHRSGRTARAGSEGVSAMICSPQESMGPLRKLRKTLATKNSVSTDLNSRSTNRKPIKWQNTVPLLPIETDILSQLRERSRLAGELADHEIASNSLRKDDNWLKKAADELGIDVDSDEDDISKSNSDTFLLKNKNKKMQKTINKDKVKAMRATLNELLSVPIRKDRRQKYLTGGLVNLADNLVKKRGHNSIIGHEKTNALETLKKKKKRNN | |
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 |
---|---|---|---|---|---|
12 | Phosphorylation | RAPQKGKTVTKPQEI CCCCCCCCCCCCCEE | 41.92 | 29688323 | |
14 | Phosphorylation | PQKGKTVTKPQEIIV CCCCCCCCCCCEEEE | 42.09 | 29688323 | |
15 | Acetylation | QKGKTVTKPQEIIVD CCCCCCCCCCEEEEC | 40.13 | 24489116 | |
24 | Phosphorylation | QEIIVDESKLNWKPV CEEEECHHHHCCEEC | 37.67 | 29688323 | |
69 | Phosphorylation | TFVTKKDSKVLKDSN EEEECCCCCCCCCCC | 33.28 | 28889911 | |
86 | Phosphorylation | KVGDDQESVENESGS CCCCCHHHHCCCCCC | 29.15 | 19795423 | |
91 | Phosphorylation | QESVENESGSDSESE HHHHCCCCCCCCHHH | 56.00 | 19795423 | |
93 | Phosphorylation | SVENESGSDSESELL HHCCCCCCCCHHHHH | 47.44 | 19795423 | |
95 | Phosphorylation | ENESGSDSESELLEF CCCCCCCCHHHHHEE | 44.73 | 19795423 | |
97 | Phosphorylation | ESGSDSESELLEFKN CCCCCCHHHHHEECC | 37.18 | 19795423 | |
114 | Phosphorylation | DIKEGELSAASYSSS HHCCCCCCCCCCCCC | 19.93 | 19795423 | |
117 | Phosphorylation | EGELSAASYSSSDED CCCCCCCCCCCCCCC | 25.84 | 19795423 | |
118 | Phosphorylation | GELSAASYSSSDEDE CCCCCCCCCCCCCCC | 14.08 | 19795423 | |
119 | Phosphorylation | ELSAASYSSSDEDEQ CCCCCCCCCCCCCCC | 22.37 | 19795423 | |
120 | Phosphorylation | LSAASYSSSDEDEQG CCCCCCCCCCCCCCC | 33.31 | 19795423 | |
121 | Phosphorylation | SAASYSSSDEDEQGN CCCCCCCCCCCCCCC | 38.79 | 19795423 | |
135 | Phosphorylation | NIESSKLTDPSEDVD CCCCCCCCCCCCCCC | 49.99 | 17330950 | |
138 | Phosphorylation | SSKLTDPSEDVDEDV CCCCCCCCCCCCCCC | 49.60 | 22369663 | |
436 | Phosphorylation | TNPESKVSSQIKESL CCCCHHHCHHHHHHH | 21.91 | 21126336 | |
575 | Phosphorylation | GRTARAGSEGVSAMI CCCCCCCCCCCCEEE | 30.14 | 28889911 | |
604 | Phosphorylation | KTLATKNSVSTDLNS HHHHHCCCCCCCCCC | 20.99 | 28889911 | |
678 | Phosphorylation | ELGIDVDSDEDDISK HHCCCCCCCCCHHHH | 42.63 | 22369663 | |
684 | Phosphorylation | DSDEDDISKSNSDTF CCCCCHHHHCCCCCE | 36.71 | 22890988 | |
686 | Phosphorylation | DEDDISKSNSDTFLL CCCHHHHCCCCCEEE | 34.47 | 22369663 | |
688 | Phosphorylation | DDISKSNSDTFLLKN CHHHHCCCCCEEEEC | 45.15 | 22369663 | |
690 | Phosphorylation | ISKSNSDTFLLKNKN HHHCCCCCEEEECCC | 18.92 | 21440633 | |
694 | Acetylation | NSDTFLLKNKNKKMQ CCCCEEEECCCHHHH | 68.94 | 25381059 | |
703 | Phosphorylation | KNKKMQKTINKDKVK CCHHHHHHCCHHHHH | 16.94 | 21440633 | |
752 | Phosphorylation | VKKRGHNSIIGHEKT HHHCCCCCCCCCHHH | 15.20 | 30377154 |
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 MAK5_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MAK5_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 MAK5_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-95; THR-135; SER-138;SER-575; SER-678 AND SER-688, AND MASS SPECTROMETRY. | |
"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-138 AND SER-678, ANDMASS SPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135; SER-138 ANDSER-678, AND MASS SPECTROMETRY. | |
"A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND MASSSPECTROMETRY. |