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PR domain zinc finger protein 1 (EC 2.1.1.-) (BLIMP-1) (Beta-interferon gene positive regulatory domain I-binding factor) (PR domain-containing protein 1) (Positive regulatory domain I-binding factor 1) (PRDI-BF1) (PRDI-binding factor 1)

 PRDM1_HUMAN             Reviewed;         825 AA.
O75626; B2REA6; E1P5E0; Q86WM7;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
12-SEP-2018, entry version 167.
RecName: Full=PR domain zinc finger protein 1;
EC=2.1.1.-;
AltName: Full=BLIMP-1;
AltName: Full=Beta-interferon gene positive regulatory domain I-binding factor;
AltName: Full=PR domain-containing protein 1;
AltName: Full=Positive regulatory domain I-binding factor 1;
Short=PRDI-BF1;
Short=PRDI-binding factor 1;
Name=PRDM1; Synonyms=BLIMP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
PubMed=1851123; DOI=10.1101/gad.5.5.868;
Keller A.D., Maniatis T.;
"Identification and characterization of a novel repressor of beta-
interferon gene expression.";
Genes Dev. 5:868-879(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND FUNCTION.
PubMed=12626569; DOI=10.4049/jimmunol.170.6.3125;
Gyory I., Fejer G., Ghosh N., Seto E., Wright K.L.;
"Identification of a functionally impaired positive regulatory domain
I binding factor 1 transcription repressor in myeloma cell lines.";
J. Immunol. 170:3125-3133(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[6]
SUBCELLULAR LOCATION.
PubMed=21421998; DOI=10.1093/hmg/ddr114;
Julaton V.T., Reijo Pera R.A.;
"NANOS3 function in human germ cell development.";
Hum. Mol. Genet. 20:2238-2250(2011).
[7]
SUMOYLATION AT LYS-816.
PubMed=22555612; DOI=10.1038/embor.2012.60;
Ying H.Y., Su S.T., Hsu P.H., Chang C.C., Lin I.Y., Tseng Y.H.,
Tsai M.D., Shih H.M., Lin K.I.;
"SUMOylation of Blimp-1 is critical for plasma cell differentiation.";
EMBO Rep. 13:631-637(2012).
[8]
INTERACTION WITH FBXO10 AND FBXO11, AND UBIQUITINATION.
PubMed=24613396; DOI=10.1016/j.devcel.2014.01.028;
Horn M., Geisen C., Cermak L., Becker B., Nakamura S., Klein C.,
Pagano M., Antebi A.;
"DRE-1/FBXO11-dependent degradation of BLMP-1/BLIMP-1 governs C.
elegans developmental timing and maturation.";
Dev. Cell 28:697-710(2014).
[9]
INTERACTION WITH FBXO11.
PubMed=24968003; DOI=10.1371/journal.pgen.1004428;
Huang T.F., Cho C.Y., Cheng Y.T., Huang J.W., Wu Y.Z., Yeh A.Y.,
Nishiwaki K., Chang S.C., Wu Y.C.;
"BLMP-1/Blimp-1 regulates the spatiotemporal cell migration pattern in
C. elegans.";
PLoS Genet. 10:E1004428-E1004428(2014).
[10]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-816, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[11]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 38-223.
Structural genomics consortium (SGC);
"The crystal structure of methyltransferase domain of human PR domain-
containing protein 1.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: Transcription factor that mediates a transcriptional
program in various innate and adaptive immune tissue-resident
lymphocyte T cell types such as tissue-resident memory T (Trm),
natural killer (trNK) and natural killer T (NKT) cells and
negatively regulates gene expression of proteins that promote the
egress of tissue-resident T-cell populations from non-lymphoid
organs. Plays a role in the development, retention and long-term
establishment of adaptive and innate tissue-resident lymphocyte T
cell types in non-lymphoid organs, such as the skin and gut, but
also in other nonbarrier tissues like liver and kidney, and
therefore may provide immediate immunological protection against
reactivating infections or viral reinfection (By similarity).
Binds specifically to the PRDI element in the promoter of the
beta-interferon gene (PubMed:1851123). Drives the maturation of B-
lymphocytes into Ig secreting cells (PubMed:12626569). Associates
with the transcriptional repressor ZNF683 to chromatin at gene
promoter regions (By similarity). {ECO:0000250|UniProtKB:Q60636,
ECO:0000269|PubMed:12626569, ECO:0000269|PubMed:1851123}.
-!- SUBUNIT: Interacts with PRMT5 (By similarity). Interacts with
FBXO10 (PubMed:24613396). Interacts with FBXO11 (PubMed:24613396,
PubMed:24968003). {ECO:0000250|UniProtKB:Q60636,
ECO:0000269|PubMed:24613396, ECO:0000269|PubMed:24968003}.
-!- INTERACTION:
O75925:PIAS1; NbExp=2; IntAct=EBI-948789, EBI-629434;
P63165:SUMO1; NbExp=2; IntAct=EBI-7839538, EBI-80140;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q60636}.
Cytoplasm {ECO:0000269|PubMed:21421998}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O75626-1; Sequence=Displayed;
Name=2;
IsoId=O75626-2; Sequence=VSP_039188;
Name=3;
IsoId=O75626-3; Sequence=VSP_043646, VSP_043647;
-!- PTM: Sumoylation at Lys-816 by PIAS1 augments transcriptional
repressor activity, and is critical for plasma cell
differentiation. {ECO:0000269|PubMed:22555612}.
-!- PTM: Ubiquitinated by the SCF(FBXO11) complex, leading to its
degradation by the proteasome. {ECO:0000269|PubMed:24613396}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=AAO45623.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PRDM1ID41831ch6q21.html";
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EMBL; AF084199; AAC33300.1; -; mRNA.
EMBL; AY198414; AAO45623.1; ALT_INIT; mRNA.
EMBL; AY198415; AAO45624.1; -; mRNA.
EMBL; AL358952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL022067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48419.1; -; Genomic_DNA.
EMBL; CH471051; EAW48421.1; -; Genomic_DNA.
EMBL; CH471051; EAW48422.1; -; Genomic_DNA.
EMBL; BC103832; AAI03833.1; -; mRNA.
EMBL; BC103833; AAI03834.1; -; mRNA.
EMBL; BC103834; AAI03835.1; -; mRNA.
CCDS; CCDS34505.1; -. [O75626-3]
CCDS; CCDS5054.2; -. [O75626-1]
PIR; A39564; A39564.
RefSeq; NP_001189.2; NM_001198.3. [O75626-1]
RefSeq; NP_878911.1; NM_182907.2. [O75626-3]
RefSeq; XP_011534365.1; XM_011536063.2. [O75626-2]
RefSeq; XP_016866676.1; XM_017011187.1. [O75626-2]
UniGene; Hs.436023; -.
PDB; 3DAL; X-ray; 1.65 A; A/B=38-223.
PDBsum; 3DAL; -.
ProteinModelPortal; O75626; -.
SMR; O75626; -.
BioGrid; 107108; 32.
IntAct; O75626; 7.
MINT; O75626; -.
STRING; 9606.ENSP00000358092; -.
iPTMnet; O75626; -.
PhosphoSitePlus; O75626; -.
BioMuta; PRDM1; -.
MaxQB; O75626; -.
PaxDb; O75626; -.
PeptideAtlas; O75626; -.
PRIDE; O75626; -.
ProteomicsDB; 50124; -.
ProteomicsDB; 50125; -. [O75626-2]
ProteomicsDB; 50126; -. [O75626-3]
DNASU; 639; -.
Ensembl; ENST00000369089; ENSP00000358085; ENSG00000057657. [O75626-3]
Ensembl; ENST00000369091; ENSP00000358087; ENSG00000057657. [O75626-2]
Ensembl; ENST00000369096; ENSP00000358092; ENSG00000057657. [O75626-1]
GeneID; 639; -.
KEGG; hsa:639; -.
UCSC; uc003prd.3; human. [O75626-1]
CTD; 639; -.
DisGeNET; 639; -.
EuPathDB; HostDB:ENSG00000057657.14; -.
GeneCards; PRDM1; -.
H-InvDB; HIX0006099; -.
HGNC; HGNC:9346; PRDM1.
HPA; HPA030033; -.
MIM; 603423; gene.
neXtProt; NX_O75626; -.
OpenTargets; ENSG00000057657; -.
PharmGKB; PA33707; -.
eggNOG; KOG2461; Eukaryota.
eggNOG; ENOG410ZFVU; LUCA.
GeneTree; ENSGT00880000137973; -.
HOGENOM; HOG000059670; -.
HOVERGEN; HBG053670; -.
InParanoid; O75626; -.
OMA; KRNMTGY; -.
OrthoDB; EOG091G0467; -.
PhylomeDB; O75626; -.
TreeFam; TF316545; -.
Reactome; R-HSA-6804754; Regulation of TP53 Expression.
SIGNOR; O75626; -.
ChiTaRS; PRDM1; human.
EvolutionaryTrace; O75626; -.
GeneWiki; PRDM1; -.
GenomeRNAi; 639; -.
PRO; PR:O75626; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000057657; Expressed in 179 organ(s), highest expression level in ectocervix.
CleanEx; HS_PRDM1; -.
ExpressionAtlas; O75626; baseline and differential.
Genevisible; O75626; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0035904; P:aorta development; IEA:Ensembl.
GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0003170; P:heart valve development; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0060576; P:intestinal epithelial cell development; IEA:Ensembl.
GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
GO; GO:0001763; P:morphogenesis of a branching structure; IEA:Ensembl.
GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0033082; P:regulation of extrathymic T cell differentiation; ISS:UniProtKB.
GO; GO:0032823; P:regulation of natural killer cell differentiation; ISS:UniProtKB.
GO; GO:0051136; P:regulation of NK T cell differentiation; ISS:UniProtKB.
GO; GO:1990654; P:sebum secreting cell proliferation; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
InterPro; IPR001214; SET_dom.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00856; SET; 1.
SMART; SM00317; SET; 1.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS50280; SET; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing;
Complete proteome; Cytoplasm; DNA-binding; Immunity; Innate immunity;
Isopeptide bond; Metal-binding; Methyltransferase; Nucleus;
Polymorphism; Reference proteome; Repeat; Repressor;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 825 PR domain zinc finger protein 1.
/FTId=PRO_0000047757.
DOMAIN 84 201 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
ZN_FING 575 597 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 603 625 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 631 653 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 659 681 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 527 574 Interaction with PIAS1.
CROSSLNK 816 816 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000269|PubMed:22555612}.
CROSSLNK 816 816 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 36 Missing (in isoform 2).
{ECO:0000303|PubMed:1851123}.
/FTId=VSP_039188.
VAR_SEQ 1 3 MLD -> MEK (in isoform 3).
{ECO:0000303|PubMed:12626569,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_043646.
VAR_SEQ 4 137 Missing (in isoform 3).
{ECO:0000303|PubMed:12626569,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_043647.
VARIANT 74 74 G -> S (in dbSNP:rs2185379).
/FTId=VAR_019983.
VARIANT 203 203 D -> E (in dbSNP:rs811925).
/FTId=VAR_024221.
HELIX 51 57 {ECO:0000244|PDB:3DAL}.
STRAND 60 62 {ECO:0000244|PDB:3DAL}.
HELIX 78 81 {ECO:0000244|PDB:3DAL}.
STRAND 87 91 {ECO:0000244|PDB:3DAL}.
STRAND 98 105 {ECO:0000244|PDB:3DAL}.
STRAND 111 113 {ECO:0000244|PDB:3DAL}.
STRAND 119 121 {ECO:0000244|PDB:3DAL}.
TURN 123 125 {ECO:0000244|PDB:3DAL}.
STRAND 135 140 {ECO:0000244|PDB:3DAL}.
STRAND 143 149 {ECO:0000244|PDB:3DAL}.
HELIX 158 161 {ECO:0000244|PDB:3DAL}.
TURN 168 170 {ECO:0000244|PDB:3DAL}.
STRAND 173 178 {ECO:0000244|PDB:3DAL}.
STRAND 181 188 {ECO:0000244|PDB:3DAL}.
STRAND 197 200 {ECO:0000244|PDB:3DAL}.
HELIX 202 207 {ECO:0000244|PDB:3DAL}.
HELIX 218 222 {ECO:0000244|PDB:3DAL}.
SEQUENCE 825 AA; 91771 MW; 07B389BACCD6172F CRC64;
MLDICLEKRV GTTLAAPKCN SSTVRFQGLA EGTKGTMKMD MEDADMTLWT EAEFEEKCTY
IVNDHPWDSG ADGGTSVQAE ASLPRNLLFK YATNSEEVIG VMSKEYIPKG TRFGPLIGEI
YTNDTVPKNA NRKYFWRIYS RGELHHFIDG FNEEKSNWMR YVNPAHSPRE QNLAACQNGM
NIYFYTIKPI PANQELLVWY CRDFAERLHY PYPGELTMMN LTQTQSSLKQ PSTEKNELCP
KNVPKREYSV KEILKLDSNP SKGKDLYRSN ISPLTSEKDL DDFRRRGSPE MPFYPRVVYP
IRAPLPEDFL KASLAYGIER PTYITRSPIP SSTTPSPSAR SSPDQSLKSS SPHSSPGNTV
SPVGPGSQEH RDSYAYLNAS YGTEGLGSYP GYAPLPHLPP AFIPSYNAHY PKFLLPPYGM
NCNGLSAVSS MNGINNFGLF PRLCPVYSNL LGGGSLPHPM LNPTSLPSSL PSDGARRLLQ
PEHPREVLVP APHSAFSFTG AAASMKDKAC SPTSGSPTAG TAATAEHVVQ PKATSAAMAA
PSSDEAMNLI KNKRNMTGYK TLPYPLKKQN GKIKYECNVC AKTFGQLSNL KVHLRVHSGE
RPFKCQTCNK GFTQLAHLQK HYLVHTGEKP HECQVCHKRF SSTSNLKTHL RLHSGEKPYQ
CKVCPAKFTQ FVHLKLHKRL HTRERPHKCS QCHKNYIHLC SLKVHLKGNC AAAPAPGLPL
EDLTRINEEI EKFDISDNAD RLEDVEDDIS VISVVEKEIL AVVRKEKEET GLKVSLQRNM
GNGLLSSGCS LYESSDLPLM KLPPSNPLPL VPVKVKQETV EPMDP


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15-288-21968A Zinc finger protein 395 - Papillomavirus-binding factor; Papillomavirus regulatory factor 1; PRF-1; Huntington disease gene regulatory region-binding protein 2; HDBP-2; HD gene regulatory region-bindi 0.1 mg
10-288-21968F Zinc finger protein 395 - Papillomavirus-binding factor; Papillomavirus regulatory factor 1; PRF-1; Huntington disease gene regulatory region-binding protein 2; HDBP-2; HD gene regulatory region-bindi 0.1 mg
10-288-21968F Zinc finger protein 395 - Papillomavirus-binding factor; Papillomavirus regulatory factor 1; PRF-1; Huntington disease gene regulatory region-binding protein 2; HDBP-2; HD gene regulatory region-bindi 0.05 mg
18-003-43101 Zinc finger protein 395 - Papillomavirus-binding factor; Papillomavirus regulatory factor 1; PRF-1; Huntington disease gene regulatory region-binding protein 2; HDBP-2; HD gene regulatory region-bindi 0.05 mg Aff Pur
15-288-21968A Zinc finger protein 395 - Papillomavirus-binding factor; Papillomavirus regulatory factor 1; PRF-1; Huntington disease gene regulatory region-binding protein 2; HDBP-2; HD gene regulatory region-bindi 0.05 mg
15-288-21968B Zinc finger protein 395 - Papillomavirus-binding factor; Papillomavirus regulatory factor 1; PRF-1; Huntington disease gene regulatory region-binding protein 2; HDBP-2; HD gene regulatory region-bindi 0.1 mg
15-288-21968B Zinc finger protein 395 - Papillomavirus-binding factor; Papillomavirus regulatory factor 1; PRF-1; Huntington disease gene regulatory region-binding protein 2; HDBP-2; HD gene regulatory region-bindi 0.05 mg
EIAAB34440 DNA-binding protein RFX7,Homo sapiens,Human,Regulatory factor X 7,Regulatory factor X domain-containing protein 2,RFX7,RFXDC2
EIAAB34439 DNA-binding protein RFX6,Homo sapiens,Human,Regulatory factor X 6,Regulatory factor X domain-containing protein 1,RFX6,RFXDC1
EIAAB34438 DNA-binding protein RFX6,Mouse,Mus musculus,Regulatory factor X 6,Regulatory factor X domain-containing protein 1,Rfx6,Rfxdc1
EIAAB47434 HD gene regulatory region-binding protein 2,HDBP2,HDBP-2,HD-regulating factor 2,HDRF-2,Homo sapiens,Human,Huntington disease gene regulatory region-binding protein 2,Papillomavirus regulatory factor 1
EIAAB32306 GATA-3-binding protein G3B,Homo sapiens,Human,KMT8,Lysine N-methyltransferase 8,MTB-ZF,MTE-binding protein,PR domain zinc finger protein 2,PR domain-containing protein 2,PRDM2,Retinoblastoma protein-i
E1602h ELISA Homo sapiens,Human,OCT6,Oct-6,Octamer-binding protein 6,Octamer-binding transcription factor 6,OTF6,OTF-6,POU domain transcription factor SCIP,POU domain, class 3, transcription factor 1,POU3F1 96T
U1602h CLIA Homo sapiens,Human,OCT6,Oct-6,Octamer-binding protein 6,Octamer-binding transcription factor 6,OTF6,OTF-6,POU domain transcription factor SCIP,POU domain, class 3, transcription factor 1,POU3F1 96T
25-416 RFX1 is a member of the regulatory factor X protein family, which are transcription factors that contain a highly-conserved winged helix DNA binding domain. RFX1 is structurally related to regulatory 0.05 mg
E1602h ELISA kit Homo sapiens,Human,OCT6,Oct-6,Octamer-binding protein 6,Octamer-binding transcription factor 6,OTF6,OTF-6,POU domain transcription factor SCIP,POU domain, class 3, transcription factor 1,PO 96T
31-202 Interferon regulatory factor 8 (IRF8, interferon consensus sequence-binding protein, Ion ChannelSBP) is a transcription factor of the interferon (IFN) regulatory factor (IRF) family. Proteins of this 0.05 mg


 

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