UniProt ID | SNF2_YEAST | |
---|---|---|
UniProt AC | P22082 | |
Protein Name | Transcription regulatory protein SNF2 | |
Gene Name | SNF2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1703 | |
Subcellular Localization | Nucleus. | |
Protein Description | Involved in transcriptional activation. Catalytic component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.. | |
Protein Sequence | MNIPQRQFSNEEVNRCYLRWQHLRNEHGMNAPSVPEFIYLTKVLQFAAKQRQELQMQRQQQGISGSQQNIVPNSSDQAELPNNASSHISASASPHLAPNMQLNGNETFSTSAHQSPIMQTQMPLNSNGGNNMLPQRQSSVGSLNATNFSPTPANNGENAAEKPDNSNHNNLNLNNSELQPQNRSLQEHNIQDSNVMPGSQINSPMPQQAQMQQAQFQAQQAQQAQQAQQAQQAQARLQQGRRLPMTMFTAEQSELLKAQITSLKCLVNRKPIPFEFQAVIQKSINHPPDFKRMLLSLSEFARRRQPTDQNNQSNLNGGNNTQQPGTNSHYNNTNTDNVSGLTRNAPLDSKDENFASVSPAGPSSVHNAKNGTLDKNSQTVSGTPITQTESKKEENETISNVAKTAPNSNKTHTEQNNPPKPQKPVPLNVLQDQYKEGIKVVDIDDPDMMVDSFTMPNISHSNIDYQTLLANSDHAKFTIEPGVLPVGIDTHTATDIYQTLIALNLDTTVNDCLDKLLNDECTESTRENALYDYYALQLLPLQKAVRGHVLQFEWHQNSLLTNTHPNFLSKIRNINVQDALLTNQLYKNHELLKLERKKTEAVARLKSMNKSAINQYNRRQDKKNKRLKFGHRLIATHTNLERDEQKRAEKKAKERLQALKANDEEAYIKLLDQTKDTRITHLLRQTNAFLDSLTRAVKDQQKYTKEMIDSHIKEASEEVDDLSMVPKMKDEEYDDDDDNSNVDYYNVAHRIKEDIKKQPSILVGGTLKDYQIKGLQWMVSLFNNHLNGILADEMGLGKTIQTISLLTYLYEMKNIRGPYLVIVPLSTLSNWSSEFAKWAPTLRTISFKGSPNERKAKQAKIRAGEFDVVLTTFEYIIKERALLSKVKWVHMIIDEGHRMKNAQSKLSLTLNTHYHADYRLILTGTPLQNNLPELWALLNFVLPKIFNSVKSFDEWFNTPFANTGGQDKIELSEEETLLVIRRLHKVLRPFLLRRLKKDVEKELPDKVEKVVKCKMSALQQIMYQQMLKYRRLFIGDQNNKKMVGLRGFNNQIMQLKKICNHPFVFEEVEDQINPTRETNDDIWRVAGKFELLDRILPKLKATGHRVLIFFQMTQIMDIMEDFLRYINIKYLRLDGHTKSDERSELLRLFNAPDSEYLCFILSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQKNEVRILRLITTNSVEEVILERAYKKLDIDGKVIQAGKFDNKSTSEEQEALLRSLLDAEEERRKKRESGVEEEEELKDSEINEILARNDEEMAVLTRMDEDRSKKEEELGVKSRLLEKSELPDIYSRDIGAELKREESESAAVYNGRGARERKTATYNDNMSEEQWLRQFEVSDDEKNDKQARKQRTKKEDKSEAIDGNGEIKGENIDADNDGPRINNISAEDRADTDLAMNDDDFLSKKRKAGRPRGRPKKVKLEGSENSEPPALESSPVTGDNSPSEDFMDIPKPRTAGKTSVKSARTSTRGRGRGRGRGRGRGRGRGRPPKARNGLDYVRTPAAATSPIDIREKVAKQALDLYHFALNYENEAGRKLSDIFLSKPSKALYPDYYMIIKYPVAFDNINTHIETLAYNSLKETLQDFHLIFSNARIYNTEGSVVYEDSLELEKVVTKKYCEIMGDNSQLDFTEFDEQYGTRPLVLPPVVTSSVAESFTDEADSSMTEASV | |
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 |
---|---|---|---|---|---|
149 | Phosphorylation | SLNATNFSPTPANNG CCCCCCCCCCCCCCC | 29.90 | 27738172 | |
349 | Phosphorylation | TRNAPLDSKDENFAS CCCCCCCCCCCCCCC | 50.09 | 19779198 | |
356 | Phosphorylation | SKDENFASVSPAGPS CCCCCCCCCCCCCCH | 20.99 | 29136822 | |
358 | Phosphorylation | DENFASVSPAGPSSV CCCCCCCCCCCCHHH | 13.41 | 17330950 | |
363 | Phosphorylation | SVSPAGPSSVHNAKN CCCCCCCHHHCCCCC | 44.04 | 19779198 | |
364 | Phosphorylation | VSPAGPSSVHNAKNG CCCCCCHHHCCCCCC | 30.45 | 27017623 | |
372 | Phosphorylation | VHNAKNGTLDKNSQT HCCCCCCCCCCCCCC | 40.97 | 30377154 | |
377 | Phosphorylation | NGTLDKNSQTVSGTP CCCCCCCCCCCCCCC | 32.73 | 19823750 | |
379 | Phosphorylation | TLDKNSQTVSGTPIT CCCCCCCCCCCCCCC | 19.23 | 28889911 | |
381 | Phosphorylation | DKNSQTVSGTPITQT CCCCCCCCCCCCCCC | 40.09 | 21440633 | |
383 | Phosphorylation | NSQTVSGTPITQTES CCCCCCCCCCCCCCC | 12.19 | 19823750 | |
386 | Phosphorylation | TVSGTPITQTESKKE CCCCCCCCCCCCCHH | 30.55 | 19823750 | |
388 | Phosphorylation | SGTPITQTESKKEEN CCCCCCCCCCCHHHC | 33.31 | 19823750 | |
390 | Phosphorylation | TPITQTESKKEENET CCCCCCCCCHHHCCC | 53.03 | 19823750 | |
391 | Ubiquitination | PITQTESKKEENETI CCCCCCCCHHHCCCH | 58.95 | 24961812 | |
392 | Ubiquitination | ITQTESKKEENETIS CCCCCCCHHHCCCHH | 78.51 | 24961812 | |
397 | Phosphorylation | SKKEENETISNVAKT CCHHHCCCHHHHHHC | 41.09 | 19823750 | |
399 | Phosphorylation | KEENETISNVAKTAP HHHCCCHHHHHHCCC | 32.44 | 21551504 | |
403 | Ubiquitination | ETISNVAKTAPNSNK CCHHHHHHCCCCCCC | 40.72 | 24961812 | |
543 | Ubiquitination | LQLLPLQKAVRGHVL HHHHHHHHHHCCCEE | 57.44 | 23749301 | |
611 | Phosphorylation | RLKSMNKSAINQYNR HHHHCCHHHHHHHHH | 29.40 | 23749301 | |
646 | Ubiquitination | NLERDEQKRAEKKAK CCHHHHHHHHHHHHH | 52.07 | 17644757 | |
660 | Acetylation | KERLQALKANDEEAY HHHHHHHHCCCHHHH | 48.43 | 25381059 | |
675 | Ubiquitination | IKLLDQTKDTRITHL HHHHHHCCHHHHHHH | 52.01 | 23749301 | |
680 | Phosphorylation | QTKDTRITHLLRQTN HCCHHHHHHHHHHHH | 11.81 | 27017623 | |
686 | Phosphorylation | ITHLLRQTNAFLDSL HHHHHHHHHHHHHHH | 23.29 | 27017623 | |
694 | Phosphorylation | NAFLDSLTRAVKDQQ HHHHHHHHHHHHHHH | 22.12 | 27017623 | |
710 | Phosphorylation | YTKEMIDSHIKEASE HHHHHHHHHHHHHHH | 19.04 | 19795423 | |
713 | Ubiquitination | EMIDSHIKEASEEVD HHHHHHHHHHHHHCC | 41.63 | 24961812 | |
716 | Phosphorylation | DSHIKEASEEVDDLS HHHHHHHHHHCCCCC | 35.07 | 21551504 | |
727 | Ubiquitination | DDLSMVPKMKDEEYD CCCCCCCCCCCCCCC | 47.36 | 24961812 | |
810 | Phosphorylation | ISLLTYLYEMKNIRG HHHHHHHHHHCCCCC | 11.99 | 28132839 | |
837 | Ubiquitination | NWSSEFAKWAPTLRT CCCHHHHHHCCEECE | 49.57 | 17644757 | |
846 | Phosphorylation | APTLRTISFKGSPNE CCEECEEEECCCCCH | 21.94 | 19779198 | |
850 | Phosphorylation | RTISFKGSPNERKAK CEEEECCCCCHHHHH | 25.74 | 19779198 | |
1028 | Methylation | IMYQQMLKYRRLFIG HHHHHHHHHHHHHCC | 31.22 | 20137074 | |
1088 | Acetylation | DIWRVAGKFELLDRI HHHHHHHHHHHHHHH | 26.40 | 24489116 | |
1240 | Acetylation | GKVIQAGKFDNKSTS CCEEEECCCCCCCCH | 53.19 | 24489116 | |
1244 | Acetylation | QAGKFDNKSTSEEQE EECCCCCCCCHHHHH | 57.88 | 24489116 | |
1245 | Phosphorylation | AGKFDNKSTSEEQEA ECCCCCCCCHHHHHH | 43.34 | 30377154 | |
1247 | Phosphorylation | KFDNKSTSEEQEALL CCCCCCCHHHHHHHH | 46.34 | 30377154 | |
1320 | Ubiquitination | VKSRLLEKSELPDIY HHHHHHHHCCCCHHH | 49.56 | 24961812 | |
1340 | Phosphorylation | AELKREESESAAVYN HHHCHHHHHCCCCCC | 31.90 | 17563356 | |
1342 | Phosphorylation | LKREESESAAVYNGR HCHHHHHCCCCCCCC | 30.70 | 27214570 | |
1375 | Phosphorylation | WLRQFEVSDDEKNDK HHHHCCCCCCHHCHH | 31.95 | 22369663 | |
1422 | Phosphorylation | GPRINNISAEDRADT CCCCCCCCHHHHHCC | 27.94 | 27214570 | |
1429 | Phosphorylation | SAEDRADTDLAMNDD CHHHHHCCCCCCCCH | 31.74 | 28889911 | |
1440 | Phosphorylation | MNDDDFLSKKRKAGR CCCHHHHHHHHHCCC | 35.80 | 27017623 | |
1460 | Phosphorylation | KKVKLEGSENSEPPA CCCCCCCCCCCCCCC | 24.99 | 19779198 | |
1463 | Phosphorylation | KLEGSENSEPPALES CCCCCCCCCCCCHHC | 47.64 | 23749301 | |
1470 | Phosphorylation | SEPPALESSPVTGDN CCCCCHHCCCCCCCC | 40.57 | 23749301 | |
1471 | Phosphorylation | EPPALESSPVTGDNS CCCCHHCCCCCCCCC | 17.64 | 25752575 | |
1474 | Phosphorylation | ALESSPVTGDNSPSE CHHCCCCCCCCCCCC | 42.05 | 21440633 | |
1478 | Phosphorylation | SPVTGDNSPSEDFMD CCCCCCCCCCCCCCC | 34.25 | 21551504 | |
1480 | Phosphorylation | VTGDNSPSEDFMDIP CCCCCCCCCCCCCCC | 50.01 | 21440633 | |
1494 | Acetylation | PKPRTAGKTSVKSAR CCCCCCCCCCCCCCC | 34.85 | 24489116 | |
1498 | Acetylation | TAGKTSVKSARTSTR CCCCCCCCCCCCCCC | 37.86 | 24489116 | |
1541 | Phosphorylation | VRTPAAATSPIDIRE CCCCCCCCCCCCHHH | 30.24 | 27214570 | |
1542 | Phosphorylation | RTPAAATSPIDIREK CCCCCCCCCCCHHHH | 18.35 | 23749301 |
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 SNF2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SNF2_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 SNF2_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-358; SER-381; SER-710;SER-716; SER-1340; SER-1470 AND SER-1478, 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-358; SER-1340; SER-1375AND SER-1478, 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-358, AND MASSSPECTROMETRY. |