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

Transcription factor HIVEP3 (Human immunodeficiency virus type I enhancer-binding protein 3) (Kappa-B and V(D)J recombination signal sequences-binding protein) (Kappa-binding protein 1) (KBP-1) (Zinc finger protein ZAS3)

 ZEP3_HUMAN              Reviewed;        2406 AA.
Q5T1R4; A7YY91; Q5T1R5; Q9BZS0; Q9HCL7;
29-APR-2008, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
10-OCT-2018, entry version 134.
RecName: Full=Transcription factor HIVEP3;
AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 3;
AltName: Full=Kappa-B and V(D)J recombination signal sequences-binding protein;
AltName: Full=Kappa-binding protein 1;
Short=KBP-1;
AltName: Full=Zinc finger protein ZAS3;
Name=HIVEP3; Synonyms=KBP1, KIAA1555, KRC, ZAS3;
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 1), FUNCTION, ALTERNATIVE
SPLICING, DOMAIN, AND VARIANTS ARG-575; PRO-2023; ALA-2109; ARG-2272
AND ALA-2339.
TISSUE=Brain;
PubMed=11161801; DOI=10.1006/geno.2000.6425;
Hicar M.D., Liu Y., Allen C.E., Wu L.-C.;
"Structure of the human zinc finger protein HIVEP3: molecular cloning,
expression, exon-intron structure, and comparison with paralogous
genes HIVEP1 and HIVEP2.";
Genomics 71:89-100(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
ARG-575; PRO-2023; ALA-2109 AND ALA-2339.
TISSUE=Brain;
PubMed=10997877; DOI=10.1093/dnares/7.4.271;
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes.
XVIII. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro.";
DNA Res. 7:273-281(2000).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
ARG-575; PRO-2023; ALA-2109 AND ALA-2339.
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]
VARIANT [LARGE SCALE ANALYSIS] MET-484.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Plays a role of transcription factor; binds to
recognition signal sequences (Rss heptamer) for somatic
recombination of immunoglobulin and T-cell receptor gene segments;
Binds also to the kappa-B motif of gene such as S100A4, involved
in cell progression and differentiation. Kappa-B motif is a gene
regulatory element found in promoters and enhancers of genes
involved in immunity, inflammation, and growth and that responds
to viral antigens, mitogens, and cytokines. Involvement of HIVEP3
in cell growth is strengthened by the fact that its down-
regulation promotes cell cycle progression with ultimate formation
of multinucleated giant cells. Strongly inhibits TNF-alpha-induced
NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B
by several mechanisms: as transcription factor, by competing for
Kappa-B motif and by repressing transcription in the nucleus;
through a non transcriptional process, by inhibiting nuclear
translocation of RELA by association with TRAF2, an adapter
molecule in the tumor necrosis factor signaling, which blocks the
formation of IKK complex. Interaction with TRAF proteins inhibits
both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated
responses that include apoptosis and proinflammatory cytokine gene
expression. Positively regulates the expression of IL2 in T-cell.
Essential regulator of adult bone formation.
{ECO:0000269|PubMed:11161801}.
-!- SUBUNIT: Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms
a multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms can be generated by alternative
splicing or polyadenylation. HIVEP3L transcript may lack exon 7
leading to a premature codon stop.
{ECO:0000269|PubMed:11161801};
Name=1; Synonyms=HIVEP3S;
IsoId=Q5T1R4-1; Sequence=Displayed;
Name=2;
IsoId=Q5T1R4-2; Sequence=VSP_033279;
-!- INDUCTION: By 12-O-tetradecanoylphorbol-13 acetate (TPA).
-!- DOMAIN: The ZAS2 domain binds DNA as dimers, tetramers, and
multiple of tetramers and readily forms highly ordred DNA-protein
structures. {ECO:0000250}.
-!- PTM: Phosphorylated on threonine and serine residues.
{ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=BAB13381.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF278765; AAK01082.1; -; mRNA.
EMBL; AB046775; BAB13381.2; ALT_INIT; mRNA.
EMBL; AL445933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC152563; AAI52564.1; -; mRNA.
CCDS; CCDS44124.1; -. [Q5T1R4-2]
CCDS; CCDS463.1; -. [Q5T1R4-1]
RefSeq; NP_001121186.1; NM_001127714.2. [Q5T1R4-2]
RefSeq; NP_078779.2; NM_024503.4. [Q5T1R4-1]
RefSeq; XP_011540186.1; XM_011541884.2. [Q5T1R4-1]
RefSeq; XP_016857481.1; XM_017001992.1. [Q5T1R4-1]
RefSeq; XP_016857482.1; XM_017001993.1. [Q5T1R4-1]
RefSeq; XP_016857483.1; XM_017001994.1. [Q5T1R4-2]
UniGene; Hs.403972; -.
UniGene; Hs.648369; -.
ProteinModelPortal; Q5T1R4; -.
SMR; Q5T1R4; -.
BioGrid; 121861; 10.
STRING; 9606.ENSP00000247584; -.
iPTMnet; Q5T1R4; -.
PhosphoSitePlus; Q5T1R4; -.
BioMuta; HIVEP3; -.
DMDM; 74756245; -.
EPD; Q5T1R4; -.
MaxQB; Q5T1R4; -.
PaxDb; Q5T1R4; -.
PeptideAtlas; Q5T1R4; -.
PRIDE; Q5T1R4; -.
ProteomicsDB; 64282; -.
ProteomicsDB; 64283; -. [Q5T1R4-2]
Ensembl; ENST00000372583; ENSP00000361664; ENSG00000127124. [Q5T1R4-1]
Ensembl; ENST00000372584; ENSP00000361665; ENSG00000127124. [Q5T1R4-2]
Ensembl; ENST00000643665; ENSP00000494598; ENSG00000127124. [Q5T1R4-2]
GeneID; 59269; -.
KEGG; hsa:59269; -.
UCSC; uc001cgz.5; human. [Q5T1R4-1]
CTD; 59269; -.
DisGeNET; 59269; -.
EuPathDB; HostDB:ENSG00000127124.13; -.
GeneCards; HIVEP3; -.
HGNC; HGNC:13561; HIVEP3.
HPA; HPA005728; -.
MIM; 606649; gene.
neXtProt; NX_Q5T1R4; -.
OpenTargets; ENSG00000127124; -.
PharmGKB; PA29299; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00530000063161; -.
HOGENOM; HOG000155774; -.
HOVERGEN; HBG095595; -.
InParanoid; Q5T1R4; -.
KO; K09239; -.
OMA; MERIPGE; -.
OrthoDB; EOG091G00EA; -.
PhylomeDB; Q5T1R4; -.
TreeFam; TF331837; -.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
ChiTaRS; HIVEP3; human.
GeneWiki; HIVEP3; -.
GenomeRNAi; 59269; -.
PRO; PR:Q5T1R4; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000127124; Expressed in 177 organ(s), highest expression level in buccal mucosa cell.
CleanEx; HS_HIVEP3; -.
Genevisible; Q5T1R4; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
InterPro; IPR034729; ZF_CCHC_HIVEP.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00096; zf-C2H2; 4.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS51811; ZF_CCHC_HIVEP; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
2: Evidence at transcript level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation;
Zinc; Zinc-finger.
CHAIN 1 2406 Transcription factor HIVEP3.
/FTId=PRO_0000331627.
REPEAT 1964 1967 1.
REPEAT 1970 1973 2.
REPEAT 1993 1996 3.
REPEAT 1998 2001 4.
REPEAT 2067 2070 5.
REPEAT 2079 2082 6.
ZN_FING 192 214 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 220 242 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 640 670 CCHC HIVEP-type. {ECO:0000255|PROSITE-
ProRule:PRU01154}.
ZN_FING 1754 1776 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1782 1806 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 192 242 ZAS1.
REGION 211 1074 No DNA binding activity or
transactivation activity, but complete
prevention of TRAF-dependent NF-Kappa-B
activation; associates with TRAF2 and
JUN. {ECO:0000250}.
REGION 264 287 Acidic 1.
REGION 862 883 Acidic 2.
REGION 1754 1806 ZAS2.
REGION 1817 1872 Acidic 3.
REGION 2053 2148 6 X 4 AA tandem repeats of S-P-X-[RK].
COILED 1442 1466 {ECO:0000255}.
MOTIF 903 909 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 308 334 Ser-rich.
COMPBIAS 378 414 Ser-rich.
COMPBIAS 797 819 Ser-rich.
COMPBIAS 844 880 Glu/Pro-rich.
COMPBIAS 916 948 Ser-rich.
COMPBIAS 1907 1936 Ser-rich.
VAR_SEQ 2136 2136 Missing (in isoform 2).
{ECO:0000303|PubMed:10997877,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_033279.
VARIANT 35 35 V -> I (in dbSNP:rs2146315).
/FTId=VAR_042910.
VARIANT 484 484 V -> M (in a colorectal cancer sample;
somatic mutation; dbSNP:rs780211835).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_042911.
VARIANT 575 575 H -> R (in dbSNP:rs2810566).
{ECO:0000269|PubMed:10997877,
ECO:0000269|PubMed:11161801,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_042912.
VARIANT 1087 1087 Q -> H (in dbSNP:rs17363472).
/FTId=VAR_042913.
VARIANT 2023 2023 A -> P (in dbSNP:rs2483689).
{ECO:0000269|PubMed:10997877,
ECO:0000269|PubMed:11161801,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_042914.
VARIANT 2109 2109 D -> A (in dbSNP:rs2991344).
{ECO:0000269|PubMed:10997877,
ECO:0000269|PubMed:11161801,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_042915.
VARIANT 2272 2272 G -> R (in dbSNP:rs11809423).
{ECO:0000269|PubMed:11161801}.
/FTId=VAR_042916.
VARIANT 2339 2339 T -> A (in dbSNP:rs9439043).
{ECO:0000269|PubMed:10997877,
ECO:0000269|PubMed:11161801,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_042917.
CONFLICT 44 44 A -> P (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 94 95 QL -> HV (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 123 123 D -> S (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 127 127 P -> L (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 133 134 FV -> LL (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 589 589 R -> P (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 901 901 L -> A (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 961 961 S -> D (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 1034 1035 RV -> GE (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 1048 1049 QA -> SP (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 1110 1110 P -> A (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 1180 1180 P -> L (in Ref. 2; BAB13381 and 5;
AAI52564). {ECO:0000305}.
CONFLICT 1279 1279 T -> Q (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 1524 1524 T -> Q (in Ref. 1; AAK01082).
{ECO:0000305}.
CONFLICT 2376 2376 P -> S (in Ref. 1; AAK01082).
{ECO:0000305}.
SEQUENCE 2406 AA; 259465 MW; AFCCFDAF87014A7D CRC64;
MDPEQSVKGT KKAEGSPRKR LTKGEAIQTS VSSSVPYPGS GTAATQESPA QELLAPQPFP
GPSSVLREGS QEKTGQQQKP PKRPPIEASV HISQLPQHPL TPAFMSPGKP EHLLEGSTWQ
LVDPMRPGPS GSFVAPGLHP QSQLLPSHAS IIPPEDLPGV PKVFVPRPSQ VSLKPTEEAH
KKERKPQKPG KYICQYCSRP CAKPSVLQKH IRSHTGERPY PCGPCGFSFK TKSNLYKHRK
SHAHRIKAGL ASGMGGEMYP HGLEMERIPG EEFEEPTEGE STDSEEETSA TSGHPAELSP
RPKQPLLSSG LYSSGSHSSS HERCSLSQSS TAQSLEDPPP FVEPSSEHPL SHKPEDTHTI
KQKLALRLSE RKKVIDEQAF LSPGSKGSTE SGYFSRSESA EQQVSPPNTN AKSYAEIIFG
KCGRIGQRTA MLTATSTQPL LPLSTEDKPS LVPLSVPRTQ VIEHITKLIT INEAVVDTSE
IDSVKPRRSS LSRRSSMESP KSSLYREPLS SHSEKTKPEQ SLLSLQHPPS TAPPVPLLRS
HSMPSAACTI STPHHPFRGS YSFDDHITDS EALSHSSHVF TSHPRMLKRQ PAIELPLGGE
YSSEEPGPSS KDTASKPSDE VEPKESELTK KTKKGLKTKG VIYECNICGA RYKKRDNYEA
HKKYYCSELQ IAKPISAGTH TSPEAEKSQI EHEPWSQMMH YKLGTTLELT PLRKRRKEKS
LGDEEEPPAF ESTKSQFGSP GPSDAARNLP LESTKSPAEP SKSVPSLEGP TGFQPRTPKP
GSGSESGKER RTTSKEISVI QHTSSFEKSD SLEQPSGLEG EDKPLAQFPS PPPAPHGRSA
HSLQPKLVRQ PNIQVPEILV TEEPDRPDTE PEPPPKEPEK TEEFQWPQRS QTLAQLPAEK
LPPKKKRLRL AEMAQSSGES SFESSVPLSR SPSQESNVSL SGSSRSASFE RDDHGKAEAP
SPSSDMRPKP LGTHMLTVPS HHPHAREMRR SASEQSPNVS HSAHMTETRS KSFDYGSLSL
TGPSAPAPVA PPARVAPPER RKCFLVRQAS LSRPPESELE VAPKGRQESE EPQPSSSKPS
AKSSLSQISS AATSHGGPPG GKGPGQDRPP LGPTVPYTEA LQVFHHPVAQ TPLHEKPYLP
PPVSLFSFQH LVQHEPGQSP EFFSTQAMSS LLSSPYSMPP LPPSLFQAPP LPLQPTVLHP
GQLHLPQLMP HPANIPFRQP PSFLPMPYPT SSALSSGFFL PLQSQFALQL PGDVESHLPQ
IKTSLAPLAT GSAGLSPSTE YSSDIRLPPV APPASSSAPT SAPPLALPAC PDTMVSLVVP
VRVQTNMPSY GSAMYTTLSQ ILVTQSQGSS ATVALPKFEE PPSKGTTVCG ADVHEVGPGP
SGLSEEQSRA FPTPYLRVPV TLPERKGTSL SSESILSLEG SSSTAGGSKR VLSPAGSLEL
TMETQQQKRV KEEEASKADE KLELVKPCSV VLTSTEDGKR PEKSHLGNQG QGRRELEMLS
SLSSDPSDTK EIPPLPHPAL SHGTAPGSEA LKEYPQPSGK PHRRGLTPLS VKKEDSKEQP
DLPSLAPPSS LPLSETSSRP AKSQEGTDSK KVLQFPSLHT TTNVSWCYLN YIKPNHIQHA
DRRSSVYAGW CISLYNPNLP GVSTKAALSL LRSKQKVSKE TYTMATAPHP EAGRLVPSSS
RKPRMTEVHL PSLVSPEGQK DLARVEKEEE RRGEPEEDAP ASQRGEPARI KIFEGGYKSN
EEYVYVRGRG RGKYVCEECG IRCKKPSMLK KHIRTHTDVR PYVCKHCHFA FKTKGNLTKH
MKSKAHSKKC QETGVLEELE AEEGTSDDLF QDSEGREGSE AVEEHQFSDL EDSDSDSDLD
EDEDEDEEES QDELSRPSSE APPPGPPHAL RADSSPILGP QPPDAPASGT EATRGSSVSE
AERLTASSCS MSSQSMPGLP WLGPAPLGSV EKDTGSALSY KPVSPRRPWS PSKEAGSRPP
LARKHSLTKN DSSPQRCSPA REPQASAPSP PGLHVDPGRG MGALPCGSPR LQLSPLTLCP
LGRELAPRAH VLSKLEGTTD PGLPRYSPTR RWSPGQAESP PRSAPPGKWA LAGPGSPSAG
EHGPGLGLDP RVLFPPAPLP HKLLSRSPET CASPWQKAES RSPSCSPGPA HPLSSRPFSA
LHDFHGHILA RTEENIFSHL PLHSQHLTRA PCPLIPIGGI QMVQARPGAH PTLLPGPTAA
WVSGFSGGGS DLTGAREAQE RGRWSPTESS SASVSPVAKV SKFTLSSELE GGDYPKERER
TGGGPGRPPD WTPHGTGAPA EPTPTHSPCT PPDTLPRPPQ GRRAAQSWSP RLESPRAPTN
PEPSATPPLD RSSSVGCLAE ASARFPARTR NLSGEPRTRQ DSPKPSGSGE PRAHPHQPED
RVPPNA


Related products :

Catalog number Product name Quantity
EIAAB47038 Hivep3,Human immunodeficiency virus type I enhancer-binding protein 3 homolog,Kappa-B and V(D)J recombination signal sequences-binding protein,Kappa-binding protein 1,KB-binding and regognition compon
EIAAB47037 HIVEP3,Homo sapiens,Human,Human immunodeficiency virus type I enhancer-binding protein 3,Kappa-B and V(D)J recombination signal sequences-binding protein,Kappa-binding protein 1,KBP1,KBP-1,KIAA1555,KR
EIAAB47067 Alpha-fetoprotein enhancer-binding protein,AT motif-binding factor,ATBF1,AT-binding transcription factor 1,Homo sapiens,Human,ZFH-3,ZFHX3,Zinc finger homeobox protein 3,Zinc finger homeodomain protein
EIAAB47066 Alpha-fetoprotein enhancer-binding protein,AT motif-binding factor,Atbf1,AT-binding transcription factor 1,Mouse,Mus musculus,ZFH-3,Zfhx3,Zinc finger homeobox protein 3,Zinc finger homeodomain protein
EIAAB40542 CBF-1,Homo sapiens,Human,IGKJRB,IGKJRB1,J kappa-recombination signal-binding protein,RBPJ,RBP-J,RBP-J kappa,RBPJK,RBP-JK,RBPSUH,Recombining binding protein suppressor of hairless,Renal carcinoma antig
EIAAB40543 Bos taurus,Bovine,J kappa-recombination signal-binding protein,RBPJ,RBP-J kappa,RBPSUH,Recombining binding protein suppressor of hairless
EIAAB40541 Igkjrb1,Igkrsbp,J kappa-recombination signal-binding protein,Mouse,Mus musculus,Rbpj,RBP-J kappa,Rbpsuh,Recombining binding protein suppressor of hairless
18-003-43011 Recombining binding protein suppressor of hairless - J kappa-recombination signal-binding protein; RBP-J kappa; RBP-J; RBP-JK; CBF-1; NY-REN-30 antigen Polyclonal 0.1 mg Protein A
18-003-42028 Recombining binding protein suppressor of hairless - J kappa-recombination signal-binding protein; RBP-J kappa; RBP-J; RBP-JK; CBF-1; NY-REN-30 antigen Polyclonal 0.05 mg Aff Pur
20-372-60085 recombining binding protein suppressor of hairless (Drosophila) (RBPSUH) - Mouse monoclonal anti-human RBPSUH antibody; J kappa-recombination signal-binding protein; RBP-J kappa; RBP-J; RBP-JK; CBF-1; 0.1 mg
EIAAB47036 Hivep2,Human immunodeficiency virus type I enhancer-binding protein 2 homolog,Mibp1,MIBP-1,Mouse,Mus musculus,Myc intron-binding protein 1,Transcription factor HIVEP2
EIAAB47034 Agie-bp1,Angiotensinogen gene-inducible enhancer-binding protein 1,DNA-binding protein AGIE-BP1,Hivep2,Human immunodeficiency virus type I enhancer-binding protein 2 homolog,Mibp1,MIBP-1,Myc intron-bi
HIVEP3 HIVEP1 Gene human immunodeficiency virus type I enhancer binding protein 1
HJURP HIVEP3 Gene human immunodeficiency virus type I enhancer binding protein 3
EIAAB47035 HIVEP2,HIV-EP2,Homo sapiens,Human,Human immunodeficiency virus type I enhancer-binding protein 2,MBP-2,MHC-binding protein 2,Transcription factor HIVEP2
EIAAB47360 GC-box-binding zinc finger protein 1,GZP1,Homo sapiens,Human,Transcription factor ZBP-99,ZBP99,Zinc finger DNA-binding protein 99,Zinc finger protein 281,ZNF281
EIAAB47028 Rat,Rattus norvegicus,Tcf8,TCF-8,Transcription factor 8,Zeb1,Zfhep,Zinc finger E-box-binding homeobox 1,Zinc finger homeodomain enhancer-binding protein
EIAAB35961 FINB,Finger protein in nuclear bodies,Homo sapiens,Human,Raf-responsive zinc finger protein LZ321,Ras-responsive element-binding protein 1,RREB1,RREB-1,Zep-1,Zinc finger motif enhancer-binding protein
EIAAB47268 Beta enolase repressor factor 1,G-rich box-binding protein,Mouse,Mus musculus,Transcription factor BFCOL1,Transcription factor ZBP-89,Zbp89,Zfp148,Zinc finger DNA-binding protein 89,Zinc finger protei
CSB-EL010466HU Human human immunodeficiency virus type I enhancer binding protein 3 (HIVEP3) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB27094 DNA-binding protein R kappa-B,Homo sapiens,Human,INO80 complex subunit G,INO80G,NFRKB,Nuclear factor related to kappa-B-binding protein
CSB-EL010466MO Mouse human immunodeficiency virus type I enhancer binding protein 3 (HIVEP3) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB27093 DNA-binding protein R kappa-B,Mouse,Mus musculus,Nfrkb,Nuclear factor related to kappa-B-binding protein
CSB-EL019487HU Human recombination signal binding protein for immunoglobulin kappa J region-like (RBPJL) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL019486HU Human recombination signal binding protein for immunoglobulin kappa J region (RBPJ) ELISA kit, Species Human, Sample Type serum, plasma 96T


 

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