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Histone-binding protein RBBP4 (Chromatin assembly factor 1 subunit C) (CAF-1 subunit C) (Chromatin assembly factor I p48 subunit) (CAF-I 48 kDa subunit) (CAF-I p48) (Nucleosome-remodeling factor subunit RBAP48) (Retinoblastoma-binding protein 4) (RBBP-4) (Retinoblastoma-binding protein p48)

 RBBP4_HUMAN             Reviewed;         425 AA.
Q09028; B2R6G9; B4DRH0; D3DPQ3; P31149; Q53H02; Q96BV9;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-DEC-2017, entry version 197.
RecName: Full=Histone-binding protein RBBP4;
AltName: Full=Chromatin assembly factor 1 subunit C;
Short=CAF-1 subunit C;
AltName: Full=Chromatin assembly factor I p48 subunit;
Short=CAF-I 48 kDa subunit;
Short=CAF-I p48;
AltName: Full=Nucleosome-remodeling factor subunit RBAP48;
AltName: Full=Retinoblastoma-binding protein 4;
Short=RBBP-4;
AltName: Full=Retinoblastoma-binding protein p48;
Name=RBBP4; Synonyms=RBAP48;
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 PROTEIN SEQUENCE OF
134-158 AND 254-271.
PubMed=8350924; DOI=10.1038/364648a0;
Qian Y.-W., Wang Y.-C.J., Hollingsworth R.E. Jr., Jones D., Ling N.,
Lee E.Y.-H.P.;
"A retinoblastoma-binding protein related to a negative regulator of
Ras in yeast.";
Nature 364:648-652(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Nielsen M.S., Rasmussen H.H., Celis J.E., Leffers H.;
"Molecular cloning and expression of two novel human cDNAs encoding
proteins containing WD-40 repeats and sharing similarity to yeast MSI1
a negative regulation of the RAS-cAMP pathway.";
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Brain;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
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).
[7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow, Brain, Eye, and Uterus;
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).
[9]
PROTEIN SEQUENCE OF 2-15 AND 297-304, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (FEB-2005) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 60-65; 144-160 AND 221-240.
TISSUE=Keratinocyte;
PubMed=1699755; DOI=10.1002/elps.1150110703;
Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M.,
Gesser B., Celis J.E., Vandekerckhove J.;
"Two-dimensional gel electrophoresis, protein electroblotting and
microsequencing: a direct link between proteins and genes.";
Electrophoresis 11:528-536(1990).
[11]
PROTEIN SEQUENCE OF 60-65; 144-160 AND 221-240.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[12]
PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE CAF-1 COMPLEX, AND
INTERACTION WITH HISTONE H4.
PubMed=8858152; DOI=10.1016/S0092-8674(00)81326-4;
Verreault A., Kaufman P.D., Kobayashi R., Stillman B.;
"Nucleosome assembly by a complex of CAF-1 and acetylated histones
H3/H4.";
Cell 87:95-104(1996).
[13]
PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
PubMed=9150135; DOI=10.1016/S0092-8674(00)80216-0;
Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.;
"Histone deacetylases and SAP18, a novel polypeptide, are components
of a human Sin3 complex.";
Cell 89:357-364(1997).
[14]
INTERACTION WITH RB1.
PubMed=7503932; DOI=10.1074/jbc.270.43.25507;
Qian Y.-W., Lee E.Y.-H.P.;
"Dual retinoblastoma-binding proteins with properties related to a
negative regulator of ras in yeast.";
J. Biol. Chem. 270:25507-25513(1995).
[15]
INTERACTION WITH HDAC1.
PubMed=8602529; DOI=10.1126/science.272.5260.408;
Taunton J., Hassig C.A., Schreiber S.L.;
"A mammalian histone deacetylase related to the yeast transcriptional
regulator Rpd3p.";
Science 272:408-411(1996).
[16]
IDENTIFICATION IN THE NURD COMPLEX.
PubMed=9790534; DOI=10.1016/S0092-8674(00)81758-4;
Zhang Y., LeRoy G., Seelig H.-P., Lane W.S., Reinberg D.;
"The dermatomyositis-specific autoantigen Mi2 is a component of a
complex containing histone deacetylase and nucleosome remodeling
activities.";
Cell 95:279-289(1998).
[17]
INTERACTION WITH HISTONE H4.
PubMed=9427644; DOI=10.1016/S0960-9822(98)70040-5;
Verreault A., Kaufman P.D., Kobayashi R., Stillman B.;
"Nucleosomal DNA regulates the core-histone-binding subunit of the
human Hat1 acetyltransferase.";
Curr. Biol. 8:96-108(1998).
[18]
IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
PubMed=9651585; DOI=10.1016/S1097-2765(00)80102-1;
Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P.,
Hampsey M., Reinberg D.;
"SAP30, a novel protein conserved between human and yeast, is a
component of a histone deacetylase complex.";
Mol. Cell 1:1021-1031(1998).
[19]
INTERACTION WITH HDAC1.
PubMed=9520398; DOI=10.1073/pnas.95.7.3519;
Hassig C.A., Tong J.K., Fleischer T.C., Owa T., Grable P.G.,
Ayer D.E., Schreiber S.L.;
"A role for histone deacetylase activity in HDAC1-mediated
transcriptional repression.";
Proc. Natl. Acad. Sci. U.S.A. 95:3519-3524(1998).
[20]
IDENTIFICATION IN THE NURD COMPLEX.
PubMed=10444591; DOI=10.1101/gad.13.15.1924;
Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A.,
Reinberg D.;
"Analysis of the NuRD subunits reveals a histone deacetylase core
complex and a connection with DNA methylation.";
Genes Dev. 13:1924-1935(1999).
[21]
INTERACTION WITH BRCA1.
PubMed=10220405; DOI=10.1073/pnas.96.9.4983;
Yarden R.I., Brody L.C.;
"BRCA1 interacts with components of the histone deacetylase complex.";
Proc. Natl. Acad. Sci. U.S.A. 96:4983-4988(1999).
[22]
INTERACTION WITH HDAC1 AND RB1.
PubMed=10734134; DOI=10.1074/jbc.275.13.9797;
Nicolas E., Morales V., Magnaghi-Jaulin L., Harel-Bellan A.,
Richard-Foy H., Trouche D.;
"RbAp48 belongs to the histone deacetylase complex that associates
with the retinoblastoma protein.";
J. Biol. Chem. 275:9797-9804(2000).
[23]
FUNCTION, AND INTERACTION WITH CREBBP.
PubMed=10866654; DOI=10.1128/MCB.20.14.4970-4978.2000;
Zhang Q., Vo N., Goodman R.H.;
"Histone binding protein RbAp48 interacts with a complex of CREB
binding protein and phosphorylated CREB.";
Mol. Cell. Biol. 20:4970-4978(2000).
[24]
INTERACTION WITH SPEN.
PubMed=11331609; DOI=10.1101/gad.871201;
Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C.,
Hon M., Evans R.M.;
"Sharp, an inducible cofactor that integrates nuclear receptor
repression and activation.";
Genes Dev. 15:1140-1151(2001).
[25]
IDENTIFICATION IN THE NURD COMPLEX.
PubMed=11102443; DOI=10.1074/jbc.M007372200;
Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
Howard B.H.;
"Stable histone deacetylase complexes distinguished by the presence of
SANT domain proteins CoREST/kiaa0071 and Mta-L1.";
J. Biol. Chem. 276:6817-6824(2001).
[26]
IDENTIFICATION IN A SIN3 HDAC COMPLEX.
PubMed=11118440; DOI=10.1074/jbc.M007664200;
Skowyra D., Zeremski M., Neznanov N., Li M., Choi Y., Uesugi M.,
Hauser C.A., Gu W., Gudkov A.V., Qin J.;
"Differential association of products of alternative transcripts of
the candidate tumor suppressor ING1 with the mSin3/HDAC1
transcriptional corepressor complex.";
J. Biol. Chem. 276:8734-8739(2001).
[27]
IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH EED; EZH2; RBBP7 AND
SUZ12, TRANSIENT INTERACTION WITH HDAC1, AND METHYLTRANSFERASE
ACTIVITY OF THE COMPLEX.
PubMed=12435631; DOI=10.1101/gad.1035902;
Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P.,
Reinberg D.;
"Histone methyltransferase activity associated with a human
multiprotein complex containing the Enhancer of Zeste protein.";
Genes Dev. 16:2893-2905(2002).
[28]
IDENTIFICATION IN MULTIPLE SIN3 HDAC COMPLEXES.
PubMed=11784859; DOI=10.1128/MCB.22.3.835-848.2002;
Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.;
"Role of the Sin3-histone deacetylase complex in growth regulation by
the candidate tumor suppressor p33(ING1).";
Mol. Cell. Biol. 22:835-848(2002).
[29]
IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH AEBP2; EED; EZH2 AND
SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
PubMed=12351676; DOI=10.1126/science.1076997;
Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P.,
Jones R.S., Zhang Y.;
"Role of histone H3 lysine 27 methylation in Polycomb-group
silencing.";
Science 298:1039-1043(2002).
[30]
IDENTIFICATION IN THE NURF COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=14609955; DOI=10.1093/emboj/cdg582;
Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J.,
Shiekhattar R.;
"Isolation of human NURF: a regulator of Engrailed gene expression.";
EMBO J. 22:6089-6100(2003).
[31]
INTERACTION WITH MTA1.
PubMed=12920132; DOI=10.1074/jbc.M302955200;
Yao Y.-L., Yang W.-M.;
"The metastasis-associated proteins 1 and 2 form distinct protein
complexes with histone deacetylase activity.";
J. Biol. Chem. 278:42560-42568(2003).
[32]
INTERACTION WITH MBD3L1.
PubMed=15456747; DOI=10.1074/jbc.M409149200;
Jiang C.-L., Jin S.-G., Pfeifer G.P.;
"MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-
binding protein 2 (MBD2) and components of the NuRD complex.";
J. Biol. Chem. 279:52456-52464(2004).
[33]
INTERACTION WITH MBD3L2.
PubMed=15701600; DOI=10.1074/jbc.M413492200;
Jin S.-G., Jiang C.-L., Rauch T., Li H., Pfeifer G.P.;
"MBD3L2 interacts with MBD3 and components of the NuRD complex and can
oppose MBD2-MeCP1-mediated methylation silencing.";
J. Biol. Chem. 280:12700-12709(2005).
[34]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=17671431; DOI=10.4161/cc.6.15.4512;
Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C.,
von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.;
"LINC, a human complex that is related to pRB-containing complexes in
invertebrates regulates the expression of G2/M genes.";
Cell Cycle 6:1903-1913(2007).
[35]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
"Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein
complex represses human cell cycle-dependent genes in quiescence.";
Mol. Cell 26:539-551(2007).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, 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).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND 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).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[40]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-355, 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).
[43]
INTERACTION WITH PHF6.
PubMed=24554700; DOI=10.1074/jbc.M113.535351;
Liu Z., Li F., Ruan K., Zhang J., Mei Y., Wu J., Shi Y.;
"Structural and functional insights into the human Borjeson-Forssman-
Lehmann syndrome-associated protein PHF6.";
J. Biol. Chem. 289:10069-10083(2014).
[44]
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).
[45]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-160, 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).
[46]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4 AND LYS-160, 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).
-!- FUNCTION: Core histone-binding subunit that may target chromatin
assembly factors, chromatin remodeling factors and histone
deacetylases to their histone substrates in a manner that is
regulated by nucleosomal DNA. Component of several complexes which
regulate chromatin metabolism. These include the chromatin
assembly factor 1 (CAF-1) complex, which is required for chromatin
assembly following DNA replication and DNA repair; the core
histone deacetylase (HDAC) complex, which promotes histone
deacetylation and consequent transcriptional repression; the
nucleosome remodeling and histone deacetylase complex (the NuRD
complex), which promotes transcriptional repression by histone
deacetylation and nucleosome remodeling; the PRC2/EED-EZH2
complex, which promotes repression of homeotic genes during
development; and the NURF (nucleosome remodeling factor) complex.
{ECO:0000269|PubMed:10866654}.
-!- SUBUNIT: Interacts with SUV39H1 and HDAC7 (By similarity). Binds
directly to helix 1 of the histone fold of histone H4, a region
that is not accessible when H4 is in chromatin. Subunit of the
chromatin assembly factor 1 (CAF-1) complex, which is composed of
RBBP4, CHAF1B and CHAF1A. Subunit of the core histone deacetylase
(HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4 and
RBBP7. The core HDAC complex associates with SIN3A, ARID4B/SAP180,
SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly ARID4A/RBP1 and
ING1 to form the SIN3 HDAC complex. The core HDAC complex may also
associate with MTA2, MBD3, CHD3 and CHD4 to form the nucleosome
remodeling and histone deacetylase complex (the NuRD complex). The
NuRD complex may also interact with MBD3L1 and MBD3L2. Interacts
with MTA1. Subunit of the PRC2/EED-EZH2 complex, which is composed
of at least EED, EZH2, RBBP4, RBBP7 and SUZ12. The PRC2/EED-EZH2
complex may also associate with HDAC1. Component of the PRC2/EED-
EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2.
Part of the nucleosome remodeling factor (NURF) complex which
consists of SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the
viral protein-binding domain of the retinoblastoma protein (RB1).
Interacts with SPEN/MINT. Interacts with BRCA1. Interacts with
CREBBP, and this interaction may be enhanced by the binding of
phosphorylated CREB1 to CREBBP. Component of the DREAM complex
(also named LINC complex) at least composed of E2F4, E2F5, LIN9,
LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and
TFDP2. The complex exists in quiescent cells where it represses
cell cycle-dependent genes. It dissociates in S phase when LIN9,
LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2.
Interacts with PHF6 (By similarity). Found in a complex composed
of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (By
similarity). {ECO:0000250|UniProtKB:Q60972,
ECO:0000269|PubMed:10220405, ECO:0000269|PubMed:10444591,
ECO:0000269|PubMed:10734134, ECO:0000269|PubMed:10866654,
ECO:0000269|PubMed:11102443, ECO:0000269|PubMed:11118440,
ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:11784859,
ECO:0000269|PubMed:12351676, ECO:0000269|PubMed:12435631,
ECO:0000269|PubMed:12920132, ECO:0000269|PubMed:14609955,
ECO:0000269|PubMed:15456747, ECO:0000269|PubMed:15701600,
ECO:0000269|PubMed:17531812, ECO:0000269|PubMed:17671431,
ECO:0000269|PubMed:24554700, ECO:0000269|PubMed:7503932,
ECO:0000269|PubMed:8602529, ECO:0000269|PubMed:8858152,
ECO:0000269|PubMed:9150135, ECO:0000269|PubMed:9427644,
ECO:0000269|PubMed:9520398, ECO:0000269|PubMed:9651585,
ECO:0000269|PubMed:9790534}.
-!- INTERACTION:
Q9BRL8:-; NbExp=3; IntAct=EBI-620823, EBI-10297046;
Q7L2E3:DHX30; NbExp=3; IntAct=EBI-620823, EBI-1211456;
O14929:HAT1; NbExp=3; IntAct=EBI-620823, EBI-2339359;
Q13547:HDAC1; NbExp=7; IntAct=EBI-620823, EBI-301834;
Q13330:MTA1; NbExp=8; IntAct=EBI-620823, EBI-714236;
Q9Y5X4:NR2E3; NbExp=2; IntAct=EBI-620823, EBI-7216962;
Q16576:RBBP7; NbExp=3; IntAct=EBI-620823, EBI-352227;
Q8IX07:ZFPM1; NbExp=4; IntAct=EBI-620823, EBI-3942619;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q09028-1; Sequence=Displayed;
Name=2;
IsoId=Q09028-2; Sequence=VSP_040088;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q09028-3; Sequence=VSP_040089;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q09028-4; Sequence=VSP_040087;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X74262; CAA52321.1; -; mRNA.
EMBL; X71810; CAA50685.1; -; mRNA.
EMBL; BT007309; AAP35973.1; -; mRNA.
EMBL; AK299251; BAG61282.1; -; mRNA.
EMBL; AK312571; BAG35466.1; -; mRNA.
EMBL; AK222779; BAD96499.1; -; mRNA.
EMBL; AC114489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07513.1; -; Genomic_DNA.
EMBL; CH471059; EAX07514.1; -; Genomic_DNA.
EMBL; BC003092; AAH03092.1; -; mRNA.
EMBL; BC015123; AAH15123.1; -; mRNA.
EMBL; BC053904; AAH53904.1; -; mRNA.
EMBL; BC075836; AAH75836.1; -; mRNA.
CCDS; CCDS366.1; -. [Q09028-1]
CCDS; CCDS44105.1; -. [Q09028-2]
CCDS; CCDS44106.1; -. [Q09028-4]
PIR; S36112; S36112.
RefSeq; NP_001128727.1; NM_001135255.1. [Q09028-2]
RefSeq; NP_001128728.1; NM_001135256.1. [Q09028-4]
RefSeq; NP_005601.1; NM_005610.2. [Q09028-1]
UniGene; Hs.16003; -.
PDB; 2XU7; X-ray; 1.90 A; A/B=1-425.
PDB; 3GFC; X-ray; 2.30 A; A=1-425.
PDB; 4PBY; X-ray; 2.50 A; A/B=1-425.
PDB; 4PBZ; X-ray; 2.15 A; A=1-425.
PDB; 4PC0; X-ray; 2.50 A; A/B=1-425.
PDB; 4R7A; X-ray; 1.85 A; B=1-425.
PDB; 5FXY; X-ray; 3.20 A; A/C/E/G=1-425.
PDBsum; 2XU7; -.
PDBsum; 3GFC; -.
PDBsum; 4PBY; -.
PDBsum; 4PBZ; -.
PDBsum; 4PC0; -.
PDBsum; 4R7A; -.
PDBsum; 5FXY; -.
ProteinModelPortal; Q09028; -.
SMR; Q09028; -.
BioGrid; 111863; 187.
CORUM; Q09028; -.
DIP; DIP-33495N; -.
IntAct; Q09028; 119.
MINT; MINT-90543; -.
STRING; 9606.ENSP00000362592; -.
BindingDB; Q09028; -.
ChEMBL; CHEMBL3137287; -.
iPTMnet; Q09028; -.
PhosphoSitePlus; Q09028; -.
SwissPalm; Q09028; -.
BioMuta; RBBP4; -.
DMDM; 1172846; -.
EPD; Q09028; -.
MaxQB; Q09028; -.
PaxDb; Q09028; -.
PeptideAtlas; Q09028; -.
PRIDE; Q09028; -.
DNASU; 5928; -.
Ensembl; ENST00000373485; ENSP00000362584; ENSG00000162521. [Q09028-3]
Ensembl; ENST00000373493; ENSP00000362592; ENSG00000162521. [Q09028-1]
Ensembl; ENST00000414241; ENSP00000398242; ENSG00000162521. [Q09028-2]
Ensembl; ENST00000458695; ENSP00000396057; ENSG00000162521. [Q09028-4]
GeneID; 5928; -.
KEGG; hsa:5928; -.
UCSC; uc001bvr.3; human. [Q09028-1]
CTD; 5928; -.
DisGeNET; 5928; -.
EuPathDB; HostDB:ENSG00000162521.18; -.
GeneCards; RBBP4; -.
HGNC; HGNC:9887; RBBP4.
HPA; CAB006264; -.
HPA; HPA060710; -.
HPA; HPA060724; -.
MIM; 602923; gene.
neXtProt; NX_Q09028; -.
OpenTargets; ENSG00000162521; -.
PharmGKB; PA34251; -.
eggNOG; KOG0264; Eukaryota.
eggNOG; ENOG410XNU9; LUCA.
GeneTree; ENSGT00570000079069; -.
HOVERGEN; HBG053236; -.
InParanoid; Q09028; -.
KO; K10752; -.
OMA; TNHLADF; -.
OrthoDB; EOG091G0A20; -.
PhylomeDB; Q09028; -.
TreeFam; TF106485; -.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-HSA-1538133; G0 and Early G1.
Reactome; R-HSA-156711; Polo-like kinase mediated events.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
SignaLink; Q09028; -.
SIGNOR; Q09028; -.
ChiTaRS; RBBP4; human.
EvolutionaryTrace; Q09028; -.
GeneWiki; RBBP4; -.
GenomeRNAi; 5928; -.
PRO; PR:Q09028; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162521; -.
CleanEx; HS_RBBP4; -.
ExpressionAtlas; Q09028; baseline and differential.
Genevisible; Q09028; HS.
GO; GO:0033186; C:CAF-1 complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
GO; GO:0016589; C:NURF complex; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0016580; C:Sin3 complex; NAS:BHF-UCL.
GO; GO:0042393; F:histone binding; NAS:BHF-UCL.
GO; GO:0004407; F:histone deacetylase activity; TAS:Reactome.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0034080; P:CENP-A containing nucleosome assembly; TAS:Reactome.
GO; GO:0031497; P:chromatin assembly; IDA:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; IDA:HGNC.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; IDA:UniProtKB.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0051726; P:regulation of cell cycle; TAS:Reactome.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR022052; Histone-bd_RBBP4_N.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12265; CAF1C_H4-bd; 1.
Pfam; PF00400; WD40; 5.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 3.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Chromatin regulator; Complete proteome; Direct protein sequencing;
DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.9}.
CHAIN 2 425 Histone-binding protein RBBP4.
/FTId=PRO_0000051186.
REPEAT 122 155 WD 1.
REPEAT 175 206 WD 2.
REPEAT 225 256 WD 3.
REPEAT 271 302 WD 4.
REPEAT 315 346 WD 5.
REPEAT 372 403 WD 6.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.9}.
MOD_RES 4 4 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 160 160 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q60972}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
CROSSLNK 160 160 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 35 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040087.
VAR_SEQ 7 7 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_040088.
VAR_SEQ 405 425 AENIYNDEDPEGSVDPEGQGS -> ELVLDH (in
isoform 3). {ECO:0000303|Ref.2}.
/FTId=VSP_040089.
CONFLICT 61 61 F -> G (in Ref. 8; AAH15123).
{ECO:0000305}.
TURN 12 14 {ECO:0000244|PDB:2XU7}.
HELIX 16 31 {ECO:0000244|PDB:4R7A}.
STRAND 32 39 {ECO:0000244|PDB:4R7A}.
STRAND 47 54 {ECO:0000244|PDB:4R7A}.
STRAND 60 69 {ECO:0000244|PDB:4R7A}.
STRAND 73 75 {ECO:0000244|PDB:4R7A}.
STRAND 77 87 {ECO:0000244|PDB:4R7A}.
HELIX 95 98 {ECO:0000244|PDB:4PBY}.
TURN 100 103 {ECO:0000244|PDB:4PC0}.
STRAND 115 125 {ECO:0000244|PDB:4R7A}.
STRAND 128 133 {ECO:0000244|PDB:4R7A}.
STRAND 136 143 {ECO:0000244|PDB:4R7A}.
STRAND 145 147 {ECO:0000244|PDB:4R7A}.
STRAND 149 153 {ECO:0000244|PDB:4R7A}.
HELIX 154 156 {ECO:0000244|PDB:4R7A}.
STRAND 170 174 {ECO:0000244|PDB:4R7A}.
STRAND 183 185 {ECO:0000244|PDB:4R7A}.
STRAND 187 189 {ECO:0000244|PDB:4R7A}.
STRAND 192 196 {ECO:0000244|PDB:4R7A}.
STRAND 202 206 {ECO:0000244|PDB:4R7A}.
HELIX 207 209 {ECO:0000244|PDB:3GFC}.
HELIX 211 213 {ECO:0000244|PDB:4PC0}.
STRAND 216 218 {ECO:0000244|PDB:4R7A}.
STRAND 220 223 {ECO:0000244|PDB:4R7A}.
STRAND 230 235 {ECO:0000244|PDB:4R7A}.
STRAND 242 247 {ECO:0000244|PDB:4R7A}.
STRAND 250 256 {ECO:0000244|PDB:4R7A}.
STRAND 262 264 {ECO:0000244|PDB:4R7A}.
STRAND 266 270 {ECO:0000244|PDB:4R7A}.
STRAND 276 281 {ECO:0000244|PDB:4R7A}.
STRAND 288 293 {ECO:0000244|PDB:4R7A}.
STRAND 296 302 {ECO:0000244|PDB:4R7A}.
STRAND 306 308 {ECO:0000244|PDB:5FXY}.
STRAND 310 314 {ECO:0000244|PDB:4R7A}.
STRAND 320 325 {ECO:0000244|PDB:4R7A}.
STRAND 332 337 {ECO:0000244|PDB:4R7A}.
STRAND 342 346 {ECO:0000244|PDB:4R7A}.
HELIX 347 349 {ECO:0000244|PDB:4R7A}.
HELIX 356 361 {ECO:0000244|PDB:4PBZ}.
STRAND 366 370 {ECO:0000244|PDB:4R7A}.
STRAND 377 382 {ECO:0000244|PDB:4R7A}.
STRAND 384 386 {ECO:0000244|PDB:4R7A}.
STRAND 389 394 {ECO:0000244|PDB:4R7A}.
STRAND 397 404 {ECO:0000244|PDB:4R7A}.
HELIX 406 409 {ECO:0000244|PDB:4R7A}.
SEQUENCE 425 AA; 47656 MW; B71E2D55A444C360 CRC64;
MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPEGKD
FSIHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS EKGEFGGFGS VSGKIEIEIK
INHEGEVNRA RYMPQNPCII ATKTPSSDVL VFDYTKHPSK PDPSGECNPD LRLRGHQKEG
YGLSWNPNLS GHLLSASDDH TICLWDISAV PKEGKVVDAK TIFTGHTAVV EDVSWHLLHE
SLFGSVADDQ KLMIWDTRSN NTSKPSHSVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL
WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI GEEQSPEDAE
DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ VWQMAENIYN DEDPEGSVDP
EGQGS


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EIAAB05137 CAF-1 subunit B,CAF1P60,CAF-I 60 kDa subunit,CAF-I p60,CHAF1B,Chicken,Chromatin assembly factor 1 subunit B,Chromatin assembly factor I p60 subunit,Gallus gallus,RCJMB04_5h12
EIAAB05136 Bos taurus,Bovine,CAF,CAF-1 subunit A,CAF1P150,CAF-I 150 kDa subunit,CAF-I p150,CHAF1A,Chromatin assembly factor 1 subunit A,Chromatin assembly factor I p150 subunit
EIAAB05134 CAF-1 subunit A,CAF-I 150 kDa subunit,CAF-I p150,CAIP150,CHAF1A,Chicken,Chromatin assembly factor 1 subunit A,Chromatin assembly factor I p150 subunit,Gallus gallus,RCJMB04_12f19
EIAAB46626 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Homo sapiens,Human,NSEP1,Nuclease-sensitive element-binding protein 1,YB1,YB-1,Y-box t
EIAAB46625 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Mouse,Msy1,Msy-1,Mus musculus,Nsep1,Nuclease-sensitive element-binding protein 1,Yb1,Y
EIAAB46627 Bos taurus,Bovine,CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,NSEP1,Nuclease-sensitive element-binding protein 1,YB1,YB-1,Y-box tr
EIAAB46624 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Msy-1,Nsep1,Nuclease-sensitive element-binding protein 1,Rat,Rattus norvegicus,Yb1,YB-
EIAAB27109 CAAT box DNA-binding protein subunit B,CBF-A,CCAAT-binding transcription factor subunit A,Nfyb,NF-YB,Nuclear transcription factor Y subunit B,Nuclear transcription factor Y subunit beta,Rat,Rattus nor
EIAAB27106 CAAT box DNA-binding protein subunit A,CBF-B,CCAAT-binding transcription factor subunit B,Nfya,NF-YA,Nuclear transcription factor Y subunit A,Nuclear transcription factor Y subunit alpha,Rat,Rattus no
EIAAB27113 CAAT box DNA-binding protein subunit C,CBF-C,CCAAT-binding transcription factor subunit C,Nfyc,NF-YC,Nuclear transcription factor Y subunit C,Nuclear transcription factor Y subunit gamma,Rat,Rattus no
EIAAB39003 Homo sapiens,Human,Proximal sequence element-binding transcription factor subunit alpha,PSE-binding factor subunit alpha,PTF subunit alpha,SNAP190,SNAPc 190 kDa subunit,SNAPc subunit 4,SNAPC4,snRNA-ac
EIAAB34352 A1 140 kDa subunit,Activator 1 140 kDa subunit,Activator 1 large subunit,Activator 1 subunit 1,DNA-binding protein PO-GA,Homo sapiens,Human,Replication factor C 140 kDa subunit,Replication factor C la
18-003-42521 Nuclease sensitive element-binding protein 1 - Y-box-binding protein 1; Y-box transcription factor; YB-1; CCAAT-binding transcription factor I subunit A; CBF-A; Enhancer factor I subunit A; EFI-A; DNA 0.05 mg Aff Pur


 

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