CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006461
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 General transcription factor IIF subunit 1 
Protein Synonyms/Alias
 General transcription factor IIF 74 kDa subunit; Transcription initiation factor IIF subunit alpha; TFIIF-alpha; Transcription initiation factor RAP74 
Gene Name
 GTF2F1 
Gene Synonyms/Alias
 RAP74 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55ERDLSNKKIYQEEEMubiquitination[1, 2]
89KKYGIVLKEFRPEDQubiquitination[2]
169EEWERRNKVLNHFSIubiquitination[2, 3, 4, 5]
183IMQQRRLKDQDQDEDubiquitination[1]
407TLRAAASKLEQGKRVacetylation[6]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 217 217 Phosphoserine.
 MOD_RES 218 218 Phosphoserine.
 MOD_RES 221 221 Phosphoserine.
 MOD_RES 224 224 Phosphoserine.
 MOD_RES 331 331 Phosphothreonine.
 MOD_RES 377 377 Phosphoserine.
 MOD_RES 380 380 Phosphoserine.
 MOD_RES 381 381 Phosphoserine.
 MOD_RES 385 385 Phosphoserine.
 MOD_RES 389 389 Phosphothreonine.
 MOD_RES 391 391 Phosphoserine.
 MOD_RES 407 407 N6-acetyllysine.
 MOD_RES 431 431 Phosphoserine.
 MOD_RES 433 433 Phosphoserine.
 MOD_RES 436 436 Phosphoserine.
 MOD_RES 446 446 Phosphothreonine.
 MOD_RES 449 449 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 517 AA 
Protein Sequence
MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE 60
EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL RVNGKSGRKF KGIKKGGVTE 120
NTSYYIFTQC PDGAFEAFPV HNWYNFTPLA RHRTLTAEEA EEEWERRNKV LNHFSIMQQR 180
RLKDQDQDED EEEKEKRGRR KASELRIHDL EDDLEMSSDA SDASGEEGGR VPKAKKKAPL 240
AKGGRKKKKK KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SQEEPESKAK APQQEEGPKG 300
VDEQSDSSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSEESDSSEE SDIDSEASSA 360
LFMAKKKTPP KRERKPSGGS SRGNSRPGTP SAEGGSTSST LRAAASKLEQ GKRVSEMPAA 420
KRLRLDTGPQ SLSGKSTPQP PSGKTTPNSG DVQVTEDAVR RYLTRKPMTT KDLLKKFQTK 480
KTGLSSEQTV NVLAQILKRL NPERKMINDK MHFSLKE 517 
Gene Ontology
 GO:0030054; C:cell junction; IDA:HPA.
 GO:0005674; C:transcription factor TFIIF complex; TAS:ProtInc.
 GO:0003824; F:catalytic activity; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0019211; F:phosphatase activator activity; IDA:UniProtKB.
 GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
 GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
 GO:0009615; P:response to virus; IEP:UniProtKB.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 
Interpro
 IPR008851; TFIIF-alpha.
 IPR011039; TFIIF_interaction.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF05793; TFIIF_alpha 
SMART
  
PROSITE
  
PRINTS