| UniProt ID | ABF1_YEAST | |
|---|---|---|
| UniProt AC | P14164 | |
| Protein Name | ARS-binding factor 1 | |
| Gene Name | ABF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 731 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | General regulatory factor (GRF) that contributes to transcriptional activation of a large number of genes, as well as to DNA replication, silencing and telomere structure. Involved in the transcription activation of a subset of ribosomal protein genes. Binds the ARS-elements found in many promoters. Binds to the sequence 5'-TCN(7)ACG-3'. Influences on genome-wide nucleosome occupancy and affects chromatin structure, and probably dynamics. As a component of the global genome repair (GGR) complex, promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. Component of the regulatory network controlling mitotic and meiotic cell cycle progression.. | |
| Protein Sequence | MDKLVVNYYEYKHPIINKDLAIGAHGGKKFPTLGAWYDVINEYEFQTRCPIILKNSHRNKHFTFACHLKNCPFKVLLSYAGNAASSETSSPSANNNTNPPGTPDHIHHHSNNMNNEDNDNNNGSNNKVSNDSKLDFVTDDLEYHLANTHPDDTNDKVESRSNEVNGNNDDDADANNIFKQQGVTIKNDTEDDSINKASIDRGLDDESGPTHGNDSGNHRHNEEDDVHTQMTKNYSDVVNDEDINVAIANAVANVDSQSNNKHDGKDDDATNNNDGQDNNTNNDHNNNSNINNNNVGSHGISSHSPSSIRDTSMNLDVFNSATDDIPGPFVVTKIEPYHSHPLEDNLSLGKFILTKIPKILQNDLKFDQILESSYNNSNHTVSKFKVSHYVEESGLLDILMQRYGLTAEDFEKRLLSQIARRITTYKARFVLKKKKMGEYNDLQPSSSSNNNNNNDGELSGTNLRSNSIDYAKHQEISSAGTSSNTTKNVNNNKNDSNDDNNGNNNNDASNLMESVLDKTSSHRYQPKKMPSVNKWSKPDQITHSDVSMVGLDESNDGGNENVHPTLAEVDAQEARETAQLAIDKINSYKRSIDDKNGDGHNNSSRNVVDENLINDMDSEDAHKSKRQHLSDITLEERNEDDKLPHEVAEQLRLLSSHLKEVENLHQNNDDDVDDVMVDVDVESQYNKNTTHHNNHHSQPHHDEEDVAGLIGKADDEEDLSDENIQPELRGQ | |
| 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 |
|---|---|---|---|---|---|
| 18 | Ubiquitination | YKHPIINKDLAIGAH ECCCCCCCCCEECCC | 43.65 | 22106047 | |
| 32 | Phosphorylation | HGGKKFPTLGAWYDV CCCCCCCCCCHHHHH | 40.74 | 28889911 | |
| 132 | Phosphorylation | NNKVSNDSKLDFVTD CCCCCCHHHCCEECC | 39.09 | 19779198 | |
| 153 | Phosphorylation | ANTHPDDTNDKVESR HCCCCCCCCCHHHHC | 53.34 | 25704821 | |
| 161 | Phosphorylation | NDKVESRSNEVNGNN CCHHHHCCCCCCCCC | 46.77 | 27214570 | |
| 184 | Phosphorylation | IFKQQGVTIKNDTED HHHHCCCEECCCCCC | 32.81 | 22369663 | |
| 189 | Phosphorylation | GVTIKNDTEDDSINK CCEECCCCCCCCCCH | 51.19 | 22369663 | |
| 193 | Phosphorylation | KNDTEDDSINKASID CCCCCCCCCCHHHHH | 40.14 | 22369663 | |
| 196 | Acetylation | TEDDSINKASIDRGL CCCCCCCHHHHHCCC | 41.67 | 25381059 | |
| 198 | Phosphorylation | DDSINKASIDRGLDD CCCCCHHHHHCCCCC | 26.99 | 19795423 | |
| 207 | Phosphorylation | DRGLDDESGPTHGND HCCCCCCCCCCCCCC | 58.00 | 27214570 | |
| 210 | Phosphorylation | LDDESGPTHGNDSGN CCCCCCCCCCCCCCC | 46.04 | 19795423 | |
| 215 | Phosphorylation | GPTHGNDSGNHRHNE CCCCCCCCCCCCCCC | 45.56 | 25704821 | |
| 235 | Phosphorylation | TQMTKNYSDVVNDED HHHCCCHHHCCCHHH | 33.07 | 21440633 | |
| 256 | Phosphorylation | NAVANVDSQSNNKHD HHHHCCCCCCCCCCC | 31.09 | 27214570 | |
| 258 | Phosphorylation | VANVDSQSNNKHDGK HHCCCCCCCCCCCCC | 46.45 | 28889911 | |
| 297 | Phosphorylation | INNNNVGSHGISSHS CCCCCCCCCCCCCCC | 17.79 | 29136822 | |
| 301 | Phosphorylation | NVGSHGISSHSPSSI CCCCCCCCCCCCCCH | 26.96 | 29136822 | |
| 302 | Phosphorylation | VGSHGISSHSPSSIR CCCCCCCCCCCCCHH | 26.51 | 29136822 | |
| 304 | Phosphorylation | SHGISSHSPSSIRDT CCCCCCCCCCCHHCC | 28.55 | 29136822 | |
| 306 | Phosphorylation | GISSHSPSSIRDTSM CCCCCCCCCHHCCCC | 41.22 | 29136822 | |
| 307 | Phosphorylation | ISSHSPSSIRDTSMN CCCCCCCCHHCCCCC | 25.65 | 29136822 | |
| 311 | Phosphorylation | SPSSIRDTSMNLDVF CCCCHHCCCCCEEHH | 21.74 | 28132839 | |
| 312 | Phosphorylation | PSSIRDTSMNLDVFN CCCHHCCCCCEEHHC | 15.23 | 28132839 | |
| 383 | Acetylation | NSNHTVSKFKVSHYV CCCCCEEEEEEHHHH | 44.88 | 24489116 | |
| 387 | Phosphorylation | TVSKFKVSHYVEESG CEEEEEEHHHHHHCC | 15.08 | 24930733 | |
| 389 | Phosphorylation | SKFKVSHYVEESGLL EEEEEHHHHHHCCHH | 11.31 | 24930733 | |
| 439 | Phosphorylation | KKKKMGEYNDLQPSS ECCCCCCCCCCCCCC | 14.30 | 19823750 | |
| 445 | Phosphorylation | EYNDLQPSSSSNNNN CCCCCCCCCCCCCCC | 29.86 | 19823750 | |
| 446 | Phosphorylation | YNDLQPSSSSNNNNN CCCCCCCCCCCCCCC | 44.46 | 19823750 | |
| 447 | Phosphorylation | NDLQPSSSSNNNNNN CCCCCCCCCCCCCCC | 41.23 | 19823750 | |
| 448 | Phosphorylation | DLQPSSSSNNNNNND CCCCCCCCCCCCCCC | 45.59 | 19823750 | |
| 459 | Phosphorylation | NNNDGELSGTNLRSN CCCCCCCCCCCHHCC | 38.99 | 22369663 | |
| 461 | Phosphorylation | NDGELSGTNLRSNSI CCCCCCCCCHHCCCC | 27.92 | 22369663 | |
| 465 | Phosphorylation | LSGTNLRSNSIDYAK CCCCCHHCCCCCHHH | 37.79 | 22890988 | |
| 467 | Phosphorylation | GTNLRSNSIDYAKHQ CCCHHCCCCCHHHHH | 20.34 | 22369663 | |
| 470 | Phosphorylation | LRSNSIDYAKHQEIS HHCCCCCHHHHHCHH | 18.84 | 22890988 | |
| 478 | Phosphorylation | AKHQEISSAGTSSNT HHHHCHHCCCCCCCC | 36.06 | 27214570 | |
| 482 | Phosphorylation | EISSAGTSSNTTKNV CHHCCCCCCCCCCCC | 22.22 | 30377154 | |
| 483 | Phosphorylation | ISSAGTSSNTTKNVN HHCCCCCCCCCCCCC | 37.72 | 28889911 | |
| 487 | Acetylation | GTSSNTTKNVNNNKN CCCCCCCCCCCCCCC | 57.78 | 22865919 | |
| 496 | Phosphorylation | VNNNKNDSNDDNNGN CCCCCCCCCCCCCCC | 52.10 | 22369663 | |
| 509 | Phosphorylation | GNNNNDASNLMESVL CCCCHHHHHHHHHHH | 33.10 | 22369663 | |
| 514 | Phosphorylation | DASNLMESVLDKTSS HHHHHHHHHHHHCCC | 17.64 | 22369663 | |
| 518 | Acetylation | LMESVLDKTSSHRYQ HHHHHHHHCCCCCCC | 46.26 | 24489116 | |
| 531 | Phosphorylation | YQPKKMPSVNKWSKP CCCCCCCCCCCCCCC | 34.52 | 23749301 | |
| 554 | Phosphorylation | SMVGLDESNDGGNEN EEECCCCCCCCCCCC | 39.63 | 28889911 | |
| 584 | Acetylation | TAQLAIDKINSYKRS HHHHHHHHHHHCCCC | 37.36 | 24489116 | |
| 591 | Phosphorylation | KINSYKRSIDDKNGD HHHHCCCCCCCCCCC | 26.64 | 30377154 | |
| 618 | Phosphorylation | NLINDMDSEDAHKSK HHHCCCCHHHHHHHH | 30.64 | 22369663 | |
| 624 | Phosphorylation | DSEDAHKSKRQHLSD CHHHHHHHHHHHHHH | 24.17 | 2034654 | |
| 630 | Phosphorylation | KSKRQHLSDITLEER HHHHHHHHHCCHHHC | 25.49 | 28889911 | |
| 633 | Phosphorylation | RQHLSDITLEERNED HHHHHHCCHHHCCCC | 32.86 | 28132839 | |
| 655 | Phosphorylation | AEQLRLLSSHLKEVE HHHHHHHHHHHHHHH | 21.94 | 25704821 | |
| 656 | Phosphorylation | EQLRLLSSHLKEVEN HHHHHHHHHHHHHHH | 32.57 | 30377154 | |
| 683 | Phosphorylation | MVDVDVESQYNKNTT EEEEEHHHHHCCCCC | 37.50 | 24961812 | |
| 685 | Phosphorylation | DVDVESQYNKNTTHH EEEHHHHHCCCCCCC | 37.07 | 24961812 | |
| 720 | Phosphorylation | ADDEEDLSDENIQPE CCCCCCCCCCCCCHH | 56.02 | 22369663 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 624 | S | Phosphorylation | Kinase | PKC | - | Uniprot |
| 720 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 720 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 720 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ABF1_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 ABF1_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-189; SER-193; SER-258;SER-302; SER-304; SER-467; SER-554; SER-618 AND SER-720, 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 THR-189; SER-193 ANDSER-618, 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-467 AND SER-720, ANDMASS SPECTROMETRY. | |
| "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-467, AND MASSSPECTROMETRY. | |
| "ABF1 Ser-720 is a predominant phosphorylation site for casein kinaseII of Saccharomyces cerevisiae."; Upton T., Wiltshire S., Francesconi S., Eisenberg S.; J. Biol. Chem. 270:16153-16159(1995). Cited for: PHOSPHORYLATION AT SER-720, AND MUTAGENESIS OF SER-720. | |
