| UniProt ID | TAF5_YEAST | |
|---|---|---|
| UniProt AC | P38129 | |
| Protein Name | Transcription initiation factor TFIID subunit 5 | |
| Gene Name | TAF5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 798 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.. | |
| Protein Sequence | MSQKQSTNQNQNGTHQPQPVKNQRTNNAAGANSGQQPQQQSQGQSQQQGRSNGPFSASDLNRIVLEYLNKKGYHRTEAMLRAESGRTLTPQNKQSPANTKTGKFPEQSSIPPNPGKTAKPISNPTNLSSKRDAEGGIVSSGRLEGLNAPENYIRAYSMLKNWVDSSLEIYKPELSYIMYPIFIYLFLNLVAKNPVYARRFFDRFSPDFKDFHGSEINRLFSVNSIDHIKENEVASAFQSHKYRITMSKTTLNLLLYFLNENESIGGSLIISVINQHLDPNIVESVTAREKLADGIKVLSDSENGNGKQNLEMNSVPVKLGPFPKDEEFVKEIETELKIKDDQEKQLNQQTAGDNYSGANNRTLLQEYKAMNNEKFKDNTGDDDKDKIKDKIAKDEEKKESELKVDGEKKDSNLSSPARDILPLPPKTALDLKLEIQKVKESRDAIKLDNLQLALPSVCMYTFQNTNKDMSCLDFSDDCRIAAAGFQDSYIKIWSLDGSSLNNPNIALNNNDKDEDPTCKTLVGHSGTVYSTSFSPDNKYLLSGSEDKTVRLWSMDTHTALVSYKGHNHPVWDVSFSPLGHYFATASHDQTARLWSCDHIYPLRIFAGHLNDVDCVSFHPNGCYVFTGSSDKTCRMWDVSTGDSVRLFLGHTAPVISIAVCPDGRWLSTGSEDGIINVWDIGTGKRLKQMRGHGKNAIYSLSYSKEGNVLISGGADHTVRVWDLKKATTEPSAEPDEPFIGYLGDVTASINQDIKEYGRRRTVIPTSDLVASFYTKKTPVFKVKFSRSNLALAGGAFRP | |
| 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 |
|---|---|---|---|---|---|
| 14 | Phosphorylation | TNQNQNGTHQPQPVK CCCCCCCCCCCCCCC | 25.53 | 28889911 | |
| 21 | Ubiquitination | THQPQPVKNQRTNNA CCCCCCCCCCCCCCC | 54.79 | 23749301 | |
| 41 | Phosphorylation | GQQPQQQSQGQSQQQ CCCCCHHHHCCCCHH | 31.75 | 23749301 | |
| 67 | Phosphorylation | LNRIVLEYLNKKGYH HHHHHHHHHHHCCCC | 16.06 | 28889911 | |
| 70 | Acetylation | IVLEYLNKKGYHRTE HHHHHHHHCCCCCHH | 45.00 | 24489116 | |
| 89 | Phosphorylation | AESGRTLTPQNKQSP CCCCCCCCCCCCCCC | 23.40 | 22369663 | |
| 93 | Ubiquitination | RTLTPQNKQSPANTK CCCCCCCCCCCCCCC | 47.08 | 23749301 | |
| 95 | Phosphorylation | LTPQNKQSPANTKTG CCCCCCCCCCCCCCC | 27.82 | 22369663 | |
| 99 | Phosphorylation | NKQSPANTKTGKFPE CCCCCCCCCCCCCCC | 31.89 | 22369663 | |
| 103 | Acetylation | PANTKTGKFPEQSSI CCCCCCCCCCCCCCC | 64.08 | 24489116 | |
| 122 | Phosphorylation | GKTAKPISNPTNLSS CCCCCCCCCCCCCCC | 45.33 | 27214570 | |
| 139 | Phosphorylation | DAEGGIVSSGRLEGL CCCCCCCCCCCCCCC | 25.75 | 27214570 | |
| 140 | Phosphorylation | AEGGIVSSGRLEGLN CCCCCCCCCCCCCCC | 19.62 | 27214570 | |
| 209 | Acetylation | DRFSPDFKDFHGSEI HHCCCCHHHCCHHHH | 67.85 | 24489116 | |
| 229 | Acetylation | VNSIDHIKENEVASA CCCCCHHCHHHHHHH | 51.58 | 24489116 | |
| 241 | Acetylation | ASAFQSHKYRITMSK HHHHHHCCCEEEECH | 41.28 | 24489116 | |
| 299 | Phosphorylation | ADGIKVLSDSENGNG CCCEEEECCCCCCCC | 41.92 | 27214570 | |
| 314 | Phosphorylation | KQNLEMNSVPVKLGP CCCEEECCCEEECCC | 26.87 | 23749301 | |
| 411 | Phosphorylation | VDGEKKDSNLSSPAR CCCCCCCCCCCCCHH | 48.85 | 22369663 | |
| 414 | Phosphorylation | EKKDSNLSSPARDIL CCCCCCCCCCHHHCC | 38.23 | 25521595 | |
| 415 | Phosphorylation | KKDSNLSSPARDILP CCCCCCCCCHHHCCC | 26.24 | 25521595 | |
| 531 | Phosphorylation | HSGTVYSTSFSPDNK CCCEEEEEEECCCCC | 18.99 | 19779198 | |
| 542 | Phosphorylation | PDNKYLLSGSEDKTV CCCCEEECCCCCCCE | 37.36 | 28889911 | |
| 544 | Phosphorylation | NKYLLSGSEDKTVRL CCEEECCCCCCCEEE | 38.97 | 28889911 | |
| 547 | Acetylation | LLSGSEDKTVRLWSM EECCCCCCCEEEEEE | 44.88 | 24489116 | |
| 701 | Phosphorylation | KNAIYSLSYSKEGNV CCEEEEEEECCCCCE | 22.78 | 30377154 | |
| 775 | Acetylation | LVASFYTKKTPVFKV HHHHHCCCCCCEEEE | 43.18 | 24489116 | |
| 785 | Phosphorylation | PVFKVKFSRSNLALA CEEEEEECCCCCEEC | 29.14 | 30377154 | |
| 787 | Phosphorylation | FKVKFSRSNLALAGG EEEEECCCCCEECCC | 34.69 | 21551504 |
| 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 TAF5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TAF5_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 TAF5_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 TYR-67; SER-140; SER-299;SER-411 AND SER-787, 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-411; SER-414; SER-415AND SER-787, AND MASS SPECTROMETRY. | |
