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Protein

Retinoblastoma-binding protein 5

Gene

Rbbp5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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. Does not affect ES cell self-renewal.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-201722. Formation of the beta-catenin:TCF transactivating complex.
R-MMU-3214841. PKMTs methylate histone lysines.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoblastoma-binding protein 5
Short name:
RBBP-5
Gene namesi
Name:Rbbp5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1918367. Rbbp5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Retinoblastoma-binding protein 5By similarityPRO_0000390999Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei252 – 2521Phosphothreonine; by CDK1By similarity
Modified residuei350 – 3501PhosphoserineBy similarity
Modified residuei388 – 3881PhosphoserineBy similarity
Modified residuei389 – 3891PhosphoserineBy similarity
Modified residuei497 – 4971Phosphoserine; by CDK1By similarity
Modified residuei525 – 5251PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BX09.
MaxQBiQ8BX09.
PaxDbiQ8BX09.
PeptideAtlasiQ8BX09.
PRIDEiQ8BX09.

PTM databases

iPTMnetiQ8BX09.
PhosphoSiteiQ8BX09.

Expressioni

Gene expression databases

BgeeiQ8BX09.
ExpressionAtlasiQ8BX09. baseline and differential.
GenevisibleiQ8BX09. MM.

Interactioni

Subunit structurei

Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, CFC1 and DPY30 (By similarity). Interacts with WDR82 and SETD1A (By similarity). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (By similarity). Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, DPY30, WDR5, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Interacts with ZNF335.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ash2lQ91X207EBI-1556543,EBI-1556554

GO - Molecular functioni

Protein-protein interaction databases

BioGridi229436. 12 interactions.
DIPiDIP-61809N.
IntActiQ8BX09. 12 interactions.
MINTiMINT-4113307.
STRINGi10090.ENSMUSP00000027700.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XL2X-ray2.40C/D369-381[»]
2XL3X-ray2.70C/E369-381[»]
ProteinModelPortaliQ8BX09.
SMRiQ8BX09. Positions 30-320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8BX09.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati22 – 6342WD 1Add
BLAST
Repeati64 – 10340WD 2Add
BLAST
Repeati148 – 18841WD 3Add
BLAST
Repeati196 – 23540WD 4Add
BLAST
Repeati249 – 29143WD 5Add
BLAST
Repeati293 – 33139WD 6Add
BLAST

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1273. Eukaryota.
ENOG410XTA2. LUCA.
GeneTreeiENSGT00530000064100.
HOGENOMiHOG000204856.
HOVERGENiHBG054324.
InParanoidiQ8BX09.
KOiK14961.
OMAiEQGVIEW.
OrthoDBiEOG7S21X6.
PhylomeDBiQ8BX09.
TreeFamiTF313289.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BX09-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNLELLESFG QNYPEEADGT LDCISMALTC TFNRWGTLLA VGCNDGRIVI
60 70 80 90 100
WDFLTRGIAK IISAHIHPVC SLCWSRDGHK LVSASTDNIV SQWDVLSGDC
110 120 130 140 150
DQRFRFPSPI LKVQYHPRDQ NKVLVCPMKS APVMLTLSDS KHVVLPVDDD
160 170 180 190 200
SDLNVVASFD RRGEYIYTGN AKGKILVLKT DSQDLVASFR VTTGTSNTTA
210 220 230 240 250
IKSIEFARKG SCFLINTADR IIRVYDGREI LTCGRDGEPE PMQKLQDLVN
260 270 280 290 300
RTPWKKCCFS GDGEYIVAGS ARQHALYIWE KSIGNLVKIL HGTRGELLLD
310 320 330 340 350
VAWHPVRPII ASISSGVVSI WAQNQVENWS AFAPDFKELD ENVEYEERES
360 370 380 390 400
EFDIEDEDKS EPEQTGADAA EDEEVDVTSV DPIAAFCSSD EELEDSKALL
410 420 430 440 450
YLPIAPEVED PEENPYGPPP DAVPSSLMDE GASSEKKRQS SADGSQPPKK
460 470 480 490 500
KPKTTNIELQ GVPNDEVHPL LGVKGDGKSK KKQAGRPKGS KGKEKDSPFK
510 520 530
PKLYKGDRGL PLEGSTKGKV QAELSQSLAA GGAISELL
Length:538
Mass (Da):59,098
Last modified:January 19, 2010 - v2
Checksum:i7D4E9FD5B38A7EB0
GO
Isoform 2 (identifier: Q8BX09-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.
     492-529: Missing.

Note: No experimental confirmation available.
Show »
Length:373
Mass (Da):40,764
Checksum:iD5BD12F61C597B19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 2431Q → K in BAC33635 (PubMed:16141072).Curated
Sequence conflicti529 – 5291Missing in BAE42295 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 127127Missing in isoform 2. 1 PublicationVSP_038671Add
BLAST
Alternative sequencei492 – 52938Missing in isoform 2. 1 PublicationVSP_038672Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK049247 mRNA. Translation: BAC33635.1.
AK154782 mRNA. Translation: BAE32825.1.
AK171177 mRNA. Translation: BAE42295.1.
CH466520 Genomic DNA. Translation: EDL39676.1.
BC057632 mRNA. Translation: AAH57632.1.
BC060186 mRNA. Translation: AAH60186.2.
CCDSiCCDS15286.1. [Q8BX09-1]
RefSeqiNP_766105.2. NM_172517.2. [Q8BX09-1]
UniGeneiMm.132868.

Genome annotation databases

EnsembliENSMUST00000027700; ENSMUSP00000027700; ENSMUSG00000026439. [Q8BX09-2]
ENSMUST00000190997; ENSMUSP00000141003; ENSMUSG00000026439. [Q8BX09-1]
GeneIDi213464.
KEGGimmu:213464.
UCSCiuc007cow.2. mouse. [Q8BX09-1]
uc007coy.2. mouse. [Q8BX09-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK049247 mRNA. Translation: BAC33635.1.
AK154782 mRNA. Translation: BAE32825.1.
AK171177 mRNA. Translation: BAE42295.1.
CH466520 Genomic DNA. Translation: EDL39676.1.
BC057632 mRNA. Translation: AAH57632.1.
BC060186 mRNA. Translation: AAH60186.2.
CCDSiCCDS15286.1. [Q8BX09-1]
RefSeqiNP_766105.2. NM_172517.2. [Q8BX09-1]
UniGeneiMm.132868.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XL2X-ray2.40C/D369-381[»]
2XL3X-ray2.70C/E369-381[»]
ProteinModelPortaliQ8BX09.
SMRiQ8BX09. Positions 30-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229436. 12 interactions.
DIPiDIP-61809N.
IntActiQ8BX09. 12 interactions.
MINTiMINT-4113307.
STRINGi10090.ENSMUSP00000027700.

PTM databases

iPTMnetiQ8BX09.
PhosphoSiteiQ8BX09.

Proteomic databases

EPDiQ8BX09.
MaxQBiQ8BX09.
PaxDbiQ8BX09.
PeptideAtlasiQ8BX09.
PRIDEiQ8BX09.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027700; ENSMUSP00000027700; ENSMUSG00000026439. [Q8BX09-2]
ENSMUST00000190997; ENSMUSP00000141003; ENSMUSG00000026439. [Q8BX09-1]
GeneIDi213464.
KEGGimmu:213464.
UCSCiuc007cow.2. mouse. [Q8BX09-1]
uc007coy.2. mouse. [Q8BX09-2]

Organism-specific databases

CTDi5929.
MGIiMGI:1918367. Rbbp5.

Phylogenomic databases

eggNOGiKOG1273. Eukaryota.
ENOG410XTA2. LUCA.
GeneTreeiENSGT00530000064100.
HOGENOMiHOG000204856.
HOVERGENiHBG054324.
InParanoidiQ8BX09.
KOiK14961.
OMAiEQGVIEW.
OrthoDBiEOG7S21X6.
PhylomeDBiQ8BX09.
TreeFamiTF313289.

Enzyme and pathway databases

ReactomeiR-MMU-201722. Formation of the beta-catenin:TCF transactivating complex.
R-MMU-3214841. PKMTs methylate histone lysines.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Miscellaneous databases

EvolutionaryTraceiQ8BX09.
PROiQ8BX09.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BX09.
ExpressionAtlasiQ8BX09. baseline and differential.
GenevisibleiQ8BX09. MM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J and NMRI.
    Tissue: Brain and Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Spleen and Testis.
  5. "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains."
    Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.
    Cell 144:513-525(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE MLL COMPLEX, INTERACTION WITH ASH2L; DPY30; KMT2A; KMT2D AND WDR5.
  6. Cited for: INTERACTION WITH ZNF335.

Entry informationi

Entry nameiRBBP5_MOUSE
AccessioniPrimary (citable) accession number: Q8BX09
Secondary accession number(s): Q3TBL4
, Q3U3G1, Q6PAP0, Q6PFC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: January 19, 2010
Last modified: July 6, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.