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P35269 (T2FA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
General transcription factor IIF 74 kDa subunit
Transcription initiation factor IIF subunit alpha
Short name=TFIIF-alpha
Transcription initiation factor RAP74
Gene names
Name:GTF2F1
Synonyms:RAP74
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length517 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. Ref.9

Subunit structure

Heterodimer of an alpha and a beta subunit. Interacts with GTF2F2, CTDP1, TAF6/TAFII80 and URI1. Ref.7 Ref.10

Subcellular location

Nucleus.

Induction

Up-regulated in response to enterovirus 71 (EV71) infection. Ref.12

Post-translational modification

Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases. Ref.8 Ref.9

Sequence similarities

Belongs to the TFIIF alpha subunit family.

Caution

Was reported (Ref.9) to have a protein kinase activity and to autophosphorylates on Ser-385 and Thr-389.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

positive regulation of catalytic activity

Inferred from direct assay PubMed 12721286. Source: GOC

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of viral transcription

Traceable author statement. Source: Reactome

response to virus

Inferred from expression pattern Ref.12. Source: UniProtKB

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcell junction

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

transcription factor TFIIF complex

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

catalytic activity

Inferred from electronic annotation. Source: InterPro

phosphatase activator activity

Inferred from direct assay PubMed 12721286. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12721286Ref.10PubMed 7590250Ref.7. Source: UniProtKB

transcription coactivator activity

Traceable author statement PubMed 7854423. Source: ProtInc

transcription factor binding

Inferred from physical interaction Ref.8. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 517516General transcription factor IIF subunit 1
PRO_0000211231

Regions

Compositional bias283 – 35068Glu-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.15 Ref.21 Ref.22
Modified residue2171Phosphoserine Ref.8 Ref.11 Ref.16 Ref.18 Ref.20
Modified residue2181Phosphoserine Ref.8 Ref.11 Ref.16 Ref.18 Ref.20
Modified residue2211Phosphoserine Ref.8 Ref.11 Ref.16 Ref.18
Modified residue2241Phosphoserine Ref.8 Ref.11 Ref.16 Ref.18 Ref.20
Modified residue3311Phosphothreonine Ref.8 Ref.20
Modified residue3771Phosphoserine Ref.8 Ref.14
Modified residue3801Phosphoserine Ref.8 Ref.14
Modified residue3811Phosphoserine Ref.8 Ref.14
Modified residue3851Phosphoserine Ref.8 Ref.9 Ref.14 Ref.16 Ref.20
Modified residue3891Phosphothreonine Ref.8 Ref.9 Ref.14 Ref.16
Modified residue3911Phosphoserine Ref.8 Ref.20
Modified residue4071N6-acetyllysine Ref.17
Modified residue4311Phosphoserine Ref.8 Ref.14
Modified residue4331Phosphoserine Ref.8 Ref.13 Ref.14 Ref.18
Modified residue4361Phosphoserine Ref.8 Ref.14
Modified residue4461Phosphothreonine Ref.8 Ref.14
Modified residue4491Phosphoserine Ref.8 Ref.14

Natural variations

Natural variant31A → V.
Corresponds to variant rs34826931 [ dbSNP | Ensembl ].
VAR_039004

Experimental info

Mutagenesis3851S → A: Eliminates putative kinase activity; when associated with A-389. Ref.9
Mutagenesis3891T → A: Eliminates putative kinase activity; when associated with A-385. Ref.9
Sequence conflict2311V → I in CAA45404. Ref.2
Sequence conflict3611L → F in CAA45408. Ref.1

Secondary structure

........................................ 517
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35269 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 1032B04A36BDC24F

FASTA51758,240
        10         20         30         40         50         60 
MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE 

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

       130        140        150        160        170        180 
NTSYYIFTQC PDGAFEAFPV HNWYNFTPLA RHRTLTAEEA EEEWERRNKV LNHFSIMQQR 

       190        200        210        220        230        240 
RLKDQDQDED EEEKEKRGRR KASELRIHDL EDDLEMSSDA SDASGEEGGR VPKAKKKAPL 

       250        260        270        280        290        300 
AKGGRKKKKK KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SQEEPESKAK APQQEEGPKG 

       310        320        330        340        350        360 
VDEQSDSSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSEESDSSEE SDIDSEASSA 

       370        380        390        400        410        420 
LFMAKKKTPP KRERKPSGGS SRGNSRPGTP SAEGGSTSST LRAAASKLEQ GKRVSEMPAA 

       430        440        450        460        470        480 
KRLRLDTGPQ SLSGKSTPQP PSGKTTPNSG DVQVTEDAVR RYLTRKPMTT KDLLKKFQTK 

       490        500        510 
KTGLSSEQTV NVLAQILKRL NPERKMINDK MHFSLKE 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of cDNA for the large subunit of the transcription initiation factor TFIIF."
Aso T., Vasavada H.A., Kawaguchi T., Germino F.J., Ganguly S., Kitajima S., Weissman S.M., Yasukochi Y.
Nature 355:461-464(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"A cDNA encoding RAP74, a general initiation factor for transcription by RNA polymerase II."
Finkelstein A., Kostrub C.F., Li J., Chavez D.P., Wang B.Q., Fang S.M., Greenblatt J., Burton Z.F.
Nature 355:464-467(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Stomach.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye and Muscle.
[7]"Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors."
Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M., Nakatani Y., Roeder R.G.
Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAF6.
[8]"TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74."
Dikstein R., Ruppert S., Tjian R.
Cell 84:781-790(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SERINE RESIDUES.
[9]"Kinase activity and phosphorylation of the largest subunit of TFIIF transcription factor."
Rossignol M., Keriel A., Staub A., Egly J.-M.
J. Biol. Chem. 274:22387-22392(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-385 AND THR-389, MUTAGENESIS OF SER-385 AND THR-389.
[10]"Interaction with general transcription factor IIF (TFIIF) is required for the suppression of activated transcription by RPB5-mediating protein (RMP)."
Wei W., Gu J.X., Zhu C.Q., Sun F.Y., Dorjsuren D., Lin Y., Murakami S.
Cell Res. 13:111-120(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH URI1.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
Leong W.F., Chow V.T.
Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-380; SER-381; SER-385; THR-389; SER-431; SER-433; SER-436; THR-446 AND SER-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221; SER-224; SER-385 AND THR-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221; SER-224 AND SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-224; THR-331; SER-385 AND SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution."
Gaiser F., Tan S., Richmond T.J.
J. Mol. Biol. 302:1119-1127(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 5-153 IN COMPLEX WITH GTF2F2.
[24]"Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF."
Kamada K., De Angelis J., Roeder R.G., Burley S.K.
Proc. Natl. Acad. Sci. U.S.A. 98:3115-3120(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF 451-517.
[25]"Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF."
Kamada K., Roeder R.G., Burley S.K.
Proc. Natl. Acad. Sci. U.S.A. 100:2296-2299(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 449-517 IN COMPLEX WITH CTDP1.
[26]"Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB."
Nguyen B.D., Chen H.T., Kobor M.S., Greenblatt J., Legault P., Omichinski J.G.
Biochemistry 42:1460-1469(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 451-517.
[27]"NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1."
Nguyen B.D., Abbott K.L., Potempa K., Kobor M.S., Archambault J., Greenblatt J., Legault P., Omichinski J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:5688-5693(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 451-517.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64037 mRNA. Translation: CAA45408.1.
X64002 mRNA. Translation: CAA45404.1.
BT007097 mRNA. Translation: AAP35761.1.
AK315240 mRNA. Translation: BAG37667.1.
CH471139 Genomic DNA. Translation: EAW69098.1.
BC000120 mRNA. Translation: AAH00120.1.
BC013007 mRNA. Translation: AAH13007.1.
CCDSCCDS12165.1.
PIRS20248.
RefSeqNP_002087.2. NM_002096.2.
UniGeneHs.68257.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F3UX-ray1.70B/D/F/H2-172[»]
1I27X-ray1.02A449-517[»]
1J2XX-ray2.00A449-517[»]
1NHANMR-A436-517[»]
1ONVNMR-A436-517[»]
2K7LNMR-A451-517[»]
ProteinModelPortalP35269.
SMRP35269. Positions 7-168, 449-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109217. 64 interactions.
DIPDIP-677N.
IntActP35269. 11 interactions.
MINTMINT-1403790.
STRING9606.ENSP00000377969.

PTM databases

PhosphoSiteP35269.

Polymorphism databases

DMDM46397744.

Proteomic databases

MaxQBP35269.
PaxDbP35269.
PeptideAtlasP35269.
PRIDEP35269.

Protocols and materials databases

DNASU2962.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394456; ENSP00000377969; ENSG00000125651.
GeneID2962.
KEGGhsa:2962.
UCSCuc002meq.2. human.

Organism-specific databases

CTD2962.
GeneCardsGC19M006381.
HGNCHGNC:4652. GTF2F1.
HPAHPA022793.
MIM189968. gene.
neXtProtNX_P35269.
PharmGKBPA29038.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG244830.
HOGENOMHOG000059644.
HOVERGENHBG000729.
InParanoidP35269.
KOK03138.
OMAEMPAAKR.
OrthoDBEOG7GXPBV.
PhylomeDBP35269.
TreeFamTF313850.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP35269.
BgeeP35269.
CleanExHS_GTF2F1.
GenevestigatorP35269.

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

ChiTaRSGTF2F1. human.
EvolutionaryTraceP35269.
GeneWikiGTF2F1.
GenomeRNAi2962.
NextBio11742.
PMAP-CutDBP35269.
PROP35269.
SOURCESearch...

Entry information

Entry nameT2FA_HUMAN
AccessionPrimary (citable) accession number: P35269
Secondary accession number(s): B2RCS0, Q9BWN0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: April 13, 2004
Last modified: July 9, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM