CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007518
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription initiation factor IIF subunit alpha 
Protein Synonyms/Alias
 TFIIF-alpha; TFIIF large subunit; Transcription factor G 105 kDa subunit; P105 
Gene Name
 TFG1 
Gene Synonyms/Alias
 SSU71; YGR186W; G7526 
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
23TNASPFIKRDRMRRNacetylation[1]
120NMRTHLLKFQSKKKIacetylation[1]
340KVLDENAKKLRFEEFubiquitination[2]
394IPADKVYKFTARNKYubiquitination[2]
426EVPRWLMKHLDNIGTacetylation[1]
604ATNAHVHKEPTLRVKacetylation[1]
628KGDKKILKSFPEGEWacetylation[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]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 TFIIF is a general transcription initiation factor that binds to RNA polymerase II. Its functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation. 
Sequence Annotation
 MOD_RES 198 198 Phosphoserine.
 MOD_RES 200 200 Phosphothreonine.
 MOD_RES 515 515 Phosphoserine.
 MOD_RES 560 560 Phosphoserine.
 MOD_RES 562 562 Phosphoserine.
 MOD_RES 571 571 Phosphoserine.
 MOD_RES 655 655 Phosphoserine.  
Keyword
 Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 735 AA 
Protein Sequence
MSRRNPPGSR NGGGPTNASP FIKRDRMRRN FLRMRMGQNG SNSSSPGVPN GDNSRGSLVK 60
KDDPEYAEER EKMLLQIGVE ADAGRSNVKV KDEDPNEYNE FPLRAIPKED LENMRTHLLK 120
FQSKKKINPV TDFHLPVRLH RKDTRNLQFQ LTRAEIVQRQ KEISEYKKKA EQERSTPNSG 180
GMNKSGTVSL NNTVKDGSQT PTVDSVTKDN TANGVNSSIP TVTGSSVPPA SPTTVSAVES 240
NGLSNGSTSA ANGLDGNAST ANLANGRPLV TKLEDAGPAE DPTKVGMVKY DGKEVTNEPE 300
FEEGTMDPLA DVAPDGGGRA KRGNLRRKTR QLKVLDENAK KLRFEEFYPW VMEDFDGYNT 360
WVGSYEAGNS DSYVLLSVED DGSFTMIPAD KVYKFTARNK YATLTIDEAE KRMDKKSGEV 420
PRWLMKHLDN IGTTTTRYDR TRRKLKAVAD QQAMDEDDRD DNSEVELDYD EEFADDEEAP 480
IIDGNEQENK ESEQRIKKEM LQANAMGLRD EEAPSENEED ELFGEKKIDE DGERIKKALQ 540
KTELAALYSS DENEINPYLS ESDIENKENE SPVKKEEDSD TLSKSKRSSP KKQQKKATNA 600
HVHKEPTLRV KSIKNCVIIL KGDKKILKSF PEGEWNPQTT KAVDSSNNAS NTVPSPIKQE 660
EGLNSTVAER EETPAPTITE KDIIEAIGDG KVNIKEFGKF IRRKYPGAEN KKLMFAIVKK 720
LCRKVGNDHM ELKKE 735 
Gene Ontology
 GO:0005674; C:transcription factor TFIIF complex; IDA:SGD.
 GO:0003824; F:catalytic activity; IEA:InterPro.
 GO:0000991; F:core RNA polymerase II binding transcription factor activity; IDA:SGD.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0072542; F:protein phosphatase activator activity; IDA:SGD.
 GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IEA:InterPro.
 GO:0001111; P:promoter clearance from RNA polymerase II promoter; IC:SGD.
 GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IDA:SGD.
 GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; IC:SGD.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
 GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IMP:SGD. 
Interpro
 IPR008851; TFIIF-alpha.
 IPR011039; TFIIF_interaction. 
Pfam
 PF05793; TFIIF_alpha 
SMART
  
PROSITE
  
PRINTS