Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

General transcription factor IIF subunit 1 (General transcription factor IIF 74 kDa subunit) (Transcription initiation factor IIF subunit alpha) (TFIIF-alpha) (Transcription initiation factor RAP74)

 T2FA_HUMAN              Reviewed;         517 AA.
P35269; B2RCS0; Q9BWN0;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
23-MAY-2018, entry version 188.
RecName: Full=General transcription factor IIF subunit 1;
AltName: Full=General transcription factor IIF 74 kDa subunit;
AltName: Full=Transcription initiation factor IIF subunit alpha;
Short=TFIIF-alpha;
AltName: Full=Transcription initiation factor RAP74;
Name=GTF2F1; Synonyms=RAP74;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1734283; DOI=10.1038/355461a0;
Aso T., Vasavada H.A., Kawaguchi T., Germino F.J., Ganguly S.,
Kitajima S., Weissman S.M., Yasukochi Y.;
"Characterization of cDNA for the large subunit of the transcription
initiation factor TFIIF.";
Nature 355:461-464(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1734284; DOI=10.1038/355464a0;
Finkelstein A., Kostrub C.F., Li J., Chavez D.P., Wang B.Q.,
Fang S.M., Greenblatt J., Burton Z.F.;
"A cDNA encoding RAP74, a general initiation factor for transcription
by RNA polymerase II.";
Nature 355:464-467(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Stomach;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH TAF6.
PubMed=7667268; DOI=10.1073/pnas.92.18.8195;
Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M.,
Nakatani Y., Roeder R.G.;
"Evolutionary conservation of human TATA-binding-polypeptide-
associated factors TAFII31 and TAFII80 and interactions of TAFII80
with other TAFs and with general transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995).
[8]
PHOSPHORYLATION AT SERINE RESIDUES.
PubMed=8625415; DOI=10.1016/S0092-8674(00)81055-7;
Dikstein R., Ruppert S., Tjian R.;
"TAFII250 is a bipartite protein kinase that phosphorylates the base
transcription factor RAP74.";
Cell 84:781-790(1996).
[9]
FUNCTION, PHOSPHORYLATION AT SER-385 AND THR-389, AND MUTAGENESIS OF
SER-385 AND THR-389.
PubMed=10428810; DOI=10.1074/jbc.274.32.22387;
Rossignol M., Keriel A., Staub A., Egly J.-M.;
"Kinase activity and phosphorylation of the largest subunit of TFIIF
transcription factor.";
J. Biol. Chem. 274:22387-22392(1999).
[10]
INTERACTION WITH URI1.
PubMed=12737519; DOI=10.1038/sj.cr.7290155;
Wei W., Gu J.X., Zhu C.Q., Sun F.Y., Dorjsuren D., Lin Y.,
Murakami S.;
"Interaction with general transcription factor IIF (TFIIF) is required
for the suppression of activated transcription by RPB5-mediating
protein (RMP).";
Cell Res. 13:111-120(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221
AND SER-224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
Leong W.F., Chow V.T.;
"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
reveal differential cellular gene expression in response to
enterovirus 71 infection.";
Cell. Microbiol. 8:565-580(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
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, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-385 AND
THR-389, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-221;
SER-224 AND SER-433, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-218; SER-224;
THR-331; SER-385 AND SER-391, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156; SER-377; SER-385;
THR-389; SER-431; SER-433 AND THR-437, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 5-153 IN COMPLEX WITH GTF2F2.
PubMed=11183778; DOI=10.1006/jmbi.2000.4110;
Gaiser F., Tan S., Richmond T.J.;
"Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A
resolution.";
J. Mol. Biol. 302:1119-1127(2000).
[26]
X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF 451-517.
PubMed=11248041; DOI=10.1073/pnas.051631098;
Kamada K., De Angelis J., Roeder R.G., Burley S.K.;
"Crystal structure of the C-terminal domain of the RAP74 subunit of
human transcription factor IIF.";
Proc. Natl. Acad. Sci. U.S.A. 98:3115-3120(2001).
[27]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 449-517 IN COMPLEX WITH
CTDP1.
PubMed=12591941; DOI=10.1073/pnas.262798199;
Kamada K., Roeder R.G., Burley S.K.;
"Molecular mechanism of recruitment of TFIIF-associating RNA
polymerase C-terminal domain phosphatase (FCP1) by transcription
factor IIF.";
Proc. Natl. Acad. Sci. U.S.A. 100:2296-2299(2003).
[28]
STRUCTURE BY NMR OF 451-517.
PubMed=12578358; DOI=10.1021/bi0265473;
Nguyen B.D., Chen H.T., Kobor M.S., Greenblatt J., Legault P.,
Omichinski J.G.;
"Solution structure of the carboxyl-terminal domain of RAP74 and NMR
characterization of the FCP1-binding sites of RAP74 and human TFIIB.";
Biochemistry 42:1460-1469(2003).
[29]
STRUCTURE BY NMR OF 451-517.
PubMed=12732728; DOI=10.1073/pnas.1031524100;
Nguyen B.D., Abbott K.L., Potempa K., Kobor M.S., Archambault J.,
Greenblatt J., Legault P., Omichinski J.G.;
"NMR structure of a complex containing the TFIIF subunit RAP74 and the
RNA polymerase II carboxyl-terminal domain phosphatase FCP1.";
Proc. Natl. Acad. Sci. U.S.A. 100:5688-5693(2003).
-!- 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. {ECO:0000269|PubMed:10428810}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts
with GTF2F2, CTDP1, TAF6/TAFII80 and URI1.
{ECO:0000269|PubMed:11183778, ECO:0000269|PubMed:12591941,
ECO:0000269|PubMed:12737519, ECO:0000269|PubMed:7667268}.
-!- INTERACTION:
P13984:GTF2F2; NbExp=2; IntAct=EBI-457886, EBI-1030560;
P11831:SRF; NbExp=2; IntAct=EBI-457886, EBI-493034;
P21675:TAF1; NbExp=3; IntAct=EBI-457886, EBI-491289;
O94763:URI1; NbExp=3; IntAct=EBI-457886, EBI-357067;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71)
infection. {ECO:0000269|PubMed:16548883}.
-!- PTM: Phosphorylated on Ser and other residues by TAF1 and casein
kinase II-like kinases. {ECO:0000269|PubMed:10428810,
ECO:0000269|PubMed:8625415}.
-!- SIMILARITY: Belongs to the TFIIF alpha subunit family.
{ECO:0000305}.
-!- CAUTION: Was reported to have a protein kinase activity and to
autophosphorylates on Ser-385 and Thr-389.
{ECO:0000305|PubMed:10428810}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X64037; CAA45408.1; -; mRNA.
EMBL; X64002; CAA45404.1; -; mRNA.
EMBL; BT007097; AAP35761.1; -; mRNA.
EMBL; AK315240; BAG37667.1; -; mRNA.
EMBL; CH471139; EAW69098.1; -; Genomic_DNA.
EMBL; BC000120; AAH00120.1; -; mRNA.
EMBL; BC013007; AAH13007.1; -; mRNA.
CCDS; CCDS12165.1; -.
PIR; S20248; S20248.
RefSeq; NP_002087.2; NM_002096.2.
UniGene; Hs.68257; -.
PDB; 1F3U; X-ray; 1.70 A; B/D/F/H=2-172.
PDB; 1I27; X-ray; 1.02 A; A=449-517.
PDB; 1J2X; X-ray; 2.00 A; A=449-517.
PDB; 1NHA; NMR; -; A=436-517.
PDB; 1ONV; NMR; -; A=436-517.
PDB; 2K7L; NMR; -; A=451-517.
PDB; 5IY6; EM; 7.20 A; S=1-517.
PDB; 5IY7; EM; 8.60 A; S=1-517.
PDB; 5IY8; EM; 7.90 A; S=1-517.
PDB; 5IY9; EM; 6.30 A; S=1-517.
PDB; 5IYA; EM; 5.40 A; S=1-517.
PDB; 5IYB; EM; 3.90 A; S=1-517.
PDB; 5IYC; EM; 3.90 A; S=1-517.
PDB; 5IYD; EM; 3.90 A; S=1-517.
PDBsum; 1F3U; -.
PDBsum; 1I27; -.
PDBsum; 1J2X; -.
PDBsum; 1NHA; -.
PDBsum; 1ONV; -.
PDBsum; 2K7L; -.
PDBsum; 5IY6; -.
PDBsum; 5IY7; -.
PDBsum; 5IY8; -.
PDBsum; 5IY9; -.
PDBsum; 5IYA; -.
PDBsum; 5IYB; -.
PDBsum; 5IYC; -.
PDBsum; 5IYD; -.
ProteinModelPortal; P35269; -.
SMR; P35269; -.
BioGrid; 109217; 109.
CORUM; P35269; -.
DIP; DIP-677N; -.
IntAct; P35269; 28.
MINT; P35269; -.
STRING; 9606.ENSP00000377969; -.
iPTMnet; P35269; -.
PhosphoSitePlus; P35269; -.
BioMuta; GTF2F1; -.
DMDM; 46397744; -.
EPD; P35269; -.
MaxQB; P35269; -.
PaxDb; P35269; -.
PeptideAtlas; P35269; -.
PRIDE; P35269; -.
TopDownProteomics; P35269; -.
DNASU; 2962; -.
Ensembl; ENST00000394456; ENSP00000377969; ENSG00000125651.
GeneID; 2962; -.
KEGG; hsa:2962; -.
UCSC; uc002meq.3; human.
CTD; 2962; -.
DisGeNET; 2962; -.
EuPathDB; HostDB:ENSG00000125651.13; -.
GeneCards; GTF2F1; -.
HGNC; HGNC:4652; GTF2F1.
HPA; HPA022793; -.
HPA; HPA028707; -.
MIM; 189968; gene.
neXtProt; NX_P35269; -.
OpenTargets; ENSG00000125651; -.
PharmGKB; PA29038; -.
eggNOG; KOG2393; Eukaryota.
eggNOG; ENOG410XSRW; LUCA.
GeneTree; ENSGT00440000038032; -.
HOGENOM; HOG000059644; -.
HOVERGEN; HBG000729; -.
InParanoid; P35269; -.
KO; K03138; -.
OMA; GAIEAYP; -.
OrthoDB; EOG091G0N3J; -.
PhylomeDB; P35269; -.
TreeFam; TF313850; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
Reactome; R-HSA-167287; HIV elongation arrest and recovery.
Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-6803529; FGFR2 alternative splicing.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-HSA-72086; mRNA Capping.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
SIGNOR; P35269; -.
ChiTaRS; GTF2F1; human.
EvolutionaryTrace; P35269; -.
GeneWiki; GTF2F1; -.
GenomeRNAi; 2962; -.
PMAP-CutDB; P35269; -.
PRO; PR:P35269; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000125651; -.
CleanEx; HS_GTF2F1; -.
ExpressionAtlas; P35269; baseline and differential.
Genevisible; P35269; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0005674; C:transcription factor TFIIF complex; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0019211; F:phosphatase activator activity; IDA:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0019903; F:protein phosphatase binding; IPI:CAFA.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:InterPro.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0042795; P:snRNA transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR008851; TFIIF-alpha.
InterPro; IPR011039; TFIIF_interaction.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF05793; TFIIF_alpha; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF50916; SSF50916; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 517 General transcription factor IIF subunit
1.
/FTId=PRO_0000211231.
COMPBIAS 283 350 Glu-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 156 156 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 331 331 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 381 381 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10428810}.
MOD_RES 389 389 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10428810}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 407 407 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 431 431 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 433 433 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 436 436 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 437 437 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 446 446 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VARIANT 3 3 A -> V (in dbSNP:rs34826931).
/FTId=VAR_039004.
MUTAGEN 385 385 S->A: Eliminates putative kinase
activity; when associated with A-389.
{ECO:0000269|PubMed:10428810}.
MUTAGEN 389 389 T->A: Eliminates putative kinase
activity; when associated with A-385.
{ECO:0000269|PubMed:10428810}.
CONFLICT 231 231 V -> I (in Ref. 2; CAA45404).
{ECO:0000305}.
CONFLICT 361 361 L -> F (in Ref. 1; CAA45408).
{ECO:0000305}.
STRAND 10 17 {ECO:0000244|PDB:1F3U}.
STRAND 23 31 {ECO:0000244|PDB:1F3U}.
HELIX 33 35 {ECO:0000244|PDB:1F3U}.
HELIX 39 41 {ECO:0000244|PDB:1F3U}.
STRAND 45 49 {ECO:0000244|PDB:1F3U}.
HELIX 52 55 {ECO:0000244|PDB:1F3U}.
STRAND 58 61 {ECO:0000244|PDB:1F3U}.
HELIX 76 78 {ECO:0000244|PDB:1F3U}.
STRAND 84 87 {ECO:0000244|PDB:1F3U}.
STRAND 98 104 {ECO:0000244|PDB:1F3U}.
STRAND 109 114 {ECO:0000244|PDB:1F3U}.
STRAND 120 129 {ECO:0000244|PDB:1F3U}.
STRAND 135 148 {ECO:0000244|PDB:1F3U}.
HELIX 149 151 {ECO:0000244|PDB:1F3U}.
HELIX 157 167 {ECO:0000244|PDB:1F3U}.
HELIX 456 465 {ECO:0000244|PDB:1I27}.
HELIX 470 475 {ECO:0000244|PDB:1I27}.
HELIX 479 482 {ECO:0000244|PDB:1I27}.
HELIX 486 500 {ECO:0000244|PDB:1I27}.
STRAND 503 507 {ECO:0000244|PDB:1I27}.
STRAND 510 515 {ECO:0000244|PDB:1I27}.
SEQUENCE 517 AA; 58240 MW; 1032B04A36BDC24F CRC64;
MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE
EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL RVNGKSGRKF KGIKKGGVTE
NTSYYIFTQC PDGAFEAFPV HNWYNFTPLA RHRTLTAEEA EEEWERRNKV LNHFSIMQQR
RLKDQDQDED EEEKEKRGRR KASELRIHDL EDDLEMSSDA SDASGEEGGR VPKAKKKAPL
AKGGRKKKKK KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SQEEPESKAK APQQEEGPKG
VDEQSDSSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSEESDSSEE SDIDSEASSA
LFMAKKKTPP KRERKPSGGS SRGNSRPGTP SAEGGSTSST LRAAASKLEQ GKRVSEMPAA
KRLRLDTGPQ SLSGKSTPQP PSGKTTPNSG DVQVTEDAVR RYLTRKPMTT KDLLKKFQTK
KTGLSSEQTV NVLAQILKRL NPERKMINDK MHFSLKE


Related products :

Catalog number Product name Quantity
EIAAB41099 General transcription factor IIF 74 kDa subunit,General transcription factor IIF subunit 1,GTF2F1,Homo sapiens,Human,RAP74,TFIIF-alpha,Transcription initiation factor IIF subunit alpha,Transcription i
18-003-43305 Transcription initiation factor IIF subunit alpha - EC 2.7.11.1; TFIIF-alpha; General transcription factor IIF subunit 1; Transcription initiation factor RAP74; General transcription factor IIF polype 0.05 mg Aff Pur
EIAAB41095 General transcription factor IIE 56 kDa subunit,General transcription factor IIE subunit 1,GTF2E1,Homo sapiens,Human,TF2E1,TFIIE-alpha,Transcription initiation factor IIE subunit alpha
EIAAB41105 ATP-dependent helicase GTF2F2,General transcription factor IIF 30 kDa subunit,General transcription factor IIF subunit 2,GTF2F2,Homo sapiens,Human,RAP30,TFIIF-beta,Transcription initiation factor IIF
EIAAB41093 General transcription factor IIE 56 kDa subunit,General transcription factor IIE subunit 1,Gtf2e1,Mouse,Mus musculus,TFIIE-alpha,Transcription initiation factor IIE subunit alpha
EIAAB41101 Bos taurus,Bovine,General transcription factor IIF subunit 1,GTF2F1,TFIIF-alpha,Transcription initiation factor IIF subunit alpha
EIAAB41102 General transcription factor IIF subunit 1,Gtf2f1,Mouse,Mus musculus,TFIIF-alpha,Transcription initiation factor IIF subunit alpha
EIAAB41100 General transcription factor IIF subunit 1,Gtf2f1,Rat,Rattus norvegicus,TFIIF-alpha,Transcription initiation factor IIF subunit alpha
EIAAB41103 ATP-dependent helicase GTF2F2,General transcription factor IIF subunit 2,Gtf2f2,Rap30,Rat,Rattus norvegicus,TFIIF-beta,Transcription initiation factor IIF subunit beta,Transcription initiation factor
EIAAB42031 General transcription factor IIA subunit 1,GTF2A1,Homo sapiens,Human,TF2A1,TFIIA-42,TFIIAL,Transcription initiation factor IIA subunit 1,Transcription initiation factor TFIIA 42 kDa subunit
EIAAB41094 Bos taurus,Bovine,General transcription factor IIE subunit 1,GTF2E1,TFIIE-alpha,Transcription initiation factor IIE subunit alpha
EIAAB41090 General transcription factor IIA subunit 2,Gtf2a2,Rat,Rattus norvegicus,TFIIA-gamma,Transcription initiation factor IIA gamma chain,Transcription initiation factor IIA subunit 2
EIAAB41092 General transcription factor IIA subunit 2,Gtf2a2,Mouse,Mus musculus,TFIIA-gamma,Transcription initiation factor IIA gamma chain,Transcription initiation factor IIA subunit 2
EIAAB42050 Basic transcription factor 2 52 kDa subunit,BTF2 p52,General transcription factor IIH polypeptide 4,General transcription factor IIH subunit 4,GTF2H4,Homo sapiens,Human,TFIIH basal transcription facto
EIAAB42045 Basic transcription factor 2 34 kDa subunit,BTF2 p34,General transcription factor IIH polypeptide 3,General transcription factor IIH subunit 3,GTF2H3,Homo sapiens,Human,TFIIH basal transcription facto
EIAAB42048 Basic transcription factor 2 34 kDa subunit,BTF2 p34,General transcription factor IIH polypeptide 3,General transcription factor IIH subunit 3,Gtf2h3,Mouse,Mus musculus,TFIIH basal transcription facto
EIAAB42039 Basic transcription factor 2 62 kDa subunit,BTF2 p62,General transcription factor IIH polypeptide 1,General transcription factor IIH subunit 1,Gtf2h1,Mouse,Mus musculus,TFIIH basal transcription facto
EIAAB42049 Basic transcription factor 2 52 kDa subunit,BTF2 p52,General transcription factor IIH polypeptide 4,General transcription factor IIH subunit 4,Gtf2h4,Mouse,Mus musculus,TFIIH basal transcription facto
18-003-43034 Transcription initiation factor IIE subunit alpha - TFIIE-alpha; General transcription factor IIE 56 kDa subunit Polyclonal 0.05 mg Aff Pur
EIAAB42042 Basic transcription factor 2 44 kDa subunit,BTF2 p44,General transcription factor IIH polypeptide 2,General transcription factor IIH subunit 2,Gtf2h2,Rat,Rattus norvegicus,TFIIH basal transcription fa
EIAAB41091 General transcription factor IIA subunit 2,GTF2A2,Homo sapiens,Human,TF2A2,TFIIA p12 subunit,TFIIA-12,TFIIA-gamma,TFIIAS,Transcription initiation factor IIA gamma chain,Transcription initiation factor
EIAAB42053 C6orf175,General transcription factor IIH polypeptide 5,General transcription factor IIH subunit 5,GTF2H5,Homo sapiens,Human,TFB5 ortholog,TFIIH basal transcription factor complex TTD-A subunit,TTDA
EIAAB42043 Basic transcription factor 2 44 kDa subunit,BTF2 p44,BTF2P44,General transcription factor IIH polypeptide 2,General transcription factor IIH subunit 2,GTF2H2,Homo sapiens,Human,TFIIH basal transcripti
EIAAB42052 D17Wsu155e,General transcription factor IIH polypeptide 5,General transcription factor IIH subunit 5,Gtf2h5,Mouse,Mus musculus,TFB5 ortholog,TFIIH basal transcription factor complex TTD-A subunit
EIAAB42044 Basic transcription factor 2 44 kDa subunit,BTF2 p44,Btf2p44,General transcription factor IIH polypeptide 2,General transcription factor IIH subunit 2,Gtf2h2,Mouse,Mus musculus,TFIIH basal transcripti


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur