RBBP4_HUMAN
ID RBBP4_HUMAN Reviewed; 425 AA.
AC Q09028; B2R6G9; B4DRH0; D3DPQ3; P31149; Q53H02; Q96BV9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Histone-binding protein RBBP4;
DE AltName: Full=Chromatin assembly factor 1 subunit C;
DE Short=CAF-1 subunit C;
DE AltName: Full=Chromatin assembly factor I p48 subunit;
DE Short=CAF-I 48 kDa subunit;
DE Short=CAF-I p48;
DE AltName: Full=Nucleosome-remodeling factor subunit RBAP48;
DE AltName: Full=Retinoblastoma-binding protein 4;
DE Short=RBBP-4;
DE AltName: Full=Retinoblastoma-binding protein p48;
GN Name=RBBP4; Synonyms=RBAP48;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 134-158 AND
RP 254-271.
RX PubMed=8350924; DOI=10.1038/364648a0;
RA Qian Y.-W., Wang Y.-C.J., Hollingsworth R.E. Jr., Jones D., Ling N.,
RA Lee E.Y.-H.P.;
RT "A retinoblastoma-binding protein related to a negative regulator of Ras in
RT yeast.";
RL Nature 364:648-652(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Nielsen M.S., Rasmussen H.H., Celis J.E., Leffers H.;
RT "Molecular cloning and expression of two novel human cDNAs encoding
RT proteins containing WD-40 repeats and sharing similarity to yeast MSI1 a
RT negative regulation of the RAS-cAMP pathway.";
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Brain, Eye, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-15 AND 297-304, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (FEB-2005) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 60-65; 144-160 AND 221-240.
RC TISSUE=Keratinocyte;
RX PubMed=1699755; DOI=10.1002/elps.1150110703;
RA Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M.,
RA Gesser B., Celis J.E., Vandekerckhove J.;
RT "Two-dimensional gel electrophoresis, protein electroblotting and
RT microsequencing: a direct link between proteins and genes.";
RL Electrophoresis 11:528-536(1990).
RN [11]
RP PROTEIN SEQUENCE OF 60-65; 144-160 AND 221-240.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [12]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE CAF-1 COMPLEX, INTERACTION
RP WITH HISTONE H4, AND SUBCELLULAR LOCATION.
RX PubMed=8858152; DOI=10.1016/s0092-8674(00)81326-4;
RA Verreault A., Kaufman P.D., Kobayashi R., Stillman B.;
RT "Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4.";
RL Cell 87:95-104(1996).
RN [13]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
RX PubMed=9150135; DOI=10.1016/s0092-8674(00)80216-0;
RA Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.;
RT "Histone deacetylases and SAP18, a novel polypeptide, are components of a
RT human Sin3 complex.";
RL Cell 89:357-364(1997).
RN [14]
RP INTERACTION WITH RB1.
RX PubMed=7503932; DOI=10.1074/jbc.270.43.25507;
RA Qian Y.-W., Lee E.Y.-H.P.;
RT "Dual retinoblastoma-binding proteins with properties related to a negative
RT regulator of ras in yeast.";
RL J. Biol. Chem. 270:25507-25513(1995).
RN [15]
RP INTERACTION WITH HDAC1.
RX PubMed=8602529; DOI=10.1126/science.272.5260.408;
RA Taunton J., Hassig C.A., Schreiber S.L.;
RT "A mammalian histone deacetylase related to the yeast transcriptional
RT regulator Rpd3p.";
RL Science 272:408-411(1996).
RN [16]
RP IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=9790534; DOI=10.1016/s0092-8674(00)81758-4;
RA Zhang Y., LeRoy G., Seelig H.-P., Lane W.S., Reinberg D.;
RT "The dermatomyositis-specific autoantigen Mi2 is a component of a complex
RT containing histone deacetylase and nucleosome remodeling activities.";
RL Cell 95:279-289(1998).
RN [17]
RP INTERACTION WITH HISTONE H4.
RX PubMed=9427644; DOI=10.1016/s0960-9822(98)70040-5;
RA Verreault A., Kaufman P.D., Kobayashi R., Stillman B.;
RT "Nucleosomal DNA regulates the core-histone-binding subunit of the human
RT Hat1 acetyltransferase.";
RL Curr. Biol. 8:96-108(1998).
RN [18]
RP IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
RX PubMed=9651585; DOI=10.1016/s1097-2765(00)80102-1;
RA Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P.,
RA Hampsey M., Reinberg D.;
RT "SAP30, a novel protein conserved between human and yeast, is a component
RT of a histone deacetylase complex.";
RL Mol. Cell 1:1021-1031(1998).
RN [19]
RP INTERACTION WITH HDAC1.
RX PubMed=9520398; DOI=10.1073/pnas.95.7.3519;
RA Hassig C.A., Tong J.K., Fleischer T.C., Owa T., Grable P.G., Ayer D.E.,
RA Schreiber S.L.;
RT "A role for histone deacetylase activity in HDAC1-mediated transcriptional
RT repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3519-3524(1998).
RN [20]
RP IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=10444591; DOI=10.1101/gad.13.15.1924;
RA Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A., Reinberg D.;
RT "Analysis of the NuRD subunits reveals a histone deacetylase core complex
RT and a connection with DNA methylation.";
RL Genes Dev. 13:1924-1935(1999).
RN [21]
RP INTERACTION WITH BRCA1, AND SUBCELLULAR LOCATION.
RX PubMed=10220405; DOI=10.1073/pnas.96.9.4983;
RA Yarden R.I., Brody L.C.;
RT "BRCA1 interacts with components of the histone deacetylase complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4983-4988(1999).
RN [22]
RP INTERACTION WITH HDAC1 AND RB1.
RX PubMed=10734134; DOI=10.1074/jbc.275.13.9797;
RA Nicolas E., Morales V., Magnaghi-Jaulin L., Harel-Bellan A.,
RA Richard-Foy H., Trouche D.;
RT "RbAp48 belongs to the histone deacetylase complex that associates with the
RT retinoblastoma protein.";
RL J. Biol. Chem. 275:9797-9804(2000).
RN [23]
RP FUNCTION, INTERACTION WITH CREBBP, AND SUBCELLULAR LOCATION.
RX PubMed=10866654; DOI=10.1128/mcb.20.14.4970-4978.2000;
RA Zhang Q., Vo N., Goodman R.H.;
RT "Histone binding protein RbAp48 interacts with a complex of CREB binding
RT protein and phosphorylated CREB.";
RL Mol. Cell. Biol. 20:4970-4978(2000).
RN [24]
RP INTERACTION WITH SPEN.
RX PubMed=11331609; DOI=10.1101/gad.871201;
RA Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M.,
RA Evans R.M.;
RT "Sharp, an inducible cofactor that integrates nuclear receptor repression
RT and activation.";
RL Genes Dev. 15:1140-1151(2001).
RN [25]
RP IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=11102443; DOI=10.1074/jbc.m007372200;
RA Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
RA Howard B.H.;
RT "Stable histone deacetylase complexes distinguished by the presence of SANT
RT domain proteins CoREST/kiaa0071 and Mta-L1.";
RL J. Biol. Chem. 276:6817-6824(2001).
RN [26]
RP IDENTIFICATION IN A SIN3 HDAC COMPLEX.
RX PubMed=11118440; DOI=10.1074/jbc.m007664200;
RA Skowyra D., Zeremski M., Neznanov N., Li M., Choi Y., Uesugi M.,
RA Hauser C.A., Gu W., Gudkov A.V., Qin J.;
RT "Differential association of products of alternative transcripts of the
RT candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional
RT corepressor complex.";
RL J. Biol. Chem. 276:8734-8739(2001).
RN [27]
RP IDENTIFICATION IN THE PRC2/EZH2 COMPLEX WITH EED; EZH2; RBBP7 AND SUZ12,
RP TRANSIENT INTERACTION WITH HDAC1, AND METHYLTRANSFERASE ACTIVITY OF THE
RP COMPLEX.
RX PubMed=12435631; DOI=10.1101/gad.1035902;
RA Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D.;
RT "Histone methyltransferase activity associated with a human multiprotein
RT complex containing the Enhancer of Zeste protein.";
RL Genes Dev. 16:2893-2905(2002).
RN [28]
RP IDENTIFICATION IN MULTIPLE SIN3 HDAC COMPLEXES.
RX PubMed=11784859; DOI=10.1128/mcb.22.3.835-848.2002;
RA Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.;
RT "Role of the Sin3-histone deacetylase complex in growth regulation by the
RT candidate tumor suppressor p33(ING1).";
RL Mol. Cell. Biol. 22:835-848(2002).
RN [29]
RP INTERACTION WITH SMARCA5.
RX PubMed=12198550; DOI=10.1038/nature01024;
RA Hakimi M.-A., Bochar D.A., Schmiesing J.A., Dong Y., Barak O.G.,
RA Speicher D.W., Yokomori K., Shiekhattar R.;
RT "A chromatin remodelling complex that loads cohesin onto human
RT chromosomes.";
RL Nature 418:994-998(2002).
RN [30]
RP IDENTIFICATION IN THE PRC2/EZH2 COMPLEX WITH AEBP2; EED; EZH2 AND SUZ12,
RP AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
RX PubMed=12351676; DOI=10.1126/science.1076997;
RA Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P.,
RA Jones R.S., Zhang Y.;
RT "Role of histone H3 lysine 27 methylation in Polycomb-group silencing.";
RL Science 298:1039-1043(2002).
RN [31]
RP IDENTIFICATION IN THE NURF-1 COMPLEX, INTERACTION WITH SMARCA1, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14609955; DOI=10.1093/emboj/cdg582;
RA Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J.,
RA Shiekhattar R.;
RT "Isolation of human NURF: a regulator of Engrailed gene expression.";
RL EMBO J. 22:6089-6100(2003).
RN [32]
RP INTERACTION WITH MTA1.
RX PubMed=12920132; DOI=10.1074/jbc.m302955200;
RA Yao Y.-L., Yang W.-M.;
RT "The metastasis-associated proteins 1 and 2 form distinct protein complexes
RT with histone deacetylase activity.";
RL J. Biol. Chem. 278:42560-42568(2003).
RN [33]
RP IDENTIFICATION IN COMPLEXES WITH SMARCA1, AND INTERACTION WITH SMARCA1.
RX PubMed=15310751; DOI=10.1074/jbc.m406212200;
RA Barak O., Lazzaro M.A., Cooch N.S., Picketts D.J., Shiekhattar R.;
RT "A tissue-specific, naturally occurring human SNF2L variant inactivates
RT chromatin remodeling.";
RL J. Biol. Chem. 279:45130-45138(2004).
RN [34]
RP INTERACTION WITH MBD3L1.
RX PubMed=15456747; DOI=10.1074/jbc.m409149200;
RA Jiang C.-L., Jin S.-G., Pfeifer G.P.;
RT "MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-
RT binding protein 2 (MBD2) and components of the NuRD complex.";
RL J. Biol. Chem. 279:52456-52464(2004).
RN [35]
RP INTERACTION WITH MBD3L2.
RX PubMed=15701600; DOI=10.1074/jbc.m413492200;
RA Jin S.-G., Jiang C.-L., Rauch T., Li H., Pfeifer G.P.;
RT "MBD3L2 interacts with MBD3 and components of the NuRD complex and can
RT oppose MBD2-MeCP1-mediated methylation silencing.";
RL J. Biol. Chem. 280:12700-12709(2005).
RN [36]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17671431; DOI=10.4161/cc.6.15.4512;
RA Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B.,
RA Gagrica S., Haenel F., Brehm A., Gaubatz S.;
RT "LINC, a human complex that is related to pRB-containing complexes in
RT invertebrates regulates the expression of G2/M genes.";
RL Cell Cycle 6:1903-1913(2007).
RN [37]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
RA Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
RA Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
RT "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex
RT represses human cell cycle-dependent genes in quiescence.";
RL Mol. Cell 26:539-551(2007).
RN [38]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [40]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [41]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [42]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [43]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [44]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-355, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [45]
RP INTERACTION WITH PHF6.
RX PubMed=24554700; DOI=10.1074/jbc.m113.535351;
RA Liu Z., Li F., Ruan K., Zhang J., Mei Y., Wu J., Shi Y.;
RT "Structural and functional insights into the human Borjeson-Forssman-
RT Lehmann syndrome-associated protein PHF6.";
RL J. Biol. Chem. 289:10069-10083(2014).
RN [46]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [47]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-160, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [48]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [49]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4 AND LYS-160, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [50]
RP INTERACTION WITH ARMC12, MUTAGENESIS OF VAL-35, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=30026490; DOI=10.1038/s41467-018-05286-2;
RA Li D., Song H., Mei H., Fang E., Wang X., Yang F., Li H., Chen Y.,
RA Huang K., Zheng L., Tong Q.;
RT "Armadillo repeat containing 12 promotes neuroblastoma progression through
RT interaction with retinoblastoma binding protein 4.";
RL Nat. Commun. 9:2829-2829(2018).
RN [51] {ECO:0007744|PDB:5XXQ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 6-410 IN COMPLEX WITH ZNF827,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-43; SER-73; 126-GLU--ASN-128;
RP GLU-126; ASN-128; GLU-179; TYR-181; GLU-231; ASN-277 AND GLU-395.
RX PubMed=30045876; DOI=10.1042/bcj20180310;
RA Yang S.F., Sun A.A., Shi Y., Li F., Pickett H.A.;
RT "Structural and functional characterization of the RBBP4-ZNF827 interaction
RT and its role in NuRD recruitment to telomeres.";
RL Biochem. J. 475:2667-2679(2018).
RN [52] {ECO:0007744|PDB:5WAI, ECO:0007744|PDB:5WAK}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH SUZ12; AEBP2 AND
RP JARID2, FUNCTION, IDENTIFICATION IN THE PRC2 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29499137; DOI=10.1016/j.molcel.2018.01.039;
RA Chen S., Jiao L., Shubbar M., Yang X., Liu X.;
RT "Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for
RT Chromatin Binding.";
RL Mol. Cell 69:840-852.e5(2018).
RN [53] {ECO:0007744|PDB:6NQ3}
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) IN COMPLEX WITH SUZ12; PHF19 AND
RP JARID2, FUNCTION, AND IDENTIFICATION IN THE PRC2 COMPLEX.
RX PubMed=31959557; DOI=10.1016/j.molcel.2019.12.019;
RA Chen S., Jiao L., Liu X., Yang X., Liu X.;
RT "A Dimeric Structural Scaffold for PRC2-PCL Targeting to CpG Island
RT Chromatin.";
RL Mol. Cell 77:1265-1278.e7(2020).
CC -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC assembly factors, chromatin remodeling factors and histone deacetylases
CC to their histone substrates in a manner that is regulated by
CC nucleosomal DNA. Component of several complexes which regulate
CC chromatin metabolism. These include the chromatin assembly factor 1
CC (CAF-1) complex, which is required for chromatin assembly following DNA
CC replication and DNA repair; the core histone deacetylase (HDAC)
CC complex, which promotes histone deacetylation and consequent
CC transcriptional repression; the nucleosome remodeling and histone
CC deacetylase complex (the NuRD complex), which promotes transcriptional
CC repression by histone deacetylation and nucleosome remodeling; the PRC2
CC complex, which promotes repression of homeotic genes during
CC development; and the NURF (nucleosome remodeling factor) complex.
CC {ECO:0000269|PubMed:10866654, ECO:0000269|PubMed:29499137,
CC ECO:0000269|PubMed:31959557}.
CC -!- SUBUNIT: Interacts with SUV39H1 and HDAC7 (By similarity). Binds
CC directly to helix 1 of the histone fold of histone H4, a region that is
CC not accessible when H4 is in chromatin (PubMed:8858152,
CC PubMed:9427644). Subunit of the chromatin assembly factor 1 (CAF-1)
CC complex, which is composed of RBBP4, CHAF1B and CHAF1A
CC (PubMed:8858152). Subunit of the core histone deacetylase (HDAC)
CC complex, which is composed of HDAC1, HDAC2, RBBP4 and RBBP7
CC (PubMed:9150135). The core HDAC complex associates with SIN3A,
CC ARID4B/SAP180, SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly
CC ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex (PubMed:9150135,
CC PubMed:9651585, PubMed:11118440, PubMed:11784859). The core HDAC
CC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form the
CC nucleosome remodeling and histone deacetylase complex (the NuRD
CC complex) (PubMed:9790534, PubMed:10444591, PubMed:11102443). The NuRD
CC complex may also interact with MBD3L1 and MBD3L2 (PubMed:15456747,
CC PubMed:15701600). Interacts with MTA1 (PubMed:12920132). Component of
CC the PRC2 complex, which consists of the core subunits EED, EZH1 or
CC EZH2, SUZ12, and RBBP4, and various combinations of accessory subunits
CC including AEBP2, JARID2, PHF19, MTF2 and EPOP (PubMed:12435631,
CC PubMed:12351676, PubMed:29499137, PubMed:31959557). Forms a monomeric
CC PRC2.2 (class 2) complex consisting of at least SUZ12, RBBP4, AEBP2 and
CC JARID2 (PubMed:29499137). Forms a dimeric PRC2.1 (class 1, PRC-PCL)
CC complex consisting of at least SUZ12, RBBP4, and PHF19; PHF19
CC stabilizes the dimeric structure which enhances PRC2 interaction with
CC chromatin (PubMed:31959557). Component of the NURF-1 ISWI chromatin
CC remodeling complex (also called the nucleosome-remodeling factor (NURF)
CC complex) at least composed of SMARCA1 (isoform 2), BPTF, RBBP4 and
CC RBBP7 (PubMed:14609955, PubMed:15310751). Within the complex interacts
CC with isoform 2 of SMARCA1 (PubMed:14609955, PubMed:15310751). Component
CC of the BPFT-SMARCA1 complex at least composed of SMARCA1 (isoform 1),
CC BPFT, RBBP4 and RBBP7; the complex is catalytically inactive and does
CC not remodel chromatin (PubMed:15310751). Within the complex interacts
CC with isoform 1 of SMARCA1 (PubMed:15310751). Interacts with the ISWI
CC chromatin remodeling complex component SMARCA5; the interaction is
CC direct (PubMed:12198550). Interacts with the viral protein-binding
CC domain of the retinoblastoma protein (RB1) (PubMed:7503932,
CC PubMed:10734134). Interacts with SPEN/MINT (PubMed:11331609). Interacts
CC with BRCA1 (PubMed:10220405). Interacts with CREBBP, and this
CC interaction may be enhanced by the binding of phosphorylated CREB1 to
CC CREBBP (PubMed:10866654). Component of the DREAM complex (also named
CC LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52,
CC LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2
CC (PubMed:17671431, PubMed:17531812). The complex exists in quiescent
CC cells where it represses cell cycle-dependent genes (PubMed:17671431,
CC PubMed:17531812). It dissociates in S phase when LIN9, LIN37, LIN52 and
CC LIN54 form a subcomplex that binds to MYBL2 (PubMed:17671431,
CC PubMed:17531812). Interacts with PHF6 (PubMed:24554700). Found in a
CC complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT
CC and TET1 (By similarity). Interacts with ERCC6 (PubMed:26030138).
CC Interacts with ZNF827; the interaction is direct and recruits RBBP4 to
CC telomeres (PubMed:30045876). Interacts with ARMC12 (via ARM domains)
CC (PubMed:30026490). Interacts with PWWP2B (By similarity).
CC {ECO:0000250|UniProtKB:Q60972, ECO:0000269|PubMed:10220405,
CC ECO:0000269|PubMed:10444591, ECO:0000269|PubMed:10734134,
CC ECO:0000269|PubMed:10866654, ECO:0000269|PubMed:11102443,
CC ECO:0000269|PubMed:11118440, ECO:0000269|PubMed:11331609,
CC ECO:0000269|PubMed:11784859, ECO:0000269|PubMed:12198550,
CC ECO:0000269|PubMed:12351676, ECO:0000269|PubMed:12435631,
CC ECO:0000269|PubMed:12920132, ECO:0000269|PubMed:14609955,
CC ECO:0000269|PubMed:15310751, ECO:0000269|PubMed:15456747,
CC ECO:0000269|PubMed:15701600, ECO:0000269|PubMed:17531812,
CC ECO:0000269|PubMed:17671431, ECO:0000269|PubMed:24554700,
CC ECO:0000269|PubMed:26030138, ECO:0000269|PubMed:29499137,
CC ECO:0000269|PubMed:30026490, ECO:0000269|PubMed:30045876,
CC ECO:0000269|PubMed:31959557, ECO:0000269|PubMed:7503932,
CC ECO:0000269|PubMed:8858152, ECO:0000269|PubMed:9150135,
CC ECO:0000269|PubMed:9427644, ECO:0000269|PubMed:9651585,
CC ECO:0000269|PubMed:9790534}.
CC -!- INTERACTION:
CC Q09028; P02768-3: ALB; NbExp=3; IntAct=EBI-620823, EBI-25830928;
CC Q09028; P30038: ALDH4A1; NbExp=3; IntAct=EBI-620823, EBI-3926971;
CC Q09028; P54253: ATXN1; NbExp=3; IntAct=EBI-620823, EBI-930964;
CC Q09028; O95817: BAG3; NbExp=3; IntAct=EBI-620823, EBI-747185;
CC Q09028; P55212: CASP6; NbExp=3; IntAct=EBI-620823, EBI-718729;
CC Q09028; P36544: CHRNA7; NbExp=3; IntAct=EBI-620823, EBI-79333;
CC Q09028; O94985-2: CLSTN1; NbExp=3; IntAct=EBI-620823, EBI-16041593;
CC Q09028; P21333-2: FLNA; NbExp=3; IntAct=EBI-620823, EBI-9641086;
CC Q09028; O14929: HAT1; NbExp=4; IntAct=EBI-620823, EBI-2339359;
CC Q09028; Q13547: HDAC1; NbExp=8; IntAct=EBI-620823, EBI-301834;
CC Q09028; O00291: HIP1; NbExp=3; IntAct=EBI-620823, EBI-473886;
CC Q09028; P13473-2: LAMP2; NbExp=3; IntAct=EBI-620823, EBI-21591415;
CC Q09028; Q03112: MECOM; NbExp=4; IntAct=EBI-620823, EBI-1384862;
CC Q09028; Q13330: MTA1; NbExp=10; IntAct=EBI-620823, EBI-714236;
CC Q09028; P07237: P4HB; NbExp=3; IntAct=EBI-620823, EBI-395883;
CC Q09028; P60201-2: PLP1; NbExp=3; IntAct=EBI-620823, EBI-12188331;
CC Q09028; Q9HAZ2: PRDM16; NbExp=3; IntAct=EBI-620823, EBI-2795620;
CC Q09028; P62826: RAN; NbExp=3; IntAct=EBI-620823, EBI-286642;
CC Q09028; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-620823, EBI-2623095;
CC Q09028; P00441: SOD1; NbExp=3; IntAct=EBI-620823, EBI-990792;
CC Q09028; P51692: STAT5B; NbExp=3; IntAct=EBI-620823, EBI-1186119;
CC Q09028; P31948: STIP1; NbExp=3; IntAct=EBI-620823, EBI-1054052;
CC Q09028; Q13148: TARDBP; NbExp=6; IntAct=EBI-620823, EBI-372899;
CC Q09028; Q8IX07: ZFPM1; NbExp=4; IntAct=EBI-620823, EBI-3942619;
CC Q09028; Q9BRL8; NbExp=3; IntAct=EBI-620823, EBI-10297046;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10220405,
CC ECO:0000269|PubMed:10866654, ECO:0000269|PubMed:14609955,
CC ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:30026490,
CC ECO:0000269|PubMed:8858152}. Chromosome, telomere
CC {ECO:0000269|PubMed:30045876}. Note=Localizes to chromatin as part of
CC the PRC2 complex. {ECO:0000269|PubMed:29499137}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q09028-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q09028-2; Sequence=VSP_040088;
CC Name=3;
CC IsoId=Q09028-3; Sequence=VSP_040089;
CC Name=4;
CC IsoId=Q09028-4; Sequence=VSP_040087;
CC -!- TISSUE SPECIFICITY: Expressed in neuroblastoma cells.
CC {ECO:0000269|PubMed:30026490}.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
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DR EMBL; X74262; CAA52321.1; -; mRNA.
DR EMBL; X71810; CAA50685.1; -; mRNA.
DR EMBL; BT007309; AAP35973.1; -; mRNA.
DR EMBL; AK299251; BAG61282.1; -; mRNA.
DR EMBL; AK312571; BAG35466.1; -; mRNA.
DR EMBL; AK222779; BAD96499.1; -; mRNA.
DR EMBL; AC114489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07513.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07514.1; -; Genomic_DNA.
DR EMBL; BC003092; AAH03092.1; -; mRNA.
DR EMBL; BC015123; AAH15123.1; -; mRNA.
DR EMBL; BC053904; AAH53904.1; -; mRNA.
DR EMBL; BC075836; AAH75836.1; -; mRNA.
DR CCDS; CCDS366.1; -. [Q09028-1]
DR CCDS; CCDS44105.1; -. [Q09028-2]
DR CCDS; CCDS44106.1; -. [Q09028-4]
DR PIR; S36112; S36112.
DR RefSeq; NP_001128727.1; NM_001135255.1. [Q09028-2]
DR RefSeq; NP_001128728.1; NM_001135256.1. [Q09028-4]
DR RefSeq; NP_005601.1; NM_005610.2. [Q09028-1]
DR PDB; 2XU7; X-ray; 1.90 A; A/B=1-425.
DR PDB; 3GFC; X-ray; 2.30 A; A=1-425.
DR PDB; 4PBY; X-ray; 2.50 A; A/B=1-425.
DR PDB; 4PBZ; X-ray; 2.15 A; A=1-425.
DR PDB; 4PC0; X-ray; 2.50 A; A/B=1-425.
DR PDB; 4R7A; X-ray; 1.85 A; B=1-425.
DR PDB; 5FXY; X-ray; 3.20 A; A/C/E/G=1-425.
DR PDB; 5VTB; X-ray; 2.40 A; A=1-425.
DR PDB; 5WAI; X-ray; 2.90 A; A/E=1-425.
DR PDB; 5WAK; X-ray; 3.20 A; A=1-425.
DR PDB; 5XWR; X-ray; 2.69 A; A/B=1-425.
DR PDB; 5XXQ; X-ray; 1.90 A; A/B=1-425.
DR PDB; 5Y1U; X-ray; 2.14 A; A/B=1-425.
DR PDB; 6BW3; X-ray; 2.20 A; A/C=1-425.
DR PDB; 6BW4; X-ray; 2.00 A; A/C=1-425.
DR PDB; 6C23; EM; 3.90 A; N=1-425.
DR PDB; 6C24; EM; 3.50 A; N=1-425.
DR PDB; 6G16; X-ray; 2.80 A; A/C/E/G=1-425.
DR PDB; 6NQ3; X-ray; 2.89 A; A/E=1-425.
DR PDB; 6WKR; EM; 3.50 A; N=1-425.
DR PDB; 6ZRC; X-ray; 2.60 A; A/B=1-425.
DR PDB; 6ZRD; X-ray; 2.50 A; A/B=1-425.
DR PDB; 7AOA; EM; 19.40 A; F/G=1-425.
DR PDB; 7KSO; EM; 3.90 A; D=1-425.
DR PDB; 7KSR; EM; 4.10 A; D=1-425.
DR PDB; 7KTP; EM; 4.80 A; D=1-425.
DR PDB; 7M40; X-ray; 1.88 A; A/B=1-425.
DR PDB; 7N40; X-ray; 2.55 A; A=1-425.
DR PDBsum; 2XU7; -.
DR PDBsum; 3GFC; -.
DR PDBsum; 4PBY; -.
DR PDBsum; 4PBZ; -.
DR PDBsum; 4PC0; -.
DR PDBsum; 4R7A; -.
DR PDBsum; 5FXY; -.
DR PDBsum; 5VTB; -.
DR PDBsum; 5WAI; -.
DR PDBsum; 5WAK; -.
DR PDBsum; 5XWR; -.
DR PDBsum; 5XXQ; -.
DR PDBsum; 5Y1U; -.
DR PDBsum; 6BW3; -.
DR PDBsum; 6BW4; -.
DR PDBsum; 6C23; -.
DR PDBsum; 6C24; -.
DR PDBsum; 6G16; -.
DR PDBsum; 6NQ3; -.
DR PDBsum; 6WKR; -.
DR PDBsum; 6ZRC; -.
DR PDBsum; 6ZRD; -.
DR PDBsum; 7AOA; -.
DR PDBsum; 7KSO; -.
DR PDBsum; 7KSR; -.
DR PDBsum; 7KTP; -.
DR PDBsum; 7M40; -.
DR PDBsum; 7N40; -.
DR AlphaFoldDB; Q09028; -.
DR SMR; Q09028; -.
DR BioGRID; 111863; 384.
DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-569; Chromatin assembly factor 1 complex.
DR ComplexPortal; CPX-688; NuRF chromatin remodeling complex.
DR ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q09028; -.
DR DIP; DIP-33495N; -.
DR IntAct; Q09028; 174.
DR MINT; Q09028; -.
DR STRING; 9606.ENSP00000362592; -.
DR BindingDB; Q09028; -.
DR ChEMBL; CHEMBL3137287; -.
DR ChEMBL; CHEMBL3301388; -.
DR GlyGen; Q09028; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q09028; -.
DR PhosphoSitePlus; Q09028; -.
DR SwissPalm; Q09028; -.
DR BioMuta; RBBP4; -.
DR DMDM; 1172846; -.
DR EPD; Q09028; -.
DR jPOST; Q09028; -.
DR MassIVE; Q09028; -.
DR MaxQB; Q09028; -.
DR PaxDb; Q09028; -.
DR PeptideAtlas; Q09028; -.
DR PRIDE; Q09028; -.
DR ProteomicsDB; 58712; -. [Q09028-1]
DR ProteomicsDB; 58713; -. [Q09028-2]
DR ProteomicsDB; 58714; -. [Q09028-3]
DR ProteomicsDB; 58715; -. [Q09028-4]
DR Antibodypedia; 3343; 494 antibodies from 38 providers.
DR DNASU; 5928; -.
DR Ensembl; ENST00000373485.5; ENSP00000362584.1; ENSG00000162521.19. [Q09028-3]
DR Ensembl; ENST00000373493.10; ENSP00000362592.4; ENSG00000162521.19. [Q09028-1]
DR Ensembl; ENST00000414241.7; ENSP00000398242.3; ENSG00000162521.19. [Q09028-2]
DR Ensembl; ENST00000458695.6; ENSP00000396057.2; ENSG00000162521.19. [Q09028-4]
DR GeneID; 5928; -.
DR KEGG; hsa:5928; -.
DR MANE-Select; ENST00000373493.10; ENSP00000362592.4; NM_005610.3; NP_005601.1.
DR UCSC; uc001bvr.3; human. [Q09028-1]
DR CTD; 5928; -.
DR DisGeNET; 5928; -.
DR GeneCards; RBBP4; -.
DR HGNC; HGNC:9887; RBBP4.
DR HPA; ENSG00000162521; Low tissue specificity.
DR MIM; 602923; gene.
DR neXtProt; NX_Q09028; -.
DR OpenTargets; ENSG00000162521; -.
DR PharmGKB; PA34251; -.
DR VEuPathDB; HostDB:ENSG00000162521; -.
DR eggNOG; KOG0264; Eukaryota.
DR GeneTree; ENSGT00940000153375; -.
DR HOGENOM; CLU_020445_3_1_1; -.
DR InParanoid; Q09028; -.
DR OMA; PHEEGCL; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; Q09028; -.
DR TreeFam; TF106485; -.
DR PathwayCommons; Q09028; -.
DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
DR Reactome; R-HSA-1538133; G0 and Early G1.
DR Reactome; R-HSA-156711; Polo-like kinase mediated events.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9710421; Defective pyroptosis.
DR SignaLink; Q09028; -.
DR SIGNOR; Q09028; -.
DR BioGRID-ORCS; 5928; 749 hits in 1100 CRISPR screens.
DR ChiTaRS; RBBP4; human.
DR EvolutionaryTrace; Q09028; -.
DR GeneWiki; RBBP4; -.
DR GenomeRNAi; 5928; -.
DR Pharos; Q09028; Tbio.
DR PRO; PR:Q09028; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q09028; protein.
DR Bgee; ENSG00000162521; Expressed in ganglionic eminence and 189 other tissues.
DR ExpressionAtlas; Q09028; baseline and differential.
DR Genevisible; Q09028; HS.
DR GO; GO:1904949; C:ATPase complex; IDA:ComplexPortal.
DR GO; GO:0033186; C:CAF-1 complex; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
DR GO; GO:0016589; C:NURF complex; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; NAS:BHF-UCL.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IC:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031497; P:chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:HGNC-UCL.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 1.
DR IDEAL; IID00317; -.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle;
KW Chromatin regulator; Chromosome; Direct protein sequencing;
KW DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Telomere; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..425
FT /note="Histone-binding protein RBBP4"
FT /id="PRO_0000051186"
FT REPEAT 122..155
FT /note="WD 1"
FT REPEAT 175..206
FT /note="WD 2"
FT REPEAT 225..256
FT /note="WD 3"
FT REPEAT 271..302
FT /note="WD 4"
FT REPEAT 315..346
FT /note="WD 5"
FT REPEAT 372..403
FT /note="WD 6"
FT REGION 2..132
FT /note="Interaction with ARMC12"
FT /evidence="ECO:0000269|PubMed:30026490"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 160
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60972"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040087"
FT VAR_SEQ 7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_040088"
FT VAR_SEQ 405..425
FT /note="AENIYNDEDPEGSVDPEGQGS -> ELVLDH (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040089"
FT MUTAGEN 35
FT /note="V->A: Loss of interaction with ARMC12."
FT /evidence="ECO:0000269|PubMed:30026490"
FT MUTAGEN 43
FT /note="P->A: Loss of interaction with ZNF827 and loss of
FT localization to telomeres; when associated with A-73."
FT /evidence="ECO:0000269|PubMed:30045876"
FT MUTAGEN 73
FT /note="S->A: Loss of interaction with ZNF827 and loss of
FT localization to telomeres; when associated with A-43."
FT /evidence="ECO:0000269|PubMed:30045876"
FT MUTAGEN 126..128
FT /note="EVN->AVA: Loss of interaction with ZNF827."
FT /evidence="ECO:0000305|PubMed:30045876"
FT MUTAGEN 126
FT /note="E->A: Loss of interaction with ZNF827 and loss of
FT localization to telomeres; when associated with A-128 and
FT A-179."
FT /evidence="ECO:0000269|PubMed:30045876"
FT MUTAGEN 128
FT /note="N->A: Loss of interaction with ZNF827 and loss of
FT localization to telomeres; when associated with A-126 and
FT A-179."
FT /evidence="ECO:0000269|PubMed:30045876"
FT MUTAGEN 179
FT /note="E->A: Loss of interaction with ZNF827 and loss of
FT localization to telomeres; when associated with A-126 and
FT A-128."
FT /evidence="ECO:0000269|PubMed:30045876"
FT MUTAGEN 181
FT /note="Y->A: Loss of interaction with ZNF827 and loss of
FT localization to telomeres."
FT /evidence="ECO:0000269|PubMed:30045876"
FT MUTAGEN 231
FT /note="E->A: Decreased interaction with ZNF827; when
FT associated with A-277."
FT /evidence="ECO:0000305|PubMed:30045876"
FT MUTAGEN 277
FT /note="N->A: Decreased interaction with ZNF827; when
FT associated with A-231."
FT /evidence="ECO:0000305|PubMed:30045876"
FT MUTAGEN 395
FT /note="E->A: Decreased interaction with ZNF827."
FT /evidence="ECO:0000305|PubMed:30045876"
FT CONFLICT 61
FT /note="F -> G (in Ref. 8; AAH15123)"
FT /evidence="ECO:0000305"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:5Y1U"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:2XU7"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:7M40"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:7M40"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:4PC0"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7M40"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6G16"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4R7A"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6ZRD"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:7M40"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:5XXQ"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:6WKR"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:4R7A"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:5Y1U"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:5FXY"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:4R7A"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:4R7A"
FT HELIX 356..360
FT /evidence="ECO:0007829|PDB:5XXQ"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:4R7A"
FT STRAND 397..404
FT /evidence="ECO:0007829|PDB:4R7A"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:4R7A"
SQ 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
