Q09028 (RBBP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. 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
Subcellular location	Nucleus.
Sequence similarities	Belongs to the WD repeat RBAP46/RBAP48/MSI1 family. Contains 6 WD repeats.

Ontologies

Keywords
Biological process	Cell cycle DNA replication Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat WD repeat
Molecular function	Chromatin regulator Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CENP-A containing nucleosome assembly at centromere Traceable author statement. Source: Reactome DNA replication Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle Traceable author statement. Source: Reactome negative regulation of cell proliferation Traceable author statement Ref.1. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	CAF-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
Molecular_function	histone binding Non-traceable author statement PubMed 17827154. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HDAC1	Q13547	5	EBI-620823,EBI-301834
ZFPM1	Q8IX07	4	EBI-620823,EBI-3942619

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 425

424

Histone-binding protein RBBP4

PRO_0000051186

Regions

Repeat

122 – 155

34

WD 1

Repeat

175 – 206

32

WD 2

Repeat

225 – 256

32

WD 3

Repeat

271 – 302

32

WD 4

Repeat

315 – 346

32

WD 5

Repeat

372 – 403

32

WD 6

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.9 Ref.38

Modified residue

4

1

N6-acetyllysine; alternate Ref.38

Modified residue

110

1

Phosphoserine Ref.37

Cross-link

4

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.36

Natural variations

Alternative sequence

1 – 35

35

Missing in isoform 4.

VSP_040087

Alternative sequence

7

1

Missing in isoform 2.

VSP_040088

Alternative sequence

405 – 425

21

AENIY…EGQGS → ELVLDH in isoform 3.

VSP_040089

Experimental info

Sequence conflict

61

1

F → G in AAH15123. Ref.8

Secondary structure

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425

Helix Strand Turn

Details...

Helix

17 – 31

15

Beta strand

32 – 39

8

Beta strand

48 – 54

7

Beta strand

62 – 69

8

Beta strand

73 – 75

3

Beta strand

78 – 86

9

Beta strand

115 – 122

8

Beta strand

128 – 133

6

Beta strand

136 – 143

8

Beta strand

145 – 147

3

Beta strand

149 – 153

5

Helix

154 – 156

3

Beta strand

170 – 174

5

Beta strand

180 – 185

6

Beta strand

187 – 189

3

Beta strand

192 – 197

6

Beta strand

202 – 206

5

Helix

207 – 209

3

Beta strand

213 – 218

6

Beta strand

220 – 223

4

Beta strand

230 – 235

6

Beta strand

242 – 247

6

Beta strand

250 – 256

7

Beta strand

262 – 264

3

Beta strand

266 – 270

5

Beta strand

276 – 281

6

Beta strand

288 – 293

6

Beta strand

296 – 302

7

Beta strand

310 – 314

5

Beta strand

320 – 325

6

Beta strand

332 – 337

6

Beta strand

342 – 346

5

Helix

347 – 349

3

Beta strand

366 – 370

5

Beta strand

377 – 382

6

Beta strand

384 – 386

3

Beta strand

389 – 394

6

Beta strand

397 – 404

8

Helix

406 – 409

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B71E2D55A444C360	FASTA	425	47,656
	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
	Isoform 2 [UniParc]. Checksum: 52055B5C74BCF3D8	FASTA	424	47,585
	10 20 30 40 50 60 MADKEAFDDA VEERVINEEY KIWKKNTPFL YDLVMTHALE WPSLTAQWLP DVTRPEGKDF 70 80 90 100 110 120 SIHRLVLGTH TSDEQNHLVI ASVQLPNDDA QFDASHYDSE KGEFGGFGSV SGKIEIEIKI 130 140 150 160 170 180 NHEGEVNRAR YMPQNPCIIA TKTPSSDVLV FDYTKHPSKP DPSGECNPDL RLRGHQKEGY 190 200 210 220 230 240 GLSWNPNLSG HLLSASDDHT ICLWDISAVP KEGKVVDAKT IFTGHTAVVE DVSWHLLHES 250 260 270 280 290 300 LFGSVADDQK LMIWDTRSNN TSKPSHSVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW 310 320 330 340 350 360 DLRNLKLKLH SFESHKDEIF QVQWSPHNET ILASSGTDRR LNVWDLSKIG EEQSPEDAED 370 380 390 400 410 420 GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQV WQMAENIYND EDPEGSVDPE GQGS
	Isoform 3 [UniParc]. Checksum: 59B630D6055A70B2	FASTA	410	46,158
	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 DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ VWQMELVLDH
	Isoform 4 [UniParc]. Checksum: A61A43F6AC30C8CE	FASTA	390	43,482
	10 20 30 40 50 60 MTHALEWPSL TAQWLPDVTR PEGKDFSIHR LVLGTHTSDE QNHLVIASVQ LPNDDAQFDA 70 80 90 100 110 120 SHYDSEKGEF GGFGSVSGKI EIEIKINHEG EVNRARYMPQ NPCIIATKTP SSDVLVFDYT 130 140 150 160 170 180 KHPSKPDPSG ECNPDLRLRG HQKEGYGLSW NPNLSGHLLS ASDDHTICLW DISAVPKEGK 190 200 210 220 230 240 VVDAKTIFTG HTAVVEDVSW HLLHESLFGS VADDQKLMIW DTRSNNTSKP SHSVDAHTAE 250 260 270 280 290 300 VNCLSFNPYS EFILATGSAD KTVALWDLRN LKLKLHSFES HKDEIFQVQW SPHNETILAS 310 320 330 340 350 360 SGTDRRLNVW DLSKIGEEQS PEDAEDGPPE LLFIHGGHTA KISDFSWNPN EPWVICSVSE 370 380 390 DNIMQVWQMA ENIYNDEDPE GSVDPEGQGS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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, 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]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-4, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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].
+	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.

IPI

IPI00328319.
IPI00645329.
IPI00877802.
IPI00877934.

PIR

S36112.

RefSeq

NP_001128727.1. NM_001135255.1.
NP_001128728.1. NM_001135256.1.
NP_005601.1. NM_005610.2.

UniGene

Hs.16003.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XU7	X-ray	1.90	A/B	1-425	[»]
3GFC	X-ray	2.30	A	1-425	[»]

ProteinModelPortal

Q09028.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33495N.

IntAct

Q09028. 37 interactions.

MINT

MINT-90543.

STRING

9606.ENSP00000362592.

PTM databases

PhosphoSite

Q09028.

Polymorphism databases

DMDM

1172846.

Proteomic databases

PaxDb

Q09028.

PRIDE

Q09028.

Protocols and materials databases

DNASU

5928.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373485; ENSP00000362584; ENSG00000162521.
ENST00000373493; ENSP00000362592; ENSG00000162521.
ENST00000414241; ENSP00000398242; ENSG00000162521.
ENST00000458695; ENSP00000396057; ENSG00000162521.

GeneID

5928.

KEGG

hsa:5928.

UCSC

uc001bvr.3. human.
uc001bvs.3. human.

Organism-specific databases

CTD

5928.

GeneCards

GC01P033116.

HGNC

HGNC:9887. RBBP4.

HPA

CAB006264.

MIM

602923. gene.

neXtProt

NX_Q09028.

PharmGKB

PA34251.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2319.

HOVERGEN

HBG053236.

InParanoid

Q09028.

KO

K10752.

OMA

CQPDLRL.

OrthoDB

EOG4DBTDH.

PhylomeDB

Q09028.

Enzyme and pathway databases

Pathway_Interaction_DB

hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

Q09028.

Bgee

Q09028.

CleanEx

HS_RBBP4.

Genevestigator

Q09028.

GermOnline

ENSG00000162521. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.10. 1 hit.

InterPro

IPR020472. G-protein_beta_WD-40_rep.
IPR022052. Histone-bd_RBBP4.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]

Pfam

PF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]

PRINTS

PR00320. GPROTEINBRPT.

SMART

SM00320. WD40. 6 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

RBBP4. human.

EvolutionaryTrace

Q09028.

GenomeRNAi

5928.

NextBio

23094.

SOURCE

Search...

Entry information

Entry name

RBBP4_HUMAN

Accession

Primary (citable) accession number: Q09028
Secondary accession number(s): B2R6G9 , B4DRH0, D3DPQ3, P31149, Q53H02, Q96BV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 145 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.