Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  General transcription factor IIF subunit 1  

UniProtKB / Swiss-Prot ID :  T2FA_MOUSE

Gene Name (Synonyms) : 
Gtf2f1  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus (By similarity). 

Protein Function :  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 (By similarity). 

Protein Sequence MAALGSSSQNVTEYVVRVPKNTAKRYNIMAFNAADKVNFATWNQARLERDLSNKKIYQEEEMPESGAGSE...
Predicted Secondary Structure CCCCCCCCCCEEEEEEECCCCCCCCEEEEEECCCCCCCHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
154PhosphothreonineARHRTLTAE
HHHCCCCCC
23.49Phosphositeplus
Link-
156PhosphothreonineHRTLTAEEA
HCCCCCCHH
31.26Phosphositeplus
Link-
217PhosphoserineDLEMSSDAS
CCCCCCCCC
18.72Phosphositeplus
Link-
217PhosphoserineDLEMSSDAS
CCCCCCCCC
18.72SysPTM
Link-
217Phosphoserine.DLEMSSDAS
CCCCCCCCC
18.72UniProtKB
Link-
218PhosphoserineLEMSSDASD
CCCCCCCCC
35.57Phosphositeplus
Link-
218PhosphoserineLEMSSDASD
CCCCCCCCC
35.57SysPTM
Link-
218Phosphoserine.LEMSSDASD
CCCCCCCCC
35.57UniProtKB
Link-
221PhosphoserineSSDASDASG
CCCCCCCCC
38.41Phosphositeplus
Link-
221PhosphoserineSSDASDASG
CCCCCCCCC
38.41SysPTM
Link-
221Phosphoserine.SSDASDASG
CCCCCCCCC
38.41UniProtKB
Link-
224PhosphoserineASDASGEEG
CCCCCCCCC
52.29Phosphositeplus
Link-
224PhosphoserineASDASGEEG
CCCCCCCCC
52.29SysPTM
Link-
224Phosphoserine.ASDASGEEG
CCCCCCCCC
52.29UniProtKB
Link-
305PhosphoserineVDEQSESSE
CCCCCCCCC
37.08Phosphositeplus
Link-
305PhosphoserineVDEQSESSE
CCCCCCCCC
37.08SysPTM
Link-
307PhosphoserineEQSESSEES
CCCCCCCCC
48.58Phosphositeplus
Link-
307PhosphoserineEQSESSEES
CCCCCCCCC
48.58SysPTM
Link-
308PhosphoserineQSESSEESE
CCCCCCCCC
41.13Phosphositeplus
Link-
308PhosphoserineQSESSEESE
CCCCCCCCC
41.13SysPTM
Link-
311PhosphoserineSSEESEEEK
CCCCCCCCC
46.38Phosphositeplus
Link-
311PhosphoserineSSEESEEEK
CCCCCCCCC
46.38SysPTM
Link-
331PhosphothreonineKKAPTPQEK
CCCCCCCCC
42.33Phosphositeplus
Link-
331Phosphothreonine.KKAPTPQEK
CCCCCCCCC
42.33UniProtKB
Link-
377PhosphoserineERKPSGGSS
CCCCCCCCC
59.84Phosphositeplus
Link-
380PhosphoserinePSGGSSKGT
CCCCCCCCC
32.19Phosphositeplus
Link-
381PhosphoserineSGGSSKGTS
CCCCCCCCC
38.08Phosphositeplus
Link-
384PhosphothreonineSSKGTSRPG
CCCCCCCCC
25.87Phosphositeplus
Link-
384PhosphothreonineSSKGTSRPG
CCCCCCCCC
25.87SysPTM
Link-
385PhosphoserineSKGTSRPGT
CCCCCCCCC
45.18Phosphositeplus
Link-
385PhosphoserineSKGTSRPGT
CCCCCCCCC
45.18SysPTM
Link-
389PhosphothreonineSRPGTPSAE
CCCCCCCCC
19.43Phosphositeplus
Link-
389PhosphothreonineSRPGTPSAE
CCCCCCCCC
19.43SysPTM
Link-
391PhosphoserinePGTPSAEAA
CCCCCCCCC
38.28Phosphositeplus
Link-
425Methionine sulfoneKRLRMDTGP
CCCCCCCCC
6.82SysPTM
Link-
427PhosphothreonineLRMDTGPQS
CCCCCCCCC
41.22SysPTM
Link-
431PhosphoserineTGPQSLSGK
CCCCCCCCC
27.86Phosphositeplus
Link-
433PhosphoserinePQSLSGKST
CCCCCCCCC
49.80Phosphositeplus
Link-
436PhosphoserineLSGKSTPSS
CCCCCCCCC
49.42Phosphositeplus
Link-
437PhosphothreonineSGKSTPSSG
CCCCCCCCC
30.58Phosphositeplus
Link-
437PhosphothreonineSGKSTPSSG
CCCCCCCCC
30.58SysPTM
Link-
439PhosphoserineKSTPSSGDV
CCCCCCCCC
47.22Phosphositeplus
Link-
440PhosphoserineSTPSSGDVQ
CCCCCCCCC
39.97Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221AND SER-224, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-331, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures