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General transcription factor IIF subunit 2 (EC 3.6.4.12) (ATP-dependent helicase GTF2F2) (General transcription factor IIF 30 kDa subunit) (Transcription initiation factor IIF subunit beta) (TFIIF-beta) (Transcription initiation factor RAP30)

 T2FB_HUMAN              Reviewed;         249 AA.
P13984; A6NNS5; Q5W0H3;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
22-NOV-2017, entry version 185.
RecName: Full=General transcription factor IIF subunit 2;
EC=3.6.4.12;
AltName: Full=ATP-dependent helicase GTF2F2;
AltName: Full=General transcription factor IIF 30 kDa subunit;
AltName: Full=Transcription initiation factor IIF subunit beta;
Short=TFIIF-beta;
AltName: Full=Transcription initiation factor RAP30;
Name=GTF2F2; Synonyms=RAP30;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
TISSUE=Kidney;
PubMed=2477704; DOI=10.1038/341410a0;
Sopta M., Burton Z.F., Greenblatt J.;
"Structure and associated DNA-helicase activity of a general
transcription initiation factor that binds to RNA polymerase II.";
Nature 341:410-414(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1840667; DOI=10.1093/nar/19.19.5436;
Horikoshi M., Fujita H., Wang J., Takada R., Roeder R.G.;
"Nucleotide and amino acid sequence of RAP30.";
Nucleic Acids Res. 19:5436-5436(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[4]
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
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).
[8]
INTERACTION WITH HTATSF1, AND SUBCELLULAR LOCATION.
PubMed=10454543; DOI=10.1128/MCB.19.9.5960;
Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.;
"Tat-SF1 protein associates with RAP30 and human SPT5 proteins.";
Mol. Cell. Biol. 19:5960-5968(1999).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, 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).
[11]
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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-33 AND LYS-137, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, 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).
[14]
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).
[15]
STRUCTURE BY NMR OF 175-243.
PubMed=9689043; DOI=10.1073/pnas.95.16.9117;
Groft C.M., Uljon S.N., Wang R., Werner M.H.;
"Structural homology between the Rap30 DNA-binding domain and linker
histone H5: implications for preinitiation complex assembly.";
Proc. Natl. Acad. Sci. U.S.A. 95:9117-9122(1998).
-!- 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. This subunit shows ATP-dependent DNA-
helicase activity. {ECO:0000269|PubMed:2477704}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts
with HTATSF1 and GPBP1 (By similarity). Interacts with URI1.
{ECO:0000250, ECO:0000269|PubMed:10454543,
ECO:0000269|PubMed:12737519}.
-!- INTERACTION:
P35269:GTF2F1; NbExp=2; IntAct=EBI-1030560, EBI-457886;
P46776:RPL27A; NbExp=2; IntAct=EBI-1030560, EBI-350581;
Q8WW35:TCTEX1D2; NbExp=2; IntAct=EBI-1030560, EBI-2692044;
O94763:URI1; NbExp=4; IntAct=EBI-1030560, EBI-357067;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10454543}.
-!- SIMILARITY: Belongs to the TFIIF beta subunit family.
{ECO:0000305}.
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EMBL; X16901; CAA34775.1; -; mRNA.
EMBL; X59745; CAA42419.1; -; mRNA.
EMBL; AK291545; BAF84234.1; -; mRNA.
EMBL; BT019525; AAV38332.1; -; mRNA.
EMBL; AL138963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08728.1; -; Genomic_DNA.
EMBL; BC001771; AAH01771.1; -; mRNA.
CCDS; CCDS9395.1; -.
PIR; S06141; S06141.
PIR; S18677; S18677.
RefSeq; NP_004119.1; NM_004128.2.
UniGene; Hs.654582; -.
PDB; 1BBY; NMR; -; A=175-243.
PDB; 1F3U; X-ray; 1.70 A; A/C/E/G=2-119.
PDB; 2BBY; NMR; -; A=175-243.
PDB; 5IY6; EM; 7.20 A; T=1-249.
PDB; 5IY7; EM; 8.60 A; T=1-249.
PDB; 5IY8; EM; 7.90 A; T=1-249.
PDB; 5IY9; EM; 6.30 A; T=1-249.
PDB; 5IYA; EM; 5.40 A; T=1-249.
PDB; 5IYB; EM; 3.90 A; T=1-249.
PDB; 5IYC; EM; 3.90 A; T=1-249.
PDB; 5IYD; EM; 3.90 A; T=1-249.
PDBsum; 1BBY; -.
PDBsum; 1F3U; -.
PDBsum; 2BBY; -.
PDBsum; 5IY6; -.
PDBsum; 5IY7; -.
PDBsum; 5IY8; -.
PDBsum; 5IY9; -.
PDBsum; 5IYA; -.
PDBsum; 5IYB; -.
PDBsum; 5IYC; -.
PDBsum; 5IYD; -.
ProteinModelPortal; P13984; -.
SMR; P13984; -.
BioGrid; 109218; 51.
CORUM; P13984; -.
DIP; DIP-41680N; -.
IntAct; P13984; 41.
MINT; MINT-193667; -.
STRING; 9606.ENSP00000340823; -.
iPTMnet; P13984; -.
PhosphoSitePlus; P13984; -.
BioMuta; GTF2F2; -.
DMDM; 464519; -.
EPD; P13984; -.
MaxQB; P13984; -.
PaxDb; P13984; -.
PeptideAtlas; P13984; -.
PRIDE; P13984; -.
DNASU; 2963; -.
Ensembl; ENST00000340473; ENSP00000340823; ENSG00000188342.
GeneID; 2963; -.
KEGG; hsa:2963; -.
UCSC; uc001uzw.4; human.
CTD; 2963; -.
DisGeNET; 2963; -.
EuPathDB; HostDB:ENSG00000188342.11; -.
GeneCards; GTF2F2; -.
HGNC; HGNC:4653; GTF2F2.
HPA; HPA006912; -.
MIM; 189969; gene.
neXtProt; NX_P13984; -.
OpenTargets; ENSG00000188342; -.
PharmGKB; PA29039; -.
eggNOG; KOG2905; Eukaryota.
eggNOG; COG5090; LUCA.
GeneTree; ENSGT00390000016051; -.
HOGENOM; HOG000294179; -.
HOVERGEN; HBG001606; -.
InParanoid; P13984; -.
KO; K03139; -.
OMA; NMWELKK; -.
OrthoDB; EOG091G0IN2; -.
PhylomeDB; P13984; -.
TreeFam; TF314290; -.
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.
ChiTaRS; GTF2F2; human.
EvolutionaryTrace; P13984; -.
GeneWiki; GTF2F2; -.
GenomeRNAi; 2963; -.
PRO; PR:P13984; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000188342; -.
CleanEx; HS_GTF2F2; -.
ExpressionAtlas; P13984; baseline and differential.
Genevisible; P13984; HS.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005674; C:transcription factor TFIIF complex; IBA:GO_Central.
GO; GO:0097550; C:transcriptional preinitiation complex; IDA:CAFA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0000991; F:transcription factor activity, core RNA polymerase II binding; IBA:GO_Central.
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:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0042795; P:snRNA transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription 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; IPR003196; TFIIF_beta.
InterPro; IPR011039; TFIIF_interaction.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR10445; PTHR10445; 1.
Pfam; PF02270; TFIIF_beta; 1.
PIRSF; PIRSF015849; TFIIF-beta; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF50916; SSF50916; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome;
Direct protein sequencing; DNA-binding; Helicase; Hydrolase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 249 General transcription factor IIF subunit
2.
/FTId=PRO_0000211235.
NP_BIND 36 43 ATP. {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 22 22 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 33 33 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 137 137 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
STRAND 6 8 {ECO:0000244|PDB:1F3U}.
HELIX 10 13 {ECO:0000244|PDB:1F3U}.
STRAND 17 24 {ECO:0000244|PDB:1F3U}.
HELIX 25 31 {ECO:0000244|PDB:1F3U}.
STRAND 39 48 {ECO:0000244|PDB:1F3U}.
STRAND 51 58 {ECO:0000244|PDB:1F3U}.
HELIX 60 63 {ECO:0000244|PDB:1F3U}.
STRAND 80 86 {ECO:0000244|PDB:1F3U}.
STRAND 91 99 {ECO:0000244|PDB:1F3U}.
STRAND 104 116 {ECO:0000244|PDB:1F3U}.
HELIX 177 193 {ECO:0000244|PDB:1BBY}.
HELIX 199 205 {ECO:0000244|PDB:1BBY}.
HELIX 210 220 {ECO:0000244|PDB:1BBY}.
SEQUENCE 249 AA; 28380 MW; 05A1A9F8D31B749C CRC64;
MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG RTEVSFTLNE
DLANIHDIGG KPASVSAPRE HPFVLQSVGG QTLTVFTESS SDKLSLEGIV VQRAECRPAA
SENYMRLKRL QIEESSKPVR LSQQLDKVVT TNYKPVANHQ YNIEYERKKK EDGKRARADK
QHVLDMLFSA FEKHQYYNLK DLVDITKQPV VYLKEILKEI GVQNVKGIHK NTWELKPEYR
HYQGEEKSD


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EIAAB41104 ATP-dependent helicase GTF2F2,Bos taurus,Bovine,General transcription factor IIF subunit 2,GTF2F2,TFIIF-beta,Transcription initiation factor IIF subunit beta
EIAAB41106 ATP-dependent helicase GTF2F2,General transcription factor IIF subunit 2,Gtf2f2,Mouse,Mus musculus,TFIIF-beta,Transcription initiation factor IIF subunit beta
18-003-42049 Transcription initiation factor IIF subunit beta - EC 3.6.1.-; ATP-dependent helicase GTF2F2; TFIIF-beta; Transcription initiation factor RAP30 Polyclonal 0.1 mg Protein A
18-003-42049 Transcription initiation factor IIF subunit beta - EC 3.6.1.-; ATP-dependent helicase GTF2F2; TFIIF-beta; Transcription initiation factor RAP30 Polyclonal 0.05 mg Aff Pur
18-003-42048 Transcription initiation factor IIF subunit beta - EC 3.6.1.-; ATP-dependent helicase GTF2F2; TFIIF-beta; Transcription initiation factor RAP30 Polyclonal 0.05 mg Aff Pur
18-003-42050 Transcription initiation factor IIF subunit beta - EC 3.6.1.-; ATP-dependent helicase GTF2F2; TFIIF-beta; Transcription initiation factor RAP30 Polyclonal 0.1 mg Protein A
15-288-22092F Transcription initiation factor IIF subunit beta - EC 3.6.1.-; ATP-dependent helicase GTF2F2; TFIIF-beta; Transcription initiation factor RAP30 Polyclonal 0.1 mg
18-003-42050 Transcription initiation factor IIF subunit beta - EC 3.6.1.-; ATP-dependent helicase GTF2F2; TFIIF-beta; Transcription initiation factor RAP30 Polyclonal 0.05 mg Aff Pur
15-288-22092F Transcription initiation factor IIF subunit beta - EC 3.6.1.-; ATP-dependent helicase GTF2F2; TFIIF-beta; Transcription initiation factor RAP30 Polyclonal 0.05 mg
10-288-22092F Transcription initiation factor IIF subunit beta - EC 3.6.1.-; ATP-dependent helicase GTF2F2; TFIIF-beta; Transcription initiation factor RAP30 0.05 mg
10-288-22092F Transcription initiation factor IIF subunit beta - EC 3.6.1.-; ATP-dependent helicase GTF2F2; TFIIF-beta; Transcription initiation factor RAP30 0.1 mg
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
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
EIAAB41096 General transcription factor IIE subunit 2,GTF2E2,Homo sapiens,Human,TF2E2,TFIIE-beta,Transcription initiation factor IIE subunit beta
EIAAB41098 General transcription factor IIE subunit 2,Gtf2e2,Mouse,Mus musculus,TFIIE-beta,Transcription initiation factor IIE subunit beta
EIAAB41097 Bos taurus,Bovine,General transcription factor IIE subunit 2,GTF2E2,TFIIE-beta,Transcription initiation factor IIE subunit beta
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
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
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
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


 

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