| UniProt ID | RAD25_YEAST | |
|---|---|---|
| UniProt AC | Q00578 | |
| Protein Name | General transcription and DNA repair factor IIH helicase subunit XPB | |
| Gene Name | SSL2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 843 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/SSL2, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/SSL2 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. [PubMed: 8269516] | |
| Protein Sequence | MTDVEGYQPKSKGKIFPDMGESFFSSDEDSPATDAEIDENYDDNRETSEGRGERDTGAMVTGLKKPRKKTKSSRHTAADSSMNQMDAKDKALLQDTNSDIPADFVPDSVSGMFRSHDFSYLRLRPDHASRPLWISPSDGRIILESFSPLAEQAQDFLVTIAEPISRPSHIHEYKITAYSLYAAVSVGLETDDIISVLDRLSKVPVAESIINFIKGATISYGKVKLVIKHNRYFVETTQADILQMLLNDSVIGPLRIDSDHQVQPPEDVLQQQLQQTAGKPATNVNPNDVEAVFSAVIGGDNEREEEDDDIDAVHSFEIANESVEVVKKRCQEIDYPVLEEYDFRNDHRNPDLDIDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFLQWCTLQPENCAVFTSDNKEMFQTESGLVVSTYSMVANTRNRSHDSQKVMDFLTGREWGFIILDEVHVVPAAMFRRVVSTIAAHAKLGLTATLVREDDKIGDLNFLIGPKLYEANWMELSQKGHIANVQCAEVWCPMTAEFYQEYLRETARKRMLLYIMNPTKFQACQFLIQYHERRGDKIIVFSDNVYALQEYALKMGKPFIYGSTPQQERMNILQNFQYNDQINTIFLSKVGDTSIDLPEATCLIQISSHYGSRRQEAQRLGRILRAKRRNDEGFNAFFYSLVSKDTQEMYYSTKRQAFLVDQGYAFKVITHLHGMENIPNLAYASPRERRELLQEVLLKNEEAAGIEVGDDADNSVGRGSNGHKRFKSKAVRGEGSLSGLAGGEDMAYMEYSTNKNKELKEHHPLIRKMYYKNLKK | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MTDVEGYQP ------CCCCCCCCC | 49.07 | 23749301 | |
| 64 | Acetylation | GAMVTGLKKPRKKTK HCCCCCCCCCCCCCC | 63.18 | 25381059 | |
| 80 | Phosphorylation | SRHTAADSSMNQMDA CHHHHCCHHHHHCCH | 27.10 | 30377154 | |
| 81 | Phosphorylation | RHTAADSSMNQMDAK HHHHCCHHHHHCCHH | 23.46 | 25752575 | |
| 96 | Phosphorylation | DKALLQDTNSDIPAD HHHHHHCCCCCCCCC | 24.54 | 30377154 | |
| 98 | Phosphorylation | ALLQDTNSDIPADFV HHHHCCCCCCCCCCC | 38.72 | 30377154 | |
| 108 | Phosphorylation | PADFVPDSVSGMFRS CCCCCCCCCCCCCCC | 16.47 | 27017623 | |
| 174 | Ubiquitination | PSHIHEYKITAYSLY CCCCCEEEEEHEEHH | 30.51 | 17644757 | |
| 202 | Ubiquitination | SVLDRLSKVPVAESI HHHHHHCCCCHHHHH | 55.97 | 17644757 | |
| 214 | Ubiquitination | ESIINFIKGATISYG HHHHHHHHCCEEECC | 38.05 | 17644757 | |
| 392 | Ubiquitination | VLPCGAGKTLVGITA EEECCCCCCHHHHHH | 37.85 | 17644757 | |
| 404 | Ubiquitination | ITAACTIKKSVIVLC HHHHEEECCEEEEEE | 22.35 | 17644757 | |
| 405 | Ubiquitination | TAACTIKKSVIVLCT HHHEEECCEEEEEEC | 46.21 | 17644757 | |
| 472 | Acetylation | NRSHDSQKVMDFLTG CCCCCHHHHHHHHHC | 43.40 | 24489116 | |
| 510 | Ubiquitination | STIAAHAKLGLTATL HHHHHHHHHCCEEEE | 32.97 | 17644757 | |
| 523 | Ubiquitination | TLVREDDKIGDLNFL EEEECCCCCCCEEEE | 61.99 | 17644757 | |
| 523 | Acetylation | TLVREDDKIGDLNFL EEEECCCCCCCEEEE | 61.99 | 24489116 | |
| 534 | Ubiquitination | LNFLIGPKLYEANWM EEEEECHHHHCCCHH | 59.49 | 17644757 | |
| 546 | Ubiquitination | NWMELSQKGHIANVQ CHHHHHHCCCCCCEE | 49.43 | 17644757 | |
| 587 | Ubiquitination | LYIMNPTKFQACQFL HHHCCCCHHHHHHHH | 36.41 | 17644757 | |
| 604 | Ubiquitination | YHERRGDKIIVFSDN HHHHCCCEEEEECCC | 36.84 | 17644757 | |
| 621 | Ubiquitination | ALQEYALKMGKPFIY HHHHHHHHHCCCCCC | 37.12 | 17644757 | |
| 624 | Ubiquitination | EYALKMGKPFIYGST HHHHHHCCCCCCCCC | 33.00 | 17644757 | |
| 721 | Ubiquitination | QEMYYSTKRQAFLVD HHHHHHCCCCEEEEC | 36.25 | 17644757 | |
| 734 | Ubiquitination | VDQGYAFKVITHLHG ECCCHHHHHHHHHHC | 25.26 | 17644757 | |
| 752 | Phosphorylation | IPNLAYASPRERREL CCCCCCCCHHHHHHH | 16.29 | 17330950 | |
| 820 | Phosphorylation | MAYMEYSTNKNKELK CEEEEECCCCCHHHH | 49.68 | 19779198 | |
| 839 | Acetylation | LIRKMYYKNLKK--- HHHHHHHHHCCC--- | 38.01 | 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 RAD25_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD25_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 RAD25_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-752, AND MASSSPECTROMETRY. | |
