Full text data of RBBP7
RBBP7
(RBAP46)
[Confidence: low (only semi-automatic identification from reviews)]
Histone-binding protein RBBP7 (Histone acetyltransferase type B subunit 2; Nucleosome-remodeling factor subunit RBAP46; Retinoblastoma-binding protein 7; RBBP-7; Retinoblastoma-binding protein p46)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Histone-binding protein RBBP7 (Histone acetyltransferase type B subunit 2; Nucleosome-remodeling factor subunit RBAP46; Retinoblastoma-binding protein 7; RBBP-7; Retinoblastoma-binding protein p46)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q16576
ID RBBP7_HUMAN Reviewed; 425 AA.
AC Q16576; Q5JP00;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1997, sequence version 1.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Histone-binding protein RBBP7;
DE AltName: Full=Histone acetyltransferase type B subunit 2;
DE AltName: Full=Nucleosome-remodeling factor subunit RBAP46;
DE AltName: Full=Retinoblastoma-binding protein 7;
DE Short=RBBP-7;
DE AltName: Full=Retinoblastoma-binding protein p46;
GN Name=RBBP7; Synonyms=RBAP46;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND 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
RT negative regulator of ras in yeast.";
RL J. Biol. Chem. 270:25507-25513(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Nielsen M.S., Rasmussen H.H., Dejgaard K., Celis J.E., Leffers H.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
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
RT of a human Sin3 complex.";
RL Cell 89:357-364(1997).
RN [6]
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
RT complex containing histone deacetylase and nucleosome remodeling
RT activities.";
RL Cell 95:279-289(1998).
RN [7]
RP INTERACTION WITH HAT1 AND 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
RT human Hat1 acetyltransferase.";
RL Curr. Biol. 8:96-108(1998).
RN [8]
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
RT component of a histone deacetylase complex.";
RL Mol. Cell 1:1021-1031(1998).
RN [9]
RP IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=10444591;
RA Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A.,
RA Reinberg D.;
RT "Analysis of the NuRD subunits reveals a histone deacetylase core
RT complex and a connection with DNA methylation.";
RL Genes Dev. 13:1924-1935(1999).
RN [10]
RP INTERACTION WITH BRCA1 AND RB1.
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 [11]
RP FUNCTION, AND INTERACTION WITH CREBBP.
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
RT binding protein and phosphorylated CREB.";
RL Mol. Cell. Biol. 20:4970-4978(2000).
RN [12]
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
RT SANT domain proteins CoREST/kiaa0071 and Mta-L1.";
RL J. Biol. Chem. 276:6817-6824(2001).
RN [13]
RP IDENTIFICATION IN THE 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
RT the candidate tumor suppressor ING1 with the mSin3/HDAC1
RT transcriptional corepressor complex.";
RL J. Biol. Chem. 276:8734-8739(2001).
RN [14]
RP IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH EED; EZH2; RBBP4 AND
RP SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
RX PubMed=12435631; DOI=10.1101/gad.1035902;
RA Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P.,
RA Reinberg D.;
RT "Histone methyltransferase activity associated with a human
RT multiprotein complex containing the Enhancer of Zeste protein.";
RL Genes Dev. 16:2893-2905(2002).
RN [15]
RP IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
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
RT the candidate tumor suppressor p33(ING1).";
RL Mol. Cell. Biol. 22:835-848(2002).
RN [16]
RP IDENTIFICATION IN THE NURF COMPLEX, AND 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 [17]
RP IDENTIFICATION IN THE MTA1 HDAC COMPLEX.
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
RT complexes with histone deacetylase activity.";
RL J. Biol. Chem. 278:42560-42568(2003).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-4, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-13 (ISOFORM 2), MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
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.,
RA Buerckstuemmer T., 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 [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-411 IN COMPLEX WITH HISTONE
RP H4, AND DOMAINS WD REPEATS.
RX PubMed=18571423; DOI=10.1016/j.str.2008.05.006;
RA Murzina N.V., Pei X.Y., Zhang W., Sparkes M., Vicente-Garcia J.,
RA Pratap J.V., McLaughlin S.H., Ben-Shahar T.R., Verreault A.,
RA Luisi B.F., Laue E.D.;
RT "Structural basis for the recognition of histone H4 by the histone-
RT chaperone RbAp46.";
RL Structure 16:1077-1085(2008).
CC -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC remodeling factors, histone acetyltransferases and histone
CC deacetylases to their histone substrates in a manner that is
CC regulated by nucleosomal DNA. Component of several complexes which
CC regulate chromatin metabolism. These include the type B histone
CC acetyltransferase (HAT) complex, which is required for chromatin
CC assembly following DNA replication; the core histone deacetylase
CC (HDAC) complex, which promotes histone deacetylation and
CC consequent transcriptional repression; the nucleosome remodeling
CC and histone deacetylase complex (the NuRD complex), which promotes
CC transcriptional repression by histone deacetylation and nucleosome
CC remodeling; and the PRC2/EED-EZH2 complex, which promotes
CC repression of homeotic genes during development; and the NURF
CC (nucleosome remodeling factor) complex.
CC -!- SUBUNIT: Binds directly to helix 1 of the histone fold of histone
CC H4, a region that is not accessible when H4 is in chromatin.
CC Subunit of the type B histone acetyltransferase (HAT) complex,
CC composed of RBBP7 and HAT1. Subunit of the core histone
CC deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2,
CC RBBP4 and RBBP7. 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. The core HDAC
CC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form
CC the nucleosome remodeling and histone deacetylase complex (the
CC NuRD complex). The NuRD complex may also interact with MBD3L1 and
CC MBD3L2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex,
CC which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12.
CC The PRC2/EED-EZH2 complex may also associate with HDAC1. Part of
CC the nucleosome remodeling factor (NURF) complex which consists of
CC SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the viral protein-
CC binding domain of the retinoblastoma protein (RB1). Interacts with
CC CREBBP, and this interaction may be enhanced by the binding of
CC phosphorylated CREB1 to CREBBP. Interacts with BRCA1, HDAC7 and
CC SUV39H1.
CC -!- INTERACTION:
CC Q7L2E3:DHX30; NbExp=4; IntAct=EBI-352227, EBI-1211456;
CC Q13547:HDAC1; NbExp=5; IntAct=EBI-352227, EBI-301834;
CC P62805:HIST2H4B; NbExp=4; IntAct=EBI-352227, EBI-302023;
CC Q9Y5X4:NR2E3; NbExp=2; IntAct=EBI-352227, EBI-7216962;
CC Q12788:TBL3; NbExp=2; IntAct=EBI-352227, EBI-715766;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16576-2; Sequence=VSP_043016;
CC Note=No experimental confirmation available. Initiator Met-1 is
CC removed. Contains a N-acetylalanine at position 2. Contains a
CC phosphoserine at position 13;
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RBBP7ID42065chXp22.html";
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DR EMBL; U35143; AAC50231.1; -; mRNA.
DR EMBL; X72841; CAA51360.1; -; mRNA.
DR EMBL; AK091911; BAG52439.1; -; mRNA.
DR EMBL; AL929302; CAI41283.1; -; Genomic_DNA.
DR PIR; I39181; I39181.
DR RefSeq; NP_001185648.1; NM_001198719.1.
DR RefSeq; NP_002884.1; NM_002893.3.
DR UniGene; Hs.495755; -.
DR PDB; 3CFS; X-ray; 2.40 A; B=1-411.
DR PDB; 3CFV; X-ray; 2.60 A; A/B=1-411.
DR PDBsum; 3CFS; -.
DR PDBsum; 3CFV; -.
DR ProteinModelPortal; Q16576; -.
DR SMR; Q16576; 1-410.
DR DIP; DIP-436N; -.
DR IntAct; Q16576; 38.
DR MINT; MINT-90512; -.
DR STRING; 9606.ENSP00000369427; -.
DR PhosphoSite; Q16576; -.
DR DMDM; 2494891; -.
DR PaxDb; Q16576; -.
DR PeptideAtlas; Q16576; -.
DR PRIDE; Q16576; -.
DR Ensembl; ENST00000380084; ENSP00000369424; ENSG00000102054.
DR Ensembl; ENST00000380087; ENSP00000369427; ENSG00000102054.
DR GeneID; 5931; -.
DR KEGG; hsa:5931; -.
DR UCSC; uc004cxt.3; human.
DR CTD; 5931; -.
DR GeneCards; GC0XM016772; -.
DR HGNC; HGNC:9890; RBBP7.
DR HPA; CAB037084; -.
DR MIM; 300825; gene.
DR neXtProt; NX_Q16576; -.
DR PharmGKB; PA34254; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000160330; -.
DR HOVERGEN; HBG053236; -.
DR KO; K11659; -.
DR OMA; HEDAVNC; -.
DR PhylomeDB; Q16576; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_120956; Cellular responses to stress.
DR SignaLink; Q16576; -.
DR ChiTaRS; RBBP7; human.
DR EvolutionaryTrace; Q16576; -.
DR GeneWiki; RBBP7; -.
DR GenomeRNAi; 5931; -.
DR NextBio; 23110; -.
DR PMAP-CutDB; Q16576; -.
DR PRO; PR:Q16576; -.
DR ArrayExpress; Q16576; -.
DR Bgee; Q16576; -.
DR CleanEx; HS_RBBP7; -.
DR Genevestigator; Q16576; -.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0070370; P:cellular heat acclimation; IDA:UniProtKB.
DR GO; GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
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; Chaperone;
KW Chromatin regulator; Complete proteome; Direct protein sequencing;
KW DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 425 Histone-binding protein RBBP7.
FT /FTId=PRO_0000051195.
FT REPEAT 47 122 WD 1.
FT REPEAT 128 173 WD 2.
FT REPEAT 181 217 WD 3.
FT REPEAT 228 269 WD 4.
FT REPEAT 275 312 WD 5.
FT REPEAT 318 369 WD 6.
FT REPEAT 376 403 WD 7.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 3 3 Phosphoserine.
FT MOD_RES 4 4 N6-acetyllysine; alternate.
FT MOD_RES 354 354 Phosphoserine.
FT CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin);
FT alternate.
FT VAR_SEQ 1 6 MASKEM -> MAAEAGVVGAGASPDGDWRDQACGLLLHVHL
FT SSRLGRAAPVRTGRHLRTV (in isoform 2).
FT /FTId=VSP_043016.
FT HELIX 10 30
FT STRAND 31 38
FT STRAND 46 53
FT STRAND 59 67
FT STRAND 72 74
FT STRAND 76 86
FT STRAND 113 124
FT STRAND 127 131
FT STRAND 138 142
FT STRAND 144 146
FT STRAND 148 152
FT HELIX 153 155
FT STRAND 169 173
FT STRAND 182 184
FT STRAND 186 188
FT STRAND 191 195
FT STRAND 201 205
FT STRAND 214 217
FT STRAND 219 222
FT STRAND 229 234
FT STRAND 241 246
FT STRAND 249 259
FT STRAND 261 263
FT STRAND 265 269
FT STRAND 275 280
FT STRAND 287 292
FT STRAND 295 301
FT STRAND 305 307
FT STRAND 310 313
FT STRAND 319 324
FT STRAND 331 336
FT STRAND 341 345
FT HELIX 346 348
FT HELIX 355 358
FT STRAND 365 369
FT STRAND 376 381
FT STRAND 383 385
FT STRAND 388 393
FT STRAND 396 403
FT HELIX 405 408
SQ SEQUENCE 425 AA; 47820 MW; 1A4B4CD1A8E96815 CRC64;
MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP EVTKPEGKDY
ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD KGEFGGFGSV TGKIECEIKI
NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV FDYTKHPAKP DPSGECNPDL RLRGHQKEGY
GLSWNSNLSG HLLSASDDHT VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES
LFGSVADDQK LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW
DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG EEQSAEDAED
GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI WQMAENIYND EESDVTTSEL
EGQGS
//
ID RBBP7_HUMAN Reviewed; 425 AA.
AC Q16576; Q5JP00;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1997, sequence version 1.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Histone-binding protein RBBP7;
DE AltName: Full=Histone acetyltransferase type B subunit 2;
DE AltName: Full=Nucleosome-remodeling factor subunit RBAP46;
DE AltName: Full=Retinoblastoma-binding protein 7;
DE Short=RBBP-7;
DE AltName: Full=Retinoblastoma-binding protein p46;
GN Name=RBBP7; Synonyms=RBAP46;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND 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
RT negative regulator of ras in yeast.";
RL J. Biol. Chem. 270:25507-25513(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Nielsen M.S., Rasmussen H.H., Dejgaard K., Celis J.E., Leffers H.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
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
RT of a human Sin3 complex.";
RL Cell 89:357-364(1997).
RN [6]
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
RT complex containing histone deacetylase and nucleosome remodeling
RT activities.";
RL Cell 95:279-289(1998).
RN [7]
RP INTERACTION WITH HAT1 AND 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
RT human Hat1 acetyltransferase.";
RL Curr. Biol. 8:96-108(1998).
RN [8]
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
RT component of a histone deacetylase complex.";
RL Mol. Cell 1:1021-1031(1998).
RN [9]
RP IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=10444591;
RA Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A.,
RA Reinberg D.;
RT "Analysis of the NuRD subunits reveals a histone deacetylase core
RT complex and a connection with DNA methylation.";
RL Genes Dev. 13:1924-1935(1999).
RN [10]
RP INTERACTION WITH BRCA1 AND RB1.
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 [11]
RP FUNCTION, AND INTERACTION WITH CREBBP.
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
RT binding protein and phosphorylated CREB.";
RL Mol. Cell. Biol. 20:4970-4978(2000).
RN [12]
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
RT SANT domain proteins CoREST/kiaa0071 and Mta-L1.";
RL J. Biol. Chem. 276:6817-6824(2001).
RN [13]
RP IDENTIFICATION IN THE 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
RT the candidate tumor suppressor ING1 with the mSin3/HDAC1
RT transcriptional corepressor complex.";
RL J. Biol. Chem. 276:8734-8739(2001).
RN [14]
RP IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH EED; EZH2; RBBP4 AND
RP SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
RX PubMed=12435631; DOI=10.1101/gad.1035902;
RA Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P.,
RA Reinberg D.;
RT "Histone methyltransferase activity associated with a human
RT multiprotein complex containing the Enhancer of Zeste protein.";
RL Genes Dev. 16:2893-2905(2002).
RN [15]
RP IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
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
RT the candidate tumor suppressor p33(ING1).";
RL Mol. Cell. Biol. 22:835-848(2002).
RN [16]
RP IDENTIFICATION IN THE NURF COMPLEX, AND 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 [17]
RP IDENTIFICATION IN THE MTA1 HDAC COMPLEX.
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
RT complexes with histone deacetylase activity.";
RL J. Biol. Chem. 278:42560-42568(2003).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-4, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-13 (ISOFORM 2), MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
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.,
RA Buerckstuemmer T., 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 [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-411 IN COMPLEX WITH HISTONE
RP H4, AND DOMAINS WD REPEATS.
RX PubMed=18571423; DOI=10.1016/j.str.2008.05.006;
RA Murzina N.V., Pei X.Y., Zhang W., Sparkes M., Vicente-Garcia J.,
RA Pratap J.V., McLaughlin S.H., Ben-Shahar T.R., Verreault A.,
RA Luisi B.F., Laue E.D.;
RT "Structural basis for the recognition of histone H4 by the histone-
RT chaperone RbAp46.";
RL Structure 16:1077-1085(2008).
CC -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC remodeling factors, histone acetyltransferases and histone
CC deacetylases to their histone substrates in a manner that is
CC regulated by nucleosomal DNA. Component of several complexes which
CC regulate chromatin metabolism. These include the type B histone
CC acetyltransferase (HAT) complex, which is required for chromatin
CC assembly following DNA replication; the core histone deacetylase
CC (HDAC) complex, which promotes histone deacetylation and
CC consequent transcriptional repression; the nucleosome remodeling
CC and histone deacetylase complex (the NuRD complex), which promotes
CC transcriptional repression by histone deacetylation and nucleosome
CC remodeling; and the PRC2/EED-EZH2 complex, which promotes
CC repression of homeotic genes during development; and the NURF
CC (nucleosome remodeling factor) complex.
CC -!- SUBUNIT: Binds directly to helix 1 of the histone fold of histone
CC H4, a region that is not accessible when H4 is in chromatin.
CC Subunit of the type B histone acetyltransferase (HAT) complex,
CC composed of RBBP7 and HAT1. Subunit of the core histone
CC deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2,
CC RBBP4 and RBBP7. 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. The core HDAC
CC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form
CC the nucleosome remodeling and histone deacetylase complex (the
CC NuRD complex). The NuRD complex may also interact with MBD3L1 and
CC MBD3L2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex,
CC which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12.
CC The PRC2/EED-EZH2 complex may also associate with HDAC1. Part of
CC the nucleosome remodeling factor (NURF) complex which consists of
CC SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the viral protein-
CC binding domain of the retinoblastoma protein (RB1). Interacts with
CC CREBBP, and this interaction may be enhanced by the binding of
CC phosphorylated CREB1 to CREBBP. Interacts with BRCA1, HDAC7 and
CC SUV39H1.
CC -!- INTERACTION:
CC Q7L2E3:DHX30; NbExp=4; IntAct=EBI-352227, EBI-1211456;
CC Q13547:HDAC1; NbExp=5; IntAct=EBI-352227, EBI-301834;
CC P62805:HIST2H4B; NbExp=4; IntAct=EBI-352227, EBI-302023;
CC Q9Y5X4:NR2E3; NbExp=2; IntAct=EBI-352227, EBI-7216962;
CC Q12788:TBL3; NbExp=2; IntAct=EBI-352227, EBI-715766;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16576-2; Sequence=VSP_043016;
CC Note=No experimental confirmation available. Initiator Met-1 is
CC removed. Contains a N-acetylalanine at position 2. Contains a
CC phosphoserine at position 13;
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RBBP7ID42065chXp22.html";
CC -----------------------------------------------------------------------
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DR EMBL; U35143; AAC50231.1; -; mRNA.
DR EMBL; X72841; CAA51360.1; -; mRNA.
DR EMBL; AK091911; BAG52439.1; -; mRNA.
DR EMBL; AL929302; CAI41283.1; -; Genomic_DNA.
DR PIR; I39181; I39181.
DR RefSeq; NP_001185648.1; NM_001198719.1.
DR RefSeq; NP_002884.1; NM_002893.3.
DR UniGene; Hs.495755; -.
DR PDB; 3CFS; X-ray; 2.40 A; B=1-411.
DR PDB; 3CFV; X-ray; 2.60 A; A/B=1-411.
DR PDBsum; 3CFS; -.
DR PDBsum; 3CFV; -.
DR ProteinModelPortal; Q16576; -.
DR SMR; Q16576; 1-410.
DR DIP; DIP-436N; -.
DR IntAct; Q16576; 38.
DR MINT; MINT-90512; -.
DR STRING; 9606.ENSP00000369427; -.
DR PhosphoSite; Q16576; -.
DR DMDM; 2494891; -.
DR PaxDb; Q16576; -.
DR PeptideAtlas; Q16576; -.
DR PRIDE; Q16576; -.
DR Ensembl; ENST00000380084; ENSP00000369424; ENSG00000102054.
DR Ensembl; ENST00000380087; ENSP00000369427; ENSG00000102054.
DR GeneID; 5931; -.
DR KEGG; hsa:5931; -.
DR UCSC; uc004cxt.3; human.
DR CTD; 5931; -.
DR GeneCards; GC0XM016772; -.
DR HGNC; HGNC:9890; RBBP7.
DR HPA; CAB037084; -.
DR MIM; 300825; gene.
DR neXtProt; NX_Q16576; -.
DR PharmGKB; PA34254; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000160330; -.
DR HOVERGEN; HBG053236; -.
DR KO; K11659; -.
DR OMA; HEDAVNC; -.
DR PhylomeDB; Q16576; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_120956; Cellular responses to stress.
DR SignaLink; Q16576; -.
DR ChiTaRS; RBBP7; human.
DR EvolutionaryTrace; Q16576; -.
DR GeneWiki; RBBP7; -.
DR GenomeRNAi; 5931; -.
DR NextBio; 23110; -.
DR PMAP-CutDB; Q16576; -.
DR PRO; PR:Q16576; -.
DR ArrayExpress; Q16576; -.
DR Bgee; Q16576; -.
DR CleanEx; HS_RBBP7; -.
DR Genevestigator; Q16576; -.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0070370; P:cellular heat acclimation; IDA:UniProtKB.
DR GO; GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
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; Chaperone;
KW Chromatin regulator; Complete proteome; Direct protein sequencing;
KW DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 425 Histone-binding protein RBBP7.
FT /FTId=PRO_0000051195.
FT REPEAT 47 122 WD 1.
FT REPEAT 128 173 WD 2.
FT REPEAT 181 217 WD 3.
FT REPEAT 228 269 WD 4.
FT REPEAT 275 312 WD 5.
FT REPEAT 318 369 WD 6.
FT REPEAT 376 403 WD 7.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 3 3 Phosphoserine.
FT MOD_RES 4 4 N6-acetyllysine; alternate.
FT MOD_RES 354 354 Phosphoserine.
FT CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin);
FT alternate.
FT VAR_SEQ 1 6 MASKEM -> MAAEAGVVGAGASPDGDWRDQACGLLLHVHL
FT SSRLGRAAPVRTGRHLRTV (in isoform 2).
FT /FTId=VSP_043016.
FT HELIX 10 30
FT STRAND 31 38
FT STRAND 46 53
FT STRAND 59 67
FT STRAND 72 74
FT STRAND 76 86
FT STRAND 113 124
FT STRAND 127 131
FT STRAND 138 142
FT STRAND 144 146
FT STRAND 148 152
FT HELIX 153 155
FT STRAND 169 173
FT STRAND 182 184
FT STRAND 186 188
FT STRAND 191 195
FT STRAND 201 205
FT STRAND 214 217
FT STRAND 219 222
FT STRAND 229 234
FT STRAND 241 246
FT STRAND 249 259
FT STRAND 261 263
FT STRAND 265 269
FT STRAND 275 280
FT STRAND 287 292
FT STRAND 295 301
FT STRAND 305 307
FT STRAND 310 313
FT STRAND 319 324
FT STRAND 331 336
FT STRAND 341 345
FT HELIX 346 348
FT HELIX 355 358
FT STRAND 365 369
FT STRAND 376 381
FT STRAND 383 385
FT STRAND 388 393
FT STRAND 396 403
FT HELIX 405 408
SQ SEQUENCE 425 AA; 47820 MW; 1A4B4CD1A8E96815 CRC64;
MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP EVTKPEGKDY
ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD KGEFGGFGSV TGKIECEIKI
NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV FDYTKHPAKP DPSGECNPDL RLRGHQKEGY
GLSWNSNLSG HLLSASDDHT VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES
LFGSVADDQK LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW
DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG EEQSAEDAED
GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI WQMAENIYND EESDVTTSEL
EGQGS
//
MIM
300825
*RECORD*
*FIELD* NO
300825
*FIELD* TI
*300825 RETINOBLASTOMA-BINDING PROTEIN 7; RBBP7
*FIELD* TX
CLONING
The RB1 protein (614041) interacts with multiple cellular proteins that
read moremediate its functions. RBBP4 (602923) and RBBP7 were the 2 most abundant
proteins from HeLa cell lysates that were specifically retained by an
RB1 affinity column (Qian et al., 1993). By screening a HeLa cell cDNA
expression library with monoclonal antibodies against RBBP7, Qian and
Lee (1995) isolated cDNAs encoding RBBP7, which they called RbAp46.
Southern blot analysis indicated that the human genome contains a single
copy of the RBBP7 gene. The predicted 425-amino acid human RBBP7 protein
is identical to mouse Rbbp7 except for 1 conserved amino acid
substitution, and it is 89% identical to human RBBP4. RBBP7 contains
internal trp-asp (WD) repeats that are conserved with those of RBBP4. By
Western blot analysis, RBBP7 from HeLa cell lysates had a molecular mass
of 46 kD. RNase protection analysis detected Rbbp7 mRNA in all mouse
tissues examined, although the levels varied dramatically between
different tissues.
Yang et al. (2002) noted that RBBP7 is highly conserved between mammals,
flies, and plants, with highest conservation in the WD repeat region. In
developing mouse, Rbbp7 expression began at embryonic day 9.5, was
dynamic, and persisted throughout embryogenesis. RBBP7 was expressed in
all adult mouse tissues and mammalian cell lines examined, including
HEK293 and HeLa cells.
GENE FUNCTION
Qian and Lee (1995) showed that RBBP7 formed a complex with RB1 in vitro
and in vivo. In yeast, RBBP7 could mimic the function of S. cerevisiae
Msi1, a presumed negative regulator of the Ras signal transduction
pathway.
Using reporter gene assays, Yang et al. (2002) demonstrated that mouse
Rbbp7 functioned as a transcriptional repressor that inhibited
mitogen-stimulated transactivation of FOS (164810) in transfected COS-1
cells.
MAPPING
By genomic sequence analysis, Yang et al. (2002) mapped the RBBP7 gene
to chromosome Xp22.13. They mapped the mouse Rbbp7 gene to the X
chromosome.
*FIELD* RF
1. 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.
2. 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.
3. Yang, J.; Kiefer, S. M.; Rauchman, M.: Characterization of the
gene encoding mouse retinoblastoma binding protein-7, a component
of chromatin-remodeling complexes. Genomics 80: 407-415, 2002.
*FIELD* CD
Patricia A. Hartz: 11/3/2010
*FIELD* ED
carol: 06/17/2011
mgross: 11/3/2010
*RECORD*
*FIELD* NO
300825
*FIELD* TI
*300825 RETINOBLASTOMA-BINDING PROTEIN 7; RBBP7
*FIELD* TX
CLONING
The RB1 protein (614041) interacts with multiple cellular proteins that
read moremediate its functions. RBBP4 (602923) and RBBP7 were the 2 most abundant
proteins from HeLa cell lysates that were specifically retained by an
RB1 affinity column (Qian et al., 1993). By screening a HeLa cell cDNA
expression library with monoclonal antibodies against RBBP7, Qian and
Lee (1995) isolated cDNAs encoding RBBP7, which they called RbAp46.
Southern blot analysis indicated that the human genome contains a single
copy of the RBBP7 gene. The predicted 425-amino acid human RBBP7 protein
is identical to mouse Rbbp7 except for 1 conserved amino acid
substitution, and it is 89% identical to human RBBP4. RBBP7 contains
internal trp-asp (WD) repeats that are conserved with those of RBBP4. By
Western blot analysis, RBBP7 from HeLa cell lysates had a molecular mass
of 46 kD. RNase protection analysis detected Rbbp7 mRNA in all mouse
tissues examined, although the levels varied dramatically between
different tissues.
Yang et al. (2002) noted that RBBP7 is highly conserved between mammals,
flies, and plants, with highest conservation in the WD repeat region. In
developing mouse, Rbbp7 expression began at embryonic day 9.5, was
dynamic, and persisted throughout embryogenesis. RBBP7 was expressed in
all adult mouse tissues and mammalian cell lines examined, including
HEK293 and HeLa cells.
GENE FUNCTION
Qian and Lee (1995) showed that RBBP7 formed a complex with RB1 in vitro
and in vivo. In yeast, RBBP7 could mimic the function of S. cerevisiae
Msi1, a presumed negative regulator of the Ras signal transduction
pathway.
Using reporter gene assays, Yang et al. (2002) demonstrated that mouse
Rbbp7 functioned as a transcriptional repressor that inhibited
mitogen-stimulated transactivation of FOS (164810) in transfected COS-1
cells.
MAPPING
By genomic sequence analysis, Yang et al. (2002) mapped the RBBP7 gene
to chromosome Xp22.13. They mapped the mouse Rbbp7 gene to the X
chromosome.
*FIELD* RF
1. 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.
2. 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.
3. Yang, J.; Kiefer, S. M.; Rauchman, M.: Characterization of the
gene encoding mouse retinoblastoma binding protein-7, a component
of chromatin-remodeling complexes. Genomics 80: 407-415, 2002.
*FIELD* CD
Patricia A. Hartz: 11/3/2010
*FIELD* ED
carol: 06/17/2011
mgross: 11/3/2010