| UniProt ID | CHD1_YEAST | |
|---|---|---|
| UniProt AC | P32657 | |
| Protein Name | Chromo domain-containing protein 1 | |
| Gene Name | CHD1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1468 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. It recognizes H3K4me. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. Acts in opposition to the FACT complex in regulating polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the pol I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome.. | |
| Protein Sequence | MAAKDISTEVLQNPELYGLRRSHRAAAHQQNYFNDSDDEDDEDNIKQSRRKRMTTIEDDEDEFEDEEGEEDSGEDEDEEDFEEDDDYYGSPIKQNRSKPKSRTKSKSKSKPKSQSEKQSTVKIPTRFSNRQNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVHEASANPQPEDFHGIDIVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLKRLDNYCKQFIIEDQQVRLDPYVTAEDIEIMDMERERRLDEFEEFHVPERIIDSQRASLEDGTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPRFEKLSVQPPFIKGGELRDFQLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFISWLIFARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGKKTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLITGTPLQNNIKELAALVNFLMPGRFTIDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKKDVEKSLPSKTERILRVELSDVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASNHPYLFDNAEERVLQKFGDGKMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVLIFSQMVRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINLMTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILEYAIISLGVTDGNKYTKKNEPNAGELSAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAEDHVTTPDLGESHLGGEEFLKQFEVTDYKADIDWDDIIPEEELKKLQDEEQKRKDEEYVKEQLEMMNRRDNALKKIKNSVNGDGTAANSDSDDDSTSRSSRRRARANDMDSIGESEVRALYKAILKFGNLKEILDELIADGTLPVKSFEKYGETYDEMMEAAKDCVHEEEKNRKEILEKLEKHATAYRAKLKSGEIKAENQPKDNPLTRLSLKKREKKAVLFNFKGVKSLNAESLLSRVEDLKYLKNLINSNYKDDPLKFSLGNNTPKPVQNWSSNWTKEEDEKLLIGVFKYGYGSWTQIRDDPFLGITDKIFLNEVHNPVAKKSASSSDTTPTPSKKGKGITGSSKKVPGAIHLGRRVDYLLSFLRGGLNTKSPSADIGSKKLPTGPSKKRQRKPANHSKSMTPEITSSEPANGPPSKRMKALPKGPAALINNTRLSPNSPTPPLKSKVSRDNGTRQSSNPSSGSAHEKEYDSMDEEDCRHTMSAIRTSLKRLRRGGKSLDRKEWAKILKTELTTIGNHIESQKGSSRKASPEKYRKHLWSYSANFWPADVKSTKLMAMYDKITESQKK | |
| 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 |
|---|---|---|---|---|---|
| 4 | Acetylation | ----MAAKDISTEVL ----CCCCCCCHHHH | 63.76 | 24489116 | |
| 7 | Phosphorylation | -MAAKDISTEVLQNP -CCCCCCCHHHHHCH | 28.75 | 27214570 | |
| 8 | Phosphorylation | MAAKDISTEVLQNPE CCCCCCCHHHHHCHH | 30.37 | 27214570 | |
| 32 | Phosphorylation | AAAHQQNYFNDSDDE HHHHHCCCCCCCCCC | 10.22 | 22890988 | |
| 36 | Phosphorylation | QQNYFNDSDDEDDED HCCCCCCCCCCCCCC | 48.33 | 22369663 | |
| 48 | Phosphorylation | DEDNIKQSRRKRMTT CCCHHHHHHHHCCCC | 29.11 | 28889911 | |
| 54 | Phosphorylation | QSRRKRMTTIEDDED HHHHHCCCCCCCCCH | 28.75 | 19823750 | |
| 55 | Phosphorylation | SRRKRMTTIEDDEDE HHHHCCCCCCCCCHH | 17.02 | 19823750 | |
| 72 | Phosphorylation | DEEGEEDSGEDEDEE CCCCCCCCCCCCCHH | 47.57 | 28889911 | |
| 87 | Phosphorylation | DFEEDDDYYGSPIKQ HCCCCCCCCCCCCCC | 19.40 | 19823750 | |
| 88 | Phosphorylation | FEEDDDYYGSPIKQN CCCCCCCCCCCCCCC | 20.37 | 19823750 | |
| 90 | Phosphorylation | EDDDYYGSPIKQNRS CCCCCCCCCCCCCCC | 13.82 | 19823750 | |
| 117 | Acetylation | KPKSQSEKQSTVKIP CCCCCCCCCCCEECC | 55.59 | 25381059 | |
| 221 | Phosphorylation | LIKWTDESHLHNTWE EEEECCHHHCCCCHH | 33.87 | 27017623 | |
| 229 | Phosphorylation | HLHNTWETYESIGQV HCCCCHHHHHHHHHH | 24.93 | 27017623 | |
| 232 | Phosphorylation | NTWETYESIGQVRGL CCHHHHHHHHHHHCH | 22.93 | 27017623 | |
| 352 | Phosphorylation | KILPQYSSNYTSQRP CCCCCCCCCCCCCCC | 28.99 | 27017623 | |
| 504 | Phosphorylation | KDRAELGSIKWQFMA HCHHHHCCCEEEEEE | 33.35 | 28889911 | |
| 533 | Acetylation | YESLNSFKVANRMLI HHHHHHHHHHCEEEC | 40.01 | 24489116 | |
| 605 | Phosphorylation | LKKDVEKSLPSKTER HHHHHHHHCCCCCHH | 31.82 | 28889911 | |
| 608 | Phosphorylation | DVEKSLPSKTERILR HHHHHCCCCCHHEEE | 58.46 | 21551504 | |
| 610 | Phosphorylation | EKSLPSKTERILRVE HHHCCCCCHHEEEEE | 34.53 | 21551504 | |
| 619 | Phosphorylation | RILRVELSDVQTEYY HEEEEEHHHHCHHHH | 23.41 | 21551504 | |
| 693 | Phosphorylation | VLRGLIMSSGKMVLL HHHHHHHCCCCCHHH | 29.01 | 21551504 | |
| 694 | Phosphorylation | LRGLIMSSGKMVLLD HHHHHHCCCCCHHHH | 25.67 | 22369663 | |
| 705 | Phosphorylation | VLLDQLLTRLKKDGH HHHHHHHHHHHHCCC | 42.41 | 22369663 | |
| 730 | Phosphorylation | MLDILGDYLSIKGIN HHHHHHHHHEECCCC | 10.68 | 28889911 | |
| 732 | Phosphorylation | DILGDYLSIKGINFQ HHHHHHHEECCCCCE | 18.94 | 28889911 | |
| 903 | Phosphorylation | NHAEDHVTTPDLGES HHHHHCCCCCCCCCC | 29.23 | 21440633 | |
| 904 | Phosphorylation | HAEDHVTTPDLGESH HHHHCCCCCCCCCCC | 17.45 | 25521595 | |
| 910 | Phosphorylation | TTPDLGESHLGGEEF CCCCCCCCCCCHHHH | 23.39 | 25521595 | |
| 972 | Acetylation | NRRDNALKKIKNSVN HHHHHHHHHHHHHCC | 50.47 | 25381059 | |
| 977 | Phosphorylation | ALKKIKNSVNGDGTA HHHHHHHHCCCCCCC | 16.38 | 23749301 | |
| 983 | Phosphorylation | NSVNGDGTAANSDSD HHCCCCCCCCCCCCC | 27.60 | 22369663 | |
| 987 | Phosphorylation | GDGTAANSDSDDDST CCCCCCCCCCCCCCC | 33.49 | 22369663 | |
| 989 | Phosphorylation | GTAANSDSDDDSTSR CCCCCCCCCCCCCCH | 42.64 | 22369663 | |
| 993 | Phosphorylation | NSDSDDDSTSRSSRR CCCCCCCCCCHHHHH | 34.96 | 22369663 | |
| 994 | Phosphorylation | SDSDDDSTSRSSRRR CCCCCCCCCHHHHHH | 34.84 | 19779198 | |
| 995 | Phosphorylation | DSDDDSTSRSSRRRA CCCCCCCCHHHHHHH | 33.83 | 23749301 | |
| 998 | Phosphorylation | DDSTSRSSRRRARAN CCCCCHHHHHHHHHH | 28.79 | 21551504 | |
| 1020 | Acetylation | SEVRALYKAILKFGN HHHHHHHHHHHHHCC | 29.78 | 24489116 | |
| 1024 | Acetylation | ALYKAILKFGNLKEI HHHHHHHHHCCHHHH | 45.15 | 24489116 | |
| 1077 | Acetylation | NRKEILEKLEKHATA HHHHHHHHHHHHHHH | 59.51 | 24489116 | |
| 1144 | Ubiquitination | VEDLKYLKNLINSNY HHHHHHHHHHHHCCC | 46.77 | 12872131 | |
| 1152 | Acetylation | NLINSNYKDDPLKFS HHHHCCCCCCCCEEE | 60.96 | 24489116 | |
| 1159 | Phosphorylation | KDDPLKFSLGNNTPK CCCCCEEECCCCCCC | 33.51 | 24961812 | |
| 1164 | Phosphorylation | KFSLGNNTPKPVQNW EEECCCCCCCCCCCC | 36.37 | 27214570 | |
| 1223 | Phosphorylation | HNPVAKKSASSSDTT CCCCCCCCCCCCCCC | 32.45 | 27017623 | |
| 1225 | Phosphorylation | PVAKKSASSSDTTPT CCCCCCCCCCCCCCC | 37.15 | 27214570 | |
| 1226 | Phosphorylation | VAKKSASSSDTTPTP CCCCCCCCCCCCCCC | 31.76 | 21440633 | |
| 1227 | Phosphorylation | AKKSASSSDTTPTPS CCCCCCCCCCCCCCC | 36.16 | 28889911 | |
| 1229 | Phosphorylation | KSASSSDTTPTPSKK CCCCCCCCCCCCCCC | 36.30 | 23749301 | |
| 1230 | Phosphorylation | SASSSDTTPTPSKKG CCCCCCCCCCCCCCC | 30.10 | 23749301 | |
| 1232 | Phosphorylation | SSSDTTPTPSKKGKG CCCCCCCCCCCCCCC | 37.79 | 23749301 | |
| 1234 | Phosphorylation | SDTTPTPSKKGKGIT CCCCCCCCCCCCCCC | 49.86 | 28889911 | |
| 1270 | Phosphorylation | FLRGGLNTKSPSADI HHHCCCCCCCCCCCC | 37.63 | 21440633 | |
| 1272 | Phosphorylation | RGGLNTKSPSADIGS HCCCCCCCCCCCCCC | 23.27 | 17330950 | |
| 1274 | Phosphorylation | GLNTKSPSADIGSKK CCCCCCCCCCCCCCC | 45.74 | 28152593 | |
| 1280 | Acetylation | PSADIGSKKLPTGPS CCCCCCCCCCCCCCC | 53.79 | 24489116 | |
| 1281 | Acetylation | SADIGSKKLPTGPSK CCCCCCCCCCCCCCH | 62.49 | 24489116 | |
| 1284 | Phosphorylation | IGSKKLPTGPSKKRQ CCCCCCCCCCCHHCC | 72.64 | 19823750 | |
| 1287 | Phosphorylation | KKLPTGPSKKRQRKP CCCCCCCCHHCCCCC | 52.75 | 19823750 | |
| 1300 | Phosphorylation | KPANHSKSMTPEITS CCCCCCCCCCCCCCC | 30.79 | 22369663 | |
| 1302 | Phosphorylation | ANHSKSMTPEITSSE CCCCCCCCCCCCCCC | 25.51 | 22369663 | |
| 1306 | Phosphorylation | KSMTPEITSSEPANG CCCCCCCCCCCCCCC | 25.25 | 22369663 | |
| 1307 | Phosphorylation | SMTPEITSSEPANGP CCCCCCCCCCCCCCC | 38.06 | 22369663 | |
| 1308 | Phosphorylation | MTPEITSSEPANGPP CCCCCCCCCCCCCCC | 38.66 | 22369663 | |
| 1316 | Phosphorylation | EPANGPPSKRMKALP CCCCCCCCCCCCCCC | 35.71 | 22369663 | |
| 1333 | Phosphorylation | PAALINNTRLSPNSP CCCEECCCCCCCCCC | 28.62 | 22369663 | |
| 1336 | Phosphorylation | LINNTRLSPNSPTPP EECCCCCCCCCCCCC | 20.81 | 22369663 | |
| 1339 | Phosphorylation | NTRLSPNSPTPPLKS CCCCCCCCCCCCCCC | 33.27 | 22369663 | |
| 1341 | Phosphorylation | RLSPNSPTPPLKSKV CCCCCCCCCCCCCCC | 37.04 | 22369663 | |
| 1349 | Phosphorylation | PPLKSKVSRDNGTRQ CCCCCCCCCCCCCCC | 37.34 | 19823750 | |
| 1354 | Phosphorylation | KVSRDNGTRQSSNPS CCCCCCCCCCCCCCC | 31.61 | 19823750 | |
| 1357 | Phosphorylation | RDNGTRQSSNPSSGS CCCCCCCCCCCCCCC | 28.88 | 23749301 | |
| 1358 | Phosphorylation | DNGTRQSSNPSSGSA CCCCCCCCCCCCCCC | 44.41 | 17287358 | |
| 1361 | Phosphorylation | TRQSSNPSSGSAHEK CCCCCCCCCCCCCHH | 52.13 | 23749301 | |
| 1362 | Phosphorylation | RQSSNPSSGSAHEKE CCCCCCCCCCCCHHH | 37.72 | 23749301 | |
| 1364 | Phosphorylation | SSNPSSGSAHEKEYD CCCCCCCCCCHHHCC | 28.53 | 17287358 | |
| 1370 | Phosphorylation | GSAHEKEYDSMDEED CCCCHHHCCCCCHHH | 25.12 | 22890988 | |
| 1372 | Phosphorylation | AHEKEYDSMDEEDCR CCHHHCCCCCHHHHH | 27.51 | 21551504 | |
| 1397 | Acetylation | KRLRRGGKSLDRKEW HHHHCCCCCCCHHHH | 51.15 | 25381059 |
| 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 CHD1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CHD1_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 CHD1_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-36; THR-904; SER-987;SER-989; SER-1272; SER-1300; THR-1302; SER-1336 AND SER-1372, 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 SER-36; SER-987; SER-989;THR-1302; SER-1336 AND SER-1372, 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-1358 AND SER-1364, 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-36, AND MASSSPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-987 AND SER-989, ANDMASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1341, AND MASSSPECTROMETRY. | |
| 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-1144, AND MASSSPECTROMETRY. | |
