| Tag | Content |
|---|
| CPLM ID | CPLM-006215 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | RNA polymerase II transcription factor B subunit 1 |
Protein Synonyms/Alias | General transcription and DNA repair factor IIH subunit TFB1; TFIIH subunit TFB1; RNA polymerase II transcription factor B 73 kDa subunit; RNA polymerase II transcription factor B p73 subunit |
Gene Name | TFB1 |
Gene Synonyms/Alias | YDR311W; D9740.3 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 335 | MLLHPVKKIIDLDGN | acetylation | [1] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | Acts as component of the general transcription and DNA repair factor IIH (TFIIH) core, which is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase activity, and is essential for polymerase II transcription in vitro. |
Sequence Annotation | DOMAIN 165 221 BSD 1.
DOMAIN 243 295 BSD 2.
MOD_RES 150 150 Phosphothreonine. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 642 AA |
Protein Sequence | MSHSGAAIFE KVSGIIAINE DVSPAELTWR STDGDKVHTV VLSTIDKLQA TPASSEKMML 60
RLIGKVDESK KRKDNEGNEV VPKPQRHMFS FNNRTVMDNI KMTLQQIISR YKDADIYEEK 120
RRREESAQHT ETPMSSSSVT AGTPTPHLDT PQLNNGAPLI NTAKLDDSLS KEKLLTNLKL 180
QQSLLKGNKV LMKVFQETVI NAGLPPSEFW STRIPLLRAF ALSTSQKVGP YNVLSTIKPV 240
ASSENKVNVN LSREKILNIF ENYPIVKKAY TDNVPKNFKE PEFWARFFSS KLFRKLRGEK 300
IMQNDRGDVI IDRYLTLDQE FDRKDDDMLL HPVKKIIDLD GNIQDDPVVR GNRPDFTMQP 360
GVDINGNSDG TVDILKGMNR LSEKMIMALK NEYSRTNLQN KSNITNDEED EDNDERNELK 420
IDDLNESYKT NYAIIHLKRN AHEKTTDNDA KSSADSIKNA DLKVSNQQML QQLSLVMDNL 480
INKLDLNQVV PNNEVSNKIN KRVITAIKIN AKQAKHNNVN SALGSFVDNT SQANELEVKS 540
TLPIDLLESC RMLHTTCCEF LKHFYIHFQS GEQKQASTVK KLYNHLKDCI EKLNELFQDV 600
LNGDGESMSN TCTAYLKPVL NSITLATHKY DEYFNEYNNN SN 642 |
Gene Ontology | GO:0000439; C:core TFIIH complex; IDA:SGD. GO:0005829; C:cytosol; IDA:SGD. GO:0005675; C:holo TFIIH complex; IDA:SGD. GO:0000112; C:nucleotide-excision repair factor 3 complex; IDA:SGD. GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD. GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:SGD. GO:0006289; P:nucleotide-excision repair; IMP:SGD. GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD. GO:0006360; P:transcription from RNA polymerase I promoter; IMP:SGD. GO:0006366; P:transcription from RNA polymerase II promoter; IDA:SGD. |
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