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Cbp/p300-interacting transactivator 2 (MSG-related protein 1) (MRG-1) (P35srj)

 CITE2_HUMAN             Reviewed;         270 AA.
Q99967; O95426; Q5VTF4;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
20-JUN-2002, sequence version 2.
31-JAN-2018, entry version 164.
RecName: Full=Cbp/p300-interacting transactivator 2;
AltName: Full=MSG-related protein 1;
Short=MRG-1;
AltName: Full=P35srj;
Name=CITED2; Synonyms=MRG1;
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 SUBCELLULAR LOCATION.
PubMed=8901575; DOI=10.1073/pnas.93.22.12298;
Shioda T., Fenner M.H., Isselbacher K.J.;
"msg1, a novel melanocyte-specific gene, encodes a nuclear protein and
is associated with pigmentation.";
Proc. Natl. Acad. Sci. U.S.A. 93:12298-12303(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10552932; DOI=10.1006/geno.1999.5970;
Leung M.K., Jones T., Michels C.L., Livingston D.M., Bhattacharya S.;
"Molecular cloning and chromosomal localization of the human CITED2
gene encoding p35srj/Mrg1.";
Genomics 61:307-313(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EP300,
INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9887100; DOI=10.1101/gad.13.1.64;
Bhattacharya S., Michels C.M., Leung M.K., Arany Z.P., Kung A.L.,
Livingston D.M.;
"Functional role of p35srj, a novel p300/CBP binding protein, during
transactivation by HIF-1.";
Genes Dev. 13:64-75(1999).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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]
FUNCTION.
PubMed=11581164; DOI=10.1101/gad.906301;
Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y.,
Kato S., Isselbacher K.J., Brown M., Shioda T.;
"Selective coactivation of estrogen-dependent transcription by CITED1
CBP/p300-binding protein.";
Genes Dev. 15:2598-2612(2001).
[7]
INTERACTION WITH TFAP2A; TFAP2B AND TFAP2C.
PubMed=11694877; DOI=10.1038/ng768;
Bamforth S.D., Braganca J., Eloranta J.J., Murdoch J.N., Marques F.I.,
Kranc K.R., Farza H., Henderson D.J., Hurst H.C., Bhattacharya S.;
"Cardiac malformations, adrenal agenesis, neural crest defects and
exencephaly in mice lacking Cited2, a new Tfap2 co-activator.";
Nat. Genet. 29:469-474(2001).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EP300; TFAP2A;
TFAP2B AND TFAP2C.
PubMed=12586840; DOI=10.1074/jbc.M208144200;
Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C.,
Bhattacharya S.;
"Physical and functional interactions among AP-2 transcription
factors, p300/CREB-binding protein, and CITED2.";
J. Biol. Chem. 278:16021-16029(2003).
[9]
FUNCTION, AND INTERACTION WITH PPARA.
PubMed=15051727; DOI=10.1074/jbc.M401489200;
Tien E.S., Davis J.W., Vanden Heuvel J.P.;
"Identification of the CREB-binding protein/p300-interacting protein
CITED2 as a peroxisome proliferator-activated receptor alpha
coregulator.";
J. Biol. Chem. 279:24053-24063(2004).
[10]
STRUCTURE BY NMR OF 216-259 IN COMPLEX WITH 323-423 OF EP300 AND ZINC
IONS, INTERACTION WITH EP300, AND MUTAGENESIS OF 243-LEU--LEU-246;
LEU-243 AND LEU-246.
PubMed=12778114; DOI=10.1038/nsb936;
Freedman S.J., Sun Z.Y., Kung A.L., France D.S., Wagner G., Eck M.J.;
"Structural basis for negative regulation of hypoxia-inducible factor-
1alpha by CITED2.";
Nat. Struct. Biol. 10:504-512(2003).
[11]
STRUCTURE BY NMR OF 220-269 IN COMPLEX WITH 340-439 OF CREBBP AND ZINC
IONS.
PubMed=14594809; DOI=10.1074/jbc.M310348200;
De Guzman R.N., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
"Interaction of the TAZ1 domain of the CREB-binding protein with the
activation domain of CITED2: regulation by competition between
intrinsically unstructured ligands for non-identical binding sites.";
J. Biol. Chem. 279:3042-3049(2004).
[12]
VARIANT VSD2 170-SER--GLY-178 DEL, VARIANTS ASD8
GLY-GLY-SER-SER-THR-PRO-GLY-GLY-SER-179 INS AND 198-SER-GLY-199 DEL,
CHARACTERIZATION OF VARIANT VSD2 170-SER--GLY-178 DEL, AND
CHARACTERIZATION OF VARIANTS ASD8
GLY-GLY-SER-SER-THR-PRO-GLY-GLY-SER-179 INS AND 198-SER-GLY-199 DEL.
PubMed=16287139; DOI=10.1002/humu.20262;
Sperling S., Grimm C.H., Dunkel I., Mebus S., Sperling H.P., Ebner A.,
Galli R., Lehrach H., Fusch C., Berger F., Hammer S.;
"Identification and functional analysis of CITED2 mutations in
patients with congenital heart defects.";
Hum. Mutat. 26:575-582(2005).
-!- FUNCTION: Transcriptional coactivator of the p300/CBP-mediated
transcription complex. Acts as a bridge, linking TFAP2
transcription factors and the p300/CBP transcriptional coactivator
complex in order to stimulate TFAP2-mediated transcriptional
activation. Positively regulates TGF-beta signaling through its
association with the SMAD/p300/CBP-mediated transcriptional
coactivator complex. Stimulates the peroxisome proliferator-
activated receptors PPARA transcriptional activity. Enhances
estrogen-dependent transactivation mediated by estrogen receptors.
Acts also as a transcriptional corepressor; interferes with the
binding of the transcription factors HIF1A or STAT2 and the
p300/CBP transcriptional coactivator complex. Participates in sex
determination and early gonad development by stimulating
transcription activation of SRY. Plays a role in controlling left-
right patterning during embryogenesis; potentiates transcriptional
activation of NODAL-mediated gene transcription in the left
lateral plate mesoderm (LPM). Plays an essential role in
differentiation of the adrenal cortex from the adrenogonadal
primordium (AGP); stimulates WT1-mediated transcription activation
thereby up-regulating the nuclear hormone receptor NR5A1 promoter
activity. Associates with chromatin to the PITX2 P1 promoter
region. {ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:12586840,
ECO:0000269|PubMed:15051727}.
-!- SUBUNIT: Interacts (via C-terminus) with SMAD2. Interacts (via C-
terminus) with SMAD3 (via MH2 domain). Interacts with LHX2 (via
LIM domains). Interacts with WT1 (By similarity). Interacts (via
C-terminus) with EP300 (via CH1 domain); the interaction is
stimulated in response to hypoxia. Interacts with PPARA. Interacts
(via C-terminus) with TFAP2A, TFAP2B and TFAP2C. {ECO:0000250,
ECO:0000269|PubMed:11694877, ECO:0000269|PubMed:12586840,
ECO:0000269|PubMed:12778114, ECO:0000269|PubMed:14594809,
ECO:0000269|PubMed:15051727, ECO:0000269|PubMed:9887100}.
-!- INTERACTION:
Q09472:EP300; NbExp=3; IntAct=EBI-937732, EBI-447295;
P41235:HNF4A; NbExp=3; IntAct=EBI-937732, EBI-1049011;
Q92754:TFAP2C; NbExp=2; IntAct=EBI-937732, EBI-937309;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12586840,
ECO:0000269|PubMed:8901575, ECO:0000269|PubMed:9887100}.
Note=Colocalizes with EP300 in dot-like structures.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99967-1; Sequence=Displayed;
Name=2;
IsoId=Q99967-2; Sequence=VSP_001089;
-!- INDUCTION: By hypoxia and deferoxamine.
{ECO:0000269|PubMed:9887100}.
-!- DISEASE: Ventricular septal defect 2 (VSD2) [MIM:614431]: A common
form of congenital cardiovascular anomaly that may occur alone or
in combination with other cardiac malformations. It can affect any
portion of the ventricular septum, resulting in abnormal
communications between the two lower chambers of the heart.
Classification is based on location of the communication, such as
perimembranous, inlet, outlet (infundibular), central muscular,
marginal muscular, or apical muscular defect. Large defects that
go unrepaired may give rise to cardiac enlargement, congestive
heart failure, pulmonary hypertension, Eisenmenger's syndrome,
delayed fetal brain development, arrhythmias, and even sudden
cardiac death. {ECO:0000269|PubMed:16287139}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Atrial septal defect 8 (ASD8) [MIM:614433]: A congenital
heart malformation characterized by incomplete closure of the wall
between the atria resulting in blood flow from the left to the
right atria. {ECO:0000269|PubMed:16287139}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the CITED family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CITED2ID40087ch6q24.html";
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EMBL; U65093; AAC51114.1; -; mRNA.
EMBL; AF129290; AAF01263.1; -; Genomic_DNA.
EMBL; AF129290; AAF01264.1; -; Genomic_DNA.
EMBL; AF109161; AAD10055.1; -; mRNA.
EMBL; AL592429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004377; AAH04377.1; -; mRNA.
CCDS; CCDS5195.1; -. [Q99967-1]
RefSeq; NP_001161860.1; NM_001168388.2. [Q99967-1]
RefSeq; NP_001161861.2; NM_001168389.2.
RefSeq; NP_006070.2; NM_006079.4. [Q99967-1]
UniGene; Hs.82071; -.
PDB; 1P4Q; NMR; -; A=216-259.
PDB; 1R8U; NMR; -; A=220-269.
PDBsum; 1P4Q; -.
PDBsum; 1R8U; -.
DisProt; DP00356; -.
ProteinModelPortal; Q99967; -.
SMR; Q99967; -.
BioGrid; 115649; 13.
IntAct; Q99967; 7.
MINT; MINT-112487; -.
STRING; 9606.ENSP00000356623; -.
iPTMnet; Q99967; -.
PhosphoSitePlus; Q99967; -.
BioMuta; CITED2; -.
DMDM; 21542403; -.
PaxDb; Q99967; -.
PeptideAtlas; Q99967; -.
PRIDE; Q99967; -.
DNASU; 10370; -.
Ensembl; ENST00000367651; ENSP00000356623; ENSG00000164442. [Q99967-1]
Ensembl; ENST00000536159; ENSP00000442831; ENSG00000164442. [Q99967-1]
Ensembl; ENST00000618718; ENSP00000479918; ENSG00000164442. [Q99967-2]
GeneID; 10370; -.
KEGG; hsa:10370; -.
UCSC; uc003qip.3; human. [Q99967-1]
CTD; 10370; -.
DisGeNET; 10370; -.
EuPathDB; HostDB:ENSG00000164442.9; -.
GeneCards; CITED2; -.
H-InvDB; HIX0006261; -.
HGNC; HGNC:1987; CITED2.
HPA; CAB016157; -.
HPA; CAB069879; -.
MalaCards; CITED2; -.
MIM; 602937; gene.
MIM; 614431; phenotype.
MIM; 614433; phenotype.
neXtProt; NX_Q99967; -.
OpenTargets; ENSG00000164442; -.
Orphanet; 99103; Atrial septal defect, ostium secundum type.
Orphanet; 99105; Atrial septal defect, sinus venosus type.
Orphanet; 99097; Single ventricular septal defect.
Orphanet; 101063; Situs inversus totalis.
Orphanet; 3303; Tetralogy of Fallot.
PharmGKB; PA26524; -.
eggNOG; ENOG410IH9P; Eukaryota.
eggNOG; ENOG410Y09Y; LUCA.
GeneTree; ENSGT00530000063624; -.
HOGENOM; HOG000231079; -.
HOVERGEN; HBG075182; -.
InParanoid; Q99967; -.
KO; K21361; -.
PhylomeDB; Q99967; -.
TreeFam; TF331915; -.
Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-HSA-8866906; TFAP2 (AP-2) family regulates transcription of other transcription factors.
Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
SIGNOR; Q99967; -.
ChiTaRS; CITED2; human.
EvolutionaryTrace; Q99967; -.
GeneWiki; CITED2; -.
GenomeRNAi; 10370; -.
PRO; PR:Q99967; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000164442; -.
CleanEx; HS_CITED2; -.
ExpressionAtlas; Q99967; baseline and differential.
Genevisible; Q99967; HS.
GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; IDA:BHF-UCL.
GO; GO:0050693; F:LBD domain binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IBA:GO_Central.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0035802; P:adrenal cortex formation; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0007368; P:determination of left/right symmetry; ISS:UniProtKB.
GO; GO:0060971; P:embryonic heart tube left/right pattern formation; ISS:BHF-UCL.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0070986; P:left/right axis specification; ISS:BHF-UCL.
GO; GO:0060972; P:left/right pattern formation; IBA:GO_Central.
GO; GO:0001889; P:liver development; ISS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1900164; P:nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry; ISS:BHF-UCL.
GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISS:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:2000020; P:positive regulation of male gonad development; ISS:UniProtKB.
GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0003156; P:regulation of animal organ formation; ISS:UniProtKB.
GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
GO; GO:0034405; P:response to fluid shear stress; IMP:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0007530; P:sex determination; ISS:UniProtKB.
GO; GO:0048536; P:spleen development; ISS:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
InterPro; IPR007576; CITED.
PANTHER; PTHR17045; PTHR17045; 1.
Pfam; PF04487; CITED; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Atrial septal defect;
Complete proteome; Developmental protein; Differentiation;
Disease mutation; Nucleus; Reference proteome; Repressor;
Stress response; Transcription; Transcription regulation.
CHAIN 1 270 Cbp/p300-interacting transactivator 2.
/FTId=PRO_0000144726.
COMPBIAS 21 57 His-rich.
COMPBIAS 162 199 Gly-rich.
COMPBIAS 219 258 Asp/Glu-rich (acidic).
VAR_SEQ 159 215 Missing (in isoform 2).
{ECO:0000303|PubMed:8901575}.
/FTId=VSP_001089.
VARIANT 170 178 Missing (in VSD2; reduces coactivation of
the TFAP2C gene to 50% of that obtained
with wild-type and represses HIF1A with
about 60% efficiency compared to wild-
type). {ECO:0000269|PubMed:16287139}.
/FTId=VAR_067583.
VARIANT 179 179 S -> GGSSTPGGS (in ASD8; demonstrates
only about 75% of the repressive activity
of wild-type).
/FTId=VAR_067584.
VARIANT 198 199 Missing (in ASD8; demonstrates only about
75% of the repressive activity of wild-
type). {ECO:0000269|PubMed:16287139}.
/FTId=VAR_067585.
MUTAGEN 243 246 Missing: Inhibits transactivation
activity. {ECO:0000269|PubMed:12778114}.
MUTAGEN 243 243 L->E: Inhibits transactivation activity;
when associated with E-246.
{ECO:0000269|PubMed:12778114}.
MUTAGEN 246 246 L->E: Inhibits transactivation activity;
when associated with E-243.
{ECO:0000269|PubMed:12778114}.
STRAND 221 223 {ECO:0000244|PDB:1P4Q}.
HELIX 227 235 {ECO:0000244|PDB:1P4Q}.
STRAND 237 239 {ECO:0000244|PDB:1P4Q}.
HELIX 251 253 {ECO:0000244|PDB:1R8U}.
HELIX 254 256 {ECO:0000244|PDB:1P4Q}.
HELIX 266 268 {ECO:0000244|PDB:1R8U}.
SEQUENCE 270 AA; 28497 MW; 45DDE3A9E2B4C472 CRC64;
MADHMMAMNH GRFPDGTNGL HHHPAHRMGM GQFPSPHHHQ QQQPQHAFNA LMGEHIHYGA
GNMNATSGIR HAMGPGTVNG GHPPSALAPA ARFNNSQFMG PPVASQGGSL PASMQLQKLN
NQYFNHHPYP HNHYMPDLHP AAGHQMNGTN QHFRDCNPKH SGGSSTPGGS GGSSTPGGSG
SSSGGGAGSS NSGGGSGSGN MPASVAHVPA AMLPPNVIDT DFIDEEVLMS LVIEMGLDRI
KELPELWLGQ NEFDFMTDFV CKQQPSRVSC


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BMRB-9219-R7 CITED1 (CBP p300-interacting transactivator 1) BMMSP-1 7mL
BMRB-9219-B1 CITED1 (CBP p300-interacting transactivator 1) BMMSP-1 0.5mL
BMRB-9219-B0 CITED1 (CBP p300-interacting transactivator 1) BMMSP-1 0.1mL
BMRB-9219-R1 CITED1 (CBP p300-interacting transactivator 1) BMMSP-1 1mL
CITE4_HUMAN ELISA Kit FOR Cbp per p300-interacting transactivator 4; organism: Human; gene name: CITED4 96T
CITE2_HUMAN ELISA Kit FOR Cbp per p300-interacting transactivator 2; organism: Human; gene name: CITED2 96T
CITE1_HUMAN ELISA Kit FOR Cbp per p300-interacting transactivator 1; organism: Human; gene name: CITED1 96T
CITE2_MOUSE ELISA Kit FOR Cbp per p300-interacting transactivator 2; organism: Mouse; gene name: Cited2 96T


 

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