| UniProt ID | SSN2_YEAST | |
|---|---|---|
| UniProt AC | P38931 | |
| Protein Name | Mediator of RNA polymerase II transcription subunit 13 | |
| Gene Name | SSN2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1420 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II RPB1 at serines 2 and 5.. | |
| Protein Sequence | MSSDASTYRLEDVLSSFYRVEKIKKINYHQYISKAQNDQWSIQMEFMLRKQDPKTLVALLSRDLWCFSINDDPVPTPPAIEHKPVSPDKIGTFTADYSKPNLPPHYALFLKALRRKIYINLALGSHNKLIQFGNACISLSGVPNYLVQLEPHLFVNGDLTVSLCAKNMGLVPMKEENLEESFLSKHALYLAPSGIRMHLAPASKQGYLITPPKHTELLLTTLSVSHGINLQNKKNLKWVAVVPDLGHLNGHTPTIASYLTPLLEAKKLVWPLHLIFAQPVADIENSTSGDPSEFHCLQDALDAIDDFIQLKQTAAYRTPGSSGVLSSNIAGTNPLSSDGAYTEQFQHYKNNSISSQPASYHSVQETNKISPKDFSPNFTGIDKLMLSPSDQFAPAFLNTPNNNINENELFNDRKQTTVSNDLENSPLKTELEANGRSLEKVNNSVSKTGSVDTLHNKEGTLEQREQNENLPSDKSDSMVDKELFGEDEDEDLFGDSNKSNSTNESNKSISDEITEDMFEMSDEEENNNNKSINKNNKEMHTDLGKDIPFFPSSEKPNIRTMSGTTKRLNGKRKYLDIPIDEMTLPTSPLYMDPGAPLPVETPRDRRKSVFAPLNFNPIIENNVDNKYKSGGKFSFSPLQKEEALNFDISMADLSSSEEEEDEEENGSSDEDLKSLNVRDDMKPSDNISTNTNIHEPQYINYSSIPSLQDSIIKQENFNSVNDANITSNKEGFNSIWKIPQNDIPQTESPLKTVDSSIQPIESNIKMTLEDNNVTSNPSEFTPNMVNSEISNLPKDKSGIPEFTPADPNLSFESSSSLPFLLRHMPLASIPDIFITPTPVVTISEKEQDILDLIAEQVVTDYNILGNLGIPKIAYRGVKDCQEGLITTTMLQLFSTFDRLNGNDTISKFYNMKQPYVFVKKHHELIKVKHDSQPFIKFLNFRPPNGIKNFKSLLLSSSFKEDCLSFAPTLSQTYINQELGFCELLKLTNEDPPGLMYLKAFDKNKLLLLAAQIVSYCSNNKNSIKNVPPILIILPLDNATLTELVDKANIFQVIKNEVCAKMPNIELYLKVIPMDFIRNVLVTVDQYVNVAISIYNMLPPKSVKFTHIAHTLPEKVNFRTMQQQQMQQQQQQQQQQQNNSTGSSSIIYYDSYIHLAYSRSVDKEWVFAALSDSYGQGSMTKTWYVGNSRGKFDDACNQIWNIALNLASKKFGKICLILTRLNGILPDDELMNWRRLSGRNIHLAVVCVDDNSKISFIDEDKLYPSFKPIYKDTRFGGRMDMTRLYDYEIRDIDQDIHGIVFQHPFPLAHSQHRCAIRSGALIKFKKCDGDTVWDKFAVNLLNCPHSDSTQLLETILEEFRNLAALNVWYGLSDGEDGHIPWHILAVKKMMNTLVHTRVKIANTSAATVHTATSSSIILSDK | |
| 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 |
|---|---|---|---|---|---|
| 61 | Phosphorylation | KTLVALLSRDLWCFS HHHHHHHHCCEEEEE | 25.30 | 27017623 | |
| 316 | Phosphorylation | QLKQTAAYRTPGSSG HHHHHHHCCCCCCCC | 16.74 | 21440633 | |
| 318 | Phosphorylation | KQTAAYRTPGSSGVL HHHHHCCCCCCCCCC | 21.23 | 21551504 | |
| 336 | Phosphorylation | IAGTNPLSSDGAYTE CCCCCCCCCCCCCHH | 27.86 | 27017623 | |
| 341 | Phosphorylation | PLSSDGAYTEQFQHY CCCCCCCCHHHHHHH | 19.15 | 28889911 | |
| 352 | Phosphorylation | FQHYKNNSISSQPAS HHHHHCCCCCCCCCC | 32.99 | 23749301 | |
| 355 | Phosphorylation | YKNNSISSQPASYHS HHCCCCCCCCCCCCC | 38.21 | 23749301 | |
| 359 | Phosphorylation | SISSQPASYHSVQET CCCCCCCCCCCHHHC | 30.02 | 21440633 | |
| 360 | Phosphorylation | ISSQPASYHSVQETN CCCCCCCCCCHHHCC | 10.54 | 20377248 | |
| 362 | Phosphorylation | SQPASYHSVQETNKI CCCCCCCCHHHCCCC | 19.77 | 20377248 | |
| 366 | Phosphorylation | SYHSVQETNKISPKD CCCCHHHCCCCCCCC | 25.40 | 21440633 | |
| 370 | Phosphorylation | VQETNKISPKDFSPN HHHCCCCCCCCCCCC | 27.75 | 17330950 | |
| 375 | Phosphorylation | KISPKDFSPNFTGID CCCCCCCCCCCCCCC | 29.12 | 22369663 | |
| 379 | Phosphorylation | KDFSPNFTGIDKLML CCCCCCCCCCCEEEC | 39.61 | 28889911 | |
| 387 | Phosphorylation | GIDKLMLSPSDQFAP CCCEEECCCHHHCCH | 14.37 | 21440633 | |
| 389 | Phosphorylation | DKLMLSPSDQFAPAF CEEECCCHHHCCHHH | 40.44 | 21440633 | |
| 399 | Phosphorylation | FAPAFLNTPNNNINE CCHHHHCCCCCCCCH | 29.55 | 21440633 | |
| 419 | Phosphorylation | DRKQTTVSNDLENSP CCCCCCCCCCCCCCC | 23.64 | 21440633 | |
| 425 | Phosphorylation | VSNDLENSPLKTELE CCCCCCCCCCCHHHH | 23.41 | 22369663 | |
| 429 | Phosphorylation | LENSPLKTELEANGR CCCCCCCHHHHHHCC | 54.18 | 22369663 | |
| 437 | Phosphorylation | ELEANGRSLEKVNNS HHHHHCCCHHHHHCC | 42.13 | 21551504 | |
| 444 | Phosphorylation | SLEKVNNSVSKTGSV CHHHHHCCCCCCCCC | 23.67 | 17563356 | |
| 446 | Phosphorylation | EKVNNSVSKTGSVDT HHHHCCCCCCCCCHH | 25.07 | 21440633 | |
| 448 | Phosphorylation | VNNSVSKTGSVDTLH HHCCCCCCCCCHHCC | 27.47 | 22369663 | |
| 450 | Phosphorylation | NSVSKTGSVDTLHNK CCCCCCCCCHHCCCC | 23.27 | 22369663 | |
| 453 | Phosphorylation | SKTGSVDTLHNKEGT CCCCCCHHCCCCCCC | 27.97 | 22369663 | |
| 460 | Phosphorylation | TLHNKEGTLEQREQN HCCCCCCCHHHHHHH | 28.36 | 21551504 | |
| 472 | Phosphorylation | EQNENLPSDKSDSMV HHHCCCCCCCHHHHH | 61.92 | 20377248 | |
| 475 | Phosphorylation | ENLPSDKSDSMVDKE CCCCCCCHHHHHCHH | 39.65 | 20377248 | |
| 477 | Phosphorylation | LPSDKSDSMVDKELF CCCCCHHHHHCHHHH | 28.00 | 21440633 | |
| 521 | Phosphorylation | TEDMFEMSDEEENNN HHHHHHCCHHHHCCC | 34.37 | 28889911 | |
| 583 | Phosphorylation | DIPIDEMTLPTSPLY CCCCCCCCCCCCCCC | 27.77 | 21440633 | |
| 586 | Phosphorylation | IDEMTLPTSPLYMDP CCCCCCCCCCCCCCC | 46.20 | 21440633 | |
| 587 | Phosphorylation | DEMTLPTSPLYMDPG CCCCCCCCCCCCCCC | 15.80 | 21440633 | |
| 590 | Phosphorylation | TLPTSPLYMDPGAPL CCCCCCCCCCCCCCC | 11.67 | 24961812 | |
| 601 | Phosphorylation | GAPLPVETPRDRRKS CCCCCCCCCCCCCCC | 24.69 | 21440633 | |
| 608 | Phosphorylation | TPRDRRKSVFAPLNF CCCCCCCCCCCCCCC | 22.21 | 25533186 | |
| 632 | Acetylation | NKYKSGGKFSFSPLQ CCCCCCCCCCCCCCC | 41.16 | 24489116 | |
| 636 | Phosphorylation | SGGKFSFSPLQKEEA CCCCCCCCCCCHHHH | 24.41 | 22369663 | |
| 674 | Phosphorylation | SSDEDLKSLNVRDDM CCHHHHHHCCCCCCC | 32.26 | 20377248 | |
| 703 | Phosphorylation | PQYINYSSIPSLQDS CCCCCHHCCCHHHHH | 28.32 | 28889911 | |
| 746 | Phosphorylation | PQNDIPQTESPLKTV CCCCCCCCCCCCCCC | 32.83 | 25752575 | |
| 748 | Phosphorylation | NDIPQTESPLKTVDS CCCCCCCCCCCCCCC | 38.63 | 22369663 | |
| 828 | Phosphorylation | LRHMPLASIPDIFIT HHCCCHHHCCCEEEC | 42.19 | 23749301 | |
| 835 | Phosphorylation | SIPDIFITPTPVVTI HCCCEEECCCCEEEC | 15.45 | 23749301 | |
| 906 | Phosphorylation | LNGNDTISKFYNMKQ HCCCCCHHHHHCCCC | 20.85 | 27017623 | |
| 1181 | Phosphorylation | GQGSMTKTWYVGNSR CCCCCEEEEEECCCC | 16.92 | 22890988 | |
| 1183 | Phosphorylation | GSMTKTWYVGNSRGK CCCEEEEEECCCCCC | 12.05 | 22890988 | |
| 1187 | Phosphorylation | KTWYVGNSRGKFDDA EEEEECCCCCCCHHH | 36.16 | 22890988 | |
| 1236 | Phosphorylation | LMNWRRLSGRNIHLA HHCHHHHCCCCEEEE | 33.62 | 28889911 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 608 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
| 608 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 608 | S | Phosphorylation |
| 15225552 |
* 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 SSN2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-375; SER-425; SER-587;SER-636; SER-703 AND SER-748, 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-425; SER-444; SER-450AND THR-453, AND MASS 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 SER-370 AND SER-375, ANDMASS SPECTROMETRY. | |
| "The Ras/PKA signaling pathway directly targets the Srb9 protein, acomponent of the general RNA polymerase II transcription apparatus."; Chang Y.-W., Howard S.C., Herman P.K.; Mol. Cell 15:107-116(2004). Cited for: FUNCTION, PHOSPHORYLATION AT SER-608 BY PKA, AND MUTAGENESIS OFSER-608 AND SER-1236. | |
