RBBP5_HUMAN
ID RBBP5_HUMAN Reviewed; 538 AA.
AC Q15291; A8K272; Q7Z6D8; Q8NDZ7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Retinoblastoma-binding protein 5;
DE Short=RBBP-5;
DE AltName: Full=Retinoblastoma-binding protein RBQ-3;
GN Name=RBBP5; Synonyms=RBQ3;
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), PHOSPHORYLATION AT THR-252 AND
RP SER-497, AND CHARACTERIZATION.
RC TISSUE=Lung carcinoma, and Testis;
RX PubMed=7558034; DOI=10.1006/geno.1995.1084;
RA Saijo M., Sakai Y., Kishino T., Niikawa N., Matsuura Y., Morino K.,
RA Tamai K., Taya Y.;
RT "Molecular cloning of a human protein that binds to the retinoblastoma
RT protein and chromosomal mapping.";
RL Genomics 27:511-519(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
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 [3]
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
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 [6]
RP IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE COMPLEX.
RX PubMed=14992727; DOI=10.1016/s1097-2765(04)00081-4;
RA Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D., Levine S.S.,
RA Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A., Biondi C.A.,
RA Kay G.F., Hayward N.K., Hess J.L., Meyerson M.;
RT "Menin associates with a trithorax family histone methyltransferase complex
RT and with the hoxc8 locus.";
RL Mol. Cell 13:587-597(2004).
RN [7]
RP IDENTIFICATION IN THE MLL-LIKE COMPLEX.
RX PubMed=15199122; DOI=10.1128/mcb.24.13.5639-5649.2004;
RA Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I.,
RA Herr W., Cleary M.L.;
RT "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase
RT complex with menin to regulate Hox gene expression.";
RL Mol. Cell. Biol. 24:5639-5649(2004).
RN [8]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [9]
RP IDENTIFICATION IN THE SET1 COMPLEX.
RX PubMed=16253997; DOI=10.1074/jbc.m508312200;
RA Lee J.-H., Skalnik D.G.;
RT "CpG-binding protein (CXXC finger protein 1) is a component of the
RT mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of
RT the yeast Set1/COMPASS complex.";
RL J. Biol. Chem. 280:41725-41731(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SET1 COMPLEX.
RX PubMed=17355966; DOI=10.1074/jbc.m609809200;
RA Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
RT "Identification and characterization of the human Set1B histone H3-Lys4
RT methyltransferase complex.";
RL J. Biol. Chem. 282:13419-13428(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MLL2/3
RP COMPLEX.
RX PubMed=17500065; DOI=10.1074/jbc.m701574200;
RA Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
RA Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
RT "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
RT methyltransferase complex.";
RL J. Biol. Chem. 282:20395-20406(2007).
RN [13]
RP IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH SETD1A.
RX PubMed=17998332; DOI=10.1128/mcb.01356-07;
RA Lee J.H., Skalnik D.G.;
RT "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
RT Histone H3-Lys4 methyltransferase complex to transcription start sites of
RT transcribed human genes.";
RL Mol. Cell. Biol. 28:609-618(2008).
RN [14]
RP IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH WDR82.
RX PubMed=18838538; DOI=10.1128/mcb.00976-08;
RA Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
RA Shilatifard A.;
RT "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human
RT Set1/COMPASS.";
RL Mol. Cell. Biol. 28:7337-7344(2008).
RN [15]
RP FUNCTION, IDENTIFICATION IN A HISTONE METHYLATION COMPLEX, AND INTERACTION
RP WITH ZNF335; ASH2L AND EMSY.
RX PubMed=19131338; DOI=10.1074/jbc.m805872200;
RA Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.;
RT "Identification and characterization of a novel nuclear protein complex
RT involved in nuclear hormone receptor-mediated gene regulation.";
RL J. Biol. Chem. 284:7542-7552(2009).
RN [16]
RP FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, AND INTERACTION WITH
RP WDR5 AND ASH2L.
RX PubMed=19556245; DOI=10.1074/jbc.m109.014498;
RA Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.;
RT "On the mechanism of multiple lysine methylation by the human mixed lineage
RT leukemia protein-1 (MLL1) core complex.";
RL J. Biol. Chem. 284:24242-24256(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-389, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP INTERACTION WITH ZNF335.
RX PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
RA Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
RA Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
RA Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A., Mahajnah M.,
RA Shenhav R., Walsh C.A.;
RT "Microcephaly gene links trithorax and REST/NRSF to control neural stem
RT cell proliferation and differentiation.";
RL Cell 151:1097-1112(2012).
RN [21]
RP FUNCTION.
RX PubMed=22266653; DOI=10.1093/nar/gkr1235;
RA Zhang P., Lee H., Brunzelle J.S., Couture J.F.;
RT "The plasticity of WDR5 peptide-binding cleft enables the binding of the
RT SET1 family of histone methyltransferases.";
RL Nucleic Acids Res. 40:4237-4246(2012).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-129, AND IDENTIFICATION BY MASS
RP 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 [23] {ECO:0007744|PDB:3P4F}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 371-381 IN COMPLEX WITH KMT2A AND
RP WDR5, FUNCTION, INTERACTION WITH ASH2L AND WDR5, AND MUTAGENESIS OF
RP GLU-374; VAL-375; ASP-376 AND VAL-377.
RX PubMed=21220120; DOI=10.1016/j.str.2010.09.022;
RA Avdic V., Zhang P., Lanouette S., Groulx A., Tremblay V., Brunzelle J.,
RA Couture J.F.;
RT "Structural and biochemical insights into MLL1 core complex assembly.";
RL Structure 19:101-108(2011).
CC -!- FUNCTION: In embryonic stem (ES) cells, plays a crucial role in the
CC differentiation potential, particularly along the neural lineage,
CC regulating gene induction and H3 'Lys-4' methylation at key
CC developmental loci, including that mediated by retinoic acid (By
CC similarity). Does not affect ES cell self-renewal (By similarity).
CC Component or associated component of some histone methyltransferase
CC complexes which regulates transcription through recruitment of those
CC complexes to gene promoters (PubMed:19131338). As part of the MLL1/MLL
CC complex, involved in mono-, di- and trimethylation at 'Lys-4' of
CC histone H3 (PubMed:19556245). Histone H3 'Lys-4' methylation represents
CC a specific tag for epigenetic transcriptional activation
CC (PubMed:19556245). In association with ASH2L and WDR5, stimulates the
CC histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D,
CC SETD1A and SETD1B (PubMed:22266653, PubMed:21220120).
CC {ECO:0000250|UniProtKB:Q8BX09, ECO:0000269|PubMed:19131338,
CC ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:21220120,
CC ECO:0000269|PubMed:22266653}.
CC -!- SUBUNIT: Component of the SET1 complex, at least composed of the
CC catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2,
CC CXXC1/CFP1, HCFC1 and DPY30 (PubMed:16253997, PubMed:17355966,
CC PubMed:17998332, PubMed:18838538). Core component of several
CC methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also
CC named ASCOM complex) and MLL4/WBP7 (PubMed:15199122, PubMed:15960975,
CC PubMed:17500065). Each complex is at least composed of ASH2L, RBBP5,
CC WDR5, DPY30, one or more specific histone methyltransferases
CC (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the
CC facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70,
CC INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6,
CC PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin
CC (PubMed:14992727, PubMed:15199122, PubMed:15960975, PubMed:17500065).
CC Component of a histone methylation complex composed of at least ZNF335,
CC RBBP5, ASH2L and WDR5; the complex may have histone H3-specific
CC methyltransferase activity, however does not have specificity for 'Lys-
CC 4' of histone H3 (PubMed:19131338). Interacts with ZNF335
CC (PubMed:19131338, PubMed:23178126). Interacts with ASH2L; the
CC interaction is direct (PubMed:19131338, PubMed:19556245,
CC PubMed:21220120). Interacts with WDR5; the interaction is direct
CC (PubMed:19556245, PubMed:21220120). Components of the ZNF335-RBBP5-
CC ASH2L-WDR5 histone methylation complex may associate with components of
CC a nuclear receptor-mediated transcription complex to form a complex at
CC least composed of ZNF335, HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and
CC WDR5 (PubMed:19131338). Within this complex interacts with EMSY
CC (PubMed:19131338). Found in a complex with RBBP5, ASH2L, DPY30, KMT2A,
CC KMT2D and WDR5 (By similarity). Interacts with SETD1A
CC (PubMed:17998332). Interacts with WDR82 (PubMed:18838538).
CC {ECO:0000250|UniProtKB:Q8BX09, ECO:0000269|PubMed:14992727,
CC ECO:0000269|PubMed:15199122, ECO:0000269|PubMed:15960975,
CC ECO:0000269|PubMed:16253997, ECO:0000269|PubMed:17355966,
CC ECO:0000269|PubMed:17500065, ECO:0000269|PubMed:17998332,
CC ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:19131338,
CC ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:21220120,
CC ECO:0000269|PubMed:23178126}.
CC -!- INTERACTION:
CC Q15291; Q9UBL3: ASH2L; NbExp=37; IntAct=EBI-592823, EBI-540797;
CC Q15291; Q9UBL3-3: ASH2L; NbExp=9; IntAct=EBI-592823, EBI-16130425;
CC Q15291; Q9HCK8: CHD8; NbExp=2; IntAct=EBI-592823, EBI-1169146;
CC Q15291; Q13619: CUL4A; NbExp=3; IntAct=EBI-592823, EBI-456106;
CC Q15291; Q9P0U4: CXXC1; NbExp=6; IntAct=EBI-592823, EBI-949911;
CC Q15291; Q03164: KMT2A; NbExp=9; IntAct=EBI-592823, EBI-591370;
CC Q15291; Q6ZW49: PAXIP1; NbExp=11; IntAct=EBI-592823, EBI-743225;
CC Q15291; O15047: SETD1A; NbExp=3; IntAct=EBI-592823, EBI-540779;
CC Q15291; P61964: WDR5; NbExp=15; IntAct=EBI-592823, EBI-540834;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17355966}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15291-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15291-2; Sequence=VSP_035583;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
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DR EMBL; X85134; CAA59446.1; -; mRNA.
DR EMBL; AK290137; BAF82826.1; -; mRNA.
DR EMBL; AC093422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91537.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91538.1; -; Genomic_DNA.
DR EMBL; BC037284; AAH37284.1; -; mRNA.
DR EMBL; BC053856; AAH53856.1; -; mRNA.
DR EMBL; BC075059; AAH75059.1; -; mRNA.
DR EMBL; BC075060; AAH75060.1; -; mRNA.
DR CCDS; CCDS30983.1; -. [Q15291-1]
DR CCDS; CCDS53463.1; -. [Q15291-2]
DR PIR; A57624; A57624.
DR RefSeq; NP_001180201.1; NM_001193272.1. [Q15291-2]
DR RefSeq; NP_001180202.1; NM_001193273.1.
DR RefSeq; NP_005048.2; NM_005057.3. [Q15291-1]
DR PDB; 3P4F; X-ray; 2.35 A; B=371-381.
DR PDB; 4X8N; X-ray; 2.10 A; B=347-356.
DR PDB; 4X8P; X-ray; 2.20 A; B=344-355.
DR PDB; 5F6K; X-ray; 2.41 A; D/F=330-356.
DR PDB; 5F6L; X-ray; 1.90 A; J=330-356.
DR PDB; 6KIU; EM; 3.20 A; N=1-538.
DR PDB; 6KIV; EM; 4.00 A; N=1-538.
DR PDB; 6KIW; EM; 4.00 A; N=1-538.
DR PDB; 6KIX; EM; 4.10 A; N=1-538.
DR PDB; 6KIZ; EM; 4.50 A; N=1-538.
DR PDB; 6KM7; X-ray; 1.80 A; A/B=10-325, C/D=390-480.
DR PDB; 6PWV; EM; 6.20 A; A=2-538.
DR PDB; 6PWW; EM; 4.40 A; A=2-538.
DR PDB; 6PWX; EM; 4.20 A; A=2-538.
DR PDB; 6W5I; EM; 6.90 A; A=2-538.
DR PDB; 6W5M; EM; 4.60 A; A=2-538.
DR PDB; 6W5N; EM; 6.00 A; A=2-538.
DR PDB; 7BRE; X-ray; 2.80 A; C/F=330-356.
DR PDB; 7MBM; EM; -; A=2-538.
DR PDB; 7MBN; EM; -; A=2-538.
DR PDBsum; 3P4F; -.
DR PDBsum; 4X8N; -.
DR PDBsum; 4X8P; -.
DR PDBsum; 5F6K; -.
DR PDBsum; 5F6L; -.
DR PDBsum; 6KIU; -.
DR PDBsum; 6KIV; -.
DR PDBsum; 6KIW; -.
DR PDBsum; 6KIX; -.
DR PDBsum; 6KIZ; -.
DR PDBsum; 6KM7; -.
DR PDBsum; 6PWV; -.
DR PDBsum; 6PWW; -.
DR PDBsum; 6PWX; -.
DR PDBsum; 6W5I; -.
DR PDBsum; 6W5M; -.
DR PDBsum; 6W5N; -.
DR PDBsum; 7BRE; -.
DR PDBsum; 7MBM; -.
DR PDBsum; 7MBN; -.
DR AlphaFoldDB; Q15291; -.
DR SASBDB; Q15291; -.
DR SMR; Q15291; -.
DR BioGRID; 111864; 179.
DR ComplexPortal; CPX-5850; Histone-lysine N-methyltransferase complex, KMT2A variant.
DR ComplexPortal; CPX-7062; Histone-lysine N-methyltransferase complex, KMT2B variant.
DR ComplexPortal; CPX-7091; Histone-lysine N-methyltransferase complex, KMT2C variant.
DR ComplexPortal; CPX-7104; Histone-lysine N-methyltransferase complex, KMT2D variant.
DR ComplexPortal; CPX-7110; Histone-lysine N-methyltransferase complex, SET1A variant.
DR ComplexPortal; CPX-7111; Histone-lysine N-methyltransferase complex, SET1B variant.
DR CORUM; Q15291; -.
DR DIP; DIP-29224N; -.
DR IntAct; Q15291; 84.
DR MINT; Q15291; -.
DR STRING; 9606.ENSP00000264515; -.
DR BindingDB; Q15291; -.
DR ChEMBL; CHEMBL3137282; -.
DR GlyGen; Q15291; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15291; -.
DR PhosphoSitePlus; Q15291; -.
DR BioMuta; RBBP5; -.
DR DMDM; 209572664; -.
DR EPD; Q15291; -.
DR jPOST; Q15291; -.
DR MassIVE; Q15291; -.
DR MaxQB; Q15291; -.
DR PaxDb; Q15291; -.
DR PeptideAtlas; Q15291; -.
DR PRIDE; Q15291; -.
DR ProteomicsDB; 60517; -. [Q15291-1]
DR ProteomicsDB; 60518; -. [Q15291-2]
DR ABCD; Q15291; 1 sequenced antibody.
DR Antibodypedia; 34563; 301 antibodies from 38 providers.
DR DNASU; 5929; -.
DR Ensembl; ENST00000264515.11; ENSP00000264515.6; ENSG00000117222.14. [Q15291-1]
DR Ensembl; ENST00000367164.1; ENSP00000356132.1; ENSG00000117222.14. [Q15291-2]
DR GeneID; 5929; -.
DR KEGG; hsa:5929; -.
DR MANE-Select; ENST00000264515.11; ENSP00000264515.6; NM_005057.4; NP_005048.2.
DR UCSC; uc001hbu.3; human. [Q15291-1]
DR CTD; 5929; -.
DR DisGeNET; 5929; -.
DR GeneCards; RBBP5; -.
DR HGNC; HGNC:9888; RBBP5.
DR HPA; ENSG00000117222; Low tissue specificity.
DR MIM; 600697; gene.
DR neXtProt; NX_Q15291; -.
DR OpenTargets; ENSG00000117222; -.
DR PharmGKB; PA34252; -.
DR VEuPathDB; HostDB:ENSG00000117222; -.
DR eggNOG; KOG1273; Eukaryota.
DR GeneTree; ENSGT00530000064100; -.
DR HOGENOM; CLU_032142_1_0_1; -.
DR InParanoid; Q15291; -.
DR OMA; DYEDDIM; -.
DR PhylomeDB; Q15291; -.
DR TreeFam; TF313289; -.
DR PathwayCommons; Q15291; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q15291; -.
DR SIGNOR; Q15291; -.
DR BioGRID-ORCS; 5929; 724 hits in 1096 CRISPR screens.
DR ChiTaRS; RBBP5; human.
DR GeneWiki; RBBP5; -.
DR GenomeRNAi; 5929; -.
DR Pharos; Q15291; Tbio.
DR PRO; PR:Q15291; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15291; protein.
DR Bgee; ENSG00000117222; Expressed in buccal mucosa cell and 141 other tissues.
DR ExpressionAtlas; Q15291; baseline and differential.
DR Genevisible; Q15291; HS.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0044665; C:MLL1/2 complex; IPI:ComplexPortal.
DR GO; GO:0044666; C:MLL3/4 complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR IDEAL; IID00387; -.
DR InterPro; IPR037850; RBBP5/Swd1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR PANTHER; PTHR44040; PTHR44040; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat.
FT CHAIN 1..538
FT /note="Retinoblastoma-binding protein 5"
FT /id="PRO_0000051194"
FT REPEAT 22..63
FT /note="WD 1"
FT REPEAT 64..103
FT /note="WD 2"
FT REPEAT 148..188
FT /note="WD 3"
FT REPEAT 196..235
FT /note="WD 4"
FT REPEAT 249..291
FT /note="WD 5"
FT REPEAT 293..331
FT /note="WD 6"
FT REGION 330..366
FT /note="Interaction with ASH2L"
FT /evidence="ECO:0000269|PubMed:21220120"
FT REGION 344..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..380
FT /note="Interaction with WDR5"
FT /evidence="ECO:0000269|PubMed:21220120"
FT REGION 408..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7558034"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 497
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7558034"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 492..529
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035583"
FT MUTAGEN 374
FT /note="E->A: Significant reduction in its ability to
FT stimulate KMT2A methyltransferase activity in association
FT with WDR5 and ASH2L."
FT /evidence="ECO:0000269|PubMed:21220120"
FT MUTAGEN 375
FT /note="V->E: Significant reduction in its ability to
FT stimulate KMT2A methyltransferase activity in association
FT with WDR5 and ASH2L."
FT /evidence="ECO:0000269|PubMed:21220120"
FT MUTAGEN 376
FT /note="D->A: Reduced ability to stimulate KMT2A
FT methyltransferase activity in association with WDR5 and
FT ASH2L."
FT /evidence="ECO:0000269|PubMed:21220120"
FT MUTAGEN 377
FT /note="V->E: Reduced ability to stimulate KMT2A
FT methyltransferase activity in association with WDR5 and
FT ASH2L."
FT /evidence="ECO:0000269|PubMed:21220120"
FT CONFLICT 206
FT /note="F -> Y (in Ref. 2; BAF82826)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="K -> E (in Ref. 1; CAA59446)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="E -> G (in Ref. 1; CAA59446)"
FT /evidence="ECO:0000305"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6KIU"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:6KM7"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:6KM7"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:7MBM"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:6KM7"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:7MBN"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7MBM"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:6KM7"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6KIU"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:6KM7"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:7MBM"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:6KM7"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 263..280
FT /evidence="ECO:0007829|PDB:6KM7"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:6KM7"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:6KIU"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:5F6L"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:6KM7"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:6KM7"
SQ SEQUENCE 538 AA; 59153 MW; 095CCB41613CBED9 CRC64;
MNLELLESFG QNYPEEADGT LDCISMALTC TFNRWGTLLA VGCNDGRIVI WDFLTRGIAK
IISAHIHPVC SLCWSRDGHK LVSASTDNIV SQWDVLSGDC DQRFRFPSPI LKVQYHPRDQ
NKVLVCPMKS APVMLTLSDS KHVVLPVDDD SDLNVVASFD RRGEYIYTGN AKGKILVLKT
DSQDLVASFR VTTGTSNTTA IKSIEFARKG SCFLINTADR IIRVYDGREI LTCGRDGEPE
PMQKLQDLVN RTPWKKCCFS GDGEYIVAGS ARQHALYIWE KSIGNLVKIL HGTRGELLLD
VAWHPVRPII ASISSGVVSI WAQNQVENWS AFAPDFKELD ENVEYEERES EFDIEDEDKS
EPEQTGADAA EDEEVDVTSV DPIAAFCSSD EELEDSKALL YLPIAPEVED PEENPYGPPP
DAVQTSLMDE GASSEKKRQS SADGSQPPKK KPKTTNIELQ GVPNDEVHPL LGVKGDGKSK
KKQAGRPKGS KGKEKDSPFK PKLYKGDRGL PLEGSAKGKV QAELSQPLTA GGAISELL
