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Protein

Retinoblastoma-binding protein 5 homolog

Gene

Rbbp5

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of the SET1 complex that specifically di- and trimethylates 'Lys-4' of histone H3 and of the MLL3/4 complex which also methylates histone H3 'Lys-4'.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-DME-201722. Formation of the beta-catenin:TCF transactivating complex.
R-DME-3214841. PKMTs methylate histone lysines.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoblastoma-binding protein 5 homologBy similarity
Gene namesi
Name:Rbbp5Imported
ORF Names:CG5585
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036973. Rbbp5.

Subcellular locationi

GO - Cellular componenti

  • MLL1/2 complex Source: FlyBase
  • MLL3/4 complex Source: FlyBase
  • Set1C/COMPASS complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 489489Retinoblastoma-binding protein 5 homologPRO_0000429381Add
BLAST

Proteomic databases

PaxDbiQ9VPH8.
PeptideAtlasiQ9VPH8.

Expressioni

Gene expression databases

GenevisibleiQ9VPH8. DM.

Interactioni

Subunit structurei

Core component of several methyltransferase-containing complexes. Component of the SET1 complex, composed at least of the catalytic subunit Set1, wds/WDR5, Wdr82, Rbbp5, ash2, Cfp1/CXXC1, hcf and Dpy-30L1. Component of the MLL3/4 complex composed at least of the catalytic subunit trr, ash2, Rbbp5, Dpy-30L1, wds, hcf, ptip, Pa1, Utx, Lpt and Ncoa6.2 Publications

Protein-protein interaction databases

BioGridi65500. 2 interactions.
IntActiQ9VPH8. 2 interactions.
MINTiMINT-833391.
STRINGi7227.FBpp0077900.

Structurei

3D structure databases

ProteinModelPortaliQ9VPH8.
SMRiQ9VPH8. Positions 30-311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati22 – 6342WD 1Sequence analysisAdd
BLAST
Repeati64 – 10340WD 2Sequence analysisAdd
BLAST
Repeati147 – 18741WD 3Sequence analysisAdd
BLAST
Repeati195 – 23440WD 4Sequence analysisAdd
BLAST
Repeati248 – 29043WD 5Sequence analysisAdd
BLAST
Repeati292 – 33039WD 6Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1273. Eukaryota.
ENOG410XTA2. LUCA.
GeneTreeiENSGT00530000064100.
InParanoidiQ9VPH8.
KOiK14961.
OMAiEQGVIEW.
OrthoDBiEOG7S21X6.
PhylomeDBiQ9VPH8.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VPH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLELLESFG QNYPEEFDGS LDCISLAVTC AFNKYGTLLA VGCNDGRIVI
60 70 80 90 100
WDFLTRGIAK IISAHVHPVC SLSWTRNGHK LLSASTDNNV CIWDVLTGEL
110 120 130 140 150
EHKYRFPSPV LKVQFDPRND NRLLVCPMRY AAVLVEVGGT HRCLPLDSDG
160 170 180 190 200
DLNIVASFDR RGKHIYTGNA KGKILVLDVE TFEVVASFRI IVGTSSATAV
210 220 230 240 250
KSIEFARRGD AFLINTSDRV IRVYDSKEII TLGKDGEPEP IQKLQDLVNK
260 270 280 290 300
TTWKKCCFSG DGEYICAGSA RQHALYIWEK SIGNLVKILH GTKGELLLDV
310 320 330 340 350
VWHPVRPIIA SISSGLVSIW AQNQVENWSA FAPDFKELDE NVEYEERESE
360 370 380 390 400
FDIADEDKSV DLNADAQQDE EIEVDVQKVE PVAAFCSSDE EGEDENALQF
410 420 430 440 450
LPMAPEVEDP EDGWTGQDGL EPSAVMLGHM EPHDYEDDIM ASKRRRMQLY
460 470 480
DVSLPDAPTD ETHPLISSKA SKDKQQPVGG KKAAGRTKK
Length:489
Mass (Da):54,406
Last modified:March 1, 2001 - v2
Checksum:iE959B7F5AA053858
GO

Sequence cautioni

The sequence ACD81779.1 differs from that shown. Reason: Frameshift at position 207. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF51573.2.
AY071120 mRNA. Translation: AAL48742.1.
BT032759 mRNA. Translation: ACD81773.1.
BT032765 mRNA. Translation: ACD81779.1. Frameshift.
RefSeqiNP_649209.1. NM_140952.3.
UniGeneiDm.6107.

Genome annotation databases

EnsemblMetazoaiFBtr0078242; FBpp0077900; FBgn0036973.
GeneIDi40239.
KEGGidme:Dmel_CG5585.
UCSCiCG5585-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF51573.2.
AY071120 mRNA. Translation: AAL48742.1.
BT032759 mRNA. Translation: ACD81773.1.
BT032765 mRNA. Translation: ACD81779.1. Frameshift.
RefSeqiNP_649209.1. NM_140952.3.
UniGeneiDm.6107.

3D structure databases

ProteinModelPortaliQ9VPH8.
SMRiQ9VPH8. Positions 30-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65500. 2 interactions.
IntActiQ9VPH8. 2 interactions.
MINTiMINT-833391.
STRINGi7227.FBpp0077900.

Proteomic databases

PaxDbiQ9VPH8.
PeptideAtlasiQ9VPH8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078242; FBpp0077900; FBgn0036973.
GeneIDi40239.
KEGGidme:Dmel_CG5585.
UCSCiCG5585-RA. d. melanogaster.

Organism-specific databases

CTDi5929.
FlyBaseiFBgn0036973. Rbbp5.

Phylogenomic databases

eggNOGiKOG1273. Eukaryota.
ENOG410XTA2. LUCA.
GeneTreeiENSGT00530000064100.
InParanoidiQ9VPH8.
KOiK14961.
OMAiEQGVIEW.
OrthoDBiEOG7S21X6.
PhylomeDBiQ9VPH8.

Enzyme and pathway databases

ReactomeiR-DME-201722. Formation of the beta-catenin:TCF transactivating complex.
R-DME-3214841. PKMTs methylate histone lysines.

Miscellaneous databases

GenomeRNAii40239.
PROiQ9VPH8.

Gene expression databases

GenevisibleiQ9VPH8. DM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  4. Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  5. "Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with role in transcription."
    Ardehali M.B., Mei A., Zobeck K.L., Caron M., Lis J.T., Kusch T.
    EMBO J. 30:2817-2828(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SET1 COMPLEX, SUBCELLULAR LOCATION.
  6. Cited for: FUNCTION, IDENTIFICATION IN THE SET1 AND MLL3/4 COMPLEXES.

Entry informationi

Entry nameiRBBP5_DROME
AccessioniPrimary (citable) accession number: Q9VPH8
Secondary accession number(s): B3DMX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 11, 2014
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.