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RBBP5 Blocking Peptide (C-term)

Synthetic peptide

     
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Product Information
Primary Accession Q15291
Additional Information
Other Names Retinoblastoma-binding protein 5, RBBP-5, Retinoblastoma-binding protein RBQ-3, RBBP5, RBQ3
Target/Specificity The synthetic peptide sequence is selected from aa 505-539 of HUMAN RBBP5
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name RBBP5
Synonyms RBQ3
Function In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). Does not affect ES cell self-renewal (By similarity). Component or associated component of some histone methyltransferase complexes which regulates transcription through recruitment of those complexes to gene promoters (PubMed:19131338). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3 (PubMed:19556245). Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (PubMed:19556245). In association with ASH2L and WDR5, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B (PubMed:22266653, PubMed:21220120).
Cellular Location Nucleus.
Tissue Location Ubiquitously expressed. EMBL; X85134; CAA59446.1; -; mRNA EMBL; AK290137; BAF82826.1; -; mRNA EMBL; AC093422; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AL583832; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; CH471067; EAW91537.1; -; Genomic_DNA EMBL; CH471067; EAW91538.1; -; Genomic_DNA EMBL; BC037284; AAH37284.1; -; mRNA EMBL; BC053856; AAH53856.1; -; mRNA EMBL; BC075059; AAH75059.1; -; mRNA EMBL; BC075060; AAH75060.1; -; mRNA CCDS; CCDS30983.1; -. [Q15291-1] CCDS; CCDS53463.1; -. [Q15291-2] PIR; A57624; A57624 RefSeq; NP_001180201.1; NM_001193272.1. [Q15291-2] RefSeq; NP_001180202.1; NM_001193273.1 RefSeq; NP_005048.2; NM_005057.3. [Q15291-1] PDB; 3P4F; X-ray; 2.35 A; B=371-381 PDB; 4X8N; X-ray; 2.10 A; B=347-356 PDB; 4X8P; X-ray; 2.20 A; B=344-355 PDB; 5F6K; X-ray; 2.41 A; D/F=330-356 PDB; 5F6L; X-ray; 1.90 A; J=330-356 PDB; 6KIU; EM; 3.20 A; N=1-538 PDB; 6KIV; EM; 4.00 A; N=1-538 PDB; 6KIW; EM; 4.00 A; N=1-538 PDB; 6KIX; EM; 4.10 A; N=1-538 PDB; 6KIZ; EM; 4.50 A; N=1-538 PDB; 6KM7; X-ray; 1.80 A; A/B=10-325, C/D=390-480 PDB; 6PWV; EM; 6.20 A; A=2-538 PDB; 6PWW; EM; 4.40 A; A=2-538 PDB; 6PWX; EM; 4.20 A; A=2-538 PDBsum; 3P4F; - PDBsum; 4X8N; - PDBsum; 4X8P; - PDBsum; 5F6K; - PDBsum; 5F6L; - PDBsum; 6KIU; - PDBsum; 6KIV; - PDBsum; 6KIW; - PDBsum; 6KIX; - PDBsum; 6KIZ; - PDBsum; 6KM7; - PDBsum; 6PWV; - PDBsum; 6PWW; - PDBsum; 6PWX; - SMR; Q15291; - BioGRID; 111864; 112 CORUM; Q15291; - DIP; DIP-29224N; - IntAct; Q15291; 55 MINT; Q15291; - STRING; 9606.ENSP00000264515; - BindingDB; Q15291; - ChEMBL; CHEMBL3137282; - iPTMnet; Q15291; - PhosphoSitePlus; Q15291; - BioMuta; RBBP5; - DMDM; 209572664; - EPD; Q15291; - jPOST; Q15291; - MassIVE; Q15291; - MaxQB; Q15291; - PaxDb; Q15291; - PeptideAtlas; Q15291; - PRIDE; Q15291; - ProteomicsDB; 60517; -. [Q15291-1] ProteomicsDB; 60518; -. [Q15291-2] ABCD; Q15291; 1 sequenced antibody Antibodypedia; 34563; 267 antibodies DNASU; 5929; - Ensembl; ENST00000264515; ENSP00000264515; ENSG00000117222. [Q15291-1] Ensembl; ENST00000367164; ENSP00000356132; ENSG00000117222. [Q15291-2] GeneID; 5929; - KEGG; hsa:5929; - UCSC; uc001hbu.3; human. [Q15291-1] CTD; 5929; - DisGeNET; 5929; - EuPathDB; HostDB:ENSG00000117222.13; - GeneCards; RBBP5; - HGNC; HGNC:9888; RBBP5 HPA; ENSG00000117222; Low tissue specificity MIM; 600697; gene neXtProt; NX_Q15291; - OpenTargets; ENSG00000117222; - PharmGKB; PA34252; - eggNOG; KOG1273; Eukaryota GeneTree; ENSGT00530000064100; - HOGENOM; CLU_032142_1_0_1; - InParanoid; Q15291; - KO; K14961; - OMA; SLSWSRC; - PhylomeDB; Q15291; - TreeFam; TF313289; - PathwayCommons; Q15291; - Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex Reactome; R-HSA-3214841; PKMTs methylate histone lysines Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function Reactome; R-HSA-8951664; Neddylation SignaLink; Q15291; - SIGNOR; Q15291; - BioGRID-ORCS; 5929; 692 hits in 890 CRISPR screens ChiTaRS; RBBP5; human GeneWiki; RBBP5; - GenomeRNAi; 5929; - Pharos; Q15291; Tbio PRO; PR:Q15291; - Proteomes; UP000005640; Chromosome 1 RNAct; Q15291; protein Bgee; ENSG00000117222; Expressed in buccal mucosa cell and 193 other tissues ExpressionAtlas; Q15291; baseline and differential Genevisible; Q15291; HS GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB GO; GO:0044666; C:MLL3/4 complex; IDA:UniProtKB GO; GO:0005730; C:nucleolus; IDA:HPA GO; GO:0005654; C:nucleoplasm; IDA:HPA GO; GO:0005634; C:nucleus; IDA:UniProtKB GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB GO; GO:0043687; P:post-translational protein modification; TAS:Reactome GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome GO; GO:0043627; P:response to estrogen; IDA:UniProtKB Gene3D; 2.130.10.10; -; 1 IDEAL; IID00387; - InterPro; IPR037850; RBBP5/Swd1 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf InterPro; IPR001680; WD40_repeat InterPro; IPR017986; WD40_repeat_dom PANTHER; PTHR44040; PTHR44040; 1 Pfam; PF00400; WD40; 1 SMART; SM00320; WD40; 5 PROSITE; PS50082; WD_REPEATS_2; 1 PROSITE; PS50294; WD_REPEATS_REGION; 1 1: Evidence at protein level; 3D-structure; Alternative splicing; Chromatin regulator; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation; WD repeat CHAIN 1..538 /note="Retinoblastoma-binding protein 5" /id="PRO_0000051194" REPEAT 22..63 /note="WD 1" REPEAT 64..103 /note="WD 2" REPEAT 148..188 /note="WD 3" REPEAT 196..235 /note="WD 4" REPEAT 249..291 /note="WD 5" REPEAT 293..331 /note="WD 6" REGION 330..366 /note="Interaction with ASH2L" /evidence="ECO:0000269|PubMed:21220120" REGION 371..380 /note="Interaction with WDR5" /evidence="ECO:0000269|PubMed:21220120" MOD_RES 252 /note="Phosphothreonine; by CDK1" /evidence="ECO:0000269|PubMed:7558034" MOD_RES 350 /note="Phosphoserine" /evidence="ECO:0000244|PubMed:17081983" MOD_RES 388 /note="Phosphoserine" /evidence="ECO:0000244|PubMed:20068231" MOD_RES 389 /note="Phosphoserine" /evidence="ECO:0000244|PubMed:20068231" MOD_RES 497 /note="Phosphoserine; by CDK1" /evidence="ECO:0000269|PubMed:7558034" MOD_RES 525 /note="Phosphoserine" /evidence="ECO:0000244|PubMed:21406692" CROSSLNK 129 /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)" /evidence="ECO:0000244|PubMed:28112733" VAR_SEQ 492..529 /note="Missing (in isoform 2)" /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" /id="VSP_035583" MUTAGEN 374 /note="E->A: Significant reduction in its ability to stimulate KMT2A methyltransferase activity in association with WDR5 and ASH2L." /evidence="ECO:0000269|PubMed:21220120" MUTAGEN 375 /note="V->E: Significant reduction in its ability to stimulate KMT2A methyltransferase activity in association with WDR5 and ASH2L." /evidence="ECO:0000269|PubMed:21220120" MUTAGEN 376 /note="D->A: Reduced ability to stimulate KMT2A methyltransferase activity in association with WDR5 and ASH2L." /evidence="ECO:0000269|PubMed:21220120" MUTAGEN 377 /note="V->E: Reduced ability to stimulate KMT2A methyltransferase activity in association with WDR5 and ASH2L." /evidence="ECO:0000269|PubMed:21220120" CONFLICT 206 /note="F -> Y (in Ref. 2; BAF82826)" /evidence="ECO:0000305" CONFLICT 244 /note="K -> E (in Ref. 1; CAA59446)" /evidence="ECO:0000305" CONFLICT 351 /note="E -> G (in Ref. 1; CAA59446)" /evidence="ECO:0000305" STRAND 16..21 /evidence="ECO:0000244|PDB:6KM7" STRAND 23..25 /evidence="ECO:0000244|PDB:6KIU" STRAND 27..32 /evidence="ECO:0000244|PDB:6KM7" STRAND 36..43 /evidence="ECO:0000244|PDB:6KM7" STRAND 46..52 /evidence="ECO:0000244|PDB:6KM7" TURN 53..56 /evidence="ECO:0000244|PDB:6KM7" STRAND 57..63 /evidence="ECO:0000244|PDB:6KM7" STRAND 69..74 /evidence="ECO:0000244|PDB:6KM7" STRAND 78..85 /evidence="ECO:0000244|PDB:6KM7" STRAND 88..94 /evidence="ECO:0000244|PDB:6KM7" TURN 95..97 /evidence="ECO:0000244|PDB:6KM7" STRAND 100..105 /evidence="ECO:0000244|PDB:6KM7" STRAND 110..116 /evidence="ECO:0000244|PDB:6KM7" STRAND 119..127 /evidence="ECO:0000244|PDB:6KM7" STRAND 133..136 /evidence="ECO:0000244|PDB:6KM7" TURN 137..140 /evidence="ECO:0000244|PDB:6KM7" STRAND 141..144 /evidence="ECO:0000244|PDB:6KM7" STRAND 155..159 /evidence="ECO:0000244|PDB:6KM7" STRAND 163..170 /evidence="ECO:0000244|PDB:6KM7" STRAND 174..179 /evidence="ECO:0000244|PDB:6KM7" TURN 180..182 /evidence="ECO:0000244|PDB:6KM7" STRAND 185..190 /evidence="ECO:0000244|PDB:6KM7" STRAND 194..196 /evidence="ECO:0000244|PDB:6KIU" STRAND 201..206 /evidence="ECO:0000244|PDB:6KM7" STRAND 208..217 /evidence="ECO:0000244|PDB:6KM7" STRAND 222..226 /evidence="ECO:0000244|PDB:6KM7" HELIX 227..233 /evidence="ECO:0000244|PDB:6KM7" STRAND 242..245 /evidence="ECO:0000244|PDB:6KM7" TURN 248..250 /evidence="ECO:0000244|PDB:6KM7" STRAND 254..259 /evidence="ECO:0000244|PDB:6KM7" STRAND 263..280 /evidence="ECO:0000244|PDB:6KM7" TURN 281..283 /evidence="ECO:0000244|PDB:6KM7" STRAND 286..291 /evidence="ECO:0000244|PDB:6KM7" STRAND 298..303 /evidence="ECO:0000244|PDB:6KM7" STRAND 305..308 /evidence="ECO:0000244|PDB:6KM7" STRAND 310..314 /evidence="ECO:0000244|PDB:6KM7" STRAND 317..322 /evidence="ECO:0000244|PDB:6KM7" STRAND 329..332 /evidence="ECO:0000244|PDB:6KIU" TURN 349..352 /evidence="ECO:0000244|PDB:5F6L" STRAND 453..456 /evidence="ECO:0000244|PDB:6KM7" TURN 469..471 /evidence="ECO:0000244|PDB:6KM7" 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
Research Areas
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Background

In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation.

References

Saijo M.,et al.Genomics 27:511-519(1995).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Gregory S.G.,et al.Nature 441:315-321(2006).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Hughes C.M.,et al.Mol. Cell 13:587-597(2004).

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