UniProt ID | SPT6_YEAST | |
---|---|---|
UniProt AC | P23615 | |
Protein Name | Transcription elongation factor SPT6 | |
Gene Name | SPT6 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1451 | |
Subcellular Localization | Nucleus . Colocalizes with RNA polymerase II on chromatin. Recruited to the active transcribed loci. | |
Protein Description | Plays a role in maintenance of chromatin structure during RNA polymerase II transcription elongation thereby repressing transcription initiation from cryptic promoters. Mediates the reassembly of nucleosomes onto the promoters of at least a selected set of genes during repression; the nucleosome reassembly is essential for transcriptional repression. Essential for viability.. | |
Protein Sequence | MEETGDSKLVPRDEEEIVNDNDETKAPSEEEEGEDVFDSSEEDEDIDEDEDEARKVQEGFIVNDDDENEDPGTSISKKRRKHKRREREEDDRLSEDDLDLLMENAGVERTKASSSSGKFKRLKRVGDEGNAAESESDNVAASRQDSTSKLEDFFSEDEEEEESGLRNGRNNEYGRDEEDHENRNRTADKGGILDELDDFIEDDEFSDEDDETRQRRIQEKKLLREQSIKQPTQITGLSSDKIDEMYDIFGDGHDYDWALEIENEELENGNDNNEAEEEEIDEETGAIKSTKKKISLQDIYDLEDLKKNLMTEGDMKIRKTDIPERYQELRAGITDYGNMSSEDQELERNWIAEKISVDKNFDANYDLTEFKEAIGNAIKFITKENLEVPFIYAYRRNYISSREKDGFLLTEDDLWDIVSLDIEFHSLVNKKDYVQRFYAELHIDDPIVTEYFKNQNTASIAELNSLQDIYDYLEFKYANEINEMFINHTGKTGKKHLKNSSYEKFKASPLYQAVSDIGISAEDVGENISSQHQIHPPVDHPSSKPVEVIESILNANSGDLQVFTSNTKLAIDTVQKYYSLELSKNTKIREKVRSDFSKYYLADVVLTAKGKKEIQKGSLYEDIKYAINRTPMHFRRDPDVFLKMVEAESLNLLSVKLHMSSQAQYIEHLFQIALETTNTSDIAIEWNNFRKLAFNQAMDKIFQDISQEVKDNLTKNCQKLVAKTVRHKFMTKLDQAPFIPNVRDPKIPKILSLTCGQGRFGADAIIAVYVNRKGDFIRDYKIVDNPFDKTNPEKFEDTLDNIIQSCQPNAIGINGPNPKTQKFYKRLQEVLHKKQIVDSRGHTIPIIYVEDEVAIRYQNSERAAQEFPNKPPLVKYCIALARYMHSPLLEYANLTSEEVRSLSIHPHQNLLSSEQLSWALETAFVDIVNLVSVEVNKATDNNYYASALKYISGFGKRKAIDFLQSLQRLNEPLLARQQLITHNILHKTIFMNSAGFLYISWNEKRQKYEDLEHDQLDSTRIHPEDYHLATKVAADALEYDPDTIAEKEEQGTMSEFIELLREDPDRRAKLESLNLESYAEELEKNTGLRKLNNLNTIVLELLDGFEELRNDFHPLQGDEIFQSLTGESEKTFFKGSIIPVRVERFWHNDIICTTNSEVECVVNAQRHAGAQLRRPANEIYEIGKTYPAKVIYIDYANITAEVSLLDHDVKQQYVPISYSKDPSIWDLKQELEDAEEERKLMMAEARAKRTHRVINHPYYFPFNGRQAEDYLRSKERGEFVIRQSSRGDDHLVITWKLDKDLFQHIDIQELEKENPLALGKVLIVDNQKYNDLDQIIVEYLQNKVRLLNEMTSSEKFKSGTKKDVVKFIEDYSRVNPNKSVYYFSLNHDNPGWFYLMFKINANSKLYTWNVKLTNTGYFLVNYNYPSVIQLCNGFKTLLKSNSSKNRMNNYR | |
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 |
---|---|---|---|---|---|
8 | Acetylation | MEETGDSKLVPRDEE CCCCCCCCCCCCCHH | 59.24 | 25381059 | |
24 | Phosphorylation | IVNDNDETKAPSEEE HCCCCCCCCCCCHHH | 35.06 | 19823750 | |
28 | Phosphorylation | NDETKAPSEEEEGED CCCCCCCCHHHCCCC | 63.60 | 19823750 | |
39 | Phosphorylation | EGEDVFDSSEEDEDI CCCCCCCCCCCCCCC | 28.34 | 19795423 | |
40 | Phosphorylation | GEDVFDSSEEDEDID CCCCCCCCCCCCCCC | 47.02 | 19795423 | |
73 | Phosphorylation | DENEDPGTSISKKRR CCCCCCCCCHHHHHH | 28.42 | 30377154 | |
74 | Phosphorylation | ENEDPGTSISKKRRK CCCCCCCCHHHHHHH | 30.68 | 23749301 | |
76 | Phosphorylation | EDPGTSISKKRRKHK CCCCCCHHHHHHHHH | 31.71 | 28889911 | |
94 | Phosphorylation | REEDDRLSEDDLDLL HHHHHCCCHHHHHHH | 39.61 | 22369663 | |
110 | Phosphorylation | ENAGVERTKASSSSG HHCCCCCCCCCCCCC | 19.91 | 27017623 | |
111 | Acetylation | NAGVERTKASSSSGK HCCCCCCCCCCCCCC | 53.12 | 25381059 | |
116 | Phosphorylation | RTKASSSSGKFKRLK CCCCCCCCCCCEECE | 48.20 | 27017623 | |
118 | Acetylation | KASSSSGKFKRLKRV CCCCCCCCCEECEEC | 50.05 | 24489116 | |
120 | Acetylation | SSSSGKFKRLKRVGD CCCCCCCEECEECCC | 61.38 | 25381059 | |
134 | Phosphorylation | DEGNAAESESDNVAA CCCCCCCCCCCCCCH | 37.36 | 22369663 | |
136 | Phosphorylation | GNAAESESDNVAASR CCCCCCCCCCCCHHC | 43.71 | 22369663 | |
142 | Phosphorylation | ESDNVAASRQDSTSK CCCCCCHHCCCCCHH | 22.27 | 22890988 | |
146 | Phosphorylation | VAASRQDSTSKLEDF CCHHCCCCCHHHHHH | 26.66 | 22369663 | |
147 | Phosphorylation | AASRQDSTSKLEDFF CHHCCCCCHHHHHHC | 37.86 | 20377248 | |
148 | Phosphorylation | ASRQDSTSKLEDFFS HHCCCCCHHHHHHCC | 38.91 | 22369663 | |
155 | Phosphorylation | SKLEDFFSEDEEEEE HHHHHHCCCCHHHHH | 44.10 | 22369663 | |
163 | Phosphorylation | EDEEEEESGLRNGRN CCHHHHHHCCCCCCC | 46.54 | 22369663 | |
186 | Phosphorylation | DHENRNRTADKGGIL HHCCCCCCCCCCCHH | 42.64 | 26447709 | |
206 | Phosphorylation | FIEDDEFSDEDDETR HHCCCCCCCCCHHHH | 37.73 | 22369663 | |
212 | Phosphorylation | FSDEDDETRQRRIQE CCCCCHHHHHHHHHH | 38.81 | 22369663 | |
227 | Phosphorylation | KKLLREQSIKQPTQI HHHHHHCCCCCCCCC | 27.31 | 28889911 | |
229 | Acetylation | LLREQSIKQPTQITG HHHHCCCCCCCCCCC | 56.31 | 22865919 | |
232 | Phosphorylation | EQSIKQPTQITGLSS HCCCCCCCCCCCCCH | 30.06 | 21126336 | |
235 | Phosphorylation | IKQPTQITGLSSDKI CCCCCCCCCCCHHHH | 23.42 | 22369663 | |
238 | Phosphorylation | PTQITGLSSDKIDEM CCCCCCCCHHHHHHH | 37.52 | 22369663 | |
239 | Phosphorylation | TQITGLSSDKIDEMY CCCCCCCHHHHHHHH | 48.22 | 22369663 | |
295 | Phosphorylation | KSTKKKISLQDIYDL CCCCCCCCHHHHCCH | 28.94 | 22369663 | |
300 | Phosphorylation | KISLQDIYDLEDLKK CCCHHHHCCHHHHHH | 23.82 | 22369663 | |
340 | Phosphorylation | ITDYGNMSSEDQELE CCCCCCCCHHHHHHH | 34.28 | 27017623 | |
341 | Phosphorylation | TDYGNMSSEDQELER CCCCCCCHHHHHHHH | 34.13 | 27017623 | |
354 | Ubiquitination | ERNWIAEKISVDKNF HHHCHHHHHCCCCCC | 31.12 | 24961812 | |
379 | Acetylation | EAIGNAIKFITKENL HHHHHHHHHHCCCCC | 28.44 | 24489116 | |
491 | Acetylation | MFINHTGKTGKKHLK HHHCCCCCCCCHHHC | 56.08 | 24489116 | |
576 | Acetylation | LAIDTVQKYYSLELS EEHHHHHHHHHHHCC | 41.65 | 24489116 | |
746 | Acetylation | IPNVRDPKIPKILSL CCCCCCCCCCCEEEE | 75.76 | 24489116 | |
749 | Acetylation | VRDPKIPKILSLTCG CCCCCCCCEEEEECC | 60.80 | 24489116 | |
781 | Acetylation | GDFIRDYKIVDNPFD CCCCEECCCCCCCCC | 40.31 | 24489116 | |
824 | Phosphorylation | NPKTQKFYKRLQEVL CHHHHHHHHHHHHHH | 11.39 | 28889911 | |
876 | Phosphorylation | NKPPLVKYCIALARY CCCHHHHHHHHHHHH | 5.00 | 28889911 | |
883 | Phosphorylation | YCIALARYMHSPLLE HHHHHHHHHCCHHHH | 8.12 | 28889911 | |
886 | Phosphorylation | ALARYMHSPLLEYAN HHHHHHCCHHHHHCC | 10.74 | 28889911 | |
891 | Phosphorylation | MHSPLLEYANLTSEE HCCHHHHHCCCCHHH | 10.76 | 28889911 | |
895 | Phosphorylation | LLEYANLTSEEVRSL HHHHCCCCHHHHHHC | 33.62 | 28889911 | |
949 | Acetylation | NYYASALKYISGFGK CHHHHHHHHHHCCCH | 40.01 | 24489116 | |
1007 | Acetylation | SWNEKRQKYEDLEHD ECCHHHHHHHCCCCC | 55.42 | 24489116 | |
1134 | Acetylation | ESEKTFFKGSIIPVR CCCCCEECCCEEEEE | 47.78 | 22865919 | |
1239 | Acetylation | EDAEEERKLMMAEAR HHHHHHHHHHHHHHH | 43.97 | 25381059 | |
1355 | Acetylation | NEMTSSEKFKSGTKK HHCCCCCHHCCCCHH | 61.10 | 24489116 | |
1355 | Ubiquitination | NEMTSSEKFKSGTKK HHCCCCCHHCCCCHH | 61.10 | 23749301 |
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 SPT6_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPT6_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 SPT6_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-28; SER-76; SER-94;SER-134; SER-136; SER-148; SER-155 AND SER-206, 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-94; SER-134; SER-136;SER-146 AND SER-155, 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-94, 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-94; SER-134; SER-136;SER-155 AND SER-206, AND MASS SPECTROMETRY. |