UniProt ID | RAP1_YEAST | |
---|---|---|
UniProt AC | P11938 | |
Protein Name | DNA-binding protein RAP1 | |
Gene Name | RAP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 827 | |
Subcellular Localization | Nucleus . Chromosome, telomere . | |
Protein Description | Essential regulatory protein in yeast whose DNA-binding sites are found at three types of chromosomal elements: promoters, silencers, and telomeres. RAP1 is also involved in the regulation of telomere structure, where its binding sites are found within the terminal poly[C(1-3)A] sequences. The opposite regulatory functions of RAP1 are not intrinsic to its binding sites but, instead, result from interactions with different factors at promoters and silencers. RAP1 associates with SIR3 and SIR4 proteins to form a DNA-binding complex that initiates the repression at the HM loci and telomeres. May also target the binding of RIF1 and RIF2 to silencers and telomeres. Forms with GCR1 a transcriptional activation complex that is required for expression of glycolytic and ribosomal gene.. | |
Protein Sequence | MSSPDDFETAPAEYVDALDPSMVVVDSGSAAVTAPSDSAAEVKANQNEENTGATAAETSEKVDQTEVEKKDDDDTTEVGVTTTTPSIADTAATANIASTSGASVTEPTTDDTAADEKKEQVSGPPLSNMKFYLNRDADAHDSLNDIDQLARLIRANGGEVLDSKPRESKENVFIVSPYNHTNLPTVTPTYIKACCQSNSLLNMENYLVPYDNFREVVDSRLQEESHSNGVDNSNSNSDNKDSIRPKTEIISTNTNGATEDSTSEKVMVDAEQQARLQEQAQLLRQHVSSTASITSGGHNDLVQIEQPQKDTSNNNNSNVNDEDNDLLTQDNNPQTADEGNASFQAQRSMISRGALPSHNKASFTDEEDEFILDVVRKNPTRRTTHTLYDEISHYVPNHTGNSIRHRFRVYLSKRLEYVYEVDKFGKLVRDDDGNLIKTKVLPPSIKRKFSADEDYTLAIAVKKQFYRDLFQIDPDTGRSLITDEDTPTAIARRNMTMDPNHVPGSEPNFAAYRTQSRRGPIAREFFKHFAEEHAAHTENAWRDRFRKFLLAYGIDDYISYYEAEKAQNREPEPMKNLTNRPKRPGVPTPGNYNSAAKRARNYSSQRNVQPTANAASANAAAAAAAAASNSYAIPENELLDEDTMNFISSLKNDLSNISNSLPFEYPHEIAEAIRSDFSNEDIYDNIDPDTISFPPKIATTDLFLPLFFHFGSTRQFMDKLHEVISGDYEPSQAEKLVQDLCDETGIRKNFSTSILTCLSGDLMVFPRYFLNMFKDNVNPPPNVPGIWTHDDDESLKSNDQEQIRKLVKKHGTGRMEMRKRFFEKDLL | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSSPDDFET ------CCCHHHHCC | 51.05 | 30377154 | |
9 | Phosphorylation | SSPDDFETAPAEYVD CCHHHHCCCCHHHHC | 37.62 | 30377154 | |
14 | Phosphorylation | FETAPAEYVDALDPS HCCCCHHHHCCCCCC | 13.02 | 30377154 | |
29 | Phosphorylation | MVVVDSGSAAVTAPS EEEEECCCCEEECCC | 19.60 | 30377154 | |
58 | Phosphorylation | TGATAAETSEKVDQT CCCCHHHHHHCCCCC | 37.14 | 27717283 | |
59 | Phosphorylation | GATAAETSEKVDQTE CCCHHHHHHCCCCCE | 27.25 | 27717283 | |
142 | Phosphorylation | RDADAHDSLNDIDQL CCCCCCCCCCHHHHH | 21.14 | 23749301 | |
164 | Ubiquitination | GGEVLDSKPRESKEN CCCCCCCCCCCCCCC | 48.00 | 23749301 | |
169 | Acetylation | DSKPRESKENVFIVS CCCCCCCCCCEEEEC | 48.86 | 24489116 | |
197 | Phosphorylation | YIKACCQSNSLLNME HHHHHHHCCCCCCCC | 17.93 | 30377154 | |
225 | Phosphorylation | DSRLQEESHSNGVDN HHHHHHHHHHCCCCC | 31.31 | 21082442 | |
227 | Phosphorylation | RLQEESHSNGVDNSN HHHHHHHHCCCCCCC | 44.55 | 28889911 | |
233 | Phosphorylation | HSNGVDNSNSNSDNK HHCCCCCCCCCCCCC | 36.85 | 22369663 | |
235 | Phosphorylation | NGVDNSNSNSDNKDS CCCCCCCCCCCCCCC | 37.22 | 22369663 | |
237 | Phosphorylation | VDNSNSNSDNKDSIR CCCCCCCCCCCCCCC | 42.24 | 22369663 | |
251 | Phosphorylation | RPKTEIISTNTNGAT CCCCEEEECCCCCCC | 22.67 | 30377154 | |
254 | Phosphorylation | TEIISTNTNGATEDS CEEEECCCCCCCCCC | 34.81 | 30377154 | |
261 | Phosphorylation | TNGATEDSTSEKVMV CCCCCCCCCCCCEEC | 27.83 | 23749301 | |
262 | Phosphorylation | NGATEDSTSEKVMVD CCCCCCCCCCCEECC | 53.91 | 23749301 | |
263 | Phosphorylation | GATEDSTSEKVMVDA CCCCCCCCCCEECCH | 39.10 | 27017623 | |
288 | Phosphorylation | QLLRQHVSSTASITS HHHHHHHHHCCEECC | 21.61 | 22369663 | |
289 | Phosphorylation | LLRQHVSSTASITSG HHHHHHHHCCEECCC | 27.23 | 22369663 | |
290 | Phosphorylation | LRQHVSSTASITSGG HHHHHHHCCEECCCC | 19.54 | 22369663 | |
292 | Phosphorylation | QHVSSTASITSGGHN HHHHHCCEECCCCCC | 26.87 | 22369663 | |
294 | Phosphorylation | VSSTASITSGGHNDL HHHCCEECCCCCCCC | 20.87 | 22369663 | |
295 | Phosphorylation | SSTASITSGGHNDLV HHCCEECCCCCCCCE | 40.90 | 22369663 | |
335 | Phosphorylation | TQDNNPQTADEGNAS CCCCCCCCCCCCCCC | 37.02 | 24909858 | |
342 | Phosphorylation | TADEGNASFQAQRSM CCCCCCCCHHHHHHH | 23.14 | 23749301 | |
357 | Phosphorylation | ISRGALPSHNKASFT HHCCCCCCCCCCCCC | 40.31 | 27738172 | |
362 | Phosphorylation | LPSHNKASFTDEEDE CCCCCCCCCCCCCCC | 30.23 | 22369663 | |
364 | Phosphorylation | SHNKASFTDEEDEFI CCCCCCCCCCCCCCH | 39.75 | 22369663 | |
383 | Phosphorylation | RKNPTRRTTHTLYDE HHCCCCCCCCHHHHH | 21.46 | 19779198 | |
388 | Phosphorylation | RRTTHTLYDEISHYV CCCCCHHHHHHHHHC | 16.82 | 19779198 | |
392 | Phosphorylation | HTLYDEISHYVPNHT CHHHHHHHHHCCCCC | 13.50 | 19779198 | |
423 | Acetylation | EYVYEVDKFGKLVRD EEEEEECCCCCEEEC | 62.28 | 24489116 | |
479 | Phosphorylation | IDPDTGRSLITDEDT CCCCCCCCCCCCCCC | 26.01 | 21126336 | |
482 | Phosphorylation | DTGRSLITDEDTPTA CCCCCCCCCCCCCHH | 38.33 | 22369663 | |
486 | Phosphorylation | SLITDEDTPTAIARR CCCCCCCCCHHHHHC | 22.08 | 22369663 | |
488 | Phosphorylation | ITDEDTPTAIARRNM CCCCCCCHHHHHCCC | 32.56 | 22369663 | |
496 | Phosphorylation | AIARRNMTMDPNHVP HHHHCCCCCCCCCCC | 23.21 | 28889911 | |
527 | Acetylation | PIAREFFKHFAEEHA HHHHHHHHHHHHHHH | 43.04 | 24489116 | |
594 | Phosphorylation | PTPGNYNSAAKRARN CCCCCHHHHHHHHHC | 21.17 | 23749301 | |
597 | Acetylation | GNYNSAAKRARNYSS CCHHHHHHHHHCCCC | 46.43 | 25381059 | |
655 | Phosphorylation | SSLKNDLSNISNSLP HHHHHHHHCCCCCCC | 34.67 | 22369663 | |
658 | Phosphorylation | KNDLSNISNSLPFEY HHHHHCCCCCCCCCC | 25.31 | 22369663 | |
660 | Phosphorylation | DLSNISNSLPFEYPH HHHCCCCCCCCCCHH | 30.54 | 22369663 | |
665 | Phosphorylation | SNSLPFEYPHEIAEA CCCCCCCCHHHHHHH | 15.40 | 22369663 | |
731 | Phosphorylation | ISGDYEPSQAEKLVQ HHCCCCHHHHHHHHH | 30.04 | 22369663 | |
748 | Acetylation | CDETGIRKNFSTSIL HHHHCCCCCCCHHHH | 61.50 | 25381059 | |
752 | Phosphorylation | GIRKNFSTSILTCLS CCCCCCCHHHHHHHC | 18.69 | 27017623 | |
753 | Phosphorylation | IRKNFSTSILTCLSG CCCCCCHHHHHHHCC | 17.88 | 27017623 | |
759 | Phosphorylation | TSILTCLSGDLMVFP HHHHHHHCCCCEECH | 32.19 | 27017623 | |
797 | Phosphorylation | DDDESLKSNDQEQIR CCCHHHHCCCHHHHH | 51.43 | 27017623 |
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 RAP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAP1_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 RAP1_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 THR-486; THR-488; SER-660AND SER-731, 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-658, 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 THR-486, AND MASSSPECTROMETRY. |