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PR domain zinc finger protein 1 (EC 2.1.1.-) (B lymphocyte-induced maturation protein 1) (Blimp-1) (Beta-interferon gene positive regulatory domain I-binding factor) (PR domain-containing protein 1)

 PRDM1_MOUSE             Reviewed;         856 AA.
Q60636; A2VDE8; Q3UET9;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 157.
RecName: Full=PR domain zinc finger protein 1;
EC=2.1.1.-;
AltName: Full=B lymphocyte-induced maturation protein 1;
Short=Blimp-1;
AltName: Full=Beta-interferon gene positive regulatory domain I-binding factor;
AltName: Full=PR domain-containing protein 1;
Name=Prdm1; Synonyms=Blimp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=B-cell;
PubMed=8168136; DOI=10.1016/0092-8674(94)90321-2;
Turner C.A., Mack D.H., Davis M.M.;
"Blimp-1, a novel zinc finger-containing protein that can drive the
maturation of B lymphocytes into immunoglobulin-secreting cells.";
Cell 77:297-306(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1
AND 5), AND TISSUE SPECIFICITY.
STRAIN=129;
PubMed=11121475; DOI=10.1093/nar/28.24.4846;
Tunyaplin C., Shapiro M.A., Calame K.L.;
"Characterization of the B lymphocyte-induced maturation protein-1
(Blimp-1) gene, mRNA isoforms and basal promoter.";
Nucleic Acids Res. 28:4846-4855(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 1-253 (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Embryo, and Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[5]
INTERACTION WITH PRMT5.
PubMed=16699504; DOI=10.1038/ncb1413;
Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J.,
Kouzarides T., Surani M.A.;
"Blimp1 associates with Prmt5 and directs histone arginine methylation
in mouse germ cells.";
Nat. Cell Biol. 8:623-630(2006).
[6]
ALTERNATIVE PROMOTER USAGE (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING
(ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
TISSUE=Embryo, Placenta, and Yolk sac;
PubMed=19737919; DOI=10.1128/MCB.00670-09;
Morgan M.A., Magnusdottir E., Kuo T.C., Tunyaplin C., Harper J.,
Arnold S.J., Calame K., Robertson E.J., Bikoff E.K.;
"Blimp-1/Prdm1 alternative promoter usage during mouse development and
plasma cell differentiation.";
Mol. Cell. Biol. 29:5813-5827(2009).
[7]
FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN LYMPHOCYTE T
CELLS, TISSUE SPECIFICITY, AND INDUCTION (MICROBIAL INFECTION).
PubMed=27102484; DOI=10.1126/science.aad2035;
Mackay L.K., Minnich M., Kragten N.A., Liao Y., Nota B., Seillet C.,
Zaid A., Man K., Preston S., Freestone D., Braun A., Wynne-Jones E.,
Behr F.M., Stark R., Pellicci D.G., Godfrey D.I., Belz G.T.,
Pellegrini M., Gebhardt T., Busslinger M., Shi W., Carbone F.R.,
van Lier R.A., Kallies A., van Gisbergen K.P.;
"Hobit and Blimp1 instruct a universal transcriptional program of
tissue residency in lymphocytes.";
Science 352:459-463(2016).
-!- 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 (PubMed:27102484). 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 (PubMed:27102484). Binds specifically to the PRDI
element in the promoter of the beta-interferon gene (By
similarity). Drives the maturation of B-lymphocytes into Ig
secreting cells (By similarity). Associates with the
transcriptional repressor ZNF683 to chromatin at gene promoter
regions (PubMed:27102484). {ECO:0000250|UniProtKB:O75626,
ECO:0000269|PubMed:27102484}.
-!- SUBUNIT: Interacts with PRMT5 (PubMed:16699504). Interacts with
FBXO10 (By similarity). Interacts with FBXO11 (By similarity).
{ECO:0000250|UniProtKB:O75626, ECO:0000269|PubMed:16699504}.
-!- INTERACTION:
P63165:SUMO1 (xeno); NbExp=3; IntAct=EBI-7000804, EBI-80140;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8168136}.
Cytoplasm {ECO:0000250|UniProtKB:O75626}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q60636-1; Sequence=Displayed;
Note=Produced by alternative splicing.;
Name=2; Synonyms=1A;
IsoId=Q60636-2; Sequence=VSP_039189;
Note=Produced by alternative splicing of isoform 1.;
Name=3; Synonyms=1B;
IsoId=Q60636-3; Sequence=VSP_041570;
Note=Produced by alternative promoter usage of isoform 2.;
Name=4; Synonyms=1C;
IsoId=Q60636-4; Sequence=VSP_041571;
Note=Produced by alternative promoter usage of isoform 2.;
Name=5; Synonyms=delta exon 7;
IsoId=Q60636-5; Sequence=VSP_041572;
Note=Produced by alternative splicing of isoform 1. Does not
bind DNA.;
-!- TISSUE SPECIFICITY: Expressed in innate lymphocytes, including
tissue-resident conventional natural killer (cNK) cells in liver
(PubMed:27102484). Expressed also weakly in tissue-resident
natural killer (trNK) and natural killer T (NKT) cells in liver
(PubMed:27102484). Isoform 1 is detected in bone marrow, spleen
and lymph node but not in brain, heart, kidney, liver, ovary or
muscle. Weak expression detected in the lung. Isoform 3 is
detected only in yolk sac. Isoform 4 is detected in embryo, yolk
sac, placenta, splenocytes, and activated T-cells.
{ECO:0000269|PubMed:11121475, ECO:0000269|PubMed:19737919,
ECO:0000269|PubMed:27102484, ECO:0000269|PubMed:8168136}.
-!- INDUCTION: By lymphokines, specifically IL-2 and IL-5. Up-
regulated during dendritic cell maturation.
-!- INDUCTION: (Microbial infection) Up-regulated in response to
Herpes simplex virus (HSV) infection in skin and spleen memory
CD8(+) T cells. {ECO:0000269|PubMed:27102484}.
-!- INDUCTION: (Microbial infection) Up-regulated in response to
Lymphocytic choriomeningitis virus (LCMV) in memory CD8(+) T
cells. {ECO:0000269|PubMed:27102484}.
-!- PTM: Sumoylation at Lys-847 by PIAS1 augments transcriptional
repressor activity, and is critical for plasma cell
differentiation. {ECO:0000250|UniProtKB:O75626}.
-!- PTM: Ubiquitinated by SCF(FBXO11), leading to its degradation by
the proteasome. {ECO:0000250|UniProtKB:O75626}.
-!- DISRUPTION PHENOTYPE: Early embryonic lethality (PubMed:19737919).
Compound heterozygotes display germ cell defects and a rudimentary
or missing fifth digit of the forelimb (PubMed:19737919).
Conditional knockout in lymphocyte T cells show a weak reduction
in tissue-resident memory T (Trm) cell population maintenance in
the skin, gut, liver and kidney but not of splenic T cells
(PubMed:27102484). Double knockouts for PRDM1/BLIMP1 and ZNF683
result in a strong inhibition of Trm cell population maintenance
but not of circulating memory cells (PubMed:27102484). Display an
enhancement of natural killer T (NKT) cells migration
preferentially to the white pulp of the spleen in response to
chemotactic stimuli (PubMed:27102484).
{ECO:0000269|PubMed:19737919, ECO:0000269|PubMed:27102484}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=AAI29802.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U08185; AAA19252.1; -; mRNA.
EMBL; AF305539; AAG42212.1; -; Genomic_DNA.
EMBL; AF305534; AAG42212.1; JOINED; Genomic_DNA.
EMBL; AF305535; AAG42212.1; JOINED; Genomic_DNA.
EMBL; AF305536; AAG42212.1; JOINED; Genomic_DNA.
EMBL; AF305537; AAG42212.1; JOINED; Genomic_DNA.
EMBL; AF305538; AAG42212.1; JOINED; Genomic_DNA.
EMBL; AK077622; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK149344; BAE28822.1; -; mRNA.
EMBL; BC129801; AAI29802.1; ALT_INIT; mRNA.
CCDS; CCDS23825.2; -. [Q60636-2]
PIR; A53503; A53503.
RefSeq; NP_031574.2; NM_007548.4. [Q60636-2]
RefSeq; XP_006512565.1; XM_006512502.3. [Q60636-4]
RefSeq; XP_006512566.1; XM_006512503.2. [Q60636-3]
RefSeq; XP_006512568.1; XM_006512505.2. [Q60636-1]
RefSeq; XP_011241411.1; XM_011243109.1. [Q60636-3]
UniGene; Mm.4800; -.
ProteinModelPortal; Q60636; -.
SMR; Q60636; -.
BioGrid; 198355; 9.
IntAct; Q60636; 1.
MINT; Q60636; -.
STRING; 10090.ENSMUSP00000101129; -.
iPTMnet; Q60636; -.
PhosphoSitePlus; Q60636; -.
PaxDb; Q60636; -.
PeptideAtlas; Q60636; -.
PRIDE; Q60636; -.
DNASU; 12142; -.
Ensembl; ENSMUST00000039174; ENSMUSP00000039248; ENSMUSG00000038151. [Q60636-1]
Ensembl; ENSMUST00000105490; ENSMUSP00000101129; ENSMUSG00000038151. [Q60636-2]
Ensembl; ENSMUST00000218369; ENSMUSP00000151237; ENSMUSG00000038151. [Q60636-4]
GeneID; 12142; -.
KEGG; mmu:12142; -.
UCSC; uc007ezu.3; mouse. [Q60636-1]
UCSC; uc007ezv.3; mouse. [Q60636-2]
CTD; 639; -.
MGI; MGI:99655; Prdm1.
eggNOG; KOG2461; Eukaryota.
eggNOG; ENOG410ZFVU; LUCA.
GeneTree; ENSGT00880000137973; -.
HOGENOM; HOG000059670; -.
HOVERGEN; HBG053670; -.
InParanoid; Q60636; -.
OMA; KRNMTGY; -.
OrthoDB; EOG091G0467; -.
PhylomeDB; Q60636; -.
TreeFam; TF316545; -.
PRO; PR:Q60636; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000038151; -.
CleanEx; MM_PRDM1; -.
Genevisible; Q60636; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0042826; F:histone deacetylase binding; IDA:MGI.
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; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0035904; P:aorta development; IMP:MGI.
GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
GO; GO:0003279; P:cardiac septum development; IMP:MGI.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
GO; GO:0007281; P:germ cell development; IGI:MGI.
GO; GO:0003170; P:heart valve development; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0060576; P:intestinal epithelial cell development; IMP:MGI.
GO; GO:0001893; P:maternal placenta development; IMP:MGI.
GO; GO:0001763; P:morphogenesis of a branching structure; IMP:MGI.
GO; GO:0030889; P:negative regulation of B cell proliferation; IDA:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045579; P:positive regulation of B cell differentiation; IDA:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0033082; P:regulation of extrathymic T cell differentiation; IMP:UniProtKB.
GO; GO:0032823; P:regulation of natural killer cell differentiation; IMP:UniProtKB.
GO; GO:0051136; P:regulation of NK T cell differentiation; IMP:UniProtKB.
GO; GO:1990654; P:sebum secreting cell proliferation; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
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;
Adaptive immunity; Alternative promoter usage; Alternative splicing;
Complete proteome; Cytoplasm; Developmental protein; DNA-binding;
Immunity; Innate immunity; Isopeptide bond; Metal-binding;
Methyltransferase; Nucleus; Reference proteome; Repeat; Repressor;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 856 PR domain zinc finger protein 1.
/FTId=PRO_0000047758.
DOMAIN 115 233 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
ZN_FING 606 628 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 634 656 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 662 684 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 690 712 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 558 605 Interaction with PIAS1. {ECO:0000250}.
COMPBIAS 351 394 Glu/Pro/Ser/Thr-rich.
CROSSLNK 847 847 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:O75626}.
CROSSLNK 847 847 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:O75626}.
VAR_SEQ 1 67 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_041570.
VAR_SEQ 1 47 MREAYLRCWIFSWKNVWVRPCQRLHFKTVLLQGSLLYTALD
SYSTVQ -> MLDLLLEKRVGTTL (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_039189.
VAR_SEQ 1 47 MREAYLRCWIFSWKNVWVRPCQRLHFKTVLLQGSLLYTALD
SYSTVQ -> MTPGVPGHRTQQRPQHISALSDKAKDCSK
(in isoform 4). {ECO:0000305}.
/FTId=VSP_041571.
VAR_SEQ 624 666 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_041572.
CONFLICT 155 155 N -> K (in Ref. 4; AAI29802).
{ECO:0000305}.
CONFLICT 205 205 L -> M (in Ref. 3; AK077622).
{ECO:0000305}.
SEQUENCE 856 AA; 95836 MW; B9AC6FC2E29ECF4A CRC64;
MREAYLRCWI FSWKNVWVRP CQRLHFKTVL LQGSLLYTAL DSYSTVQAAP KSSSGSVKFQ
GLAETGIMKM DMEDADMTLW TEAEFEEKCT YIVNDHPWDS GADGGTSVQA EASLPRNLLF
KYAANNSKEV IGVVSKEYIP KGTRFGPLIG EVYTNDTVPK NANRKYFWRI YSREEFHHFI
DGFNEEKSNW MRYVNPAHSA REQNLAACQN GMNIYFYTIK PIPANQELLV WYCRDFAERL
HYPYPGELTV INLTQTESNP KQYSSEKNEL YPKSVPKREY SVKEILKLDS NPSKRKDIYR
SNISPFTLEK DMDGFRKNGS PDMPFYPRVV YPIRAPLPED FLKASLAYGM ERPTYITHSP
LPSSTTPSPP ASSSPEQSLK SSSPHSSPGN TVSPLAPGLP EHRDSYSYLN VSYGSEGLGS
YPGYAPAPHL PPAFIPSYNA HYPKFLLPPY GISSNGLSTM NNINGINNFS LFPRLYPVYS
NLLSGSSLPH PMLNPASLPS SLPTDGARRL LPPEHPKEVL IPAPHSAFSL TGAAASMKDE
SSPPSGSPTA GTAATSEHVV QPKATSSVMA APSTDGAMNL IKNKRNMTGY KTLPYPLKKQ
NGKIKYECNV CAKTFGQLSN LKVHLRVHSG ERPFKCQTCN KGFTQLAHLQ KHYLVHTGEK
PHECQVCHKR FSSTSNLKTH LRLHSGEKPY QCKVCPAKFT QFVHLKLHKR LHTRERPHKC
AQCHKSYIHL CSLKVHLKGN CPAGPAAGLP LEDLTRINEE IERFDISDNA DRLEDMEDSV
DVTSMVEKEI LAVVRKEKEE TSLKVSLQRN MGNGLLSSGC SLYESSDLSL MKLPHSNPLP
LVPVKVKQET VEPMDP


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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
EIAAB46820 Bif1,Bone morphogenetic protein-induced factor 1,Rat,Rattus norvegicus,Zbtb24,Zinc finger and BTB domain-containing protein 24,Zinc finger protein 450,Znf450
EIAAB47160 G patch domain-containing protein 6,GPATC6,GPATCH6,Homo sapiens,Human,KIAA1847,ZC3H9,ZC3HDC9,ZGPAT,Zinc finger and G patch domain-containing protein,Zinc finger CCCH domain-containing protein 9,Zinc f
EIAAB29341 Cellular zinc finger anti-NF-kappa-B protein,Homo sapiens,Human,OTU domain-containing protein 7B,OTUD7B,ZA20D1,Zinc finger A20 domain-containing protein 1,Zinc finger protein Cezanne
EIAAB46816 BTB_POZ domain zinc finger factor HOF,Mouse,Mus musculus,Zbtb20,Zfp288,Zinc finger and BTB domain-containing protein 20,Zinc finger protein 288
EIAAB36422 FYVE-finger protein EIP1,Homo sapiens,Human,La-binding protein 1,Rab4-interacting protein,RABIP4,RUFY1,RUN and FYVE domain-containing protein 1,ZFYVE12,Zinc finger FYVE domain-containing protein 12
EIAAB46839 Homo sapiens,Human,KIAA0414,ZBTB22B,ZBTB43,Zinc finger and BTB domain-containing protein 22B,Zinc finger and BTB domain-containing protein 43,Zinc finger protein 297B,ZNF297B,ZnF-x
27-664 The insulinoma-associated 1 (INSM1) gene is intronless and encodes a protein containing both a zinc finger DNA-binding domain and a putative prohormone domain. This gene is a sensitive marker for neur 0.05 mg
27-468 Insulinoma-associated 1 (INSM1) gene is intronless and encodes a protein containing both a zinc finger DNA-binding domain and a putative prohormone domain. This gene is a sensitive marker for neuroend 0.1 mg
30-773 CHN2 is a protein with a phorbol-ester_DAG-type zinc finger, a Rho-GAP domain and an SH2 domain. This protein has GTPase-activating protein activity that is regulated by phospholipid binding and bindi 0.05 mg
27-239 The gene encodes the DMRT1 protein is found in a cluster with two other members of the gene family, having in common a zinc finger-like DNA-binding motif (DM domain). The DM domain is an ancient, cons 0.05 mg
28-082 LIM domain only 6 is a three LIM domain-containing protein. The LIM domain is a cysteine-rich sequence motif that binds zinc atoms to form a specific protein-binding interface for protein-protein inte 0.05 mg
25-203 LIM domain only 6 is a three LIM domain-containing protein. The LIM domain is a cysteine-rich sequence motif that binds zinc atoms to form a specific protein-binding interface for protein-protein inte 0.05 mg
EIAAB32297 Kiaa1675,MDS1_EVI1-like gene 1,Mel1,Mouse,Mus musculus,PR domain zinc finger protein 16,PR domain-containing protein 16,Prdm16,Transcription factor MEL1
EIAAB32298 Homo sapiens,Human,KIAA1675,MDS1_EVI1-like gene 1,MEL1,PFM13,PR domain zinc finger protein 16,PR domain-containing protein 16,PRDM16,Transcription factor MEL1
EIAAB46813 LP-1,Mouse,Mus musculus,Polyomavirus late initiator promoter-binding protein,Zbtb17,Zfp100,Zfp-100,Zinc finger and BTB domain-containing protein 17,Zinc finger protein 100,Zinc finger protein 151,Zinc
EIAAB32307 PR domain zinc finger protein 2,PR domain-containing protein 2,Prdm2,Rat,Rattus norvegicus,Retinoblastoma protein-interacting zinc finger protein,Riz,Zinc finger protein RIZ
EIAAB46875 Homo sapiens,Human,ZBTB6,ZID,Zinc finger and BTB domain-containing protein 6,Zinc finger protein 482,Zinc finger protein with interaction domain,ZNF482


 

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