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Peregrin (Bromodomain and PHD finger-containing protein 1) (Protein Br140)

 BRPF1_HUMAN             Reviewed;        1214 AA.
P55201; B4DEZ6; Q7Z6E0; Q8TCM6; Q9UHI0;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
30-AUG-2017, entry version 163.
RecName: Full=Peregrin {ECO:0000305};
AltName: Full=Bromodomain and PHD finger-containing protein 1 {ECO:0000312|HGNC:HGNC:14255};
AltName: Full=Protein Br140 {ECO:0000303|PubMed:7906940};
Name=BRPF1 {ECO:0000312|HGNC:HGNC:14255};
Synonyms=BR140 {ECO:0000303|PubMed:7906940};
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), AND TISSUE SPECIFICITY.
PubMed=7906940; DOI=10.1006/bbrc.1994.1162;
Thompson K.A., Wang B., Argraves W.S., Giancotti F.G., Schranck D.P.,
Ruoslahti E.;
"BR140, a novel zinc-finger protein with homology to the TAF250
subunit of TFIID.";
Biochem. Biophys. Res. Commun. 198:1143-1152(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Hu S.N., Dong W., Zeng Y.X., Yu J., Yang H.M.;
"Sequencing and analyzing of BAC DNA on 3p26.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Eye;
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-462, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
FUNCTION, AND IDENTIFICATION IN THE MOZ/MORF COMPLEX.
PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
Lane W.S., Tan S., Yang X.-J., Cote J.;
"ING tumor suppressor proteins are critical regulators of chromatin
acetylation required for genome expression and perpetuation.";
Mol. Cell 21:51-64(2006).
[10]
FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH
ING5; MEAF6; KAT6A AND KAT6B, SUBCELLULAR LOCATION, AND ACETYLATION.
PubMed=18794358; DOI=10.1128/MCB.01297-08;
Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C.,
Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J.,
Yang X.-J.;
"Molecular architecture of quartet MOZ/MORF histone acetyltransferase
complexes.";
Mol. Cell. Biol. 28:6828-6843(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-1187, AND
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1076, 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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460; SER-462 AND
SER-1076, AND 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460; SER-462; SER-860
AND SER-1076, AND 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-462, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND 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).
[18]
STRUCTURE BY NMR OF 633-740.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the bromodomain of peregrin.";
Submitted (JUN-2006) to the PDB data bank.
[19]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1076-1205 IN COMPLEX WITH
HISTONE H3 PEPTIDE, AND INTERACTION WITH HISTONE H3.
PubMed=20400950; DOI=10.1038/nsmb.1797;
Vezzoli A., Bonadies N., Allen M.D., Freund S.M., Santiveri C.M.,
Kvinlaug B.T., Huntly B.J., Gottgens B., Bycroft M.;
"Molecular basis of histone H3K36me3 recognition by the PWWP domain of
Brpf1.";
Nat. Struct. Mol. Biol. 17:617-619(2010).
[20]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 1079-1207 IN COMPLEX WITH
TRIMETHYLATED HISTONE H3 PEPTIDE, AND INTERACTION WITH HISTONE H3.
PubMed=21720545; DOI=10.1371/journal.pone.0018919;
Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L.,
Qiu W., Wang Y., Min J.;
"Structural and histone binding ability characterizations of human
PWWP domains.";
PLoS ONE 6:E18919-E18919(2011).
[21]
INVOLVEMENT IN IDDDFP, VARIANTS IDDDFP SER-370; 455-ARG--ASP-1214 DEL;
833-GLY--ASP-1214 DEL AND 1100-PRO--ASP-1214 DEL, CHARACTERIZATION OF
VARIANTS IDDDFP SER-370; 455-ARG--ASP-1214 DEL; 833-GLY--ASP-1214 DEL
AND 1100-PRO--ASP-1214 DEL, FUNCTION, SUBUNIT, INTERACTION WITH KAT7,
AND SUBCELLULAR LOCATION.
PubMed=27939640; DOI=10.1016/j.ajhg.2016.11.011;
DDD Study;
CAUSES Study;
Yan K., Rousseau J., Littlejohn R.O., Kiss C., Lehman A.,
Rosenfeld J.A., Stumpel C.T., Stegmann A.P., Robak L., Scaglia F.,
Nguyen T.T., Fu H., Ajeawung N.F., Camurri M.V., Li L., Gardham A.,
Panis B., Almannai M., Sacoto M.J., Baskin B., Ruivenkamp C., Xia F.,
Bi W., Cho M.T., Potjer T.P., Santen G.W., Parker M.J., Canham N.,
McKinnon M., Potocki L., MacKenzie J.J., Roeder E.R., Campeau P.M.,
Yang X.J.;
"Mutations in the chromatin regulator gene BRPF1 cause syndromic
intellectual disability and deficient histone acetylation.";
Am. J. Hum. Genet. 100:91-104(2017).
[22]
INVOLVEMENT IN IDDDFP, AND VARIANTS IDDDFP 35-TYR--ASP-1214 DEL;
ARG-389 AND 988-LEU--ASP-1214 DEL.
PubMed=27939639; DOI=10.1016/j.ajhg.2016.11.010;
Mattioli F., Schaefer E., Magee A., Mark P., Mancini G.M.,
Dieterich K., Von Allmen G., Alders M., Coutton C.,
van Slegtenhorst M., Vieville G., Engelen M., Cobben J.M., Juusola J.,
Pujol A., Mandel J.L., Piton A.;
"Mutations in histone acetylase modifier BRPF1 cause an autosomal-
dominant form of intellectual disability with associated ptosis.";
Am. J. Hum. Genet. 100:105-116(2017).
-!- FUNCTION: Component of the MOZ/MORF complex which has a histone H3
acetyltransferase activity (PubMed:16387653, PubMed:27939640).
Preferentially mediates histone H3-K23 acetylation
(PubMed:27939640). Positively regulates the transcription of RUNX1
and RUNX2 (PubMed:18794358). {ECO:0000269|PubMed:16387653,
ECO:0000269|PubMed:18794358, ECO:0000269|PubMed:27939640}.
-!- SUBUNIT: Component of the MOZ/MORF complex composed at least of
ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3
(PubMed:16387653, PubMed:18794358, PubMed:27939640). Interacts
with trimethylated 'Lys-36' of histone H3 (H3K36me3)
(PubMed:20400950, PubMed:21720545). May interact with KAT7
(PubMed:27939640). {ECO:0000269|PubMed:16387653,
ECO:0000269|PubMed:18794358, ECO:0000269|PubMed:20400950,
ECO:0000269|PubMed:21720545, ECO:0000269|PubMed:27939640}.
-!- INTERACTION:
P0C0S8:HIST1H2AM; NbExp=8; IntAct=EBI-2837428, EBI-1390628;
P62805:HIST2H4B; NbExp=8; IntAct=EBI-2837428, EBI-302023;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18794358,
ECO:0000269|PubMed:27939640}. Cytoplasm
{ECO:0000269|PubMed:18794358, ECO:0000269|PubMed:27939640}.
Note=Localization to the nucleus depends on KAT6A, ING5 and MEAF6.
{ECO:0000269|PubMed:18794358, ECO:0000269|PubMed:27939640}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P55201-1; Sequence=Displayed;
Name=2;
IsoId=P55201-2; Sequence=VSP_037955;
Name=3;
IsoId=P55201-3; Sequence=VSP_037956;
Note=No experimental confirmation available.;
Name=4;
IsoId=P55201-4; Sequence=VSP_037957;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: High levels in testis.
{ECO:0000269|PubMed:7906940}.
-!- PTM: Acetylated by KAT6A. {ECO:0000269|PubMed:18794358}.
-!- DISEASE: Intellectual developmental disorder with dysmorphic
facies and ptosis (IDDDFP) [MIM:617333]: An autosomal dominant
neurodevelopmental disorder characterized by delayed psychomotor
development, intellectual disability, delayed language, and facial
dysmorphisms, most notably ptosis. Additional features may include
poor growth, hypotonia, and seizures.
{ECO:0000269|PubMed:27939639, ECO:0000269|PubMed:27939640}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
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EMBL; M91585; AAB02119.1; -; mRNA.
EMBL; AF176815; AAF19605.1; -; Genomic_DNA.
EMBL; AK293865; BAG57257.1; -; mRNA.
EMBL; AL713696; CAD28495.1; -; mRNA.
EMBL; AC022382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW63976.1; -; Genomic_DNA.
EMBL; BC053851; AAH53851.1; -; mRNA.
CCDS; CCDS2575.1; -. [P55201-1]
CCDS; CCDS33692.1; -. [P55201-2]
CCDS; CCDS82729.1; -. [P55201-4]
CCDS; CCDS82730.1; -. [P55201-3]
PIR; JC2069; JC2069.
RefSeq; NP_001003694.1; NM_001003694.1. [P55201-2]
RefSeq; NP_001305978.1; NM_001319049.1. [P55201-4]
RefSeq; NP_001305979.1; NM_001319050.1. [P55201-3]
RefSeq; NP_004625.2; NM_004634.2. [P55201-1]
UniGene; Hs.1004; -.
PDB; 2D9E; NMR; -; A=633-740.
PDB; 2RS9; NMR; -; B=633-740.
PDB; 2X35; X-ray; 2.00 A; A=1076-1205.
PDB; 2X4W; X-ray; 1.50 A; A=1076-1205.
PDB; 2X4X; X-ray; 1.85 A; A/C/E/G=1076-1205.
PDB; 2X4Y; X-ray; 1.70 A; A/C/E/G/I/K/M/O=1076-1205.
PDB; 3L42; X-ray; 1.30 A; A=1079-1207.
PDB; 3MO8; X-ray; 1.69 A; A=1079-1207.
PDB; 4LC2; X-ray; 1.65 A; A=626-740.
PDB; 4QYD; X-ray; 1.94 A; A=629-742.
PDB; 4QYL; X-ray; 1.80 A; A/B/C/D=629-742.
PDB; 4UYE; X-ray; 1.65 A; A/B=622-738.
PDB; 5C6S; X-ray; 1.30 A; A=1079-1207.
PDB; 5C7N; X-ray; 1.75 A; A=626-740.
PDB; 5C85; X-ray; 1.70 A; A=626-740.
PDB; 5C87; X-ray; 1.55 A; A=626-740.
PDB; 5C89; X-ray; 1.65 A; A=627-740.
PDB; 5D7X; X-ray; 1.35 A; A=626-740.
PDB; 5DY7; X-ray; 1.69 A; A=626-740.
PDB; 5DYA; X-ray; 1.65 A; A=626-740.
PDB; 5DYC; X-ray; 1.65 A; A=626-740.
PDB; 5E3D; X-ray; 1.71 A; A=626-740.
PDB; 5E3G; X-ray; 1.65 A; A=626-740.
PDB; 5EM3; X-ray; 1.40 A; A=626-740.
PDB; 5EPR; X-ray; 1.65 A; A=626-740.
PDB; 5EPS; X-ray; 1.47 A; A=627-740.
PDB; 5EQ1; X-ray; 1.55 A; A=626-740.
PDB; 5ERC; X-ray; 2.05 A; A=274-450.
PDB; 5ETB; X-ray; 1.33 A; A=626-740.
PDB; 5ETD; X-ray; 1.40 A; A=626-740.
PDB; 5EV9; X-ray; 1.45 A; A=626-740.
PDB; 5EVA; X-ray; 1.45 A; A=626-740.
PDB; 5EWC; X-ray; 1.75 A; A=626-740.
PDB; 5EWD; X-ray; 1.58 A; A=626-740.
PDB; 5EWH; X-ray; 1.63 A; A=626-740.
PDB; 5EWV; X-ray; 1.67 A; A=626-740.
PDB; 5EWW; X-ray; 1.73 A; A=626-740.
PDB; 5FFV; X-ray; 1.30 A; A/B=626-740.
PDB; 5FFW; X-ray; 1.50 A; A/B=626-740.
PDB; 5FFY; X-ray; 1.55 A; A=626-740.
PDB; 5FG4; X-ray; 1.65 A; A=626-740.
PDB; 5FG5; X-ray; 1.50 A; A/B=626-740.
PDB; 5G4R; X-ray; 1.96 A; A/B/C/D=622-738.
PDB; 5G4S; X-ray; 1.60 A; A=624-738.
PDB; 5T4U; X-ray; 1.50 A; A=627-740.
PDB; 5T4V; X-ray; 1.65 A; A=627-740.
PDBsum; 2D9E; -.
PDBsum; 2RS9; -.
PDBsum; 2X35; -.
PDBsum; 2X4W; -.
PDBsum; 2X4X; -.
PDBsum; 2X4Y; -.
PDBsum; 3L42; -.
PDBsum; 3MO8; -.
PDBsum; 4LC2; -.
PDBsum; 4QYD; -.
PDBsum; 4QYL; -.
PDBsum; 4UYE; -.
PDBsum; 5C6S; -.
PDBsum; 5C7N; -.
PDBsum; 5C85; -.
PDBsum; 5C87; -.
PDBsum; 5C89; -.
PDBsum; 5D7X; -.
PDBsum; 5DY7; -.
PDBsum; 5DYA; -.
PDBsum; 5DYC; -.
PDBsum; 5E3D; -.
PDBsum; 5E3G; -.
PDBsum; 5EM3; -.
PDBsum; 5EPR; -.
PDBsum; 5EPS; -.
PDBsum; 5EQ1; -.
PDBsum; 5ERC; -.
PDBsum; 5ETB; -.
PDBsum; 5ETD; -.
PDBsum; 5EV9; -.
PDBsum; 5EVA; -.
PDBsum; 5EWC; -.
PDBsum; 5EWD; -.
PDBsum; 5EWH; -.
PDBsum; 5EWV; -.
PDBsum; 5EWW; -.
PDBsum; 5FFV; -.
PDBsum; 5FFW; -.
PDBsum; 5FFY; -.
PDBsum; 5FG4; -.
PDBsum; 5FG5; -.
PDBsum; 5G4R; -.
PDBsum; 5G4S; -.
PDBsum; 5T4U; -.
PDBsum; 5T4V; -.
ProteinModelPortal; P55201; -.
SMR; P55201; -.
BioGrid; 113614; 25.
DIP; DIP-59001N; -.
IntAct; P55201; 26.
STRING; 9606.ENSP00000373340; -.
BindingDB; P55201; -.
ChEMBL; CHEMBL3132741; -.
GuidetoPHARMACOLOGY; 2730; -.
iPTMnet; P55201; -.
PhosphoSitePlus; P55201; -.
BioMuta; BRPF1; -.
DMDM; 116241271; -.
EPD; P55201; -.
MaxQB; P55201; -.
PaxDb; P55201; -.
PeptideAtlas; P55201; -.
PRIDE; P55201; -.
TopDownProteomics; P55201-2; -. [P55201-2]
Ensembl; ENST00000383829; ENSP00000373340; ENSG00000156983. [P55201-2]
Ensembl; ENST00000424362; ENSP00000398863; ENSG00000156983. [P55201-3]
Ensembl; ENST00000433861; ENSP00000402485; ENSG00000156983. [P55201-4]
Ensembl; ENST00000457855; ENSP00000410210; ENSG00000156983. [P55201-1]
GeneID; 7862; -.
KEGG; hsa:7862; -.
UCSC; uc003bsf.4; human. [P55201-1]
CTD; 7862; -.
DisGeNET; 7862; -.
GeneCards; BRPF1; -.
HGNC; HGNC:14255; BRPF1.
HPA; HPA003359; -.
MIM; 602410; gene.
MIM; 617333; phenotype.
neXtProt; NX_P55201; -.
OpenTargets; ENSG00000156983; -.
PharmGKB; PA25424; -.
eggNOG; KOG0955; Eukaryota.
eggNOG; COG5141; LUCA.
GeneTree; ENSGT00740000114866; -.
HOGENOM; HOG000000705; -.
HOVERGEN; HBG004895; -.
InParanoid; P55201; -.
KO; K11348; -.
OMA; PIPQEIF; -.
OrthoDB; EOG091G00VK; -.
PhylomeDB; P55201; -.
TreeFam; TF316118; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
ChiTaRS; BRPF1; human.
EvolutionaryTrace; P55201; -.
GenomeRNAi; 7862; -.
PRO; PR:P55201; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000156983; -.
CleanEx; HS_BRPF1; -.
ExpressionAtlas; P55201; baseline and differential.
Genevisible; P55201; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
GO; GO:0043972; P:histone H3-K23 acetylation; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd05839; BR140_related; 1.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR035502; BR140-rel_PWWD.
InterPro; IPR001487; Bromodomain.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR019542; Enhancer_polycomb-like_N.
InterPro; IPR034732; EPHD.
InterPro; IPR000313; PWWP_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF10513; EPL1; 1.
Pfam; PF00855; PWWP; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SMART; SM00249; PHD; 2.
SMART; SM00293; PWWP; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51805; EPHD; 1.
PROSITE; PS50812; PWWP; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Bromodomain; Chromatin regulator; Complete proteome; Cytoplasm;
Disease mutation; DNA-binding; Mental retardation; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 1214 Peregrin.
/FTId=PRO_0000211187.
DOMAIN 645 715 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 1085 1168 PWWP. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
ZN_FING 21 47 C2H2-type. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 273 323 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 327 360 C2HC pre-PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
ZN_FING 384 448 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
REGION 59 222 Interaction with KAT6A and KAT6B.
{ECO:0000269|PubMed:18794358}.
REGION 501 821 Interaction with MEAF6 and ING5.
{ECO:0000269|PubMed:18794358}.
REGION 543 1079 Required for RUNX1 and RUNX2
transcriptional activation.
MOD_RES 120 120 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 147 147 N6-acetyllysine.
{ECO:0000250|UniProtKB:B2RRD7}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 462 462 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 580 580 N6-acetyllysine.
{ECO:0000250|UniProtKB:B2RRD7}.
MOD_RES 858 858 Phosphothreonine.
{ECO:0000250|UniProtKB:B2RRD7}.
MOD_RES 860 860 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 917 917 Phosphoserine.
{ECO:0000250|UniProtKB:B2RRD7}.
MOD_RES 922 922 Phosphoserine.
{ECO:0000250|UniProtKB:B2RRD7}.
MOD_RES 926 926 Phosphoserine.
{ECO:0000250|UniProtKB:B2RRD7}.
MOD_RES 1076 1076 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1187 1187 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 660 660 S -> SEVTELD (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037955.
VAR_SEQ 765 765 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_037956.
VAR_SEQ 873 967 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037957.
VARIANT 35 1214 Missing (in IDDDFP).
{ECO:0000269|PubMed:27939639}.
/FTId=VAR_078076.
VARIANT 370 370 P -> S (in IDDDFP; decreased histone H3-
K23 acetylation; changed cytoplasmic
localization; no effect on expression and
assembly of the MOZ/MORF complex).
{ECO:0000269|PubMed:27939640}.
/FTId=VAR_078077.
VARIANT 389 389 C -> R (in IDDDFP).
{ECO:0000269|PubMed:27939639}.
/FTId=VAR_078078.
VARIANT 455 1214 Missing (in IDDDFP; decreased histone H3-
K23 acetylation; increased localization
to the nucleus; decreased expression and
assembly of the MOZ/MORF complex).
{ECO:0000269|PubMed:27939640}.
/FTId=VAR_078079.
VARIANT 833 1214 Missing (in IDDDFP; no effect on histone
H3-K23 acetylation; increased aggregation
in the cytoplasm; no effect on expression
and assembly of the MOZ/MORF complex).
{ECO:0000269|PubMed:27939640}.
/FTId=VAR_078080.
VARIANT 988 1214 Missing (in IDDDFP).
{ECO:0000269|PubMed:27939639}.
/FTId=VAR_078081.
VARIANT 1100 1214 Missing (in IDDDFP; no effect on histone
H3-K23 acetylation; no effect on
expression and assembly of the MOZ/MORF
complex). {ECO:0000269|PubMed:27939640}.
/FTId=VAR_078082.
VARIANT 1117 1117 G -> E (in dbSNP:rs1042294).
/FTId=VAR_028232.
VARIANT 1193 1193 H -> Q (in dbSNP:rs36081837).
/FTId=VAR_048430.
CONFLICT 5 5 F -> L (in Ref. 3; BAG57257).
{ECO:0000305}.
CONFLICT 299 299 A -> E (in Ref. 1; AAB02119).
{ECO:0000305}.
CONFLICT 306 306 G -> D (in Ref. 3; BAG57257).
{ECO:0000305}.
CONFLICT 341 341 K -> R (in Ref. 3; BAG57257).
{ECO:0000305}.
CONFLICT 729 729 L -> V (in Ref. 1; AAB02119).
{ECO:0000305}.
CONFLICT 1035 1035 F -> S (in Ref. 3; BAG57257).
{ECO:0000305}.
TURN 277 279 {ECO:0000244|PDB:5ERC}.
STRAND 286 288 {ECO:0000244|PDB:5ERC}.
STRAND 290 292 {ECO:0000244|PDB:5ERC}.
TURN 294 296 {ECO:0000244|PDB:5ERC}.
STRAND 299 301 {ECO:0000244|PDB:5ERC}.
HELIX 302 305 {ECO:0000244|PDB:5ERC}.
HELIX 318 321 {ECO:0000244|PDB:5ERC}.
STRAND 324 326 {ECO:0000244|PDB:5ERC}.
STRAND 340 343 {ECO:0000244|PDB:5ERC}.
STRAND 348 350 {ECO:0000244|PDB:5ERC}.
HELIX 351 356 {ECO:0000244|PDB:5ERC}.
STRAND 361 364 {ECO:0000244|PDB:5ERC}.
TURN 365 368 {ECO:0000244|PDB:5ERC}.
STRAND 369 372 {ECO:0000244|PDB:5ERC}.
HELIX 374 376 {ECO:0000244|PDB:5ERC}.
HELIX 380 383 {ECO:0000244|PDB:5ERC}.
TURN 387 389 {ECO:0000244|PDB:5ERC}.
STRAND 392 395 {ECO:0000244|PDB:5ERC}.
HELIX 411 416 {ECO:0000244|PDB:5ERC}.
STRAND 420 424 {ECO:0000244|PDB:5ERC}.
STRAND 439 443 {ECO:0000244|PDB:5ERC}.
HELIX 625 627 {ECO:0000244|PDB:5G4S}.
HELIX 630 646 {ECO:0000244|PDB:5FFV}.
STRAND 653 655 {ECO:0000244|PDB:5FFV}.
TURN 659 661 {ECO:0000244|PDB:5FFV}.
HELIX 665 668 {ECO:0000244|PDB:5FFV}.
HELIX 675 683 {ECO:0000244|PDB:5FFV}.
HELIX 690 707 {ECO:0000244|PDB:5FFV}.
STRAND 710 712 {ECO:0000244|PDB:5FFW}.
HELIX 713 736 {ECO:0000244|PDB:5FFV}.
STRAND 1081 1083 {ECO:0000244|PDB:3L42}.
STRAND 1088 1091 {ECO:0000244|PDB:3L42}.
STRAND 1099 1104 {ECO:0000244|PDB:3L42}.
STRAND 1113 1115 {ECO:0000244|PDB:3L42}.
STRAND 1118 1120 {ECO:0000244|PDB:3L42}.
HELIX 1125 1137 {ECO:0000244|PDB:3L42}.
STRAND 1138 1140 {ECO:0000244|PDB:3MO8}.
STRAND 1142 1149 {ECO:0000244|PDB:3L42}.
STRAND 1154 1158 {ECO:0000244|PDB:3L42}.
HELIX 1159 1161 {ECO:0000244|PDB:3L42}.
STRAND 1162 1167 {ECO:0000244|PDB:3L42}.
HELIX 1169 1176 {ECO:0000244|PDB:3L42}.
HELIX 1182 1202 {ECO:0000244|PDB:3L42}.
SEQUENCE 1214 AA; 137499 MW; 618F359F21F4CBF7 CRC64;
MGVDFDVKTF CHNLRATKPP YECPVETCRK VYKSYSGIEY HLYHYDHDNP PPPQQTPLRK
HKKKGRQSRP ANKQSPSPSE VSQSPGREVM SYAQAQRMVE VDLHGRVHRI SIFDNLDVVS
EDEEAPEEAP ENGSNKENTE TPAATPKSGK HKNKEKRKDS NHHHHHNVSA STTPKLPEVV
YRELEQDTPD APPRPTSYYR YIEKSAEELD EEVEYDMDEE DYIWLDIMNE RRKTEGVSPI
PQEIFEYLMD RLEKESYFES HNKGDPNALV DEDAVCCICN DGECQNSNVI LFCDMCNLAV
HQECYGVPYI PEGQWLCRRC LQSPSRAVDC ALCPNKGGAF KQTDDGRWAH VVCALWIPEV
CFANTVFLEP IDSIEHIPPA RWKLTCYICK QRGSGACIQC HKANCYTAFH VTCAQQAGLY
MKMEPVRETG ANGTSFSVRK TAYCDIHTPP GSARRLPALS HSEGEEDEDE EEDEGKGWSS
EKVKKAKAKS RIKMKKARKI LAEKRAAAPV VSVPCIPPHR LSKITNRLTI QRKSQFMQRL
HSYWTLKRQS RNGVPLLRRL QTHLQSQRNC DQVGRDSEDK NWALKEQLKS WQRLRHDLER
ARLLVELIRK REKLKRETIK VQQIAMEMQL TPFLILLRKT LEQLQEKDTG NIFSEPVPLS
EVPDYLDHIK KPMDFFTMKQ NLEAYRYLNF DDFEEDFNLI VSNCLKYNAK DTIFYRAAVR
LREQGGAVLR QARRQAEKMG IDFETGMHIP HSLAGDEATH HTEDAAEEER LVLLENQKHL
PVEEQLKLLL ERLDEVNASK QSVGRSRRAK MIKKEMTALR RKLAHQRETG RDGPERHGPS
SRGSLTPHPA ACDKDGQTDS AAEESSSQET SKGLGPNMSS TPAHEVGRRT SVLFSKKNPK
TAGPPKRPGR PPKNRESQMT PSHGGSPVGP PQLPIMSSLR QRKRGRSPRP SSSSDSDSDK
STEDPPMDLP ANGFSGGNQP VKKSFLVYRN DCSLPRSSSD SESSSSSSSS AASDRTSTTP
SKQGRGKPSF SRGTFPEDSS EDTSGTENEA YSVGTGRGVG HSMVRKSLGR GAGWLSEDED
SPLDALDLVW AKCRGYPSYP ALIIDPKMPR EGMFHHGVPI PVPPLEVLKL GEQMTQEARE
HLYLVLFFDN KRTWQWLPRT KLVPLGVNQD LDKEKMLEGR KSNIRKSVQI AYHRALQHRS
KVQGEQSSET SDSD


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