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AT-rich interactive domain-containing protein 4A (ARID domain-containing protein 4A) (Retinoblastoma-binding protein 1) (RBBP-1)

 ARI4A_HUMAN             Reviewed;        1257 AA.
P29374; Q15991; Q15992; Q15993;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 3.
23-MAY-2018, entry version 169.
RecName: Full=AT-rich interactive domain-containing protein 4A;
Short=ARID domain-containing protein 4A;
AltName: Full=Retinoblastoma-binding protein 1;
Short=RBBP-1;
Name=ARID4A; Synonyms=RBBP1, RBP1;
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 I), AND VARIANT ALA-779.
PubMed=8414517;
Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E.,
Vuocolo G.A., Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D.,
Jones R.E.;
"Characterization of the retinoblastoma binding proteins RBP1 and
RBP2.";
Oncogene 8:3149-3156(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 338-1257 (ISOFORMS I; II AND III),
SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
PubMed=8455946;
Otterson G.A., Kratzke R.A., Lin A.Y., Johnston P.G., Kaye F.J.;
"Alternative splicing of the RBP1 gene clusters in an internal exon
that encodes potential phosphorylation sites.";
Oncogene 8:949-957(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 855-1203 (ISOFORM I).
PubMed=1857421; DOI=10.1038/352251a0;
Defeo-Jones D., Huang P.S., Jones R.E., Haskell K.M., Vuocolo G.A.,
Hanobik M.G., Huber H.E., Oliff A.;
"Cloning of cDNAs for cellular proteins that bind to the
retinoblastoma gene product.";
Nature 352:251-254(1991).
[5]
IDENTIFICATION IN A COMPLEX WITH WITH SIN3A; SIN3B; HDAC1; HDAC2;
SAP30; BRMS1; RBBP4 AND RBBP7.
PubMed=14581478; DOI=10.1074/jbc.M307969200;
Meehan W.J., Samant R.S., Hopper J.E., Carrozza M.J., Shevde L.A.,
Workman J.L., Eckert K.A., Verderame M.F., Welch D.R.;
"Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with
retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone
deacetylase complex and represses transcription.";
J. Biol. Chem. 279:1562-1569(2004).
[6]
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676 AND SER-1109, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[8]
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).
[9]
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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716; SER-864 AND
SER-1145, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481 AND LYS-718, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-513; LYS-718; LYS-738 AND
LYS-759, 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).
[16]
STRUCTURE BY NMR OF 170-277.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RBB1NT domain of human RB(Retinoblastoma)-
binding protein 1.";
Submitted (APR-2008) to the PDB data bank.
-!- FUNCTION: Interacts with the viral protein-binding domain of the
retinoblastoma protein.
-!- SUBUNIT: Interacts with BRMS1. Identified in mSin3A corepressor
complexes together with SIN3A, SIN3B, RBBP4, RBBP7, SAP30, BRMS1,
HDAC1 and HDAC2. {ECO:0000269|PubMed:14581478}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00355, ECO:0000269|PubMed:8455946}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=I;
IsoId=P29374-1; Sequence=Displayed;
Name=II;
IsoId=P29374-2; Sequence=VSP_004373;
Name=III;
IsoId=P29374-3; Sequence=VSP_004371, VSP_004372;
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EMBL; S66427; AAB28543.1; -; mRNA.
EMBL; AL132989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL139021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; S57153; AAB25833.1; -; mRNA.
EMBL; S57160; AAB25834.1; -; mRNA.
EMBL; S57162; AAB25835.2; -; mRNA.
CCDS; CCDS45114.1; -. [P29374-2]
CCDS; CCDS9732.1; -. [P29374-1]
CCDS; CCDS9733.1; -. [P29374-3]
PIR; I58383; I58383.
RefSeq; NP_002883.3; NM_002892.3. [P29374-1]
RefSeq; NP_075376.2; NM_023000.2. [P29374-2]
RefSeq; NP_075377.2; NM_023001.2. [P29374-3]
UniGene; Hs.161000; -.
PDB; 2LCC; NMR; -; A=568-635.
PDB; 2MAM; NMR; -; A=4-121.
PDB; 2YRV; NMR; -; A=170-273.
PDB; 6BPH; X-ray; 1.85 A; A=568-635.
PDBsum; 2LCC; -.
PDBsum; 2MAM; -.
PDBsum; 2YRV; -.
PDBsum; 6BPH; -.
ProteinModelPortal; P29374; -.
SMR; P29374; -.
BioGrid; 111861; 32.
CORUM; P29374; -.
DIP; DIP-463N; -.
IntAct; P29374; 9.
MINT; P29374; -.
STRING; 9606.ENSP00000347602; -.
iPTMnet; P29374; -.
PhosphoSitePlus; P29374; -.
BioMuta; ARID4A; -.
DMDM; 206729929; -.
EPD; P29374; -.
MaxQB; P29374; -.
PaxDb; P29374; -.
PeptideAtlas; P29374; -.
PRIDE; P29374; -.
DNASU; 5926; -.
Ensembl; ENST00000348476; ENSP00000344556; ENSG00000032219. [P29374-3]
Ensembl; ENST00000355431; ENSP00000347602; ENSG00000032219. [P29374-1]
Ensembl; ENST00000395168; ENSP00000378597; ENSG00000032219. [P29374-2]
Ensembl; ENST00000431317; ENSP00000397368; ENSG00000032219. [P29374-3]
GeneID; 5926; -.
KEGG; hsa:5926; -.
UCSC; uc001xdo.4; human. [P29374-1]
CTD; 5926; -.
DisGeNET; 5926; -.
EuPathDB; HostDB:ENSG00000032219.18; -.
GeneCards; ARID4A; -.
H-InvDB; HIX0037655; -.
HGNC; HGNC:9885; ARID4A.
HPA; HPA048899; -.
MIM; 180201; gene.
neXtProt; NX_P29374; -.
OpenTargets; ENSG00000032219; -.
PharmGKB; PA34249; -.
eggNOG; KOG2744; Eukaryota.
eggNOG; KOG3001; Eukaryota.
eggNOG; ENOG410Y2AP; LUCA.
GeneTree; ENSGT00900000140901; -.
HOGENOM; HOG000015398; -.
HOVERGEN; HBG058247; -.
InParanoid; P29374; -.
KO; K19194; -.
OMA; RLVYHQG; -.
OrthoDB; EOG091G0EG4; -.
PhylomeDB; P29374; -.
TreeFam; TF106427; -.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
SIGNOR; P29374; -.
ChiTaRS; ARID4A; human.
EvolutionaryTrace; P29374; -.
GeneWiki; ARID4A; -.
GenomeRNAi; 5926; -.
PRO; PR:P29374; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000032219; -.
CleanEx; HS_ARID4A; -.
CleanEx; HS_RBP1; -.
ExpressionAtlas; P29374; baseline and differential.
Genevisible; P29374; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:GDB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0017053; C:transcriptional repressor complex; IDA:GDB.
GO; GO:0003677; F:DNA binding; IDA:GDB.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0004407; F:histone deacetylase activity; TAS:Reactome.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
GO; GO:0097368; P:establishment of Sertoli cell barrier; IEA:Ensembl.
GO; GO:0080182; P:histone H3-K4 trimethylation; IEA:Ensembl.
GO; GO:0036124; P:histone H3-K9 trimethylation; IEA:Ensembl.
GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:GDB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
CDD; cd00024; CHROMO; 1.
Gene3D; 1.10.150.60; -; 1.
InterPro; IPR001606; ARID_dom.
InterPro; IPR036431; ARID_dom_sf.
InterPro; IPR016197; Chromo-like_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR012603; RBB1NT.
InterPro; IPR002999; Tudor.
InterPro; IPR025995; Tudor-knot.
Pfam; PF01388; ARID; 1.
Pfam; PF08169; RBB1NT; 1.
Pfam; PF11717; Tudor-knot; 1.
SMART; SM00501; BRIGHT; 1.
SMART; SM00298; CHROMO; 1.
SMART; SM00333; TUDOR; 1.
SUPFAM; SSF46774; SSF46774; 1.
SUPFAM; SSF54160; SSF54160; 1.
PROSITE; PS51011; ARID; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 1257 AT-rich interactive domain-containing
protein 4A.
/FTId=PRO_0000200580.
DOMAIN 309 401 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
REGION 951 964 Retinoblastoma protein binding.
{ECO:0000255}.
MOD_RES 676 676 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 716 716 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 864 864 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1109 1109 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1145 1145 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 481 481 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364}.
CROSSLNK 513 513 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 718 718 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 738 738 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 759 759 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1106 1174 Missing (in isoform III).
{ECO:0000303|PubMed:8455946}.
/FTId=VSP_004371.
VAR_SEQ 1121 1174 Missing (in isoform II).
{ECO:0000303|PubMed:8455946}.
/FTId=VSP_004373.
VAR_SEQ 1175 1175 N -> D (in isoform III).
{ECO:0000303|PubMed:8455946}.
/FTId=VSP_004372.
VARIANT 412 412 H -> P (in dbSNP:rs34982206).
/FTId=VAR_031566.
VARIANT 724 724 N -> S (in dbSNP:rs2230098).
/FTId=VAR_031567.
VARIANT 779 779 T -> A (in dbSNP:rs1051858).
{ECO:0000269|PubMed:8414517}.
/FTId=VAR_031568.
CONFLICT 385 385 V -> L (in Ref. 1; AAB28543).
{ECO:0000305}.
CONFLICT 618 618 R -> S (in Ref. 1; AAB28543).
{ECO:0000305}.
CONFLICT 653 653 K -> V (in Ref. 3; AAB25833/AAB25834/
AAB25835). {ECO:0000305}.
CONFLICT 1178 1178 D -> S (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1196 1201 IRKYYM -> SENIICL (in Ref. 4; no
nucleotide entry). {ECO:0000305}.
STRAND 8 10 {ECO:0000244|PDB:2MAM}.
STRAND 15 20 {ECO:0000244|PDB:2MAM}.
STRAND 23 42 {ECO:0000244|PDB:2MAM}.
TURN 43 45 {ECO:0000244|PDB:2MAM}.
STRAND 48 52 {ECO:0000244|PDB:2MAM}.
TURN 53 55 {ECO:0000244|PDB:2MAM}.
STRAND 56 58 {ECO:0000244|PDB:2MAM}.
STRAND 65 69 {ECO:0000244|PDB:2MAM}.
STRAND 75 93 {ECO:0000244|PDB:2MAM}.
STRAND 98 102 {ECO:0000244|PDB:2MAM}.
HELIX 103 105 {ECO:0000244|PDB:2MAM}.
STRAND 112 114 {ECO:0000244|PDB:2MAM}.
STRAND 177 182 {ECO:0000244|PDB:2YRV}.
STRAND 190 196 {ECO:0000244|PDB:2YRV}.
STRAND 211 218 {ECO:0000244|PDB:2YRV}.
STRAND 221 224 {ECO:0000244|PDB:2YRV}.
TURN 226 228 {ECO:0000244|PDB:2YRV}.
HELIX 239 244 {ECO:0000244|PDB:2YRV}.
HELIX 246 256 {ECO:0000244|PDB:2YRV}.
TURN 262 264 {ECO:0000244|PDB:2YRV}.
HELIX 269 272 {ECO:0000244|PDB:2YRV}.
STRAND 578 584 {ECO:0000244|PDB:6BPH}.
HELIX 586 588 {ECO:0000244|PDB:6BPH}.
STRAND 590 602 {ECO:0000244|PDB:6BPH}.
STRAND 605 612 {ECO:0000244|PDB:6BPH}.
HELIX 617 619 {ECO:0000244|PDB:6BPH}.
STRAND 621 624 {ECO:0000244|PDB:6BPH}.
HELIX 625 627 {ECO:0000244|PDB:6BPH}.
SEQUENCE 1257 AA; 142752 MW; 5B3F6A5AFB7588CF CRC64;
MKAADEPAYL TVGTDVSAKY RGAFCEAKIK TVKRLVKVKV LLKQDNTTQL VQDDQVKGPL
RVGAIVETRT SDGSFQEAII SKLTDASWYT VVFDDGDERT LRRTSLCLKG ERHFAESETL
DQLPLTNPEH FGTPVIAKKT NRGRRSSLPV TEDEKEEESS EEEDEDKRRL NDELLGKVVS
VVSATERTEW YPALVISPSC NDDITVKKDQ CLVRSFIDSK FYSIARKDIK EVDILNLPES
ELSTKPGLQK ASIFLKTRVV PDNWKMDISE ILESSSSDDE DGPAEENDEE KEKEAKKTEE
EVPEEELDPE ERDNFLQQLY KFMEDRGTPI NKPPVLGYKD LNLFKLFRLV YHQGGCDNID
SGAVWKQIYM DLGIPILNSA ASYNVKTAYR KYLYGFEEYC RSANIQFRTV HHHEPKVKEE
KKDLEESMEE ALKLDQEMPL TEVKSEPEEN IDSNSESERE EIELKSPRGR RRIARDVNSI
KKEIEEEKTE DKLKDNDTEN KDVDDDYETA EKKENELLLG RKNTPKQKEK KIKKQEDSDK
DSDEEEEKSQ EREETESKCD SEGEEDEEDM EPCLTGTKVK VKYGRGKTQK IYEASIKSTE
IDDGEVLYLV HYYGWNVRYD EWVKADRIIW PLDKGGPKKK QKKKAKNKED SEKDEKRDEE
RQKSKRGRPP LKSTLSSNMP YGLSKTANSE GKSDSCSSDS ETEDALEKNL INEELSLKDE
LEKNENLNDD KLDEENPKIS AHILKENDRT QMQPLETLKL EVGENEQIVQ IFGNKMEKTE
EVKKEAEKSP KGKGRRSKTK DLSLEIIKIS SFGQNEAGSE PHIEAHSLEL SSLDNKNFSS
ATEDEIDQCV KEKKLKRKIL GQSSPEKKIR IENGMEMTNT VSQERTSDCI GSEGMKNLNF
EQHFERENEG MPSLIAESNQ CIQQLTSERF DSPAEETVNI PLKEDEDAMP LIGPETLVCH
EVDLDDLDEK DKTSIEDVAV ESSESNSLVS IPPALPPVVQ HNFSVASPLT LSQDESRSVK
SESDITIEVD SIAEESQEGL CERESANGFE TNVASGTCSI IVQERESREK GQKRPSDGNS
GLMAKKQKRT PKRTSAAAKN EKNGTGQSSD SEDLPVLDNS SKCTPVKHLN VSKPQKLARS
PARISPHIKD GEKDKHREKH PNSSPRTYKW SFQLNELDNM NSTERISFLQ EKLQEIRKYY
MSLKSEVATI DRRRKRLKKK DREVSHAGAS MSSASSDTGM SPSSSSPPQN VLAVECR


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18-003-43093 AT-rich interactive domain-containing protein 3A - ARID domain-containing protein 3A; B-cell regulator of IgH transcription; Bright; E2F-binding protein 1 Polyclonal 0.05 mg Aff Pur
20-372-60070 AT rich interactive domain 3A (BRIGHT- like) - Mouse monoclonal anti-human ARID3A antibody; ARID domain-containing protein 3A; Dead ringer-like protein 1; Bright; E2F-binding protein 1 Monoclonal 0.1 mg
18-003-44091 AT-rich interactive domain-containing protein 3B - ARID domain-containing protein 3B; Bright-like; Bright and dead ringer protein Polyclonal 0.05 mg Aff Pur
20-372-60127 AT rich interactive domain 1A (SWI- like) (ARID1A). transcript variant 1. mRNA - Mouse monoclonal anti-human ARID1A antibody; ARID domain-containing protein 1A; SWI_SNF-related. matrix-associated. act 0.1 mg
EIAAB33918 B5T-overexpressed gene protein,BOG,Homo sapiens,Human,Protein BOG,Putative hydrolase RBBP9,RBBP10,RBBP-10,RBBP9,RBBP-9,Retinoblastoma-binding protein 10,Retinoblastoma-binding protein 9
28-043 ARID3B is a member of the ARID (AT-rich interaction domain) family of DNA-binding proteins. The protein is homologous with two proteins that bind to the retinoblastoma gene product, and also with the 0.1 mg
28-946 ARID3B is a member of the ARID (AT-rich interaction domain) family of DNA-binding proteins. The protein is homologous with two proteins that bind to the retinoblastoma gene product, and also with the 0.05 mg
26-522 ARID3C is a member of the ARID (AT-rich interaction domain) family of proteins. The ARID domain is a helix-turn-helix motif-based DNA-binding domain. ARID family members have roles in embryonic patter 0.05 mg
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
25-803 This gene is a member of the PAR6 family and encodes a protein with a PSD95_Discs-large_ZO1 (PDZ) domain, an OPR domain and a semi-Cdc42_Rac interactive binding (CRIB) domain. This cytoplasmic protein 0.05 mg
GWB-FD34A2 AT rich interactive domain 2 (ARID RFX-like) (ARID2), Antibody
ARID3B ARID2 Gene AT rich interactive domain 2 (ARID, RFX-like)
60157 IgG,AT rich interactive domain 2 (ARID, RFX_like) (ARID2) 0.1 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
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
18-003-42905 Transcription factor E2F1 - E2F-1; Retinoblastoma-binding protein 3; RBBP-3; PRB-binding protein E2F-1; PBR3; Retinoblastoma-associated protein 1; RBAP-1 Polyclonal 0.05 mg Aff Pur
18-003-43023 Transcription factor E2F1 - E2F-1; Retinoblastoma-binding protein 3; RBBP-3; PRB-binding protein E2F-1; PBR3; Retinoblastoma-associated protein 1; RBAP-1 Polyclonal 0.1 mg Protein A
EIAAB12253 E2F1,E2F-1,Homo sapiens,Human,PBR3,PRB-binding protein E2F-1,RBAP-1,RBBP3,RBBP-3,Retinoblastoma-associated protein 1,Retinoblastoma-binding protein 3,Transcription factor E2F1
EIAAB33910 Homo sapiens,Human,RBBP5,RBBP-5,RBQ3,Retinoblastoma-binding protein 5,Retinoblastoma-binding protein RBQ-3
31-212 LHX2 is a protein belonging to a large protein family, members of which carry the LIM domain, a unique cysteine-rich zinc-binding domain. The encoded protein may function as a transcriptional regulato 0.1 mg
20-272-190684 E2F1 - Mouse monoclonal [KH129] to E2F1; E2F-1; Retinoblastoma-binding protein 3; RBBP-3; PRB-binding protein E2F-1; PBR3; Retinoblastoma-associated protein 1; RBAP-1 Monoclonal 0.05 ml
EIAAB38236 FASH3,Fovea-associated SH3 domain-binding protein,Homo sapiens,Human,SH3 domain-binding glutamic acid-rich-like protein 2,SH3BGRL2
EIAAB38239 Homo sapiens,Human,P1725,SH3 domain-binding glutamic acid-rich-like protein 3,SH3 domain-binding protein 1,SH3BGRL3,SH3BP-1
EIAAB33914 Chicken,Gallus gallus,Histone-binding protein RBBP7,RBAP46,RBBP7,RBBP-7,Retinoblastoma-binding protein 7,Retinoblastoma-binding protein p46


 

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