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Q3THK3 (T2FA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
General transcription factor IIF subunit 1
Alternative name(s):
Transcription initiation factor IIF subunit alpha
Short name=TFIIF-alpha
Gene names
Name:Gtf2f1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

Heterodimer of an alpha and a beta subunit. Interacts with GTF2F2, CTDP1, TAF6/TAFII80 and URI1 By similarity.

Subcellular location

Nucleus By similarity.

Post-translational modification

Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases By similarity.

Sequence similarities

Belongs to the TFIIF alpha subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 508507General transcription factor IIF subunit 1
PRO_0000260322

Regions

Compositional bias283 – 35068Glu-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2171Phosphoserine By similarity
Modified residue2181Phosphoserine By similarity
Modified residue2211Phosphoserine Ref.2
Modified residue2241Phosphoserine Ref.2
Modified residue3311Phosphothreonine By similarity
Modified residue3771Phosphoserine By similarity
Modified residue3801Phosphoserine By similarity
Modified residue3811Phosphoserine By similarity
Modified residue3851Phosphoserine By similarity
Modified residue3891Phosphothreonine By similarity
Modified residue3911Phosphoserine By similarity
Modified residue4071N6-acetyllysine Ref.4
Modified residue4311Phosphoserine By similarity
Modified residue4331Phosphoserine By similarity
Modified residue4361Phosphoserine By similarity
Modified residue4371Phosphothreonine By similarity
Modified residue4401Phosphoserine By similarity

Experimental info

Sequence conflict1391P → T in BAE40186. Ref.1
Sequence conflict1391P → T in BAE40193. Ref.1
Sequence conflict1851Q → E in BAE40186. Ref.1
Sequence conflict1851Q → E in BAE40193. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3THK3 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: EB6DDD074CFBA712

FASTA50857,241
        10         20         30         40         50         60 
MAALGSSSQN VTEYVVRVPK NTAKRYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE 

        70         80         90        100        110        120 
EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL RVNGKSGRKF KGIKKGGVTE 

       130        140        150        160        170        180 
NTAYYIFTQC ADGAFEAFPV QNWYNFTPLA RHRTLTAEEA EEEWERRNKV LNHFSIMQQR 

       190        200        210        220        230        240 
RLKDQDQDED EEEKEKRSRK KPSELRIHDL EDDLEMSSDA SDASGEEGSR TSKAKKKAPV 

       250        260        270        280        290        300 
TKAGRKKKKK KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SPDETEGKPK VPQQEDGPKG 

       310        320        330        340        350        360 
VDEQSESSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSDDSDSSEE SDIDSETSSA 

       370        380        390        400        410        420 
LFMAKKKTPP KRERKPSGGS SKGTSRPGTP SAEAASTSST LRAAASKLEQ GKRTSETPAA 

       430        440        450        460        470        480 
KRLRMDTGPQ SLSGKSTPSS GDVQVTEDAV RRYLTRKPMT TKDLLKKFQT KKTGLSSEQT 

       490        500 
VNVLAQILKR LNPERKMIGD KMHFSLKE 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: DBA/2.
[2]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Teratocarcinoma.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK168236 mRNA. Translation: BAE40186.1.
AK168243 mRNA. Translation: BAE40193.1.
CH466537 Genomic DNA. Translation: EDL38221.1.
BC023081 mRNA. Translation: AAH23081.1.
BC031123 mRNA. Translation: AAH31123.1.
CCDSCCDS37667.1.
RefSeqNP_598562.1. NM_133801.2.
UniGeneMm.24632.

3D structure databases

ProteinModelPortalQ3THK3.
SMRQ3THK3. Positions 7-168, 440-508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid220965. 2 interactions.
IntActQ3THK3. 1 interaction.
MINTMINT-4119252.

PTM databases

PhosphoSiteQ3THK3.

Proteomic databases

MaxQBQ3THK3.
PaxDbQ3THK3.
PRIDEQ3THK3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002733; ENSMUSP00000002733; ENSMUSG00000002658.
GeneID98053.
KEGGmmu:98053.
UCSCuc008ddp.1. mouse.

Organism-specific databases

CTD2962.
MGIMGI:1923848. Gtf2f1.

Phylogenomic databases

eggNOGNOG244830.
GeneTreeENSGT00440000038032.
HOGENOMHOG000059644.
HOVERGENHBG000729.
InParanoidQ8R5B7.
KOK03138.
OMAEMPAAKR.
OrthoDBEOG7GXPBV.
TreeFamTF313850.

Gene expression databases

BgeeQ3THK3.
CleanExMM_GTF2F1.
GenevestigatorQ3THK3.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR008851. TFIIF-alpha.
IPR011039. TFIIF_interaction.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF05793. TFIIF_alpha. 1 hit.
[Graphical view]
SUPFAMSSF50916. SSF50916. 2 hits.
ProtoNetSearch...

Other

NextBio353268.
PROQ3THK3.
SOURCESearch...

Entry information

Entry nameT2FA_MOUSE
AccessionPrimary (citable) accession number: Q3THK3
Secondary accession number(s): Q8R5B7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot