Reviewed, UniProtKB/Swiss-Prot Q16576 (RBBP7_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone-binding protein RBBP7
Alternative name(s):
    Retinoblastoma-binding protein 7
      Short name=RBBP-7
    Retinoblastoma-binding protein p46
    Histone acetyltransferase type B subunit 2
    Nucleosome-remodeling factor subunit RBAP46

Gene names

Name:	RBBP7
Synonyms:	RBAP46

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases 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 type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; 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; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.
Subunit structure	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 type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. 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, SDS3/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. 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 CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP. Interacts with BRCA1, HDAC7 and SUV39H1.
Subcellular location	Nucleus.
Sequence similarities	Belongs to the WD repeat RBAP46/RBAP48/MSI1 family. Contains 6 WD repeats.

Ontologies

Keywords
Biological process	DNA replication Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat WD repeat
Molecular function	Chromatin regulator Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Ref.1 Traceable author statement. Source: ProtInc chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Ref.1 Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Ref.3 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HDAC1	Q13547	1	EBI-352227,EBI-301834

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 425	425	Histone-binding protein RBBP7		PRO_0000051195
Regions
	Repeat	121 – 152	32	WD 1
	Repeat	174 – 205	32	WD 2
	Repeat	224 – 255	32	WD 3
	Repeat	270 – 301	32	WD 4
	Repeat	314 – 345	32	WD 5
	Repeat	371 – 402	32	WD 6
Amino acid modifications
	Modified residue	119	1	N6-acetyllysine
	Modified residue	354	1	Phosphoserine
	Modified residue	413	1	Phosphoserine
	Modified residue	416	1	Phosphothreonine

Sequences

	Sequence		Length	Mass (Da)
	Q16576-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 1A4B4CD1A8E96815	FASTA	425	47,820
	10 20 30 40 50 60 MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP EVTKPEGKDY 70 80 90 100 110 120 ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD KGEFGGFGSV TGKIECEIKI 130 140 150 160 170 180 NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV FDYTKHPAKP DPSGECNPDL RLRGHQKEGY 190 200 210 220 230 240 GLSWNSNLSG HLLSASDDHT VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES 250 260 270 280 290 300 LFGSVADDQK LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW 310 320 330 340 350 360 DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG EEQSAEDAED 370 380 390 400 410 420 GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI WQMAENIYND EESDVTTSEL EGQGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 7503932] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RB1.
[2]	Nielsen M.S., Rasmussen H.H., Dejgaard K., Celis J.E., Leffers H. Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 9150135] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
[4]	"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: 9790534] [Abstract] Cited for: IDENTIFICATION IN THE NURD COMPLEX.
[5]	"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: 9427644] [Abstract] Cited for: INTERACTION WITH HAT1 AND HISTONE H4.
[6]	"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: 9651585] [Abstract] Cited for: IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
[7]	"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: 10444591] [Abstract] Cited for: IDENTIFICATION IN THE NURD COMPLEX.
[8]	"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: 10220405] [Abstract] Cited for: INTERACTION WITH BRCA1 AND RB1.
[9]	"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: 10866654] [Abstract] Cited for: FUNCTION, INTERACTION WITH CREBBP.
[10]	"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: 11102443] [Abstract] Cited for: IDENTIFICATION IN THE NURD COMPLEX.
[11]	"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: 11118440] [Abstract] Cited for: IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
[12]	"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: 12435631] [Abstract] Cited for: IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH EED; EZH2; RBBP4 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
[13]	"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: 11784859] [Abstract] Cited for: IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
[14]	"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: 14609955] [Abstract] Cited for: IDENTIFICATION IN THE NURF COMPLEX, MASS SPECTROMETRY.
[15]	"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: 12920132] [Abstract] Cited for: IDENTIFICATION IN THE MTA1 HDAC COMPLEX.
[16]	"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: 15456747] [Abstract] Cited for: INTERACTION WITH MBD3L1.
[17]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-119, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND THR-416, MASS SPECTROMETRY.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U35143 mRNA. Translation: AAC50231.1.
X72841 mRNA. Translation: CAA51360.1.

PIR

I39181.

RefSeq

NP_002884.1.

UniGene

Hs.495755

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CFS	X-ray	2.40	B	2-411	[»]
3CFV	X-ray	2.60	A/B	1-411	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:436N.

IntAct

Q16576.

PTM databases

PhosphoSite

Q16576.

2-D gel databases

Aarhus/Ghent-2DPAGE

7442. IEF.

Proteomic databases

PeptideAtlas

Q16576.

Genome annotation databases

Ensembl

ENSG00000102054. Homo sapiens. [Contig view]

GeneID

5931.

KEGG

hsa:5931.

Organism-specific databases

H-InvDB

HIX0021315.

HGNC

HGNC:9890. RBBP7.

MIM

602922. gene.

PharmGKB

PA34254.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOVERGEN

Q16576.

Gene expression databases

ArrayExpress

Q16576.

CleanEx

HS_RBBP7.

GermOnline

ENSG00000102054. Homo sapiens.

Family and domain databases

InterPro

IPR015943. WD40/YVTN_repeat-like.
IPR001680. WD40_repeat.
[Graphical view]

Gene3D

G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.

Pfam

PF00400. WD40. 5 hits.
[Graphical view]

PRINTS

PR00320. GPROTEINBRPT.

ProDom

PD000018. WD40. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00320. WD40. 6 hits.
[Graphical view]

PROSITE

PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

Q16576.

NextBio

23110.

SOURCE

Search...

Entry information

Entry name

RBBP7_HUMAN

Accession

Primary (citable) accession number: Q16576

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 25, 2008
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)