| UniProt ID | SUB2_YEAST | |
|---|---|---|
| UniProt AC | Q07478 | |
| Protein Name | ATP-dependent RNA helicase SUB2 | |
| Gene Name | SUB2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 446 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | ATP-binding RNA helicase component of the TREX complex involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 plays also a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity.. | |
| Protein Sequence | MSHEGEEDLLEYSDNEQEIQIDASKAAEAGETGAATSATEGDNNNNTAAGDKKGSYVGIHSTGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKNKDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTLHGLQQYYIKLEEREKNRKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEDEEVLAKIQERFDVKIAEFPEEGIDPSTYLNN | |
| 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 | Acetylation | ------MSHEGEEDL ------CCCCCCCCH | 30.19 | 15665377 | |
| 2 | Phosphorylation | ------MSHEGEEDL ------CCCCCCCCH | 30.19 | 22369663 | |
| 12 | Phosphorylation | GEEDLLEYSDNEQEI CCCCHHHCCCCCCEE | 22.69 | 22369663 | |
| 13 | Phosphorylation | EEDLLEYSDNEQEIQ CCCHHHCCCCCCEEE | 25.28 | 22369663 | |
| 24 | Phosphorylation | QEIQIDASKAAEAGE CEEEEEHHHHHHCCC | 21.05 | 22369663 | |
| 32 | Phosphorylation | KAAEAGETGAATSAT HHHHCCCCCCCCCCC | 31.07 | 22890988 | |
| 36 | Phosphorylation | AGETGAATSATEGDN CCCCCCCCCCCCCCC | 20.54 | 22369663 | |
| 37 | Phosphorylation | GETGAATSATEGDNN CCCCCCCCCCCCCCC | 28.59 | 22369663 | |
| 39 | Phosphorylation | TGAATSATEGDNNNN CCCCCCCCCCCCCCC | 40.02 | 25521595 | |
| 47 | Phosphorylation | EGDNNNNTAAGDKKG CCCCCCCCCCCCCCC | 21.73 | 22890988 | |
| 52 | Acetylation | NNTAAGDKKGSYVGI CCCCCCCCCCCEEEE | 59.10 | 24489116 | |
| 52 | Ubiquitination | NNTAAGDKKGSYVGI CCCCCCCCCCCEEEE | 59.10 | 23749301 | |
| 55 | Phosphorylation | AAGDKKGSYVGIHST CCCCCCCCEEEEECC | 26.06 | 22369663 | |
| 56 | Phosphorylation | AGDKKGSYVGIHSTG CCCCCCCEEEEECCC | 16.03 | 22369663 | |
| 61 | Phosphorylation | GSYVGIHSTGFKDFL CCEEEEECCCCCHHH | 28.45 | 17287358 | |
| 65 | Acetylation | GIHSTGFKDFLLKPE EEECCCCCHHHCCHH | 49.25 | 24489116 | |
| 70 | Succinylation | GFKDFLLKPELSRAI CCCHHHCCHHHHHHH | 38.30 | 23954790 | |
| 70 | Acetylation | GFKDFLLKPELSRAI CCCHHHCCHHHHHHH | 38.30 | 24489116 | |
| 155 | Acetylation | NEYLRFSKYMPDVKT HHHHHHHHCCCCCCE | 42.74 | 24489116 | |
| 161 | Ubiquitination | SKYMPDVKTAVFYGG HHCCCCCCEEEEECC | 37.84 | 24961812 | |
| 161 | Succinylation | SKYMPDVKTAVFYGG HHCCCCCCEEEEECC | 37.84 | 23954790 | |
| 169 | Phosphorylation | TAVFYGGTPISKDAE EEEEECCCCCCCCHH | 17.06 | 11156603 | |
| 173 | Ubiquitination | YGGTPISKDAELLKN ECCCCCCCCHHHHCC | 62.77 | 24961812 | |
| 173 | Acetylation | YGGTPISKDAELLKN ECCCCCCCCHHHHCC | 62.77 | 24489116 | |
| 179 | Acetylation | SKDAELLKNKDTAPH CCCHHHHCCCCCCCC | 74.67 | 24489116 | |
| 181 | Acetylation | DAELLKNKDTAPHIV CHHHHCCCCCCCCEE | 55.67 | 24489116 | |
| 191 | Phosphorylation | APHIVVATPGRLKAL CCCEEEECCHHHHHH | 18.05 | 20377248 | |
| 202 | 2-Hydroxyisobutyrylation | LKALVREKYIDLSHV HHHHHHHHCCCHHHH | 36.62 | - | |
| 202 | Acetylation | LKALVREKYIDLSHV HHHHHHHHCCCHHHH | 36.62 | 24489116 | |
| 287 | Acetylation | GLQQYYIKLEEREKN HHHHHHHHHHHHHHH | 33.45 | 24489116 | |
| 324 | Acetylation | TRANELTKLLNASNF CCHHHHHHHHHHCCC | 64.70 | 24489116 | |
| 341 | Acetylation | ITVHGHMKQEERIAR EEECCCCCHHHHHHH | 49.21 | 24489116 | |
| 353 | Acetylation | IARYKAFKDFEKRIC HHHHHHHHHHHHHEE | 67.38 | 25381059 | |
| 408 | Phosphorylation | GTKGLAISFVSSKED CCCCEEEEEECCCCC | 17.62 | 27017623 | |
| 411 | Phosphorylation | GLAISFVSSKEDEEV CEEEEEECCCCCHHH | 33.41 | 27017623 |
| 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 SUB2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SUB2_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 SUB2_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 TYR-12; SER-13; SER-37;SER-55 AND THR-169, AND MASS SPECTROMETRY. | |
| "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-55 AND SER-61, AND MASSSPECTROMETRY. | |
| "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 SER-13, 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 THR-36, AND MASSSPECTROMETRY. | |
