| UniProt ID | TFB1_YEAST | |
|---|---|---|
| UniProt AC | P32776 | |
| Protein Name | General transcription and DNA repair factor IIH subunit TFB1 | |
| Gene Name | TFB1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 642 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | 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. 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. 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.. | |
| Protein Sequence | MSHSGAAIFEKVSGIIAINEDVSPAELTWRSTDGDKVHTVVLSTIDKLQATPASSEKMMLRLIGKVDESKKRKDNEGNEVVPKPQRHMFSFNNRTVMDNIKMTLQQIISRYKDADIYEEKRRREESAQHTETPMSSSSVTAGTPTPHLDTPQLNNGAPLINTAKLDDSLSKEKLLTNLKLQQSLLKGNKVLMKVFQETVINAGLPPSEFWSTRIPLLRAFALSTSQKVGPYNVLSTIKPVASSENKVNVNLSREKILNIFENYPIVKKAYTDNVPKNFKEPEFWARFFSSKLFRKLRGEKIMQNDRGDVIIDRYLTLDQEFDRKDDDMLLHPVKKIIDLDGNIQDDPVVRGNRPDFTMQPGVDINGNSDGTVDILKGMNRLSEKMIMALKNEYSRTNLQNKSNITNDEEDEDNDERNELKIDDLNESYKTNYAIIHLKRNAHEKTTDNDAKSSADSIKNADLKVSNQQMLQQLSLVMDNLINKLDLNQVVPNNEVSNKINKRVITAIKINAKQAKHNNVNSALGSFVDNTSQANELEVKSTLPIDLLESCRMLHTTCCEFLKHFYIHFQSGEQKQASTVKKLYNHLKDCIEKLNELFQDVLNGDGESMSNTCTAYLKPVLNSITLATHKYDEYFNEYNNNSN | |
| 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 |
|---|---|---|---|---|---|
| 54 | Phosphorylation | KLQATPASSEKMMLR HHCCCCCCCHHHHHH | 39.99 | 27214570 | |
| 103 | Phosphorylation | VMDNIKMTLQQIISR HHHHHHHHHHHHHHH | 19.20 | 28889911 | |
| 143 | Phosphorylation | SSSVTAGTPTPHLDT CCCCCCCCCCCCCCC | 22.86 | 24961812 | |
| 150 | Phosphorylation | TPTPHLDTPQLNNGA CCCCCCCCCCCCCCC | 21.21 | 28889911 | |
| 223 | Phosphorylation | LLRAFALSTSQKVGP HHHHHHHCCCCCCCC | 23.68 | 30377154 | |
| 252 | Phosphorylation | NKVNVNLSREKILNI CCEECCCCHHHHHHH | 32.94 | 28889911 | |
| 335 | Acetylation | MLLHPVKKIIDLDGN CCCCCCEEEECCCCC | 45.16 | 24489116 | |
| 390 | Acetylation | EKMIMALKNEYSRTN HHHHHHHHHHHHHHH | 37.89 | 25381059 | |
| 402 | Phosphorylation | RTNLQNKSNITNDEE HHHCCCCCCCCCCCC | 40.80 | 28889911 | |
| 465 | Phosphorylation | KNADLKVSNQQMLQQ HHCCCCCCHHHHHHH | 27.60 | 19823750 | |
| 474 | Phosphorylation | QQMLQQLSLVMDNLI HHHHHHHHHHHHHHH | 17.99 | 19823750 | |
| 521 | Phosphorylation | AKHNNVNSALGSFVD HCCCCHHHHHHHHCC | 22.16 | 28889911 | |
| 641 | Phosphorylation | FNEYNNNSN------ HHHHCCCCC------ | 46.14 | 30377154 |
| 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 TFB1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TFB1_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 TFB1_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-150 AND SER-521, ANDMASS SPECTROMETRY. | |
