UniProt ID | CTR9_YEAST | |
---|---|---|
UniProt AC | P89105 | |
Protein Name | RNA polymerase-associated protein CTR9 | |
Gene Name | CTR9 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1077 | |
Subcellular Localization | Nucleus, nucleoplasm . | |
Protein Description | The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. In complex with PAF1, required for normal CLN1 and CLN2 G1 cyclin expression in late G1. Also has a role in chromosome segregation where it appears to be involved in microtubule placement.. | |
Protein Sequence | MTNAMKVEGYPSMEWPTSLDIPLKASEELVGIDLETDLPDDPTDLKTLLVEENSEKEHWLTIALAYCNHGKTNEGIKLIEMALDVFQNSERASLHTFLTWAHLNLAKGQSLSVETKEHELTQAELNLKDAIGFDPTWIGNMLATVELYYQRGHYDKALETSDLFVKSIHAEDHRSGRQSKPNCLFLLLRAKLLYQKKNYMASLKIFQELLVINPVLQPDPRIGIGLCFWQLKDSKMAIKSWQRALQLNPKNTSASILVLLGEFRESFTNSTNDKTFKEAFTKALSDLNNIFSENQHNPVLLTLLQTYYYFKGDYQTVLDIYHHRILKMSPMIAKIVLSESSFWCGRAHYALGDYRKSFIMFQESLKKNEDNLLAKLGLGQTQIKNNLLEESIITFENLYKTNESLQELNYILGMLYAGKAFDAKTAKNTSAKEQSNLNEKALKYLERYLKLTLATKNQLVISRAYLVISQLYELQNQYKTSLDYLSKALEEMEFIKKEIPLEVLNNLACYHFINGDFIKADDLFKQAKAKVSDKDESVNITLEYNIARTNEKNDCEKSESIYSQVTSLHPAYIAARIRNLYLKFAQSKIEDSDMSTEMNKLLDLNKSDLEIRSFYGWYLKNSKERKNNEKSTTHNKETLVKYNSHDAYALISLANLYVTIARDGKKSRNPKEQEKSKHSYLKAIQLYQKVLQVDPFNIFAAQGLAIIFAESKRLGPALEILRKVRDSLDNEDVQLNLAHCYLEMREYGKAIENYELVLKKFDNEKTRPHILNLLGRAWYARAIKERSVNFYQKALENAKTALDLFVKESSKSKFIHSVKFNIALLHFQIAETLRRSNPKFRTVQQIKDSLEGLKEGLELFRELNDLKEFNMIPKEELEQRIQLGETTMKSALERSLNEQEEFEKEQSAKIDEARKILEENELKEQGWMKQEEEARRLKLEKQAEEYRKLQDEAQKLIQEREAMAISEHNVKDDSDLSDKDNEYDEEKPRQKRKRSTKTKNSGESKRRKAAKKTLSDSDEDDDDVVKKPSHNKGKKSQLSNEFIEDSDEEEAQMSGSEQNKNDDNDENNDNDDNDGLF | |
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 |
---|---|---|---|---|---|
156 | Acetylation | YQRGHYDKALETSDL HHCCCHHHHHHHCCC | 47.94 | 24489116 | |
196 | Ubiquitination | RAKLLYQKKNYMASL HHHHHHHCCCHHHHH | 29.45 | 12872131 | |
270 | Phosphorylation | FRESFTNSTNDKTFK HHHHHCCCCCCHHHH | 26.06 | 28889911 | |
277 | Acetylation | STNDKTFKEAFTKAL CCCCHHHHHHHHHHH | 54.05 | 24489116 | |
435 | Phosphorylation | NTSAKEQSNLNEKAL CCCHHHHCCCCHHHH | 44.36 | 21440633 | |
496 | Acetylation | LEEMEFIKKEIPLEV HHHHHHHHCCCCHHH | 50.07 | 24489116 | |
583 | Acetylation | RIRNLYLKFAQSKIE HHHHHHHHHHHHHCC | 25.70 | 24489116 | |
606 | Acetylation | NKLLDLNKSDLEIRS HHHHCCCHHHHHHHH | 53.28 | 24489116 | |
642 | Phosphorylation | NKETLVKYNSHDAYA CHHHHEECCCHHHHH | 17.89 | 27738172 | |
644 | Phosphorylation | ETLVKYNSHDAYALI HHHEECCCHHHHHHH | 21.47 | 27738172 | |
648 | Phosphorylation | KYNSHDAYALISLAN ECCCHHHHHHHHHHH | 14.16 | 27738172 | |
682 | Acetylation | KSKHSYLKAIQLYQK HHHHHHHHHHHHHHH | 34.90 | 24489116 | |
759 | Acetylation | ENYELVLKKFDNEKT HCHHHHHHHCCCCCC | 43.87 | 24489116 | |
854 | Acetylation | KDSLEGLKEGLELFR HHHHHHHHHHHHHHH | 61.67 | 24489116 | |
867 | Acetylation | FRELNDLKEFNMIPK HHHHHHHHHCCCCCH | 64.22 | 24489116 | |
955 | Acetylation | KLQDEAQKLIQEREA HHHHHHHHHHHHHHH | 55.39 | 25381059 | |
966 | Phosphorylation | EREAMAISEHNVKDD HHHHHHHHHCCCCCC | 24.22 | 22369663 | |
974 | Phosphorylation | EHNVKDDSDLSDKDN HCCCCCCCCCCCCCC | 51.05 | 22369663 | |
977 | Phosphorylation | VKDDSDLSDKDNEYD CCCCCCCCCCCCCCC | 47.83 | 22369663 | |
983 | Phosphorylation | LSDKDNEYDEEKPRQ CCCCCCCCCCCCHHH | 34.60 | 21551504 | |
1013 | Phosphorylation | RRKAAKKTLSDSDED HHHHHHHHCCCCCCC | 30.68 | 19823750 | |
1015 | Phosphorylation | KAAKKTLSDSDEDDD HHHHHHCCCCCCCCC | 40.06 | 25521595 | |
1017 | Phosphorylation | AKKTLSDSDEDDDDV HHHHCCCCCCCCCCC | 39.25 | 25521595 | |
1036 | Phosphorylation | SHNKGKKSQLSNEFI CCCCCCHHHHCCCCC | 39.58 | 21440633 | |
1039 | Phosphorylation | KGKKSQLSNEFIEDS CCCHHHHCCCCCCCC | 27.03 | 21440633 | |
1046 | Phosphorylation | SNEFIEDSDEEEAQM CCCCCCCCHHHHHHH | 33.85 | 22369663 | |
1054 | Phosphorylation | DEEEAQMSGSEQNKN HHHHHHHCCCCCCCC | 27.38 | 22369663 | |
1056 | Phosphorylation | EEAQMSGSEQNKNDD HHHHHCCCCCCCCCC | 28.80 | 20377248 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of CTR9_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of CTR9_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 CTR9_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-974; SER-977; SER-1015AND SER-1017, 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-1015 AND SER-1017, ANDMASS 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-1015 AND SER-1017, 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 SER-966; SER-974; SER-977;SER-1015 AND SER-1017, AND MASS SPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-196, AND MASSSPECTROMETRY. |