RBBP5_MOUSE
ID RBBP5_MOUSE Reviewed; 538 AA.
AC Q8BX09; Q3TBL4; Q3U3G1; Q6PAP0; Q6PFC2;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Retinoblastoma-binding protein 5;
DE Short=RBBP-5;
GN Name=Rbbp5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and NMRI; TISSUE=Brain, and Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH ASH2L; DPY30; KMT2A; KMT2D
RP AND WDR5.
RX PubMed=21335234; DOI=10.1016/j.cell.2011.01.020;
RA Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.;
RT "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4
RT methylation within bivalent domains.";
RL Cell 144:513-525(2011).
RN [6]
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).
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
CC (PubMed:21335234). Does not affect ES cell self-renewal
CC (PubMed:21335234). Component or associated component of some histone
CC methyltransferase complexes which regulates transcription through
CC recruitment of those complexes to gene promoters (By similarity). As
CC part of the MLL1/MLL complex, involved in mono-, di- and trimethylation
CC at 'Lys-4' of histone H3 (By similarity). Histone H3 'Lys-4'
CC methylation represents a specific tag for epigenetic transcriptional
CC activation (By similarity). In association with ASH2L and WDR5,
CC stimulates the histone methyltransferase activities of KMT2A, KMT2B,
CC KMT2C, KMT2D, SETD1A and SETD1B (By similarity).
CC {ECO:0000250|UniProtKB:Q15291, ECO:0000269|PubMed:21335234}.
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 (By similarity). Core component of several
CC methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also
CC named ASCOM complex) and MLL4/WBP7 (By similarity). Each complex is at
CC least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific
CC histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and
CC KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8, E2F6,
CC HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1,
CC MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10
CC and alpha- and beta-tubulin (By similarity). Component of a histone
CC methylation complex composed of at least ZNF335, RBBP5, ASH2L and WDR5;
CC the complex may have histone H3-specific methyltransferase activity,
CC however does not have specificity for 'Lys-4' of histone H3 (By
CC similarity). Interacts with ZNF335 (PubMed:23178126). Interacts with
CC ASH2L; the interaction is direct (By similarity). Interacts with WDR5;
CC the interaction is direct (By similarity). Components of the ZNF335-
CC RBBP5-ASH2L-WDR5 histone methylation complex may associate with
CC components of a nuclear receptor-mediated transcription complex to form
CC a complex at least composed of ZNF335, HCFC1, CCAR2, EMSY, MKI67,
CC RBBP5, ASH2L and WDR5 (By similarity). Within this complex interacts
CC with EMSY (By similarity). Found in a complex with RBBP5, ASH2L, DPY30,
CC KMT2A, KMT2D and WDR5 (PubMed:21335234). Interacts with SETD1A (By
CC similarity). Interacts with WDR82 (By similarity).
CC {ECO:0000250|UniProtKB:Q15291, ECO:0000269|PubMed:21335234,
CC ECO:0000269|PubMed:23178126}.
CC -!- INTERACTION:
CC Q8BX09; Q91X20: Ash2l; NbExp=10; IntAct=EBI-1556543, EBI-1556554;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BX09-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BX09-2; Sequence=VSP_038671, VSP_038672;
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DR EMBL; AK049247; BAC33635.1; -; mRNA.
DR EMBL; AK154782; BAE32825.1; -; mRNA.
DR EMBL; AK171177; BAE42295.1; -; mRNA.
DR EMBL; CH466520; EDL39676.1; -; Genomic_DNA.
DR EMBL; BC057632; AAH57632.1; -; mRNA.
DR EMBL; BC060186; AAH60186.2; -; mRNA.
DR CCDS; CCDS15286.1; -. [Q8BX09-1]
DR CCDS; CCDS87875.1; -. [Q8BX09-2]
DR RefSeq; NP_766105.2; NM_172517.2. [Q8BX09-1]
DR PDB; 2XL2; X-ray; 2.40 A; C/D=369-381.
DR PDB; 2XL3; X-ray; 2.70 A; C/E=369-381.
DR PDBsum; 2XL2; -.
DR PDBsum; 2XL3; -.
DR AlphaFoldDB; Q8BX09; -.
DR SMR; Q8BX09; -.
DR BioGRID; 229436; 32.
DR DIP; DIP-61809N; -.
DR IntAct; Q8BX09; 14.
DR MINT; Q8BX09; -.
DR STRING; 10090.ENSMUSP00000141003; -.
DR iPTMnet; Q8BX09; -.
DR PhosphoSitePlus; Q8BX09; -.
DR EPD; Q8BX09; -.
DR MaxQB; Q8BX09; -.
DR PaxDb; Q8BX09; -.
DR PeptideAtlas; Q8BX09; -.
DR PRIDE; Q8BX09; -.
DR ProteomicsDB; 253177; -. [Q8BX09-1]
DR ProteomicsDB; 253178; -. [Q8BX09-2]
DR Antibodypedia; 34563; 301 antibodies from 38 providers.
DR DNASU; 213464; -.
DR Ensembl; ENSMUST00000027700; ENSMUSP00000027700; ENSMUSG00000026439. [Q8BX09-2]
DR Ensembl; ENSMUST00000190997; ENSMUSP00000141003; ENSMUSG00000026439. [Q8BX09-1]
DR GeneID; 213464; -.
DR KEGG; mmu:213464; -.
DR UCSC; uc007cow.2; mouse. [Q8BX09-1]
DR UCSC; uc007coy.2; mouse. [Q8BX09-2]
DR CTD; 5929; -.
DR MGI; MGI:1918367; Rbbp5.
DR VEuPathDB; HostDB:ENSMUSG00000026439; -.
DR eggNOG; KOG1273; Eukaryota.
DR GeneTree; ENSGT00530000064100; -.
DR HOGENOM; CLU_032142_1_0_1; -.
DR InParanoid; Q8BX09; -.
DR OMA; DYEDDIM; -.
DR OrthoDB; 1001705at2759; -.
DR PhylomeDB; Q8BX09; -.
DR TreeFam; TF313289; -.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 213464; 22 hits in 76 CRISPR screens.
DR ChiTaRS; Rbbp5; mouse.
DR EvolutionaryTrace; Q8BX09; -.
DR PRO; PR:Q8BX09; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BX09; protein.
DR Bgee; ENSMUSG00000026439; Expressed in manus and 234 other tissues.
DR ExpressionAtlas; Q8BX09; baseline and differential.
DR Genevisible; Q8BX09; MM.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0044665; C:MLL1/2 complex; ISO:MGI.
DR GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISO:MGI.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IMP:MGI.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR IDEAL; IID50152; -.
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 /evidence="ECO:0000250"
FT /id="PRO_0000390999"
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:0000250|UniProtKB:Q15291"
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:0000250|UniProtKB:Q15291"
FT REGION 408..519
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:0000250|UniProtKB:Q15291"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15291"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15291"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15291"
FT MOD_RES 497
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q15291"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15291"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15291"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038671"
FT VAR_SEQ 492..529
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038672"
FT CONFLICT 243
FT /note="Q -> K (in Ref. 1; BAC33635)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="Missing (in Ref. 1; BAE42295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 59098 MW; 7D4E9FD5B38A7EB0 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
DAVPSSLMDE GASSEKKRQS SADGSQPPKK KPKTTNIELQ GVPNDEVHPL LGVKGDGKSK
KKQAGRPKGS KGKEKDSPFK PKLYKGDRGL PLEGSTKGKV QAELSQSLAA GGAISELL
