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Transcription factor tau 131 kDa subunit (TFIIIC 131 kDa subunit) (Transcription factor C subunit 4)

 TFC4_YEAST              Reviewed;        1025 AA.
P33339; D6VUI4; Q45U37;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
05-DEC-2018, entry version 173.
RecName: Full=Transcription factor tau 131 kDa subunit;
AltName: Full=TFIIIC 131 kDa subunit;
AltName: Full=Transcription factor C subunit 4;
Name=TFC4; Synonyms=PCF1; OrderedLocusNames=YGR047C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND IDENTIFICATION IN
TFIIIC.
STRAIN=ATCC 204508 / S288c;
PubMed=8387209; DOI=10.1073/pnas.90.9.4027;
Marck C., Lefebvre O., Carles C., Riva M., Chaussivert N., Ruet A.,
Sentenac A.;
"The TFIIIB-assembling subunit of yeast transcription factor TFIIIC
has both tetratricopeptide repeats and basic helix-loop-helix
motifs.";
Proc. Natl. Acad. Sci. U.S.A. 90:4027-4031(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION IN TFIIIC, AND
MUTAGENESIS OF HIS-190.
PubMed=8264649; DOI=10.1128/MCB.14.1.822;
Rameau G., Puglia K., Crowe A., Sethy I., Willis I.;
"A mutation in the second largest subunit of TFIIIC increases a rate-
limiting step in transcription by RNA polymerase III.";
Mol. Cell. Biol. 14:822-830(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 147-205, AND
MUTAGENESIS OF GLU-148; PHE-162; ALA-164; THR-167; TYR-171; ALA-188;
HIS-190; ASN-192 AND TRP-199.
PubMed=9372943; DOI=10.1128/MCB.17.12.7119;
Moir R.D., Sethy-Coraci I., Puglia K., Librizzi M.D., Willis I.M.;
"A tetratricopeptide repeat mutation in yeast transcription factor
IIIC131 (TFIIIC131) facilitates recruitment of TFIIB-related factor
TFIIIB70.";
Mol. Cell. Biol. 17:7119-7125(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF HIS-190.
PubMed=12167707; DOI=10.1128/MCB.22.17.6131-6141.2002;
Moir R.D., Puglia K.V., Willis I.M.;
"A gain-of-function mutation in the second tetratricopeptide repeat of
TFIIIC131 relieves autoinhibition of Brf1 binding.";
Mol. Cell. Biol. 22:6131-6141(2002).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-280; VAL-635 AND
VAL-1025.
STRAIN=SK1;
PubMed=16273108; DOI=10.1038/ng1674;
Deutschbauer A.M., Davis R.W.;
"Quantitative trait loci mapped to single-nucleotide resolution in
yeast.";
Nat. Genet. 37:1333-1340(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[7]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[8]
FUNCTION.
PubMed=2686985;
Willis I., Schmidt P., Soell D.;
"A selection for mutants of the RNA polymerase III transcription
apparatus: PCF1 stimulates transcription of tRNA and 5S RNA genes.";
EMBO J. 8:4281-4288(1989).
[9]
IDENTIFICATION IN TFIIIC.
PubMed=2180956;
Parsons M.C., Weil P.A.;
"Purification and characterization of Saccharomyces cerevisiae
transcription factor TFIIIC. Polypeptide composition defined with
polyclonal antibodies.";
J. Biol. Chem. 265:5095-5103(1990).
[10]
INTERACTION WITH TFIIIB.
PubMed=1922038; DOI=10.1128/MCB.11.10.5181;
Bartholomew B., Kassavetis G.A., Geiduschek E.P.;
"Two components of Saccharomyces cerevisiae transcription factor IIIB
(TFIIIB) are stereospecifically located upstream of a tRNA gene and
interact with the second-largest subunit of TFIIIC.";
Mol. Cell. Biol. 11:5181-5189(1991).
[11]
INTERACTION WITH TFC1; TFC3 AND TFC6, AND PHOSPHORYLATION.
PubMed=7688737;
Conesa C., Swanson R.N., Schultz P., Oudet P., Sentenac A.;
"On the subunit composition, stoichiometry, and phosphorylation of the
yeast transcription factor TFIIIC/tau.";
J. Biol. Chem. 268:18047-18052(1993).
[12]
MUTAGENESIS OF HIS-190 AND ARG-728.
PubMed=7488859;
Sethy I., Willis I.M.;
"Recessive mutations in the second largest subunit of TFIIIC suggest a
new step in RNA polymerase III transcription.";
Gene Expr. 5:35-47(1995).
[13]
INTERACTION WITH RPC10.
PubMed=10559229; DOI=10.1074/jbc.274.47.33462;
Dumay H., Rubbi L., Sentenac A., Marck C.;
"Interaction between yeast RNA polymerase III and transcription factor
TFIIIC via ABC10alpha and tau131 subunits.";
J. Biol. Chem. 274:33462-33468(1999).
[14]
INTERACTION WITH BRF1 AND BDP1, AND MUTAGENESIS OF LEU-469; GLU-472;
VAL-504; SER-541 AND LEU-542.
PubMed=12930823; DOI=10.1074/jbc.M308354200;
Liao Y., Willis I.M., Moir R.D.;
"The Brf1 and Bdp1 subunits of transcription factor TFIIIB bind to
overlapping sites in the tetratricopeptide repeats of Tfc4.";
J. Biol. Chem. 278:44467-44474(2003).
[15]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[16]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[18]
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).
-!- FUNCTION: TFIIIC mediates tRNA and 5S RNA gene activation by
binding to intragenic promoter elements. Upstream of the
transcription start site, TFIIIC assembles the initiation complex
TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III
recruitment and function. Part of the tauA domain of TFIIIC that
binds boxA DNA promoter sites of tRNA and similar genes. TFC4 is
the TFIIIB-assembling subunit of TFIIIC and essential for
viability. {ECO:0000269|PubMed:2686985,
ECO:0000269|PubMed:8387209}.
-!- SUBUNIT: Component of the TFIIIC complex composed of TFC1, TFC3,
TFC4, TFC6, TFC7 and TFC8. The subunits are organized in two
globular domains, tauA and tauB, connected by a proteolysis-
sensitive and flexible linker. Interacts with TFC1, TFC3, TFC6,
TFIIIB subunits BRF1 and BDP1, and with RNA polymerase III subunit
RPC10. {ECO:0000269|PubMed:10559229, ECO:0000269|PubMed:12930823,
ECO:0000269|PubMed:1922038, ECO:0000269|PubMed:2180956,
ECO:0000269|PubMed:7688737, ECO:0000269|PubMed:8264649,
ECO:0000269|PubMed:8387209}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:7688737}.
-!- MISCELLANEOUS: Present with 876 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
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EMBL; L12722; AAA35145.1; -; Genomic_DNA.
EMBL; DQ115391; AAZ22462.1; -; Genomic_DNA.
EMBL; Z72832; CAA97046.1; -; Genomic_DNA.
EMBL; Z72833; CAA97048.1; -; Genomic_DNA.
EMBL; BK006941; DAA08145.1; -; Genomic_DNA.
PIR; A47453; A47453.
RefSeq; NP_011561.3; NM_001181176.3.
PDB; 5AEM; X-ray; 3.40 A; A=123-566.
PDB; 5AIO; X-ray; 3.15 A; A=123-566.
PDBsum; 5AEM; -.
PDBsum; 5AIO; -.
ProteinModelPortal; P33339; -.
SMR; P33339; -.
BioGrid; 33294; 136.
ComplexPortal; CPX-1656; Transcription factor TFIIIC complex.
DIP; DIP-230N; -.
IntAct; P33339; 16.
MINT; P33339; -.
STRING; 4932.YGR047C; -.
iPTMnet; P33339; -.
MaxQB; P33339; -.
PaxDb; P33339; -.
PRIDE; P33339; -.
EnsemblFungi; YGR047C_mRNA; YGR047C_mRNA; YGR047C.
GeneID; 852938; -.
KEGG; sce:YGR047C; -.
SGD; S000003279; TFC4.
GeneTree; ENSGT00390000016929; -.
HOGENOM; HOG000248222; -.
InParanoid; P33339; -.
KO; K15201; -.
OMA; RICMEII; -.
OrthoDB; EOG092C0CSP; -.
BioCyc; YEAST:G3O-30765-MONOMER; -.
PRO; PR:P33339; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:SGD.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0001004; F:RNA polymerase III transcription regulator recruiting activity; IEA:InterPro.
GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IDA:SGD.
GO; GO:0006383; P:transcription by RNA polymerase III; IDA:SGD.
Gene3D; 1.25.40.10; -; 4.
InterPro; IPR039340; Tfc4/TFIIIC-102/Sfc4.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR23082; PTHR23082; 1.
Pfam; PF13174; TPR_6; 1.
Pfam; PF13181; TPR_8; 1.
SMART; SM00028; TPR; 8.
SUPFAM; SSF48452; SSF48452; 2.
PROSITE; PS50005; TPR; 6.
PROSITE; PS50293; TPR_REGION; 3.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
TPR repeat; Transcription; Transcription regulation.
CHAIN 1 1025 Transcription factor tau 131 kDa subunit.
/FTId=PRO_0000106364.
REPEAT 128 161 TPR 1.
REPEAT 162 195 TPR 2.
REPEAT 196 229 TPR 3.
REPEAT 230 263 TPR 4.
REPEAT 264 297 TPR 5.
REPEAT 432 465 TPR 6.
REPEAT 467 501 TPR 7.
REPEAT 502 535 TPR 8.
REPEAT 536 569 TPR 9.
REPEAT 875 908 TPR 10.
REPEAT 959 992 TPR 11.
REGION 128 569 Sufficient to bind BDP1.
MOD_RES 311 311 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
VARIANT 280 280 I -> T (in strain: SK1).
{ECO:0000269|PubMed:16273108}.
VARIANT 635 635 M -> V (in strain: SK1).
{ECO:0000269|PubMed:16273108}.
VARIANT 1025 1025 I -> V (in strain: SK1).
{ECO:0000269|PubMed:16273108}.
MUTAGEN 148 148 E->K: In PCF1-17; increases RNA
polymerase III gene transcription.
{ECO:0000269|PubMed:9372943}.
MUTAGEN 162 162 F->L: In PCF1-12; increases RNA
polymerase III gene transcription.
{ECO:0000269|PubMed:9372943}.
MUTAGEN 162 162 F->S: In PCF1-139; increases RNA
polymerase III gene transcription.
{ECO:0000269|PubMed:9372943}.
MUTAGEN 164 164 A->V: In PCF1-19; increases RNA
polymerase III gene transcription.
{ECO:0000269|PubMed:9372943}.
MUTAGEN 167 167 T->I: In PCF1-2; increases RNA polymerase
III gene transcription due to an increase
in the recruitment of BRF1 to TFIIIC-DNA.
No effect on affinity of TFIIIC for DNA.
{ECO:0000269|PubMed:9372943}.
MUTAGEN 172 172 Y->C: In PCF1-11; increases RNA
polymerase III gene transcription.
MUTAGEN 188 188 A->T: In PCF1-23; increases RNA
polymerase III gene transcription.
{ECO:0000269|PubMed:9372943}.
MUTAGEN 190 190 H->Y: In PCF1-1; affects the rate of
recruitment of TFIIIB to the template.
Increases the amount of transcriptionally
active TFIIIB. Increases RNA polymerase
III gene transcription. Increases the
binding affinity for BRF1, but does not
affect the binding affinity for BDP1 in
the TFIIIC-dependent assembly of TFIIIB.
Overcomes autoinhibition of BRF1 binding.
{ECO:0000269|PubMed:12167707,
ECO:0000269|PubMed:7488859,
ECO:0000269|PubMed:8264649,
ECO:0000269|PubMed:9372943}.
MUTAGEN 192 192 N->L: In PCF1-138; increases RNA
polymerase III gene transcription.
{ECO:0000269|PubMed:9372943}.
MUTAGEN 199 199 W->R: In PCF1-15; increases RNA
polymerase III gene transcription.
{ECO:0000269|PubMed:9372943}.
MUTAGEN 469 469 L->K: RNA polymerase III defective.
Defect in the recruitment of BRF1 into
TFIIIB-TFIIIC-DNA complexes and
diminished direct interaction between
TFC4 and BRF1. Decreased binding affinity
for BDP1 incorporation into TFIIIB-
TFIIIC-DNA complexes and inhibited binary
interaction between BDP1 and TFC4.
{ECO:0000269|PubMed:12930823}.
MUTAGEN 472 472 E->K: RNA polymerase III defective.
{ECO:0000269|PubMed:12930823}.
MUTAGEN 504 504 V->K: RNA polymerase III defective.
{ECO:0000269|PubMed:12930823}.
MUTAGEN 541 541 S->I: RNA polymerase III defective.
{ECO:0000269|PubMed:12930823}.
MUTAGEN 542 542 L->G: RNA polymerase III defective.
{ECO:0000269|PubMed:12930823}.
MUTAGEN 728 728 R->E: In PCF1-8; increases RNA polymerase
III transcription.
{ECO:0000269|PubMed:7488859}.
MUTAGEN 728 728 R->G: In PCF1-7; increases RNA polymerase
III transcription.
{ECO:0000269|PubMed:7488859}.
MUTAGEN 728 728 R->H: In PCF1-4; increases RNA polymerase
III transcription ninefold over wild-
type. Increases the amount of
transcriptionally active TFIIIB.
{ECO:0000269|PubMed:7488859}.
MUTAGEN 728 728 R->K: In PCF1-3; increases RNA polymerase
III transcription two- to threefold over
wild-type. Increases the amount of
transcriptionally active TFIIIB.
{ECO:0000269|PubMed:7488859}.
MUTAGEN 728 728 R->M: In PCF1-5; increases RNA polymerase
III transcription.
{ECO:0000269|PubMed:7488859}.
MUTAGEN 728 728 R->V: In PCF1-6; increases RNA polymerase
III transcription.
{ECO:0000269|PubMed:7488859}.
HELIX 133 141 {ECO:0000244|PDB:5AIO}.
HELIX 146 150 {ECO:0000244|PDB:5AIO}.
HELIX 151 157 {ECO:0000244|PDB:5AIO}.
HELIX 162 175 {ECO:0000244|PDB:5AIO}.
HELIX 178 189 {ECO:0000244|PDB:5AIO}.
HELIX 196 208 {ECO:0000244|PDB:5AIO}.
HELIX 212 225 {ECO:0000244|PDB:5AIO}.
HELIX 230 243 {ECO:0000244|PDB:5AIO}.
HELIX 246 259 {ECO:0000244|PDB:5AIO}.
HELIX 264 276 {ECO:0000244|PDB:5AIO}.
HELIX 280 314 {ECO:0000244|PDB:5AIO}.
HELIX 344 349 {ECO:0000244|PDB:5AIO}.
HELIX 357 370 {ECO:0000244|PDB:5AIO}.
HELIX 374 387 {ECO:0000244|PDB:5AIO}.
HELIX 388 390 {ECO:0000244|PDB:5AIO}.
HELIX 396 399 {ECO:0000244|PDB:5AIO}.
HELIX 408 412 {ECO:0000244|PDB:5AIO}.
HELIX 414 418 {ECO:0000244|PDB:5AIO}.
TURN 421 423 {ECO:0000244|PDB:5AIO}.
STRAND 424 426 {ECO:0000244|PDB:5AIO}.
HELIX 432 443 {ECO:0000244|PDB:5AIO}.
TURN 444 446 {ECO:0000244|PDB:5AIO}.
HELIX 448 455 {ECO:0000244|PDB:5AIO}.
HELIX 456 458 {ECO:0000244|PDB:5AIO}.
HELIX 463 466 {ECO:0000244|PDB:5AIO}.
HELIX 467 479 {ECO:0000244|PDB:5AIO}.
HELIX 483 490 {ECO:0000244|PDB:5AIO}.
HELIX 491 495 {ECO:0000244|PDB:5AIO}.
HELIX 497 499 {ECO:0000244|PDB:5AIO}.
HELIX 502 514 {ECO:0000244|PDB:5AIO}.
HELIX 518 530 {ECO:0000244|PDB:5AIO}.
HELIX 536 548 {ECO:0000244|PDB:5AIO}.
HELIX 552 563 {ECO:0000244|PDB:5AIO}.
SEQUENCE 1025 AA; 120229 MW; 12DE18304AAF4862 CRC64;
MAAGKLKKEQ QNQSAERESA DTGKVNDEDE EHLYGNIDDY KHLIQDEEYD DEDVPHDLQL
SEDEYNSERD SSLLAEFSDY GEISEDDEED FMNAIREASN FKVKKKKKND KGKSYGRQRK
ERVLDPEVAQ LLSQANEAFV RNDLQVAERL FNEVIKKDAR NFAAYETLGD IYQLQGRLND
CCNSWFLAAH LNASDWEFWK IVAILSADLD HVRQAIYCFS RVISLNPMEW ESIYRRSMLY
KKTGQLARAL DGFQRLYMYN PYDANILREL AILYVDYDRI EDSIELYMKV FNANVERREA
ILAALENALD SSDEESAAEG EDADEKEPLE QDEDRQMFPD INWKKIDAKY KCIPFDWSSL
NILAELFLKL AVSEVDGIKT IKKCARWIQR RESQTFWDHV PDDSEFDNRR FKNSTFDSLL
AAEKEKSYNI PIDIRVRLGL LRLNTDNLVE ALNHFQCLYD ETFSDVADLY FEAATALTRA
EKYKEAIDFF TPLLSLEEWR TTDVFKPLAR CYKEIESYET AKEFYELAIK SEPDDLDIRV
SLAEVYYRLN DPETFKHMLV DVVEMRKHQV DETLHRISNE KSSNDTSDIS SKPLLEDSKF
RTFRKKKRTP YDAERERIER ERRITAKVVD KYEKMKKFEL NSGLNEAKQA SIWINTVSEL
VDIFSSVKNF FMKSRSRKFV GILRRTKKFN TELDFQIERL SKLAEGDSVF EGPLMEERVT
LTSATELRGL SYEQWFELFM ELSLVIAKYQ SVEDGLSVVE TAQEVNVFFQ DPERVKMMKF
VKLAIVLQMD DEEELAENLR GLLNQFQFNR KVLQVFMYSL CRGPSSLNIL SSTIQQKFFL
RQLKAFDSCR YNTEVNGQAS ITNKEVYNPN KKSSPYLYYI YAVLLYSSRG FLSALQYLTR
LEEDIPDDPM VNLLMGLSHI HRAMQRLTAQ RHFQIFHGLR YLYRYHKIRK SLYTDLEKQE
ADYNLGRAFH LIGLVSIAIE YYNRVLENYD DGKLKKHAAY NSIIIYQQSG NVELADHLME
KYLSI


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EIAAB42074 General transcription factor 3C polypeptide 6,Gtf3c6,Mouse,Mus musculus,TFIIIC 35 kDa subunit,TFIIIC35,Transcription factor IIIC 35 kDa subunit,Transcription factor IIIC subunit 6
EIAAB42071 General transcription factor 3C polypeptide 4,GTF3C4,Homo sapiens,Human,TF3C-delta,TFIIIC 90 kDa subunit,TFIIIC90,Transcription factor IIIC 90 kDa subunit,Transcription factor IIIC subunit delta
EIAAB42069 General transcription factor 3C polypeptide 3,GTF3C3,Homo sapiens,Human,TF3C-gamma,TFIIIC 102 kDa subunit,TFIIIC102,Transcription factor IIIC 102 kDa subunit,Transcription factor IIIC subunit gamma
EIAAB42070 General transcription factor 3C polypeptide 4,Gtf3c4,Mouse,Mus musculus,TF3C-delta,TFIIIC 90 kDa subunit,TFIIIC90,Transcription factor IIIC 90 kDa subunit,Transcription factor IIIC subunit delta
EIAAB42072 General transcription factor 3C polypeptide 5,Gtf3c5,Mouse,Mus musculus,TF3C-epsilon,TFIIIC 63 kDa subunit,TFIIIC63,Transcription factor IIIC 63 kDa subunit,Transcription factor IIIC subunit epsilon
EIAAB27113 CAAT box DNA-binding protein subunit C,CBF-C,CCAAT-binding transcription factor subunit C,Nfyc,NF-YC,Nuclear transcription factor Y subunit C,Nuclear transcription factor Y subunit gamma,Rat,Rattus no
EIAAB27109 CAAT box DNA-binding protein subunit B,CBF-A,CCAAT-binding transcription factor subunit A,Nfyb,NF-YB,Nuclear transcription factor Y subunit B,Nuclear transcription factor Y subunit beta,Rat,Rattus nor
EIAAB27106 CAAT box DNA-binding protein subunit A,CBF-B,CCAAT-binding transcription factor subunit B,Nfya,NF-YA,Nuclear transcription factor Y subunit A,Nuclear transcription factor Y subunit alpha,Rat,Rattus no
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
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
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
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
15-288-22005B TFIIH basal transcription factor complex p62 subunit - Basic transcription factor 62 kDa subunit; BTF2-p62; General transcription factor IIH polypeptide 1 Polyclonal 0.1 mg
15-288-22005A TFIIH basal transcription factor complex p62 subunit - Basic transcription factor 62 kDa subunit; BTF2-p62; General transcription factor IIH polypeptide 1 Polyclonal 0.05 mg
15-288-22005B TFIIH basal transcription factor complex p62 subunit - Basic transcription factor 62 kDa subunit; BTF2-p62; General transcription factor IIH polypeptide 1 Polyclonal 0.05 mg
18-003-42051 TFIIH basal transcription factor complex p34 subunit - Basic transcription factor 2 34 kDa subunit; BTF2-p34; General transcription factor IIH polypeptide 3 Polyclonal 0.05 mg Aff Pur


 

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