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Q09028 (RBBP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-binding protein RBBP4
Alternative name(s):
Chromatin assembly factor 1 subunit C
Short name=CAF-1 subunit C
Chromatin assembly factor I p48 subunit
Short name=CAF-I 48 kDa subunit
Short name=CAF-I p48
Nucleosome-remodeling factor subunit RBAP48
Retinoblastoma-binding protein 4
Short name=RBBP-4
Retinoblastoma-binding protein p48
Gene names
Name:RBBP4
Synonyms:RBAP48
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. Ref.23

Subunit structure

Interacts with SUV39H1 and HDAC7 By similarity. Binds directly to helix 1 of the histone fold of histone H4, a region that is not accessible when H4 is in chromatin. Subunit of the chromatin assembly factor 1 (CAF-1) complex, which is composed of RBBP4, CHAF1B and CHAF1A. Subunit of the core histone deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core HDAC complex associates with SIN3A, ARID4B/SAP180, SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex. The core HDAC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylase complex (the NuRD complex). The NuRD complex may also interact with MBD3L1 and MBD3L2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex, which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12. The PRC2/EED-EZH2 complex may also associate with HDAC1. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. Part of the nucleosome remodeling factor (NURF) complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the viral protein-binding domain of the retinoblastoma protein (RB1). Interacts with SPEN/MINT. Interacts with BRCA1. Interacts with CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with PHF6. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.42

Subcellular location

Nucleus.

Sequence similarities

Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.

Contains 6 WD repeats.

Ontologies

Keywords
   Biological processCell cycle
DNA replication
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.30. Source: GOC

ATP-dependent chromatin remodeling

Inferred from direct assay PubMed 16217013. Source: UniProt

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

DNA replication-dependent nucleosome assembly

Inferred from direct assay PubMed 14718166. Source: UniProt

DNA replication-independent nucleosome assembly

Inferred from direct assay PubMed 14718166. Source: UniProt

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

centromere-specific nucleosome assembly

Traceable author statement. Source: Reactome

chromatin assembly

Inferred from direct assay Ref.12. Source: UniProtKB

chromatin remodeling

Inferred from direct assay Ref.30. Source: HGNC

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Traceable author statement Ref.1. Source: ProtInc

nucleosome assembly

Traceable author statement. Source: Reactome

regulation of cell cycle

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCAF-1 complex

Inferred from direct assay Ref.12. Source: UniProtKB

ESC/E(Z) complex

Inferred from direct assay PubMed 20075857PubMed 23104054PubMed 23273982. Source: UniProtKB

NURF complex

Inferred from direct assay PubMed 20850016. Source: UniProtKB

NuRD complex

Inferred from direct assay PubMed 19644445. Source: UniProtKB

Sin3 complex

Non-traceable author statement PubMed 17827154. Source: BHF-UCL

nuclear chromatin

Inferred from direct assay PubMed 14718166PubMed 16217013. Source: UniProt

nucleoplasm

Inferred from direct assay PubMed 22720776. Source: UniProt

nucleus

Inferred from direct assay Ref.30. Source: HGNC

protein complex

Inferred from direct assay PubMed 14718166PubMed 16217013. Source: UniProt

   Molecular_functionhistone binding

Non-traceable author statement PubMed 17827154. Source: BHF-UCL

histone deacetylase binding

Inferred from physical interaction PubMed 17827154. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q09028-1)

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.
Isoform 2 (identifier: Q09028-2)

The sequence of this isoform differs from the canonical sequence as follows:
     7-7: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q09028-3)

The sequence of this isoform differs from the canonical sequence as follows:
     405-425: AENIYNDEDPEGSVDPEGQGS → ELVLDH
Note: No experimental confirmation available.
Isoform 4 (identifier: Q09028-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 425424Histone-binding protein RBBP4
PRO_0000051186

Regions

Repeat122 – 15534WD 1
Repeat175 – 20632WD 2
Repeat225 – 25632WD 3
Repeat271 – 30232WD 4
Repeat315 – 34632WD 5
Repeat372 – 40332WD 6

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.36 Ref.38 Ref.40 Ref.41
Modified residue41N6-acetyllysine; alternate Ref.38
Modified residue1101Phosphoserine Ref.37
Modified residue1601N6-acetyllysine By similarity
Cross-link4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Natural variations

Alternative sequence1 – 3535Missing in isoform 4.
VSP_040087
Alternative sequence71Missing in isoform 2.
VSP_040088
Alternative sequence405 – 42521AENIY…EGQGS → ELVLDH in isoform 3.
VSP_040089

Experimental info

Sequence conflict611F → G in AAH15123. Ref.8

Secondary structure

........................................................................... 425
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B71E2D55A444C360

FASTA42547,656
        10         20         30         40         50         60 
MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPEGKD 

        70         80         90        100        110        120 
FSIHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS EKGEFGGFGS VSGKIEIEIK 

       130        140        150        160        170        180 
INHEGEVNRA RYMPQNPCII ATKTPSSDVL VFDYTKHPSK PDPSGECNPD LRLRGHQKEG 

       190        200        210        220        230        240 
YGLSWNPNLS GHLLSASDDH TICLWDISAV PKEGKVVDAK TIFTGHTAVV EDVSWHLLHE 

       250        260        270        280        290        300 
SLFGSVADDQ KLMIWDTRSN NTSKPSHSVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL 

       310        320        330        340        350        360 
WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI GEEQSPEDAE 

       370        380        390        400        410        420 
DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ VWQMAENIYN DEDPEGSVDP 


EGQGS 

« Hide

Isoform 2 [UniParc].

Checksum: 52055B5C74BCF3D8
Show »

FASTA42447,585
Isoform 3 [UniParc].

Checksum: 59B630D6055A70B2
Show »

FASTA41046,158
Isoform 4 [UniParc].

Checksum: A61A43F6AC30C8CE
Show »

FASTA39043,482

References

« Hide 'large scale' references
[1]"A retinoblastoma-binding protein related to a negative regulator of Ras in yeast."
Qian Y.-W., Wang Y.-C.J., Hollingsworth R.E. Jr., Jones D., Ling N., Lee E.Y.-H.P.
Nature 364:648-652(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 134-158 AND 254-271.
[2]"Molecular cloning and expression of two novel human cDNAs encoding proteins containing WD-40 repeats and sharing similarity to yeast MSI1 a negative regulation of the RAS-cAMP pathway."
Nielsen M.S., Rasmussen H.H., Celis J.E., Leffers H.
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
Tissue: Brain.
[5]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Liver.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 1).
Tissue: Bone marrow, Brain, Eye and Uterus.
[9]Bienvenut W.V.
Submitted (FEB-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-15 AND 297-304, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[10]"Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes."
Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 11:528-536(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 60-65; 144-160 AND 221-240.
Tissue: Keratinocyte.
[11]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 60-65; 144-160 AND 221-240.
Tissue: Keratinocyte.
[12]"Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4."
Verreault A., Kaufman P.D., Kobayashi R., Stillman B.
Cell 87:95-104(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE CAF-1 COMPLEX, INTERACTION WITH HISTONE H4.
[13]"Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex."
Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.
Cell 89:357-364(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
[14]"Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast."
Qian Y.-W., Lee E.Y.-H.P.
J. Biol. Chem. 270:25507-25513(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RB1.
[15]"A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p."
Taunton J., Hassig C.A., Schreiber S.L.
Science 272:408-411(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC1.
[16]"The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities."
Zhang Y., LeRoy G., Seelig H.-P., Lane W.S., Reinberg D.
Cell 95:279-289(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NURD COMPLEX.
[17]"Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase."
Verreault A., Kaufman P.D., Kobayashi R., Stillman B.
Curr. Biol. 8:96-108(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HISTONE H4.
[18]"SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex."
Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P., Hampsey M., Reinberg D.
Mol. Cell 1:1021-1031(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
[19]"A role for histone deacetylase activity in HDAC1-mediated transcriptional repression."
Hassig C.A., Tong J.K., Fleischer T.C., Owa T., Grable P.G., Ayer D.E., Schreiber S.L.
Proc. Natl. Acad. Sci. U.S.A. 95:3519-3524(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC1.
[20]"Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation."
Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A., Reinberg D.
Genes Dev. 13:1924-1935(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NURD COMPLEX.
[21]"BRCA1 interacts with components of the histone deacetylase complex."
Yarden R.I., Brody L.C.
Proc. Natl. Acad. Sci. U.S.A. 96:4983-4988(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRCA1.
[22]"RbAp48 belongs to the histone deacetylase complex that associates with the retinoblastoma protein."
Nicolas E., Morales V., Magnaghi-Jaulin L., Harel-Bellan A., Richard-Foy H., Trouche D.
J. Biol. Chem. 275:9797-9804(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC1 AND RB1.
[23]"Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB."
Zhang Q., Vo N., Goodman R.H.
Mol. Cell. Biol. 20:4970-4978(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CREBBP.
[24]"Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPEN.
[25]"Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1."
Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H.
J. Biol. Chem. 276:6817-6824(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NURD COMPLEX.
[26]"Differential association of products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex."
Skowyra D., Zeremski M., Neznanov N., Li M., Choi Y., Uesugi M., Hauser C.A., Gu W., Gudkov A.V., Qin J.
J. Biol. Chem. 276:8734-8739(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A SIN3 HDAC COMPLEX.
[27]"Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein."
Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D.
Genes Dev. 16:2893-2905(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH EED; EZH2; RBBP7 AND SUZ12, TRANSIENT INTERACTION WITH HDAC1, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
[28]"Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)."
Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.
Mol. Cell. Biol. 22:835-848(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN MULTIPLE SIN3 HDAC COMPLEXES.
[29]"Role of histone H3 lysine 27 methylation in Polycomb-group silencing."
Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y.
Science 298:1039-1043(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH AEBP2; EED; EZH2 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
[30]"Isolation of human NURF: a regulator of Engrailed gene expression."
Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J., Shiekhattar R.
EMBO J. 22:6089-6100(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NURF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[31]"The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity."
Yao Y.-L., Yang W.-M.
J. Biol. Chem. 278:42560-42568(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MTA1.
[32]"MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex."
Jiang C.-L., Jin S.-G., Pfeifer G.P.
J. Biol. Chem. 279:52456-52464(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MBD3L1.
[33]"MBD3L2 interacts with MBD3 and components of the NuRD complex and can oppose MBD2-MeCP1-mediated methylation silencing."
Jin S.-G., Jiang C.-L., Rauch T., Li H., Pfeifer G.P.
J. Biol. Chem. 280:12700-12709(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MBD3L2.
[34]"LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes."
Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.
Cell Cycle 6:1903-1913(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[35]"Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence."
Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.
Mol. Cell 26:539-551(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[36]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[38]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]"Structural and functional insights into the human Borjeson-Forssman-Lehmann syndrome-associated protein PHF6."
Liu Z., Li F., Ruan K., Zhang J., Mei Y., Wu J., Shi Y.
J. Biol. Chem. 289:10069-10083(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PHF6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74262 mRNA. Translation: CAA52321.1.
X71810 mRNA. Translation: CAA50685.1.
BT007309 mRNA. Translation: AAP35973.1.
AK299251 mRNA. Translation: BAG61282.1.
AK312571 mRNA. Translation: BAG35466.1.
AK222779 mRNA. Translation: BAD96499.1.
AC114489 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX07513.1.
CH471059 Genomic DNA. Translation: EAX07514.1.
BC003092 mRNA. Translation: AAH03092.1.
BC015123 mRNA. Translation: AAH15123.1.
BC053904 mRNA. Translation: AAH53904.1.
BC075836 mRNA. Translation: AAH75836.1.
CCDSCCDS366.1. [Q09028-1]
CCDS44105.1. [Q09028-2]
CCDS44106.1. [Q09028-4]
PIRS36112.
RefSeqNP_001128727.1. NM_001135255.1. [Q09028-2]
NP_001128728.1. NM_001135256.1. [Q09028-4]
NP_005601.1. NM_005610.2. [Q09028-1]
UniGeneHs.16003.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XU7X-ray1.90A/B1-425[»]
3GFCX-ray2.30A1-425[»]
ProteinModelPortalQ09028.
SMRQ09028. Positions 11-410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111863. 148 interactions.
DIPDIP-33495N.
IntActQ09028. 55 interactions.
MINTMINT-90543.
STRING9606.ENSP00000362592.

PTM databases

PhosphoSiteQ09028.

Polymorphism databases

DMDM1172846.

Proteomic databases

MaxQBQ09028.
PaxDbQ09028.
PRIDEQ09028.

Protocols and materials databases

DNASU5928.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373485; ENSP00000362584; ENSG00000162521. [Q09028-3]
ENST00000373493; ENSP00000362592; ENSG00000162521. [Q09028-1]
ENST00000414241; ENSP00000398242; ENSG00000162521. [Q09028-2]
ENST00000458695; ENSP00000396057; ENSG00000162521. [Q09028-4]
GeneID5928.
KEGGhsa:5928.
UCSCuc001bvr.3. human. [Q09028-1]
uc001bvs.3. human. [Q09028-2]

Organism-specific databases

CTD5928.
GeneCardsGC01P033116.
HGNCHGNC:9887. RBBP4.
HPACAB006264.
MIM602923. gene.
neXtProtNX_Q09028.
PharmGKBPA34251.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOVERGENHBG053236.
InParanoidQ09028.
KOK10752.
OMACQPDLRL.
OrthoDBEOG70PBXB.
PhylomeDBQ09028.
TreeFamTF106485.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_71. Gene Expression.
SignaLinkQ09028.

Gene expression databases

ArrayExpressQ09028.
BgeeQ09028.
CleanExHS_RBBP4.
GenevestigatorQ09028.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBBP4. human.
EvolutionaryTraceQ09028.
GeneWikiRBBP4.
GenomeRNAi5928.
NextBio23094.
PROQ09028.
SOURCESearch...

Entry information

Entry nameRBBP4_HUMAN
AccessionPrimary (citable) accession number: Q09028
Secondary accession number(s): B2R6G9 expand/collapse secondary AC list , B4DRH0, D3DPQ3, P31149, Q53H02, Q96BV9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM