| UniProt ID | RLF2_YEAST | |
|---|---|---|
| UniProt AC | Q12495 | |
| Protein Name | Chromatin assembly factor 1 subunit p90 | |
| Gene Name | RLF2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 606 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Acts as a component of chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto replicating DNA in vitro. It performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. p90 may facilitate the efficient and timely assembly of histones into telomeric chromatin.. | |
| Protein Sequence | MEQHLKSIPLQDDTKKKGILSFFQNTTTVKSNKFLTKEKDVITLDDPKEDVSGPMIETVKQETMKSINKECADEMKTTPKKANAEDKLLCYKNSPIQSTKYDRNTNKQVPNGNIIAIETKSRSSSPCSKRELSSSKKEEAKREKELKKQQRAEEKHRKELLRQEEKKKKELKVEEERQRRAELKKQKEEEKRRKEEARLEAKRRKEEERLKKEEEIRLKEEAKERAQSRIGNFFKKLSDSNTPVVEKSDYEKFFLPFYAKDGVRVSNKWKLTKVELEGSKRKIDDELLNSKDKTSSDDLLNWLQSRRLPRGHKIKRKAVDVLQQMPLKEKTDDELQSLLAQVPHKYIKFYENVRPPFIGTYSMDFTLPPNDPFSTKGTGFNYDYDSDVEWVNEEEEGEVDNLESGEEEEEEEDDEDVPSEGEFDGFLDSEENSDLDGLPCAKRKFVGPLIPTICLKSNFENLSEENKRYLQQLKAEVIIETDGPIDPFKEPKTSSLPSKRSNSDLQAQTASQSQSPEKKQKAMITDPMDLLRLFDGVQDSTFSLGTVTEIAQKNLPQYNKQTIKNTIKEYAIRSSGKGDLPRKWVIKDAQNWENLRANANMPTPSL | |
| 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 |
|---|---|---|---|---|---|
| 7 | Phosphorylation | -MEQHLKSIPLQDDT -CCHHHHCCCCCCCC | 35.48 | 19795423 | |
| 14 | Phosphorylation | SIPLQDDTKKKGILS CCCCCCCCCCCCHHH | 53.72 | 19795423 | |
| 33 | Acetylation | TTTVKSNKFLTKEKD CCCEECCCCCCCCCC | 49.17 | 25381059 | |
| 65 | Acetylation | TVKQETMKSINKECA HHHHHHHHHHCHHHH | 56.45 | 25381059 | |
| 77 | Phosphorylation | ECADEMKTTPKKANA HHHHHHCCCCCCCCC | 47.20 | 28152593 | |
| 78 | Phosphorylation | CADEMKTTPKKANAE HHHHHCCCCCCCCCC | 27.82 | 21551504 | |
| 91 | Phosphorylation | AEDKLLCYKNSPIQS CCCCEEEECCCCCCC | 17.11 | 28889911 | |
| 92 | Acetylation | EDKLLCYKNSPIQST CCCEEEECCCCCCCC | 50.37 | 25381059 | |
| 94 | Phosphorylation | KLLCYKNSPIQSTKY CEEEECCCCCCCCCC | 21.16 | 25521595 | |
| 98 | Phosphorylation | YKNSPIQSTKYDRNT ECCCCCCCCCCCCCC | 27.82 | 22369663 | |
| 100 | Acetylation | NSPIQSTKYDRNTNK CCCCCCCCCCCCCCC | 50.86 | 25381059 | |
| 101 | Phosphorylation | SPIQSTKYDRNTNKQ CCCCCCCCCCCCCCC | 21.89 | 21440633 | |
| 121 | Phosphorylation | IIAIETKSRSSSPCS EEEEEECCCCCCCCC | 44.83 | 21440633 | |
| 123 | Phosphorylation | AIETKSRSSSPCSKR EEEECCCCCCCCCHH | 42.11 | 21440633 | |
| 124 | Phosphorylation | IETKSRSSSPCSKRE EEECCCCCCCCCHHH | 36.87 | 21440633 | |
| 125 | Phosphorylation | ETKSRSSSPCSKREL EECCCCCCCCCHHHH | 31.04 | 21440633 | |
| 128 | Phosphorylation | SRSSSPCSKRELSSS CCCCCCCCHHHHCCH | 37.82 | 27717283 | |
| 133 | Phosphorylation | PCSKRELSSSKKEEA CCCHHHHCCHHHHHH | 28.01 | 28889911 | |
| 238 | Phosphorylation | GNFFKKLSDSNTPVV HHHHHHHHCCCCCCC | 48.12 | 23749301 | |
| 260 | Acetylation | FFLPFYAKDGVRVSN EEECEEECCCEEECC | 43.57 | 24489116 | |
| 279 | Phosphorylation | TKVELEGSKRKIDDE EEEEECCCCCCCCHH | 21.66 | 28889911 | |
| 294 | Phosphorylation | LLNSKDKTSSDDLLN HHCCCCCCCHHHHHH | 43.53 | 19779198 | |
| 295 | Phosphorylation | LNSKDKTSSDDLLNW HCCCCCCCHHHHHHH | 37.19 | 30377154 | |
| 331 | Phosphorylation | QMPLKEKTDDELQSL HCCCCCCCHHHHHHH | 50.18 | 28889911 | |
| 493 | Phosphorylation | DPFKEPKTSSLPSKR CCCCCCCCCCCCCCC | 33.97 | 20377248 | |
| 494 | Phosphorylation | PFKEPKTSSLPSKRS CCCCCCCCCCCCCCC | 35.68 | 19823750 | |
| 495 | Phosphorylation | FKEPKTSSLPSKRSN CCCCCCCCCCCCCCC | 49.91 | 19823750 | |
| 498 | Phosphorylation | PKTSSLPSKRSNSDL CCCCCCCCCCCCHHH | 46.09 | 19823750 | |
| 501 | Phosphorylation | SSLPSKRSNSDLQAQ CCCCCCCCCHHHHHH | 44.41 | 22369663 | |
| 503 | Phosphorylation | LPSKRSNSDLQAQTA CCCCCCCHHHHHHHH | 40.73 | 25521595 | |
| 509 | Phosphorylation | NSDLQAQTASQSQSP CHHHHHHHHCCCCCH | 31.15 | 22890988 | |
| 511 | Phosphorylation | DLQAQTASQSQSPEK HHHHHHHCCCCCHHH | 33.48 | 22890988 | |
| 513 | Phosphorylation | QAQTASQSQSPEKKQ HHHHHCCCCCHHHHH | 30.08 | 22369663 | |
| 515 | Phosphorylation | QTASQSQSPEKKQKA HHHCCCCCHHHHHHH | 40.03 | 22369663 | |
| 603 | Phosphorylation | RANANMPTPSL---- HHHCCCCCCCC---- | 18.10 | 28889911 |
| 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 RLF2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RLF2_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 RLF2_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 THR-78; TYR-91; SER-94;SER-279 AND SER-503, 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-501; SER-503 ANDSER-515, AND MASS SPECTROMETRY. | |
