| UniProt ID | TAF1_YEAST | |
|---|---|---|
| UniProt AC | P46677 | |
| Protein Name | Transcription initiation factor TFIID subunit 1 | |
| Gene Name | TAF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1066 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation 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.. | |
| Protein Sequence | MVKQQGSGKTNLANEDEAYEAIFGGEFGSLEIGSYIGGDEGANSKDYTEHLPDAVDFEDEDELADDDDDLPEESDANLHPAMMTMGAYDDVNENGAVLGIDSNSLNMQLPEINGDLSQQFILEDDGGTPATSNALFMGMDANEIHLATETGVLDGSGANEIGHSQLSIGGVNGNDMSINGGFIMEPDMSDGKHKKATKLDLINHEKYLLKKYFPDFEKGKILKWNKLIYRRSVPYHWHSEISRVKKPFMPLNLKFKVQQDDKRLFNSRTISYVAPIYQGKNNLLQSNSSASRRGLIHVSIDELFPIKEQQKKRKIIHDEKTISEDLLIATDDWDQEKIINQGTSSTATLADSSMTPNLKFSGGYKLKSLIEDVAEDWQWDEDMIIDAKLKESKHAELNMNDEKLLLMIEKTNNLAQQKQQLDSSNLILPLNETILQQKFNLSNDDKYQILKKTHQTKVRSTISNLNIQHSQPAINLQSPFYKVAVPRYQLRHFHRENFGSHIRPGTKIVFSKLKARKRKRDKGKDVKESFSTSQDLTIGDTAPVYLMEYSEQTPVALSKFGMANKLINYYRKANEQDTLRPKLPVGETHVLGVQDKSPFWNFGFVEPGHIVPTLYNNMIRAPVFKHDISGTDFLLTKSSGFGISNRFYLRNINHLFTVGQTFPVEEIPGPNSRKVTSMKATRLKMIIYRILNHNHSKAISIDPIAKHFPDQDYGQNRQKVKEFMKYQRDGPEKGLWRLKDDEKLLDNEAVKSLITPEQISQVESMSQGLQFQEDNEAYNFDSKLKSLEENLLPWNITKNFINSTQMRAMIQIHGVGDPTGCGEGFSFLKTSMKGGFVKSGSPSSNNNSSNKKGTNTHSYNVAQQQKAYDEEIAKTWYTHTKSLSISNPFEEMTNPDEINQTNKHVKTDRDDKKILKIVRKKRDENGIIQRQTIFIRDPRVIQGYIKIKEQDKEDVNKLLEEDTSKINNLEELEKQKKLLQLELANLEKSQQRRAARQNSKRNGGATRTENSVDNGSDLAGVTDGKAARNKGKNTTRRCATCGQIGHIRTNKSCPMYSSKDNPASPK | |
| 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 |
|---|---|---|---|---|---|
| 206 | Acetylation | LDLINHEKYLLKKYF HHHHHHHHHHHHHHC | 33.38 | 24489116 | |
| 232 | Phosphorylation | NKLIYRRSVPYHWHS CEEEECCCCCCCCCC | 20.60 | 28889911 | |
| 280 | Ubiquitination | VAPIYQGKNNLLQSN EEEEECCCCCHHHCC | 27.43 | 23749301 | |
| 343 | Phosphorylation | EKIINQGTSSTATLA HHHHCCCCCCCCCCC | 15.11 | 27017623 | |
| 344 | Phosphorylation | KIINQGTSSTATLAD HHHCCCCCCCCCCCC | 32.30 | 27017623 | |
| 345 | Phosphorylation | IINQGTSSTATLADS HHCCCCCCCCCCCCC | 23.15 | 27017623 | |
| 346 | Phosphorylation | INQGTSSTATLADSS HCCCCCCCCCCCCCC | 24.35 | 29688323 | |
| 348 | Phosphorylation | QGTSSTATLADSSMT CCCCCCCCCCCCCCC | 23.67 | 27017623 | |
| 352 | Phosphorylation | STATLADSSMTPNLK CCCCCCCCCCCCCCE | 19.19 | 24961812 | |
| 353 | Phosphorylation | TATLADSSMTPNLKF CCCCCCCCCCCCCEE | 27.50 | 24961812 | |
| 355 | Phosphorylation | TLADSSMTPNLKFSG CCCCCCCCCCCEECC | 15.80 | 28152593 | |
| 364 | Phosphorylation | NLKFSGGYKLKSLIE CCEECCCCCHHHHHH | 19.37 | 27017623 | |
| 423 | Phosphorylation | QQKQQLDSSNLILPL HHHHHHCCCCCEEEC | 29.71 | 28889911 | |
| 424 | Phosphorylation | QKQQLDSSNLILPLN HHHHHCCCCCEEECC | 35.01 | 28889911 | |
| 478 | Phosphorylation | QPAINLQSPFYKVAV CCCCCCCCCCEEEEC | 21.83 | 23749301 | |
| 481 | Phosphorylation | INLQSPFYKVAVPRY CCCCCCCEEEECCHH | 14.13 | 24961812 | |
| 629 | Phosphorylation | PVFKHDISGTDFLLT CCEECCCCCCCEEEE | 41.52 | 27017623 | |
| 819 | Phosphorylation | IHGVGDPTGCGEGFS ECCCCCCCCCCCCCC | 50.25 | 28889911 | |
| 841 | Phosphorylation | GGFVKSGSPSSNNNS CCCEECCCCCCCCCC | 28.79 | 25752575 | |
| 856 | Phosphorylation | SNKKGTNTHSYNVAQ CCCCCCCCCCCCHHH | 16.43 | 30377154 | |
| 882 | Phosphorylation | TWYTHTKSLSISNPF HHHHCCCCCCCCCCC | 28.62 | 21440633 | |
| 884 | Phosphorylation | YTHTKSLSISNPFEE HHCCCCCCCCCCCHH | 30.94 | 28889911 | |
| 963 | Phosphorylation | NKLLEEDTSKINNLE HHHHHHHHHHCCCHH | 34.89 | 28152593 | |
| 964 | Phosphorylation | KLLEEDTSKINNLEE HHHHHHHHHCCCHHH | 43.81 | 25521595 | |
| 989 | Phosphorylation | ELANLEKSQQRRAAR HHHHHHHHHHHHHHH | 23.36 | 30377154 | |
| 1008 | Phosphorylation | RNGGATRTENSVDNG HCCCCCCCCCCCCCC | 34.85 | 27214570 | |
| 1011 | Phosphorylation | GATRTENSVDNGSDL CCCCCCCCCCCCCCC | 25.31 | 29136822 | |
| 1016 | Phosphorylation | ENSVDNGSDLAGVTD CCCCCCCCCCCCCCC | 35.39 | 23749301 | |
| 1025 | Ubiquitination | LAGVTDGKAARNKGK CCCCCCHHHHHHCCC | 41.50 | 23749301 | |
| 1040 | Phosphorylation | NTTRRCATCGQIGHI CCCCCCCCCCCCEEE | 22.31 | 30377154 | |
| 1064 | Phosphorylation | SSKDNPASPK----- CCCCCCCCCC----- | 34.18 | 25521595 |
| 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 TAF1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TAF1_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 TAF1_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 SER-478, AND MASSSPECTROMETRY. | |
